Entry
stringlengths 6
10
| Entry Name
stringlengths 5
11
| Sequence
stringlengths 2
35.2k
| EC number
stringlengths 7
118
⌀ | Cofactor
stringlengths 38
1.77k
⌀ | Gene Ontology (biological process)
stringlengths 18
11.3k
⌀ | Gene Ontology (cellular component)
stringlengths 17
1.75k
⌀ | Gene Ontology (molecular function)
stringlengths 24
2.09k
⌀ | Pfam
stringlengths 8
232
⌀ | Gene3D
stringlengths 10
250
⌀ | Protein families
stringlengths 9
237
⌀ | Post-translational modification
stringlengths 16
8.52k
⌀ | Subcellular location [CC]
stringlengths 29
6.18k
⌀ | Catalytic activity
stringlengths 64
35.7k
⌀ | Kinetics
stringlengths 69
11.7k
⌀ | Pathway
stringlengths 27
908
⌀ | pH dependence
stringlengths 64
955
⌀ | Temperature dependence
stringlengths 70
1.16k
⌀ | Function [CC]
stringlengths 17
15.3k
⌀ | Organism
stringlengths 8
196
|
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
O55156
|
CLIP2_RAT
|
MQKPSGLKPPGRGGKHSSPVGRPSIGSASSSVVASASGSKEGSPLHKQASGPSSAGATTTVSEKPGPKAAEVGDDFLGDFVVGERVWVNGVKPGVVQYLGETQFAPGQWAGVVLDDPVGKNDGAVGGLRYFECPALQGIFTRPSKLTRQPAAEGSGSDGHSVESLTAQNLSLHSGTATPPLTGRVIPLRESVLNSSVKTGNESGSNLSDSGSVKRGDKDLHLGDRVLVGGTKTGVVRYVGETDFAKGEWCGVELDEPLGKNDGAVAGTRYFQCPPKFGLFAPIHKVIRIGFPSTSPAKAKKTKRMAMGVSALTHSPSSSSISSVSSVASSVGGRPSRSGLLTETSSRYARKISGTTALQEALKEKQQHIEQLLAERDLERAEVAKATSHICEVEKEIALLKAQHEQYVAEAEEKLQRARLLVENVRKEKVDLSNQLEEERRKVEDLQFRVEEESITKGDLETQTQLEHARIGELEQSLLLEKAQAERLLRELADNRLTTVAEKSRVLQLEEELSLRRGEIEELQHCLLQSGPPPADHPEAAETLRLRERLLSASKEHQRDSTLLQDKYEHMLKTYQTEVDKLRAANEKYAQEVADLKAKVQQATTENMGLMDNWKSKLDSLASDHQKSLEDLKATLNSGPGAQQKEIGELKALVEGIKMEHQLELGNLQAKHDLETAMHGKEKEGLRQKLQEAQEELAGLQQHWRAQLEEQAAAPAELQEAQDQCRDAQLRVQELEGLDVEYRGQAQAIEFLKEQISLAEKKMLDYEMLQRAEAQSRQEAERLREKLLVAENRLQAVESLCSAQHSHVIESNDLSEEKIRMKETVEGLQDKLNKRDKEVAALTSQMDMLRAQVSALENKCKSGEKKIDSLLKEKRRLEAELEAVSRKTHDASGQLVHISQELLRKERSLNELRVLLLEANRHSPGPERDLSREVHKAEWRIKEQKLKDDIRGLREKLTGLDKEKSLSEQKRYSLIDPASAPELLRLQHQLVSTEGCLRDALDQAQQVERLVEALRGCSDRTQTISNSGSANGIHQPDKAHKQEDKH
| null | null |
cytoplasmic microtubule organization [GO:0031122]; negative regulation of microtubule depolymerization [GO:0007026]
|
cell cortex [GO:0005938]; cytoplasmic microtubule [GO:0005881]; dendrite [GO:0030425]; dendritic microtubule [GO:1901588]; lamellar body [GO:0042599]; microtubule cytoskeleton [GO:0015630]; microtubule plus-end [GO:0035371]; nucleus [GO:0005634]
|
microtubule binding [GO:0008017]; microtubule plus-end binding [GO:0051010]
|
PF01302;
|
2.30.30.190;
| null | null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:9427243}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:9427243}. Note=Localizes preferentially to the ends of tyrosinated microtubules. {ECO:0000250|UniProtKB:Q9Z0H8}.
| null | null | null | null | null |
FUNCTION: Seems to link microtubules to dendritic lamellar body (DLB), a membranous organelle predominantly present in bulbous dendritic appendages of neurons linked by dendrodendritic gap junctions. May operate in the control of brain-specific organelle translocations. {ECO:0000269|PubMed:9427243}.
|
Rattus norvegicus (Rat)
|
O55159
|
EPCAM_RAT
|
MAPPKALAFGLLLAVVTATLAAAQKDCVCNNYKLTSRCYENENGECQCTSYGTQNTVICSKLASKCLVMKAEMTHSKSGRRMKPEGAIQNNDGLYDPECDEQGLFKAKQCNGTATCWCVNTAGVRRTDKDTEITCSERVRTYWIIIELKHKERAQPYNFESLHTALQDTFASRYMLNPKFIKSIMYENNVITIDLMQNSSQKTQDDVDIADVAYYFEKDVKGESLFHSSKSMDLRVNGELLDLDPGQTLIYYVDEKAPEFSMQGLTAGIIAVIVVVVLAVIAGIVVLVISTRKRSAKYEKAEIKEMGEIHRELNA
| null | null |
cell-cell adhesion via plasma-membrane adhesion molecules [GO:0098742]; negative regulation of apoptotic process [GO:0043066]; negative regulation of cell-cell adhesion mediated by cadherin [GO:2000048]; positive regulation of cell motility [GO:2000147]; positive regulation of cell population proliferation [GO:0008284]; positive regulation of stem cell proliferation [GO:2000648]; positive regulation of transcription by RNA polymerase II [GO:0045944]; signal transduction involved in regulation of gene expression [GO:0023019]; stem cell differentiation [GO:0048863]; ureteric bud development [GO:0001657]
|
apical plasma membrane [GO:0016324]; basolateral plasma membrane [GO:0016323]; bicellular tight junction [GO:0005923]; cell surface [GO:0009986]; lateral plasma membrane [GO:0016328]; plasma membrane [GO:0005886]
|
cadherin binding involved in cell-cell adhesion [GO:0098641]; protein-containing complex binding [GO:0044877]
|
PF21283;PF18635;PF00086;
|
4.10.800.10;
|
EPCAM family
|
PTM: Glycosylation at Asn-198 is crucial for protein stability. {ECO:0000250}.
|
SUBCELLULAR LOCATION: Lateral cell membrane {ECO:0000269|PubMed:16054130}; Single-pass type I membrane protein {ECO:0000269|PubMed:16054130}. Cell junction, tight junction {ECO:0000269|PubMed:16054130}. Note=Colocalizes with CLDN7 at the lateral cell membrane and tight junction. {ECO:0000269|PubMed:16054130}.
| null | null | null | null | null |
FUNCTION: May act as a physical homophilic interaction molecule between intestinal epithelial cells (IECs) and intraepithelial lymphocytes (IELs) at the mucosal epithelium for providing immunological barrier as a first line of defense against mucosal infection. Plays a role in embryonic stem cells proliferation and differentiation. Up-regulates the expression of FABP5, MYC and cyclins A and E (By similarity). {ECO:0000250}.
|
Rattus norvegicus (Rat)
|
O55162
|
LYPD3_RAT
|
MDAARRGDTQPVMWTTRWLLLLPLLLCEGAQALECYSCVQKADDGCSPHKMKTVKCGPGVDVCTEAVGAVESIHGQFSVAVRGCGSGIPGKNDRGLDLHGLLAFIQLQQCTEDRCNAKLNLTLRGLNPAGNESAYEHNGAECYSCMGLSREKCQGAMPPVVNCYNASGRVYKGCFDGNVTLTAANVTVSLPVRGCVQDEACTRDGVTGPGFTLSGSCCQGPRCNSDLRNKTYFSPRIPPLVLLPPPTTPAPSTRTQNSSSTTSTTAPTTATTTIKPTTVQASHTSSTHETEHEVIQEEGSHLSGGATGHQDRSNMGKFPEKGGAQIPSKGGSDALGSWLSAILLTVVAGAML
| null | null |
cell-matrix adhesion [GO:0007160]; negative regulation of smooth muscle cell apoptotic process [GO:0034392]
|
membrane [GO:0016020]; plasma membrane [GO:0005886]; side of membrane [GO:0098552]
|
laminin binding [GO:0043236]
|
PF00021;
|
2.10.60.10;
| null | null |
SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor, GPI-anchor.
| null | null | null | null | null |
FUNCTION: Supports cell migration. May be involved in tumor progression. {ECO:0000269|PubMed:15729693, ECO:0000269|PubMed:9788443}.
|
Rattus norvegicus (Rat)
|
O55164
|
MPDZ_RAT
|
MLETIDKNRALQAAERLQSKLKERGDVANEDKLSLLKSVLQSPLFSQILSLQTSLQQLKDQVNVATLATANADHAHTPQFSSAIISNLQSESLLLSPSNGNLEAISGPGAPPAMDGKPACEELDQLIKSMAQGRHVEIFELLKPPCGGLGFSVVGLRSENRGELGIFVQEIQEGSVAHRDGRLKETDQILAINGQVLDQTITHQQAISILQKAKDTIQLVIARGSLPHISSPRISRSPSAASTVSAHSNPTHWQHVETIELVNDGSGLGFGIIGGKATGVIVKTILPGGVADQHGRLCSGDHILKIGDTDLAGMSSEQVAQVLRQCGNRVKLMIARGAVEETPAPSSLGITLSSSTSTSEMRVDASTQKNEESETFDVELTKNVQGLGITIAGYIGDKKLEPSGIFVKSITKSSAVELDGRIQIGDQIVAVDGTNLQGFTNQQAVEVLRHTGQTVRLTLMRKGASQEAEITSREDTAKDVDLPAENYEKDEESLSLKRSTSILPIEEEGYPLLSTELEETEDVQQEAALLTKWQRIMGINYEIVVAHVSKFSENSGLGISLEATVGHHFIRSVLPEGPVGHSGKLFSGDELLEVNGINLLGENHQDVVNILKELPIDVTMVCCRRTVPPTALSEVDSLDIHDLELTEKPHIDLGEFIGSSETEDPMLAMSDVDQNAEEIQTPLAMWEAGIQAIELEKGSRGLGFSILDYQDPIDPANTVIVIRSLVPGGIAEKDGRLFPGDRLMFVNDINLENSTLEEAVEALKGAPSGMVRIGVAKPLPLSPEEGYVSAKEDTFLCSPHTCKEMGLSDKALFRADLALIDTPDAESVAESRFESQFSPDNDSVYSTQASVLSLHDGACSDGMNYGPSLPSSPPKDVTNSSDLVLGLHLSLEELYTQNLLQRQHAGSPPTDMSPAATSGFTVSDYTPANAVEQKYECANTVAWTPSQLPSGLSTTELAPALPAVAPKYLTEQSSLVSDAESVTLQSMSQEAFERTVTIAKGSSSLGMTVSANKDGLGVIVRSIIHGGAISRDGRIAVGDCILSINEESTISLTNAQARAMLRRHSLIGPDIKITYVPAEHLEEFRVSFGQQAGGIMALDIFSSYTGRDIPELPEREEGEGEESELQNAAYSSWSQPRRVELWREPSKSLGISIVGGRGMGSRLSNGEVMRGIFIKHVLEDSPAGKNGTLKPGDRIVEVDGMDLRDASHEQAVEAIRKAGSPVVFMVQSIVNRPRKSPLPSLPHSLYPKCSFSSTNPFAESLQLTSDKAPSQSESESEKATLCSVPSSSPSVFSEMSSDYAQPSATTVAEDEDKEDEFGYSWKNIQERYGTLTGQLHMIELEKGHSGLGLSLAGNKDRTRMSVFIVGIDPTGAAGRDGRLQIADELLEINGQILYGRSHQNASSIIKCAPSKVKIIFIRNADAVNQMAVCPGSAADPLPSTSESPQNKEVEPSITTSASAVDLSSLTNVYHLELPKDQGGLGIAICEEDTLNGVTIKSLTERGGAAKDGRLKPGDRILAVDDELVAGCPIEKFISLLKTAKTTVKLTVGAENPGCQAVPSAAVTASGERKDSSQTPAVPAPDLEPIPSTSRSSTPAIFASDPATCPIIPGCETTIEISKGQTGLGLSIVGGSDTLLGAIIIHEVYEEGAACKDGRLWAGDQILEVNGIDLRKATHDEAINVLRQTPQRVRLTLYRDEAPYKEEDVCDTFTVELQKRPGKGLGLSIVGKRNDTGVFVSDIVKGGIADADGRLMQGDQILMVNGEDVRNATQEAVAALLKCSLGTVTLEVGRIKAAPFHSERRPSQSSQVSESSLSSFSLPRSGIHTSESSESSAKKNALASEIQGLRTVEIKKGPADALGLSIAGGVGSPLGDVPIFIAMMHPNGVAAQTQKLRVGDRIVTICGTSTDGMTHTQAVNLMKNASGSIEVQVVAGGDVSVVTGHQQELANPCLAFTGLTSSTIFPDDLGPPQSKTITLDRGPDGLGFSIVGGYGSPHGDLPIYVKTVFAKGAAAEDGRLKRGDQIIAVNGQSLEGVTHEEAVAILKRTKGTVTLMVLS
| null | null |
cell adhesion [GO:0007155]; dendrite development [GO:0016358]; intracellular protein transport [GO:0006886]; intracellular signal transduction [GO:0035556]; microtubule organizing center organization [GO:0031023]; myelination [GO:0042552]; regulation of microtubule cytoskeleton organization [GO:0070507]; tight junction assembly [GO:0120192]
|
apical part of cell [GO:0045177]; apical plasma membrane [GO:0016324]; apicolateral plasma membrane [GO:0016327]; bicellular tight junction [GO:0005923]; cytoplasm [GO:0005737]; cytoplasmic vesicle [GO:0031410]; dendrite [GO:0030425]; endomembrane system [GO:0012505]; glutamatergic synapse [GO:0098978]; plasma membrane [GO:0005886]; postsynaptic density [GO:0014069]; Schmidt-Lanterman incisure [GO:0043220]; subapical complex [GO:0035003]; synapse [GO:0045202]
| null |
PF09045;PF16667;PF00595;
|
2.30.42.10;1.10.287.650;
| null | null |
SUBCELLULAR LOCATION: Endomembrane system. Cell junction, tight junction. Synapse. Apical cell membrane {ECO:0000269|PubMed:11150294}. Postsynaptic density. Cell projection, dendrite. Synapse, synaptosome. Note=Associated with membranes. Enriched at the tight junctions of epithelial cells. Association to the tight junctions depends on CXADR. In the retina, localizes to the sub-apical region adjacent to the adherens junction complex at the outer limiting membrane (By similarity). Colocalizes with HTR2C on the apical membrane of epithelial choroid plexus cells (PubMed:11150294). Localized mainly in the Schmidt-Lanterman incisures of myelinating Schwann cells. Highly enriched in postsynaptic densities (PSD). Localized to punctae on dendrites of hippocampal neurons and colocalizes with the synaptic marker DLG4. {ECO:0000250, ECO:0000269|PubMed:11150294}.
| null | null | null | null | null |
FUNCTION: Member of the NMDAR signaling complex that may play a role in control of AMPAR potentiation and synaptic plasticity in excitatory synapses (PubMed:15312654). Promotes clustering of HT2RC at the cell surface (PubMed:11150294). {ECO:0000269|PubMed:11150294, ECO:0000269|PubMed:15312654}.
|
Rattus norvegicus (Rat)
|
O55165
|
KIF3C_RAT
|
MASKTKASEALKVVARCRPLSRKEEAAGHEQILTMDVKLGQVTLRNPRAAPGELPKTFTFDAVYDASSKQADLYDETVRPLIDSVLQGFNGTVFAYGQTGTGKTYTMQGTWVEPELRGVIPNAFEHIFTHISRSQNQQYLVRASYLEIYQEEIRDLLSKEPGKRLELKENPETGVYIKDLSSFVTKNVKEIEHVMNLGNQARAVGSTHMNEVSSRSHAIFVITVECSERGSDGQDHIRVGKLNLVDLAGSERQNKAGPNTPGGPATQSTAGGGGGGGGTSGSGSSGERPKEASKINLSLSALGNVIAALAGNRSTHIPYRDSKLTRLLQDSLGGNAKTIMVATLGPASHSYDESLSTLRFANRAKNIKNKPRVNEDPKDTLLREFQEEIARLKAQLEKKGMLGKRPRRKSSRRKKAVSAPAGYPEGAVIEAWVAEEEDDNNNNHRPPQPTLEAALEKNMENYLQEQKERLEEEKAAIQDDRSLVSEEKQKLLEEKEKMLEDLKREQQATELLAAKYKAMESKLLIGGRNIMDHTNEQQKMLELKRQEIAEQKRREREMQQEMLLRDEETMELRGTYSSLQQEVEVKTKKLKKLYAKLQAVKAEIQDQHEEYIRVRQDLEEAQNEQTRELKLKYLIIENFIPPEEKNKIMNRLFLDCEEEQWKFQPLVPAGVNNSQMKKRPTSAVGYKRPISQYARVAMAMGSHPRYRAENIMFLELDVSPPAIFEMEFSHDQEQDPRVLHMERLMRLDSFLERPSTSKVRKSRSWCQSPQRPPPPSTVHASMASAPLHPATVVDHD
| null | null |
microtubule-based movement [GO:0007018]; mitotic cell cycle [GO:0000278]; positive regulation of neuron projection development [GO:0010976]
|
axon [GO:0030424]; dendrite [GO:0030425]; growth cone [GO:0030426]; kinesin complex [GO:0005871]; microtubule [GO:0005874]; microtubule cytoskeleton [GO:0015630]; microtubule plus-end [GO:0035371]; neuronal cell body [GO:0043025]; neuronal ribonucleoprotein granule [GO:0071598]; synaptic vesicle [GO:0008021]
|
ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; kinesin binding [GO:0019894]; microtubule binding [GO:0008017]; microtubule motor activity [GO:0003777]
|
PF00225;
|
3.40.850.10;
|
TRAFAC class myosin-kinesin ATPase superfamily, Kinesin family, Kinesin II subfamily
| null |
SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000305}.
| null | null | null | null | null |
FUNCTION: Microtubule-based anterograde translocator for membranous organelles.
|
Rattus norvegicus (Rat)
|
O55166
|
VPS52_RAT
|
MAAAATMAAAARELVLRAGASDMEEEEGPLGAGSGLQEPLQLGELDITSDEFILDEVDVHIQANLEDELVKEALKTGVDLRHYSKQVELELQQIEQKSIRDYIQESENIASLHNQITACDAVLERMEQMLGAFQSDLSSISCEIRTLQEQSGAMNIRLRNRQAVRGKLGELVDGLVVPSALVTAILEAPVTEPRFLEQLQELDAKAAAVREQEARGTAACADVRGVLDRLRVKAVTKIREFILQKIYSFRKPMTNYQIPQTALLKYRFFYQFLLGNERATAKEVRDEYVETLSKIYLSYYRSYVGRLMKVQYEEVAEKDDLMGVEDTAKKGFFSKPSLRSRNTIFTLGTRGAVISPAELEAPILVPHTAQRGEQRYPFEALFRSQHYALLDNSCREYLFICEFFVVSGPAAHDLFHAVMGRTLSMTLKHLESYLADCYDAIAVFLCIHIVLRFRNIAAKRDVPALDRYWEQVLALLWPRFELILEMNVQSVRSTDPQRLGGLDTRPHYITRRYAEFSSALVSINQTIPNERTLQLLGQLQVEVENFVLRVAAEFSSRKEQLVFLINNYDMMLGVLMERAADDSKEVESFQQLLNARTQEFIEELLSPPFGGLVAFVKEAEALIERGQAERLRGEEARVTQLIRGFGSSWKASVESLSQDVMRSFTNFRNGTSIIQGALTQLIQLYHRFHRVLSQPQLRALPARAELINIHHLMVELKKHKPNF
| null | null |
ectodermal cell differentiation [GO:0010668]; embryonic ectodermal digestive tract development [GO:0048611]; endocytic recycling [GO:0032456]; Golgi to vacuole transport [GO:0006896]; lysosomal transport [GO:0007041]; protein targeting [GO:0006605]; protein transport [GO:0015031]; retrograde transport, endosome to Golgi [GO:0042147]; vesicle-mediated cholesterol transport [GO:0090119]
|
cytosol [GO:0005829]; EARP complex [GO:1990745]; endosome membrane [GO:0010008]; GARP complex [GO:0000938]; Golgi apparatus [GO:0005794]; membrane [GO:0016020]; perinuclear region of cytoplasm [GO:0048471]; recycling endosome [GO:0055037]
|
syntaxin binding [GO:0019905]
|
PF20655;PF04129;
| null |
VPS52 family
| null |
SUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network membrane {ECO:0000250|UniProtKB:Q8N1B4}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q8N1B4}. Endosome membrane {ECO:0000250|UniProtKB:Q8N1B4}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q8N1B4}. Recycling endosome {ECO:0000250|UniProtKB:Q8N1B4}. Note=Localizes to the trans-Golgi network as part of the GARP complex, while it localizes to recycling endosomes as part of the EARP complex. {ECO:0000250|UniProtKB:Q8N1B4}.
| null | null | null | null | null |
FUNCTION: Acts as a component of the GARP complex that is involved in retrograde transport from early and late endosomes to the trans-Golgi network (TGN). The GARP complex is required for the maintenance of the cycling of mannose 6-phosphate receptors between the TGN and endosomes, this cycling is necessary for proper lysosomal sorting of acid hydrolases such as CTSD. Acts as a component of the EARP complex that is involved in endocytic recycling. The EARP complex associates with Rab4-positive endosomes and promotes recycling of internalized transferrin receptor (TFRC) to the plasma membrane. {ECO:0000250|UniProtKB:Q8N1B4}.
|
Rattus norvegicus (Rat)
|
O55170
|
SOX10_RAT
|
MAEEQDLSEVELSPVGSEEPRCLSPSSAPSLGPDGGGGGSGLRASPGPGELGKVKKEQQDGEADDDKFPVCIREAVSQVLSGYDWTLVPMPVRVNGASKSKPHVKRPMNAFMVWAQAARRKLADQYPHLHNAELSKTLGKLWRLLNESDKRPFIEEAERLRMQHKKDHPDYKYQPRRRKNGKAAQGEAECPGGETDQGGAAAIQAHYKSAHLDHRHPEEGSPMSDGNPEHPSGQSHGPPTPPTTPKTELQSGKADPKRDGRSLGEGGKPHIDFGNVDIGEISHEVMSNMETFDVTELDQYLPPNGHPGHVGSYSAAGYGLSSALAVASGHSAWISKPPGVALPTVSPPAVDAKAQVKTETTGPQGPPHYTDQPSTSQIAYTSLSLPHYGSAFPSISRPQFDYSDHQPSGPYYGHAGQASGLYSAFSYMGPSQRPLYTAISDPSPSGPQSHSPTHWEQPVYTTLSRP
| null | null |
cell development [GO:0048468]; cell differentiation [GO:0030154]; cell maturation [GO:0048469]; cellular response to progesterone stimulus [GO:0071393]; cellular response to xenobiotic stimulus [GO:0071466]; central nervous system myelination [GO:0022010]; developmental growth [GO:0048589]; digestive tract morphogenesis [GO:0048546]; enteric nervous system development [GO:0048484]; in utero embryonic development [GO:0001701]; lacrimal gland development [GO:0032808]; melanocyte differentiation [GO:0030318]; morphogenesis of a branching epithelium [GO:0061138]; morphogenesis of an epithelium [GO:0002009]; negative regulation of apoptotic process [GO:0043066]; negative regulation of canonical Wnt signaling pathway [GO:0090090]; negative regulation of DNA-templated transcription [GO:0045892]; negative regulation of Schwann cell proliferation [GO:0010626]; negative regulation of transcription by RNA polymerase II [GO:0000122]; neural crest cell migration [GO:0001755]; neuroblast proliferation [GO:0007405]; oligodendrocyte development [GO:0014003]; oligodendrocyte differentiation [GO:0048709]; peripheral nervous system development [GO:0007422]; positive regulation of DNA-templated transcription [GO:0045893]; positive regulation of gene expression [GO:0010628]; positive regulation of gliogenesis [GO:0014015]; positive regulation of myelination [GO:0031643]; positive regulation of neuroblast proliferation [GO:0002052]; positive regulation of transcription by RNA polymerase II [GO:0045944]; regulation of DNA-templated transcription [GO:0006355]; stem cell differentiation [GO:0048863]; transcription by RNA polymerase II [GO:0006366]; transcription elongation by RNA polymerase II [GO:0006368]
|
chromatin [GO:0000785]; cytoplasm [GO:0005737]; mitochondrial outer membrane [GO:0005741]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]
|
chromatin binding [GO:0003682]; DNA binding [GO:0003677]; DNA-binding transcription activator activity [GO:0001216]; DNA-binding transcription factor activity [GO:0003700]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; DNA-binding transcription factor binding [GO:0140297]; identical protein binding [GO:0042802]; promoter-specific chromatin binding [GO:1990841]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]; sequence-specific double-stranded DNA binding [GO:1990837]; transcription cis-regulatory region binding [GO:0000976]
|
PF00505;PF12444;
|
1.10.30.10;
| null | null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q04888}. Nucleus {ECO:0000269|PubMed:9412504}. Mitochondrion outer membrane {ECO:0000250|UniProtKB:Q04888}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q04888}; Cytoplasmic side {ECO:0000250|UniProtKB:Q04888}.
| null | null | null | null | null |
FUNCTION: Transcription factor that plays a central role in developing and mature glia (By similarity). Specifically activates expression of myelin genes, during oligodendrocyte (OL) maturation, such as DUSP15 and MYRF, thereby playing a central role in oligodendrocyte maturation and CNS myelination (By similarity). Once induced, MYRF cooperates with SOX10 to implement the myelination program (By similarity). Transcriptional activator of MITF, acting synergistically with PAX3 (By similarity). Transcriptional activator of MBP, via binding to the gene promoter (PubMed:26525805). {ECO:0000250|UniProtKB:P56693, ECO:0000250|UniProtKB:Q04888, ECO:0000269|PubMed:26525805}.
|
Rattus norvegicus (Rat)
|
O55171
|
ACOT2_RAT
|
MVASSFAVLRASRLCQWGWKSWTQLSGPPPLSTGGRTTFARTNATLSLEPGSRSCWDEPLSITVRGLAPEQPVTLRAALRDEKGALFRAHARYRADAGGELDLARAPALGGSFTGLEPMGLIWAMEPERPLWRLVKRDVQKPYVVELEVLDGHEPDGGQRLAQAVHERHFMAPGVRRVPVRDGRVRATLFLPPEPGPFPEIIDLFGVGGGLLEYRASLLAGKGFAVMALAYYNYDDLPKTMETMRIEYFEEAVNYLRGHPEVKGPGIGLLGISKGGELGLAMASFLKGITAAVVINGSVAAVGNTVCYKDETIPPVSLLRDKVKMTKDGLLDVVEALQSPLVDKKSFIPVERSDTTFLFLVGQDDHNWKSEFYAREASKRLQAHGKEKPQIICYPEAGHYIEPPYFPLCSAGMHLLVGANITFGGEPKPHSVAQLDAWQQLQTFFHKQLSGKS
|
3.1.2.2
| null |
acyl-CoA metabolic process [GO:0006637]; fatty acid metabolic process [GO:0006631]; long-chain fatty acid metabolic process [GO:0001676]; long-chain fatty-acyl-CoA catabolic process [GO:0036116]; response to epidermal growth factor [GO:0070849]; response to hormone [GO:0009725]; response to hypoxia [GO:0001666]; response to nutrient levels [GO:0031667]; response to xenobiotic stimulus [GO:0009410]; very long-chain fatty acid metabolic process [GO:0000038]
|
mitochondrial matrix [GO:0005759]; mitochondrion [GO:0005739]
|
carboxylic ester hydrolase activity [GO:0052689]; fatty acyl-CoA hydrolase activity [GO:0047617]; long-chain fatty acyl-CoA hydrolase activity [GO:0052816]
|
PF08840;PF04775;
|
2.60.40.2240;3.40.50.1820;
|
C/M/P thioester hydrolase family
|
PTM: The N-terminus is blocked.
|
SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000269|PubMed:7744868}.
|
CATALYTIC ACTIVITY: Reaction=H2O + hexadecanoyl-CoA = CoA + H(+) + hexadecanoate; Xref=Rhea:RHEA:16645, ChEBI:CHEBI:7896, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:57379; EC=3.1.2.2; Evidence={ECO:0000269|PubMed:7744868}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16646; Evidence={ECO:0000305|PubMed:7744868}; CATALYTIC ACTIVITY: Reaction=H2O + tetradecanoyl-CoA = CoA + H(+) + tetradecanoate; Xref=Rhea:RHEA:40119, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30807, ChEBI:CHEBI:57287, ChEBI:CHEBI:57385; Evidence={ECO:0000269|PubMed:7744868}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40120; Evidence={ECO:0000305|PubMed:7744868}; CATALYTIC ACTIVITY: Reaction=H2O + octadecanoyl-CoA = CoA + H(+) + octadecanoate; Xref=Rhea:RHEA:30139, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:25629, ChEBI:CHEBI:57287, ChEBI:CHEBI:57394; Evidence={ECO:0000269|PubMed:7744868}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:30140; Evidence={ECO:0000305|PubMed:7744868}; CATALYTIC ACTIVITY: Reaction=eicosanoyl-CoA + H2O = CoA + eicosanoate + H(+); Xref=Rhea:RHEA:40147, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:32360, ChEBI:CHEBI:57287, ChEBI:CHEBI:57380; Evidence={ECO:0000269|PubMed:7744868}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40148; Evidence={ECO:0000305|PubMed:7744868}; CATALYTIC ACTIVITY: Reaction=decanoyl-CoA + H2O = CoA + decanoate + H(+); Xref=Rhea:RHEA:40059, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:27689, ChEBI:CHEBI:57287, ChEBI:CHEBI:61430; Evidence={ECO:0000269|PubMed:7744868}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40060; Evidence={ECO:0000305|PubMed:7744868}; CATALYTIC ACTIVITY: Reaction=dodecanoyl-CoA + H2O = CoA + dodecanoate + H(+); Xref=Rhea:RHEA:30135, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:18262, ChEBI:CHEBI:57287, ChEBI:CHEBI:57375; Evidence={ECO:0000269|PubMed:7744868}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:30136; Evidence={ECO:0000305|PubMed:7744868}; CATALYTIC ACTIVITY: Reaction=(9Z)-octadecenoyl-CoA + H2O = (9Z)-octadecenoate + CoA + H(+); Xref=Rhea:RHEA:40139, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30823, ChEBI:CHEBI:57287, ChEBI:CHEBI:57387; Evidence={ECO:0000250|UniProtKB:P49753}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40140; Evidence={ECO:0000250|UniProtKB:P49753}; CATALYTIC ACTIVITY: Reaction=(9Z)-hexadecenoyl-CoA + H2O = (9Z)-hexadecenoate + CoA + H(+); Xref=Rhea:RHEA:40131, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:32372, ChEBI:CHEBI:57287, ChEBI:CHEBI:61540; Evidence={ECO:0000250|UniProtKB:P49753}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40132; Evidence={ECO:0000250|UniProtKB:P49753}; CATALYTIC ACTIVITY: Reaction=(9E)-octadecenoyl-CoA + H2O = (9E)-octadecenoate + CoA + H(+); Xref=Rhea:RHEA:40723, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30825, ChEBI:CHEBI:57287, ChEBI:CHEBI:77537; Evidence={ECO:0000250|UniProtKB:P49753}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40724; Evidence={ECO:0000250|UniProtKB:P49753}; CATALYTIC ACTIVITY: Reaction=(9Z,12Z)-octadecadienoyl-CoA + H2O = (9Z,12Z)-octadecadienoate + CoA + H(+); Xref=Rhea:RHEA:40143, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30245, ChEBI:CHEBI:57287, ChEBI:CHEBI:57383; Evidence={ECO:0000250|UniProtKB:Q9QYR9}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40144; Evidence={ECO:0000250|UniProtKB:Q9QYR9};
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=16 uM for C10-acyl-CoA {ECO:0000269|PubMed:7744868}; KM=5 uM for C12-acyl-CoA {ECO:0000269|PubMed:7744868}; KM=3 uM for C14-acyl-CoA {ECO:0000269|PubMed:7744868}; KM=6 uM for C16-acyl-CoA {ECO:0000269|PubMed:7744868}; KM=3 uM for C18-acyl-CoA {ECO:0000269|PubMed:7744868}; KM=2 uM for C20-acyl-CoA {ECO:0000269|PubMed:7744868}; Vmax=1 umol/min/mg enzyme with C10-acyl-CoA as substrate {ECO:0000269|PubMed:7744868}; Vmax=2.2 umol/min/mg enzyme with C12-acyl-CoA as substrate {ECO:0000269|PubMed:7744868}; Vmax=4.2 umol/min/mg enzyme with C14-acyl-CoA as substrate {ECO:0000269|PubMed:7744868}; Vmax=4.5 umol/min/mg enzyme with C16-acyl-CoA as substrate {ECO:0000269|PubMed:7744868}; Vmax=3.3 umol/min/mg enzyme with C18-acyl-CoA as substrate {ECO:0000269|PubMed:7744868}; Vmax=3.1 umol/min/mg enzyme with C20-acyl-CoA as substrate {ECO:0000269|PubMed:7744868};
|
PATHWAY: Lipid metabolism; fatty acid metabolism. {ECO:0000305|PubMed:7744868}.
|
BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8-9. {ECO:0000269|PubMed:7744868};
| null |
FUNCTION: Catalyzes the hydrolysis of acyl-CoAs into free fatty acids and coenzyme A (CoASH), regulating their respective intracellular levels (By similarity). Displays higher activity toward long chain acyl CoAs (C14-C20) (PubMed:7744868). The enzyme is involved in enhancing the hepatic fatty acid oxidation in mitochondria (By similarity). {ECO:0000250|UniProtKB:Q9QYR9, ECO:0000269|PubMed:7744868}.
|
Rattus norvegicus (Rat)
|
O55173
|
PDPK1_RAT
|
MARTTSQLYDAVPIQSSVVLCSCPSPSMVRSQTEPSSSPGIPSGVSRQGSTMDGTTAEARPSTNPLQQHPAQLPPQPRKKRPEDFKFGKILGEGSFSTVVLARELATSREYAIKILEKRHIIKENKVPYVTRERDVMSRLDHPFFVKLYFTFQDDEKLYFGLSYAKNGELLKYIRKIGSFDETCTRFYTAEIVSALEYLHGKGIIHRDLKPENILLNEDMHIQITDFGTAKVLSPDSKQARANSFVGTAQYVSPELLTEKSACKSSDLWALGCIIYQLVAGLPPFRAGNEYLIFQKIIKLEYDFPEKFFPKARDLVEKLLVLDATKRLGCEEMEGYGPLKAHPFFESITWENLHQQTPPKLTAYLPAMSEDDEDCYGNYDNLLSQFGCMQVSSSSSSHSLSAVDASLPQRSGSNIEQYIHDLDTNSFELDLQFSEDEKRLLLEKQAGGNPWHQFVENNLILKMGPVDKRKGLFARRRQLLLTEGPHLYYVDPVNKVLKGEIPWSQELRPEAKNFKTFFVHTPNRTYYLMDPSGNAHKWCRKIQEVWRQQYQSSPDAAVQ
|
2.7.11.1
| null |
calcium-mediated signaling [GO:0019722]; cell migration [GO:0016477]; cellular response to brain-derived neurotrophic factor stimulus [GO:1990416]; cellular response to epidermal growth factor stimulus [GO:0071364]; cellular response to insulin stimulus [GO:0032869]; epidermal growth factor receptor signaling pathway [GO:0007173]; extrinsic apoptotic signaling pathway [GO:0097191]; focal adhesion assembly [GO:0048041]; hyperosmotic response [GO:0006972]; insulin receptor signaling pathway [GO:0008286]; insulin-like growth factor receptor signaling pathway [GO:0048009]; intracellular signal transduction [GO:0035556]; negative regulation of cardiac muscle cell apoptotic process [GO:0010667]; negative regulation of endothelial cell apoptotic process [GO:2000352]; negative regulation of neuron apoptotic process [GO:0043524]; negative regulation of toll-like receptor signaling pathway [GO:0034122]; negative regulation of transforming growth factor beta receptor signaling pathway [GO:0030512]; phosphorylation [GO:0016310]; positive regulation of angiogenesis [GO:0045766]; positive regulation of blood vessel endothelial cell migration [GO:0043536]; positive regulation of protein localization to plasma membrane [GO:1903078]; positive regulation of release of sequestered calcium ion into cytosol [GO:0051281]; positive regulation of sprouting angiogenesis [GO:1903672]; positive regulation of vascular endothelial cell proliferation [GO:1905564]; regulation of canonical NF-kappaB signal transduction [GO:0043122]; regulation of endothelial cell migration [GO:0010594]; regulation of mast cell degranulation [GO:0043304]; type B pancreatic cell development [GO:0003323]
|
cell projection [GO:0042995]; cytoplasm [GO:0005737]; cytoplasmic vesicle [GO:0031410]; focal adhesion [GO:0005925]; nucleus [GO:0005634]; perikaryon [GO:0043204]; plasma membrane [GO:0005886]; postsynaptic density [GO:0014069]
|
3-phosphoinositide-dependent protein kinase activity [GO:0004676]; ATP binding [GO:0005524]; insulin receptor binding [GO:0005158]; phospholipase activator activity [GO:0016004]; phospholipase binding [GO:0043274]; protein kinase binding [GO:0019901]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674]
|
PF14593;PF00069;
|
2.30.29.30;1.10.510.10;
|
Protein kinase superfamily, AGC Ser/Thr protein kinase family, PDPK1 subfamily
|
PTM: Phosphorylation on Ser-244 in the activation loop is required for full activity. PDPK1 itself can autophosphorylate Ser-244, leading to its own activation. Autophosphorylation is inhibited by the apoptotic C-terminus cleavage product of PKN2. Tyr-9 phosphorylation is critical for stabilization of both PDPK1 and the PDPK1/SRC complex via HSP90-mediated protection of PDPK1 degradation. Angiotensin II stimulates the tyrosine phosphorylation of PDPK1 in vascular smooth muscle in a calcium- and SRC-dependent manner. Phosphorylated on Tyr-9, Tyr-376 and Tyr-379 by INSR in response to insulin. Palmitate negatively regulates autophosphorylation at Ser-244 and palmitate-induced phosphorylation at Ser-532 and Ser-504 by PKC/PRKCQ negatively regulates its ability to phosphorylate PKB/AKT1. Phosphorylation at Thr-357 by MELK partially inhibits kinase activity, the inhibition is cooperatively enhanced by phosphorylation at Ser-397 and Ser-401 by MAP3K5 (By similarity). {ECO:0000250}.; PTM: Monoubiquitinated in the kinase domain, deubiquitinated by USP4. {ECO:0000250}.
|
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. Cell membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Cell junction, focal adhesion {ECO:0000250}. Note=Tyrosine phosphorylation seems to occur only at the cell membrane. Translocates to the cell membrane following insulin stimulation by a mechanism that involves binding to GRB14 and INSR. SRC and HSP90 promote its localization to the cell membrane. Its nuclear localization is dependent on its association with PTPN6 and its phosphorylation at Ser-396. Restricted to the nucleus in neuronal cells while in non-neuronal cells it is found in the cytoplasm. The Ser-244 phosphorylated form is distributed along the perinuclear region in neuronal cells while in non-neuronal cells it is found in both the nucleus and the cytoplasm. IGF1 transiently increases phosphorylation at Ser-244 of neuronal PDPK1, resulting in its translocation to other cellular compartments. The tyrosine-phosphorylated form colocalizes with PTK2B in focal adhesions after angiotensin II stimulation (By similarity). {ECO:0000250}.
|
CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.1;
| null | null | null | null |
FUNCTION: Serine/threonine kinase which acts as a master kinase, phosphorylating and activating a subgroup of the AGC family of protein kinases. Its targets include: protein kinase B (PKB/AKT1, PKB/AKT2, PKB/AKT3), p70 ribosomal protein S6 kinase (RPS6KB1), p90 ribosomal protein S6 kinase (RPS6KA1, RPS6KA2 and RPS6KA3), cyclic AMP-dependent protein kinase (PRKACA), protein kinase C (PRKCD and PRKCZ), serum and glucocorticoid-inducible kinase (SGK1, SGK2 and SGK3), p21-activated kinase-1 (PAK1), protein kinase PKN (PKN1 and PKN2). Plays a central role in the transduction of signals from insulin by providing the activating phosphorylation to PKB/AKT1, thus propagating the signal to downstream targets controlling cell proliferation and survival, as well as glucose and amino acid uptake and storage. Negatively regulates the TGF-beta-induced signaling by: modulating the association of SMAD3 and SMAD7 with TGF-beta receptor, phosphorylating SMAD2, SMAD3, SMAD4 and SMAD7, preventing the nuclear translocation of SMAD3 and SMAD4 and the translocation of SMAD7 from the nucleus to the cytoplasm in response to TGF-beta. Activates PPARG transcriptional activity and promotes adipocyte differentiation. Activates the NF-kappa-B pathway via phosphorylation of IKKB. The tyrosine phosphorylated form is crucial for the regulation of focal adhesions by angiotensin II. Controls proliferation, survival, and growth of developing pancreatic cells. Participates in the regulation of Ca(2+) entry and Ca(2+)-activated K(+) channels of mast cells. Essential for the motility of vascular endothelial cells (ECs) and is involved in the regulation of their chemotaxis. Plays a critical role in cardiac homeostasis by serving as a dual effector for cell survival and beta-adrenergic response. Plays an important role during thymocyte development by regulating the expression of key nutrient receptors on the surface of pre-T cells and mediating Notch-induced cell growth and proliferative responses. Provides negative feedback inhibition to toll-like receptor-mediated NF-kappa-B activation in macrophages (By similarity). {ECO:0000250, ECO:0000269|PubMed:11781095}.
|
Rattus norvegicus (Rat)
|
O55174
|
ZNT4_RAT
|
MAGPGAWKRLKSLLRKDDAPLFLNDTSAFDFLDEVSDEGLSRFNKLRVVVADDDSEAPERPVNGAHPALQADDDSLLDQELPLTNSQLSLKMDPCDNCSKRRELLKQRKVKTRLTIAAVLYLLFMIGELVGGYMANSLAIMTDALHMLTDLSAIILTLLALWLSSKSPTRRFTFGFHRLEVLSAMISVMLVYVLMGFLLYEAMQRTIHMNYEINGDVMLITAAVGVAVNVIMGFLLNQSGHHHSHAHSHSLPSNSPSMVSSGHSHGQDSLAVRAAFVHALGDLVQSVGVLIAAYIIRFKPEYKIADPICTYIFSLLVAFTTLRIIWDTVVIILEGVPSHLNVDYIKESLMKIEDVYSVEDLNIWSLTSGKATAIVHMQLIPGSSSKWEEVQSKAKHLLLNTFGMYKCTVQLQSYRQEATRTCANCQSSST
| null | null |
lactation [GO:0007595]; response to toxic substance [GO:0009636]; response to vitamin A [GO:0033189]; response to zinc ion [GO:0010043]; zinc export across plasma membrane [GO:0140882]; zinc ion import into lysosome [GO:0140916]; zinc ion transmembrane transport [GO:0071577]; zinc ion transport [GO:0006829]
|
cytoplasm [GO:0005737]; endosome membrane [GO:0010008]; late endosome [GO:0005770]; late endosome membrane [GO:0031902]; lysosomal membrane [GO:0005765]; plasma membrane [GO:0005886]
|
antiporter activity [GO:0015297]; metal ion binding [GO:0046872]; zinc ion transmembrane transporter activity [GO:0005385]
|
PF01545;
|
1.20.1510.10;
|
Cation diffusion facilitator (CDF) transporter (TC 2.A.4) family, SLC30A subfamily
| null |
SUBCELLULAR LOCATION: Endosome membrane {ECO:0000269|PubMed:10600821}; Multi-pass membrane protein {ECO:0000255}. Late endosome membrane {ECO:0000250|UniProtKB:O14863}; Multi-pass membrane protein {ECO:0000255}. Lysosome membrane {ECO:0000250|UniProtKB:O14863}; Multi-pass membrane protein {ECO:0000255}. Note=Enriched in vesicles within the basal region of epithelial cells. {ECO:0000269|PubMed:10600821, ECO:0000269|PubMed:12388418}.
|
CATALYTIC ACTIVITY: Reaction=2 H(+)(out) + Zn(2+)(in) = 2 H(+)(in) + Zn(2+)(out); Xref=Rhea:RHEA:72627, ChEBI:CHEBI:15378, ChEBI:CHEBI:29105; Evidence={ECO:0000250|UniProtKB:O14863};
| null | null | null | null |
FUNCTION: Probable proton-coupled zinc ion antiporter mediating zinc import from cytoplasm potentially into the endocytic compartment (By similarity). Controls zinc deposition in milk (By similarity). {ECO:0000250|UniProtKB:O14863, ECO:0000250|UniProtKB:O35149}.
|
Rattus norvegicus (Rat)
|
O55176
|
PJA1_MOUSE
|
MSHQERIASQRRTTAEVPMHRSTANQSKRSRSPFASTRRRWDDSESSGASLAVESEDYSRYPPREYRASGSRRGLAYGHIDTVVARDSEEEGAGPVDRLPVRGKAGKFKDDPEKGARSSRFTSVNHDAKEECGKVESPPAARCSARRAELSKQNGSSASQISSAEGRAAAKGNNSLERERQNLPARPSRAPVSICGGGENTPKSAEEPVVRPKVRNVATPNCMKPKVFFDTDDDDDVPHSTSRWRDAADAEEAHAEGLARRGRGEAASSSEPRYAEDQDARSEQAKADKVPRRRRTMADPDFWAYTDDYYRYYEEDSDSDKEWMAALRRKYRSREQPQSSSGESWELLPGKEELERQQAGAGSLASAGSNGSGYPEEVQDPSLQEEEQASLEEGEIPWLRYNENESSSEGDNESTHELIQPGMFMLDGNNNLEDDSSVSEDLEVDWSLFDGFADGLGVAEAISYVDPQFLTYMALEERLAQAMETALAHLESLAVDVEVANPPASKESIDALPEILVTEDHGAVGQEMCCPICCSEYVKGEVATELPCHHYFHKPCVSIWLQKSGTCPVCRCMFPPPL
|
2.3.2.27
| null |
protein catabolic process [GO:0030163]; protein ubiquitination [GO:0016567]
|
cytoplasm [GO:0005737]
|
metal ion binding [GO:0046872]; ubiquitin protein ligase activity [GO:0061630]
|
PF13639;
|
3.30.40.10;
| null |
PTM: Substrate for E2-dependent ubiquitination.
| null |
CATALYTIC ACTIVITY: Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.; EC=2.3.2.27;
| null | null | null | null |
FUNCTION: Has E2-dependent E3 ubiquitin-protein ligase activity. Ubiquitinates MAGED1 antigen leading to its subsequent degradation by proteasome. May be involved in protein sorting. {ECO:0000269|PubMed:10500182, ECO:0000269|PubMed:12036302}.
|
Mus musculus (Mouse)
|
O55183
|
STC1_MOUSE
|
MLQNSAVILALVISAAAAHEAEQNDSVSPRKSRVAAQNSAEVVRCLNSALQVGCGAFACLENSTCDTDGMYDICKSFLYSAAKFDTQGKAFVKESLKCIANGITSKVFLAIRRCSTFQRMIAEVQEDCYSKLNVCSIAKRNPEAITEVIQLPNHFSNRYYNRLVRSLLECDEDTVSTIRDSLMEKIGPNMASLFHILQTDHCAQTHPRADFNRRRTNEPQKLKVLLRNLRGEGDSPSHIKRTSQESA
| null | null |
cellular response to cAMP [GO:0071320]; cellular response to glucocorticoid stimulus [GO:0071385]; cellular response to hypoxia [GO:0071456]; chondrocyte proliferation [GO:0035988]; decidualization [GO:0046697]; embryo implantation [GO:0007566]; endothelial cell morphogenesis [GO:0001886]; growth plate cartilage axis specification [GO:0003421]; intracellular calcium ion homeostasis [GO:0006874]; intracellular monoatomic anion homeostasis [GO:0030002]; negative regulation of calcium ion transport [GO:0051926]; negative regulation of endothelial cell migration [GO:0010596]; negative regulation of renal phosphate excretion [GO:1903403]; ossification [GO:0001503]; positive regulation of calcium ion import [GO:0090280]; regulation of cardiac muscle cell contraction [GO:0086004]; regulation of monoatomic anion transport [GO:0044070]; response to vitamin D [GO:0033280]
|
apical plasma membrane [GO:0016324]; cytoplasm [GO:0005737]; extracellular space [GO:0005615]; nucleus [GO:0005634]
|
hormone activity [GO:0005179]; identical protein binding [GO:0042802]
|
PF03298;
| null |
Stanniocalcin family
| null |
SUBCELLULAR LOCATION: Secreted.
| null | null | null | null | null |
FUNCTION: Stimulates renal phosphate reabsorption, and could therefore prevent hypercalcemia. {ECO:0000250}.
|
Mus musculus (Mouse)
|
O55186
|
CD59A_MOUSE
|
MRAQRGLILLLLLLAVFCSTAVSLTCYHCFQPVVSSCNMNSTCSPDQDSCLYAVAGMQVYQRCWKQSDCHGEIIMDQLEETKLKFRCCQFNLCNKSDGSLGKTPLLGTSVLVAILNLCFLSHL
| null | null |
negative regulation of activation of membrane attack complex [GO:0001971]; negative regulation of angiogenesis [GO:0016525]; negative regulation of apoptotic process [GO:0043066]; negative regulation of complement activation [GO:0045916]; negative regulation of complement-dependent cytotoxicity [GO:1903660]; negative regulation of fibroblast growth factor production [GO:0090272]; negative regulation of vascular endothelial growth factor receptor signaling pathway [GO:0030948]; positive regulation of T cell proliferation [GO:0042102]; regulation of complement activation [GO:0030449]; regulation of complement-dependent cytotoxicity [GO:1903659]
|
cell surface [GO:0009986]; compact myelin [GO:0043218]; external side of plasma membrane [GO:0009897]; extracellular space [GO:0005615]; plasma membrane [GO:0005886]; sarcolemma [GO:0042383]
|
complement binding [GO:0001848]
|
PF00021;
|
2.10.60.10;
| null | null |
SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor, GPI-anchor.
| null | null | null | null | null |
FUNCTION: Potent inhibitor of the complement membrane attack complex (MAC) action. Acts by binding to the C8 and/or C9 complements of the assembling MAC, thereby preventing incorporation of the multiple copies of C9 required for complete formation of the osmolytic pore (By similarity). {ECO:0000250}.
|
Mus musculus (Mouse)
|
O55187
|
CBX4_MOUSE
|
MELPAVGEHVFAVESIEKKRIRKGRVEYLVKWRGWSPKYNTWEPEENILDPRLLIAFQNRERQEQLMGYRKRGPKPKPLVVQVPTFARRSNVLTGLQDSSADNRAKLELGTQGKGQGHQYELNSKKHHQYQPHSKERSGKPPPPGKSGKYYYQLNSKKHHPYQPDPKMYDLQYQGGHKEAPSPTCPDLGTKSHPPDKWAHGAAAKGYLGAVKPLGGGAGAPGKGSEKGPPNGMTPAPKEAVTGNGIGGKMKIVKNKNKNGRIVIVMSKYMENGMQAVKIKSGEAAEGEARSPSHKKRAAEERHPQGDRTFKKAAGASEEKKAEVPCKRREEEALVSGDAQPQDLGSRKLSPTKEAFGEQPLQLTTKPDLLAWDPARSSHPPAHHHHHHHHHHHHHTVGLNLSHARKRCLSETHGEREPCKKRLTARSISTPTCLGGSPVSEHPANVSPTAASLPQPEVILLDSDLDEPIDLRCVKMRSDAGEPPSTLQVKPEAPAVAAVVAPAPASEKPPAEAQEEPVEPLSEFKPFFGNIIITDVTANCLTVTFKEYVTV
|
2.3.2.-
| null |
chromatin organization [GO:0006325]; negative regulation of transcription by RNA polymerase II [GO:0000122]; protein sumoylation [GO:0016925]
|
nuclear body [GO:0016604]; nuclear speck [GO:0016607]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; PcG protein complex [GO:0031519]; PRC1 complex [GO:0035102]
|
chromatin binding [GO:0003682]; enzyme binding [GO:0019899]; methylated histone binding [GO:0035064]; phosphoprotein binding [GO:0051219]; single-stranded RNA binding [GO:0003727]; SUMO binding [GO:0032183]; SUMO ligase activity [GO:0061665]; SUMO transferase activity [GO:0019789]; transcription cis-regulatory region binding [GO:0000976]
|
PF17218;PF00385;
|
2.40.50.40;
| null |
PTM: Ubiquitinated. Ubiquitination regulates the function of the Polycomb group (PcG) multiprotein PRC1-like complex. Deubiquitinated by USP26. {ECO:0000250|UniProtKB:O00257}.
|
SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:O00257}. Nucleus speckle {ECO:0000250|UniProtKB:O00257}.
| null | null |
PATHWAY: Protein modification; protein sumoylation.
| null | null |
FUNCTION: E3 SUMO-protein ligase which facilitates SUMO1 conjugation by UBE2I. Involved in the sumoylation of HNRNPK, a p53/TP53 transcriptional coactivator, hence indirectly regulates p53/TP53 transcriptional activation resulting in p21/CDKN1A expression. {ECO:0000250|UniProtKB:O00257}.; FUNCTION: Component of a Polycomb group (PcG) multiprotein PRC1-like complex, a complex class required to maintain the transcriptionally repressive state of many genes, including Hox genes, throughout development (By similarity). PcG PRC1 complex acts via chromatin remodeling and modification of histones; it mediates monoubiquitination of histone H2A 'Lys-119', rendering chromatin heritably changed in its expressibility (By similarity). Binds to histone H3 trimethylated at 'Lys-9' (H3K9me3) (PubMed:16537902). Plays a role in the lineage differentiation of the germ layers in embryonic development (PubMed:22226355). {ECO:0000250|UniProtKB:O00257, ECO:0000269|PubMed:16537902, ECO:0000269|PubMed:22226355}.
|
Mus musculus (Mouse)
|
O55188
|
DMP1_MOUSE
|
MKTVILLVFLWGLSCALPVARYHNTESESSEERTGDLAGSPPPPTNSESSEESQASPEGQANSDHTDSSESGEELGYDRGQYRPAGGLSKSTGTGADKEDDEDDSGDDTFGDEDNDLGPEEGQWGGPSKLDSDEDSTDTTQSSEDSTSQENSAQDTPSDSKDHDSEDEADSRPEAGDSTQDSESEEQRVGGGSEGESSHGDGSEFDDEGMQSDDPESTRSDRGHARMSSAGIRSEESKGDHEPTSTQDSDDSQSVEFSSRKSFRRSHVSEEDYRGELTDSNSRETQSDSTEDTASKEESRSESQEDTAESQSQEDSPEGQDPSSESSEEAGEPSQESSSESQEGVTSESRGDNPDNTSQAGDQEDSESSEEDSLNTFSSSESQSTEEQADSESNESLSLSEESQESAQDGDSSSQEGLQSQSASTESRSQESQSEQDSRSEEDSDSQDSSRSKEESNSTGSASSSEEDIRPKNMEADSRKLIVDAYHNKPIGDQDDNDCQDGY
| null | null |
biomineral tissue development [GO:0031214]; extracellular matrix organization [GO:0030198]; ossification [GO:0001503]; positive regulation of cell-substrate adhesion [GO:0010811]; regulation of enamel mineralization [GO:0070173]
|
cytoplasm [GO:0005737]; extracellular matrix [GO:0031012]; extracellular region [GO:0005576]; nucleus [GO:0005634]
|
extracellular matrix binding [GO:0050840]; Hsp70 protein binding [GO:0030544]
|
PF07263;
| null | null |
PTM: Phosphorylated in the cytosol and extracellular matrix and unphosphorylated in the nucleus. Phosphorylation is necessary for nucleocytoplasmic transport and may be catalyzed by a nuclear isoform of CK2 and can be augmented by calcium. Phosphorylated (in vitro) by FAM20C in the extracellular medium at sites within the S-x-E/pS motif (By similarity). {ECO:0000250}.
|
SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm {ECO:0000250}. Secreted, extracellular space, extracellular matrix {ECO:0000250}. Note=In proliferating preosteoblasts it is nuclear, during early maturation stage is cytoplasmic and in mature osteoblast localizes in the mineralized matrix. Export from the nucleus of differentiating osteoblast is triggered by the release of calcium from intracellular stores followed by a massive influx of this pool of calcium into the nucleus (By similarity). {ECO:0000250}.
| null | null | null | null | null |
FUNCTION: May have a dual function during osteoblast differentiation. In the nucleus of undifferentiated osteoblasts, unphosphorylated form acts as a transcriptional component for activation of osteoblast-specific genes like osteocalcin. During the osteoblast to osteocyte transition phase it is phosphorylated and exported into the extracellular matrix, where it regulates nucleation of hydroxyapatite (By similarity). {ECO:0000250}.
|
Mus musculus (Mouse)
|
O55192
|
SC6A2_MOUSE
|
MLLARMNPQVQPELGGADPLPEQPLRPCKTADLLVVKERNGVQCLLASQDSDAQPRETWGKKIDFLLSVVGFAVDLANVWRFPYLCYKNGGGAFLIPYTLFLIIAGMPLFYMELALGQYNREGAATVWKICPFFKGVGYAVILIALYVGFYYNVIIAWSLYYLFASFTLNLPWTNCGHSWNSPNCTDPKLLNASVLGDHTKYSKYKFTPAAEFYERGVLHLHESSGIHDIGLPQWQLLLCLMVVIVVLYFSLWKGVKTSGKVVWITATLPYFVLFVLLVHGVTLPGASNGINAYLHIDFYRLKEATVWIDAATQIFFSLGAGFGVLIAFASYNKFDNNCYRDALLTSTINCVTSFISGFAIFSILGYMAHEHKVNIEDVATEGAGLVFILYPEAISTLSGSTFWAVLFFLMLLALGLDSSMGGMEAVITGLADDFQVLKRHRKLFTCVVTISTFLLALFCITKGGIYVLTLLDTFAAGTSILFAVLMEAIGVSWFYGVDRFSNDIQQMMGFKPGLYWRLCWKFVSPAFLLFVVVVSIINFKPLTYDDYTYPPWANWVGWGIALSSMILVPAYVIYKFLSIRGSLWERVAYGITPENEHHLVAQRDVRQFQLRHWLAI
| null | null |
amino acid transport [GO:0006865]; dopamine uptake involved in synaptic transmission [GO:0051583]; monoamine transport [GO:0015844]; neurotransmitter reuptake [GO:0098810]; neurotransmitter transport [GO:0006836]; norepinephrine transport [GO:0015874]; norepinephrine uptake [GO:0051620]; response to pain [GO:0048265]; response to xenobiotic stimulus [GO:0009410]; sodium ion transmembrane transport [GO:0035725]
|
axon [GO:0030424]; cell surface [GO:0009986]; neuronal cell body membrane [GO:0032809]; plasma membrane [GO:0005886]; presynaptic membrane [GO:0042734]
|
actin binding [GO:0003779]; alpha-tubulin binding [GO:0043014]; beta-tubulin binding [GO:0048487]; dopamine:sodium symporter activity [GO:0005330]; metal ion binding [GO:0046872]; monoamine transmembrane transporter activity [GO:0008504]; neurotransmitter transmembrane transporter activity [GO:0005326]; neurotransmitter:sodium symporter activity [GO:0005328]; norepinephrine:sodium symporter activity [GO:0005334]
|
PF00209;
| null |
Sodium:neurotransmitter symporter (SNF) (TC 2.A.22) family, SLC6A2 subfamily
| null |
SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P23975}; Multi-pass membrane protein {ECO:0000255}.
|
CATALYTIC ACTIVITY: Reaction=(R)-noradrenaline(out) + chloride(out) + Na(+)(out) = (R)-noradrenaline(in) + chloride(in) + Na(+)(in); Xref=Rhea:RHEA:70923, ChEBI:CHEBI:17996, ChEBI:CHEBI:29101, ChEBI:CHEBI:72587; Evidence={ECO:0000269|PubMed:16269905}; CATALYTIC ACTIVITY: Reaction=chloride(out) + dopamine(out) + Na(+)(out) = chloride(in) + dopamine(in) + Na(+)(in); Xref=Rhea:RHEA:70919, ChEBI:CHEBI:17996, ChEBI:CHEBI:29101, ChEBI:CHEBI:59905; Evidence={ECO:0000250|UniProtKB:P23975}; CATALYTIC ACTIVITY: Reaction=chloride(out) + dopamine(out) + 2 Na(+)(out) = chloride(in) + dopamine(in) + 2 Na(+)(in); Xref=Rhea:RHEA:70931, ChEBI:CHEBI:17996, ChEBI:CHEBI:29101, ChEBI:CHEBI:59905; Evidence={ECO:0000250|UniProtKB:P23975};
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=98 nM for noradrenaline in inbred long-sleep mice {ECO:0000269|PubMed:16269905}; KM=89.1 nM for noradrenaline in inbred short-sleep mice {ECO:0000269|PubMed:16269905};
| null | null | null |
FUNCTION: Mediates sodium- and chloride-dependent transport of norepinephrine (also known as noradrenaline) (PubMed:16269905). Can also mediate sodium- and chloride-dependent transport of dopamine (By similarity). {ECO:0000250|UniProtKB:P23975, ECO:0000269|PubMed:16269905}.
|
Mus musculus (Mouse)
|
O55193
|
CCR2_RAT
|
MEDSNMLPQFIHGILSTSHSLFPRSIQELDEGATTPYDYDDGEPCHKTSVKQIGAWILPPLYSLVFIFGFVGNMLVIIILISCKKLKSMTDIYLFNLAISDLLFLLTLPFWAHYAANEWVFGNIMCKLFTGLYHIGYFGGIFFIILLTIDRYLAIVHAVFALKARTVTFGVITSVVTWVVAVFASLPGIIFTKSEQEDDQHTCGPYFPTIWKNFQTIMRNILSLILPLLVMVICYSGILHTLFRCRNEKKRHRAVRLIFAIMIVYFLFWTPYNIVLFLTTFQEFLGMSNCVVDMHLDQAMQVTETLGMTHCCVNPIIYAFVGEKFRRYLSIFFRKHIAKNLCKQCPVFYRETADRVSSTFTPSTGEQEVSVGL
| null | null |
blood vessel remodeling [GO:0001974]; calcium-mediated signaling [GO:0019722]; cell chemotaxis [GO:0060326]; cellular defense response [GO:0006968]; cellular homeostasis [GO:0019725]; chemokine-mediated signaling pathway [GO:0070098]; cytokine-mediated signaling pathway [GO:0019221]; G protein-coupled receptor signaling pathway [GO:0007186]; hemopoiesis [GO:0030097]; homeostasis of number of cells within a tissue [GO:0048873]; humoral immune response [GO:0006959]; immune response [GO:0006955]; inflammatory response [GO:0006954]; inflammatory response to antigenic stimulus [GO:0002437]; inflammatory response to wounding [GO:0090594]; intracellular calcium ion homeostasis [GO:0006874]; leukocyte adhesion to vascular endothelial cell [GO:0061756]; macrophage migration [GO:1905517]; monocyte chemotaxis [GO:0002548]; monocyte extravasation [GO:0035696]; negative regulation of angiogenesis [GO:0016525]; negative regulation of eosinophil degranulation [GO:0043310]; negative regulation of type 2 immune response [GO:0002829]; neutrophil clearance [GO:0097350]; positive regulation of alpha-beta T cell proliferation [GO:0046641]; positive regulation of astrocyte chemotaxis [GO:2000464]; positive regulation of CD8-positive, alpha-beta T cell extravasation [GO:2000451]; positive regulation of cold-induced thermogenesis [GO:0120162]; positive regulation of cytosolic calcium ion concentration [GO:0007204]; positive regulation of hematopoietic stem cell migration [GO:2000473]; positive regulation of immune complex clearance by monocytes and macrophages [GO:0090265]; positive regulation of inflammatory response [GO:0050729]; positive regulation of interleukin-2 production [GO:0032743]; positive regulation of leukocyte tethering or rolling [GO:1903238]; positive regulation of monocyte chemotaxis [GO:0090026]; positive regulation of monocyte extravasation [GO:2000439]; positive regulation of NMDA glutamate receptor activity [GO:1904783]; positive regulation of p38MAPK cascade [GO:1900745]; positive regulation of synaptic transmission, glutamatergic [GO:0051968]; positive regulation of T cell activation [GO:0050870]; positive regulation of T cell chemotaxis [GO:0010820]; positive regulation of T-helper 1 type immune response [GO:0002827]; positive regulation of thymocyte migration [GO:2000412]; positive regulation of tumor necrosis factor production [GO:0032760]; positive regulation of type II interferon production [GO:0032729]; regulation of inflammatory response [GO:0050727]; regulation of macrophage migration [GO:1905521]; regulation of mononuclear cell migration [GO:0071675]; regulation of T cell cytokine production [GO:0002724]; regulation of T cell differentiation [GO:0045580]; regulation of T cell migration [GO:2000404]; regulation of vascular endothelial growth factor production [GO:0010574]; response to hyperoxia [GO:0055093]; response to hypoxia [GO:0001666]; sensory perception of pain [GO:0019233]; T-helper 17 cell chemotaxis [GO:0035705]
|
cytoplasm [GO:0005737]; dendrite [GO:0030425]; external side of plasma membrane [GO:0009897]; neuronal cell body [GO:0043025]; perikaryon [GO:0043204]; perinuclear region of cytoplasm [GO:0048471]; plasma membrane [GO:0005886]; primary dendrite [GO:0150001]
|
C-C chemokine receptor activity [GO:0016493]; CCR2 chemokine receptor binding [GO:0031727]; chemokine (C-C motif) ligand 12 binding [GO:0035716]; chemokine (C-C motif) ligand 2 binding [GO:0035715]; chemokine (C-C motif) ligand 5 binding [GO:0071791]; chemokine (C-C motif) ligand 7 binding [GO:0035717]; cytokine binding [GO:0019955]; identical protein binding [GO:0042802]
|
PF00001;
|
1.20.1070.10;
|
G-protein coupled receptor 1 family
|
PTM: N-glycosylated. {ECO:0000250|UniProtKB:P41597}.; PTM: Sulfation increases the affinity for both monomeric and dimeric CCL2 with stronger binding to the monomeric form (By similarity). Binding of sulfated CCR2 to CCL2 promotes conversion of CCL2 from dimer to monomer (By similarity). {ECO:0000250|UniProtKB:P41597}.
|
SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P41597}; Multi-pass membrane protein {ECO:0000255}. Note=The chemoattractant receptors are distributed throughout the cell surface; after stimulation with a ligand, such as CCL2, they are rapidly recruited into microdomain clusters at the cell membrane. {ECO:0000250|UniProtKB:P41597}.
| null | null | null | null | null |
FUNCTION: Key functional receptor for CCL2 but can also bind CCL7 and CCL12 (By similarity). Its binding with CCL2 on monocytes and macrophages mediates chemotaxis and migration induction through the activation of the PI3K cascade, the small G protein Rac and lamellipodium protrusion (By similarity). Also acts as a receptor for the beta-defensin DEFB106A/DEFB106B (By similarity). Regulates the expression of T-cell inflammatory cytokines and T-cell differentiation, promoting the differentiation of T-cells into T-helper 17 cells (Th17) during inflammation (By similarity). Facilitates the export of mature thymocytes by enhancing directional movement of thymocytes to sphingosine-1-phosphate stimulation and up-regulation of S1P1R expression; signals through the JAK-STAT pathway to regulate FOXO1 activity leading to an increased expression of S1P1R (By similarity). Plays an important role in mediating peripheral nerve injury-induced neuropathic pain (By similarity). Increases NMDA-mediated synaptic transmission in both dopamine D1 and D2 receptor-containing neurons, which may be caused by MAPK/ERK-dependent phosphorylation of GRIN2B/NMDAR2B (By similarity). Mediates the recruitment of macrophages and monocytes to the injury site following brain injury (By similarity). {ECO:0000250|UniProtKB:P41597, ECO:0000250|UniProtKB:P51683}.
|
Rattus norvegicus (Rat)
|
O55197
|
C3AR_RAT
|
MESFTADTNSTDLHSRPLFKPQDIASMVILSLTCLLGLPGNGLVLWVAGVKMKRTVNTVWFLHLTLADFLCCLSLPFSVAHLILRGHWPYGLFLCKLIPSVIILNMFASVFLLTAISLDRCLMVHKPIWCQNHRSVRTAFAVCGCVWVVTFVMCIPVFVYRDLLVVDDYSVCGYNFDSSRAYDYWDYMYNSHLPEINPPDNSTGHVDDRTAPSSSVPARDLWTATTALQSQTFHTSPEDPFSQDSASQQPHYGGKPPTVLIATIPGGFPVEDHKSNTLNTGAFLSAHTEPSLTASSSPLYAHDFPDDYFDQLMYGNHAWTPQVAITISRLVVGFLVPFFIMITCYSLIVFRMRKTNLTKSRNKTLRVAVAVVTVFFVCWIPYHIVGILLVITDQESALREVVLPWDHMSIALASANSCFNPFLYALLGKDFRKKARQSVKGILEAAFSEELTHSTSCTQDKAPSKRNHMSTDV
| null | null |
calcium-mediated signaling [GO:0019722]; chemotaxis [GO:0006935]; complement receptor mediated signaling pathway [GO:0002430]; inflammatory response [GO:0006954]; phospholipase C-activating G protein-coupled receptor signaling pathway [GO:0007200]; positive regulation of angiogenesis [GO:0045766]; positive regulation of cell migration [GO:0030335]; positive regulation of cytosolic calcium ion concentration [GO:0007204]; positive regulation of DNA biosynthetic process [GO:2000573]; positive regulation of glomerular mesangial cell proliferation [GO:0072126]; positive regulation of macrophage chemotaxis [GO:0010759]; positive regulation of neutrophil chemotaxis [GO:0090023]; positive regulation of smooth muscle cell proliferation [GO:0048661]; positive regulation of vascular endothelial growth factor production [GO:0010575]; regulation of blood pressure [GO:0008217]; tolerance induction to nonself antigen [GO:0002462]
|
plasma membrane [GO:0005886]
|
complement component C3a binding [GO:0001850]; complement component C3a receptor activity [GO:0004876]; complement component C5a receptor activity [GO:0004878]; G protein-coupled receptor activity [GO:0004930]
|
PF00001;
|
1.20.1070.10;
|
G-protein coupled receptor 1 family
| null |
SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
| null | null | null | null | null |
FUNCTION: Receptor for the chemotactic and inflammatory peptide anaphylatoxin C3a. This receptor stimulates chemotaxis, granule enzyme release and superoxide anion production.
|
Rattus norvegicus (Rat)
|
O55201
|
SPT5H_MOUSE
|
MSDSEDSNFSEEEDSERSSEAEEAEVEEDQRSAAGSEKEEEPEEEEEEEEEYDEEEEEEDDDRPPKKPRHGGFILDEADVDDEYEDEDQWEDGAEDILEKEEIEASNIDNVVLDEDRSGARRLQNLWRDQREEELGEYYMKKYAKSSVGETVYGGSDELSDDITQQQLLPGVKDPNLWTVKCKIGEERATAISLMRKFIAYQFTDTPLQIKSVVAPEHVKGYIYVEAYKQTHVKQAIEGVGNLRLGYWNQQMVPIKEMTDVLKVVKEVANLKPKSWVRLKRGIYKDDIAQVDYVEPSQNTISLKMIPRIDYDRIKARMSLKDWFAKRKKFKRPPQRLFDAEKIRSLGGDVASDGDFLIFEGNRYSRKGFLFKSFAMSAVITEGVKPTLSELEKFEDQPEGIDLEVVTESTGKEREHNFQPGDNVEVCEGELINLQGKVLSVDGNKITIMPKHEDLKDMLEFPAQELRKYFKMGDHVKVIAGRFEGDTGLIVRVEENFVILFSDLTMHELKVLPRDLQLCSETASGVDVGGQHEWGELVQLDPRTVGVIVRLERETFQVLNMHGKVVTVRHQAVTQKKDNRFAVALDSDQNNIHVKDIVKVIDGPHSGREGEIRHLYRSFAFLHCKKLVENGGMFVCKARHLVLAGGSKPRDVTNLTVGGFTPMSPRISSPMHPSAEGQHGGFGSPGGMSRGRGRRDNELIGQTVRISQGPYKGYIGVVKDATESTARVELHSTCQTISVDRQRLTTVDSQRPGGMTSTYGRTPMYGSQTPMYGSGSRTPMYGSQTPLQDGSRTPHYGSQTPLHDGSRTPAQSGAWDPNNPNTPSRAEEEYEYAFDDEPTPSPQAYGGTPNPQTPGYPDPSSPQVNPQYNPQTPGTPAMYNTDQFSPYAAPSPQGSYQPSPSPQSYHQVAPSPAGYQNTHSPASYHPTPSPMAYQASPSPSPVGYSPMTPGAPSPGGYNPHTPGSGIEQNSSDWVTTDIQVKVRDTYLDTQIVGQTGVIRSVTGGMCSVYLKDSEKVVSISSEHLEPITPTKNNKVKVILGEDREATGVLLSIDGEDGIIRMDLEDQQIKILNLRFLGKLLEA
| null | null |
negative regulation of DNA-templated transcription, elongation [GO:0032785]; negative regulation of transcription by RNA polymerase II [GO:0000122]; positive regulation of DNA-templated transcription, elongation [GO:0032786]; positive regulation of macroautophagy [GO:0016239]; positive regulation of transcription by RNA polymerase II [GO:0045944]; regulation of transcription elongation by RNA polymerase II [GO:0034243]; transcription elongation by RNA polymerase II [GO:0006368]; transcription elongation-coupled chromatin remodeling [GO:0140673]
|
DSIF complex [GO:0032044]
|
chromatin binding [GO:0003682]; enzyme binding [GO:0019899]; mRNA binding [GO:0003729]; protein heterodimerization activity [GO:0046982]
|
PF00467;PF03439;PF11942;
|
2.30.30.30;3.30.70.940;
|
SPT5 family
|
PTM: Methylated by PRMT1/HRMT1L2 and PRMT5/SKB1. Methylation negatively regulates interaction with P-TEFb and RNA polymerase II (By similarity). {ECO:0000250}.; PTM: Phosphorylated by CDK7 and CDK9. Phosphorylation by P-TEFb alleviates transcriptional pausing. Phosphorylation may also stimulate interaction with PIN1. Bulk phosphorylation occurs predominantly in mitosis (By similarity). {ECO:0000250}.
|
SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
| null | null | null | null | null |
FUNCTION: Component of the DRB sensitivity-inducing factor complex (DSIF complex), which regulates mRNA processing and transcription elongation by RNA polymerase II. DSIF positively regulates mRNA capping by stimulating the mRNA guanylyltransferase activity of RNGTT/CAP1A. DSIF also acts cooperatively with the negative elongation factor complex (NELF complex) to enhance transcriptional pausing at sites proximal to the promoter. Transcriptional pausing may facilitate the assembly of an elongation competent RNA polymerase II complex. DSIF and NELF promote pausing by inhibition of the transcription elongation factor TFIIS/S-II. TFIIS/S-II binds to RNA polymerase II at transcription pause sites and stimulates the weak intrinsic nuclease activity of the enzyme. Cleavage of blocked transcripts by RNA polymerase II promotes the resumption of transcription from the new 3' terminus and may allow repeated attempts at transcription through natural pause sites (By similarity). {ECO:0000250}.
|
Mus musculus (Mouse)
|
O55203
|
LDB2_MOUSE
|
MSSTPHDPFYSSPFGPFYRRHTPYMVQPEYRIYEMNKRLQSRTEDSDNLWWDAFATEFFEDDATLTLSFCLEDGPKRYTIGRTLIPRYFSTVFEGGVTDLYYILKHSKESYHNSSITVDCDQCAMVTQHGKPMFTKVCTEGRLILEFTFDDLMRIKTWHFTIRQYRELVPRSILAMHAQDPQVLDQLSKNITRMGLTNFTLNYLRLCVILEPMQELMSRHKTYNLSPRDCLKTCLFQKWQRMVAPPAEPTRQPTTKRRKRKNSTSSTSNSSAGNTTNSAGSKKKTPAASLSLATQVPDVMVVGEPTLMGGEFGDEDERLITRLENTQYDAANGMDDEEDFNNSPALGNNSPWNSKPPATQETKSENAPPQASQ
| null | null |
cellular component biogenesis [GO:0044085]; epithelial structure maintenance [GO:0010669]; hair follicle development [GO:0001942]; negative regulation of transcription by RNA polymerase II [GO:0000122]; nervous system development [GO:0007399]; positive regulation of cellular component biogenesis [GO:0044089]; positive regulation of transcription by RNA polymerase II [GO:0045944]; regulation of cell migration [GO:0030334]; regulation of kinase activity [GO:0043549]; somatic stem cell population maintenance [GO:0035019]
|
cell leading edge [GO:0031252]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; plasma membrane [GO:0005886]; transcription regulator complex [GO:0005667]
|
enzyme binding [GO:0019899]; LIM domain binding [GO:0030274]
|
PF17916;PF01803;
|
2.10.110.10;
|
LDB family
|
PTM: Ubiquitinated by RLIM/RNF12, leading to its degradation by the proteasome. {ECO:0000269|PubMed:11882901}.
|
SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. Note=Colocalizes with SLK at leading edges (PubMed:19675209). {ECO:0000269|PubMed:19675209}.; SUBCELLULAR LOCATION: [Isoform 1]: Nucleus {ECO:0000305|PubMed:9192866}.
| null | null | null | null | null |
FUNCTION: Transcription cofactor (PubMed:9192866). Binds to the LIM domain of a wide variety of LIM domain-containing transcription factors (PubMed:9192866). {ECO:0000269|PubMed:9192866}.; FUNCTION: [Isoform 1]: Regulates the transcriptional activity of LIM-containing proteins such as LHX3 or PITX1. {ECO:0000269|PubMed:9192866}.
|
Mus musculus (Mouse)
|
O55207
|
SYNJ2_RAT
|
MALSKGLRLLARLDPTGPSSVLLEARGRGDCLLFEAGAVATLAPEEKEVIKGLYGKPTDAYGCLGELSLKSGGVPLSFLVLVTGCTSVGRIPDAEIYKITGTEFYPLQEEAKEEDRLPALKKILSSGVFYFAWPNDGACFDLTIRAQKQGDDCSEWGTSFFWNQLLHVPLRQHQVNCHDWLLKVICGVVTIRTVYASHKQAKACLISRISCERAGARFLTRGVNDDGHVSNFVETEQAIYMDDGVSSFVQIRGSVPLFWEQPGLQVGSHHLRLHRGLEANAPAFERHMVLLKEQYGQQVVVNLLGSRGGEEVLNRAFKKLLWASCHAGDTPMINFDFHQFAKGRKLEKLENLLRPQLKLHWDDFGVFAKGENVSPRFQKGTLRMNCLDCLDRTNTVQCFIALEVLHLQLESLGLNSKPITDRFVESFKAMWSLNGHGLSKVFTGSRALEGKAKVGKLKDGARSMSRTIQSNFFDGVKQEAIKLLLVGDVYNEESTDKGRMLLDNTALLGLGSNKQNSLSGMLDGKATPRILKAMTERQSEFTNFKRIQIAMGTWNVNGGKQFRSNLLGTTELTDWLLDAPQLSGAVDSQDDGGPADIFAVGFEEMVELSAGNIVNASTTNRKMWGEQLQKAISRSHRYILLTSAQLVGVCLYIFVRPYHVPFIRDVAIDTVKTGMGGKAGNKGAVGIRFQFHSTSFCFICSHLTAGQSQVKERNEDYREITHKLSFPSGRNIFSHDYVFWCGDFNYRIDLTYEEVFYFVKRQDWKKLMEFDQLQLQKSSGKIFKDFHEGTINFGPTYKYDVGSAAYDTSDKCRTPAWTDRVLWWRKKHPYDKTAGELNLLDSDLDGDANIRHTWSPGTLKYYGRAELQASDHRPVLAIVEVEVQEVDVGARERVFQEVSSVQGPLDATVIVNLQSPTLEERNEFPEDLRTELMQTLGNYGTIILVRINQGQMLVTFADSHSALSVLDVDGMKVKGRAVKIRPKTKDWLEGLREELIRKRDSMAPVSPTANSCLLEENFDFTSLDYESEGDVLEDDEDYLADEFGQPVVSDSELGGDDSSDTMSASTPASKSPALAKKKQHPTYKDDADLMTLKLELEVAGNFRHRSPSRSLSVPNRPRPPHPPQRPPPPTGLMVKKSASDASISSGTHGQYSILQTAKLLPGAPQQPPKARTGISKPYNVKQIKTTNAQEAEAAIRCLLEAGGGVPESAPGATPLRNQGSSKPEASLGPPVLPRRPVPRVPTMKKPTLRRTGKPMLPEEQCEQQPVHFTMASQEMNLETPPPITAPIPPVPKPRTFQPGRGVERRPSGGKPEPDDAPPVTGAVELSSPEAPEAPSLAPKVPPRRKKSAPAAFHLQVLQSNSQLLQGLTCSSSSPSPPKPDTPLLYPQMALGTSSAISPETDGPRVTEPEAASFHGDYPDPFWSLLHHPKLLNNNTWLSKSSEPLDLGSRTPERTHTDSAQVNASVVERGLPPDHGGKDFSHWMAASNKDKRTTLGV
|
3.1.3.36
| null |
inositol phosphate catabolic process [GO:0071545]; phosphatidylinositol dephosphorylation [GO:0046856]; synaptic vesicle endocytosis [GO:0048488]
|
axon terminus [GO:0043679]; cytoplasmic microtubule [GO:0005881]; membrane raft [GO:0045121]; mitochondrion [GO:0005739]; perinuclear region of cytoplasm [GO:0048471]; presynapse [GO:0098793]; ruffle membrane [GO:0032587]
|
inositol-1,3,4,5-tetrakisphosphate 5-phosphatase activity [GO:0052659]; inositol-1,4,5-trisphosphate 5-phosphatase activity [GO:0052658]; PDZ domain binding [GO:0030165]; phosphatidylinositol monophosphate phosphatase activity [GO:0052744]; phosphatidylinositol-4,5-bisphosphate 5-phosphatase activity [GO:0004439]; RNA binding [GO:0003723]; SH3 domain binding [GO:0017124]
|
PF08952;PF02383;
|
3.30.70.330;3.60.10.10;
|
Synaptojanin family; Inositol 1,4,5-trisphosphate 5-phosphatase family
| null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11498538}. Cell membrane {ECO:0000269|PubMed:11498538}. Presynapse {ECO:0000269|PubMed:11498538}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:11498538}. Membrane raft. Note=Localizes at presynapse terminals in brain and at bundles of microtubules surrounding the nucleus in the elongating spermatids corresponding to the manchette (PubMed:11498538). Translocates from the cytoplasm to membrane ruffles in a RAC1-dependent manner (PubMed:11498538). {ECO:0000269|PubMed:11498538}.; SUBCELLULAR LOCATION: [Isoform 2A]: Mitochondrion {ECO:0000269|PubMed:10357812}. Note=Interaction of isoform 2A with SYNJ2BP/OMP25 results in localization to the mitochondrion (PubMed:10357812). {ECO:0000269|PubMed:10357812}.
|
CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-4,5-bisphosphate) + H2O = a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol 4-phosphate) + phosphate; Xref=Rhea:RHEA:22764, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:58178, ChEBI:CHEBI:58456; EC=3.1.3.36; Evidence={ECO:0000250|UniProtKB:Q9D2G5};
| null | null | null | null |
FUNCTION: Inositol 5-phosphatase which may be involved in distinct membrane trafficking and signal transduction pathways. May mediate the inhibitory effect of Rac1 on endocytosis (By similarity). {ECO:0000250}.
|
Rattus norvegicus (Rat)
|
O55208
|
FIGLA_MOUSE
|
MDTAPASPEPFLVTPQAEVLEELIQAQMGPLPRLAAICRLKRLPSGGYSTTDDLHLVLERRRVANAKERERIKNLNRGFAKLKALVPFLPQSRKPSKVDILKGATEYIQILGCVLEEAKVSEKQSPEEQTHSGRPSDPHVSSTRELLGNATQPTSCASGLKKEEEGPWAYAGHSEPLYSYHQSTVPETRSYFTH
| null | null |
developmental process [GO:0032502]; oogenesis [GO:0048477]; positive regulation of transcription by RNA polymerase II [GO:0045944]; regulation of transcription by RNA polymerase II [GO:0006357]
|
nucleus [GO:0005634]; transcription regulator complex [GO:0005667]
|
bHLH transcription factor binding [GO:0043425]; DNA-binding transcription activator activity, RNA polymerase II-specific [GO:0001228]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; E-box binding [GO:0070888]; protein dimerization activity [GO:0046983]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]; RNA polymerase II transcription regulatory region sequence-specific DNA binding [GO:0000977]
|
PF00010;
|
4.10.280.10;
| null | null |
SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
| null | null | null | null | null |
FUNCTION: Germ-line specific transcription factor implicated in postnatal oocyte-specific gene expression. Plays a key regulatory role in the expression of multiple oocyte-specific genes, including those that initiate folliculogenesis and those that encode the zona pellucida (ZP1, ZP2 and ZP3) required for fertilization and early embryonic survival. Essential for oocytes to survive and form primordial follicles. The persistence of FIGLA in adult females suggests that it may regulate additional pathways that are essential for normal ovarian development. Binds to the E-box (5'-CANNTG-3') of the ZPs (ZP1, ZP2, ZP3) promoters. {ECO:0000269|PubMed:11023867}.
|
Mus musculus (Mouse)
|
O55222
|
ILK_MOUSE
|
MDDIFTQCREGNAVAVRLWLDNTENDLNQGDDHGFSPLHWACREGRSAVVEMLIMRGARINVMNRGDDTPLHLAASHGHRDIVQKLLQYKADINAVNEHGNVPLHYACFWGQDQVAEDLVANGALVSICNKYGEMPVDKAKAPLRELLRERAEKMGQNLNRIPYKDTFWKGTTRTRPRNGTLNKHSGIDFKQLNFLAKLNENHSGELWKGRWQGNDIVVKVLKVRDWSTRKSRDFNEECPRLRIFSHPNVLPVLGACQAPPAPHPTLITHWMPYGSLYNVLHEGTNFVVDQSQAVKFALDMARGMAFLHTLEPLIPRHALNSRSVMIDEDMTARISMADVKFSFQCPGRMYAPAWVAPEALQKKPEDTNRRSADMWSFAVLLWELVTREVPFADLSNMEIGMKVALEGLRPTIPPGISPHVCKLMKICMNEDPAKRPKFDMIVPILEKMQDK
|
2.7.11.1
| null |
branching involved in ureteric bud morphogenesis [GO:0001658]; cell population proliferation [GO:0008283]; cell projection organization [GO:0030030]; cell-matrix adhesion [GO:0007160]; establishment or maintenance of epithelial cell apical/basal polarity [GO:0045197]; fibroblast migration [GO:0010761]; integrin-mediated signaling pathway [GO:0007229]; myelin assembly [GO:0032288]; myelination in peripheral nervous system [GO:0022011]; negative regulation of apoptotic process [GO:0043066]; negative regulation of cardiac muscle cell apoptotic process [GO:0010667]; negative regulation of neural precursor cell proliferation [GO:2000178]; negative regulation of neuron apoptotic process [GO:0043524]; negative regulation of smooth muscle cell migration [GO:0014912]; negative regulation of smooth muscle cell proliferation [GO:0048662]; nerve development [GO:0021675]; neural precursor cell proliferation [GO:0061351]; neuron projection morphogenesis [GO:0048812]; outflow tract morphogenesis [GO:0003151]; phosphatidylinositol 3-kinase/protein kinase B signal transduction [GO:0043491]; phosphorylation [GO:0016310]; positive regulation of axon extension [GO:0045773]; positive regulation of axonogenesis [GO:0050772]; positive regulation of BMP signaling pathway [GO:0030513]; positive regulation of canonical NF-kappaB signal transduction [GO:0043123]; positive regulation of canonical Wnt signaling pathway [GO:0090263]; positive regulation of cell migration [GO:0030335]; positive regulation of cell population proliferation [GO:0008284]; positive regulation of cell-matrix adhesion [GO:0001954]; positive regulation of cellular senescence [GO:2000774]; positive regulation of dendrite morphogenesis [GO:0050775]; positive regulation of DNA-templated transcription [GO:0045893]; positive regulation of MAPK cascade [GO:0043410]; positive regulation of myoblast differentiation [GO:0045663]; positive regulation of osteoblast differentiation [GO:0045669]; positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction [GO:0051897]; positive regulation of protein phosphorylation [GO:0001934]; positive regulation of substrate adhesion-dependent cell spreading [GO:1900026]; regulation of actin cytoskeleton organization [GO:0032956]; regulation of cell growth [GO:0001558]; Schwann cell development [GO:0014044]; substrate adhesion-dependent cell spreading [GO:0034446]; supramolecular fiber organization [GO:0097435]; tumor necrosis factor-mediated signaling pathway [GO:0033209]
|
axon [GO:0030424]; cell-cell junction [GO:0005911]; costamere [GO:0043034]; cytosol [GO:0005829]; dendritic shaft [GO:0043198]; focal adhesion [GO:0005925]; lamellipodium [GO:0030027]; neuronal cell body [GO:0043025]; plasma membrane [GO:0005886]; protein-containing complex [GO:0032991]; sarcomere [GO:0030017]; terminal bouton [GO:0043195]
|
ATP binding [GO:0005524]; integrin binding [GO:0005178]; protein domain specific binding [GO:0019904]; protein kinase activity [GO:0004672]; protein kinase binding [GO:0019901]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674]; protein-containing complex binding [GO:0044877]; SH3 domain binding [GO:0017124]
|
PF12796;PF07714;
|
1.25.40.20;1.10.510.10;
|
Protein kinase superfamily, TKL Ser/Thr protein kinase family
|
PTM: Autophosphorylated on serine residues. {ECO:0000250|UniProtKB:Q13418}.
|
SUBCELLULAR LOCATION: Cell junction, focal adhesion {ECO:0000269|PubMed:18325335, ECO:0000269|PubMed:18483218}. Cell membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250|UniProtKB:Q13418}. Cytoplasm, myofibril, sarcomere {ECO:0000250|UniProtKB:Q13418}. Cell projection, lamellipodium {ECO:0000269|PubMed:18325335}.
|
CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1; Evidence={ECO:0000250|UniProtKB:Q13418}; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.1; Evidence={ECO:0000250|UniProtKB:Q13418};
| null | null | null | null |
FUNCTION: Receptor-proximal protein kinase regulating integrin-mediated signal transduction. May act as a mediator of inside-out integrin signaling. Focal adhesion protein part of the complex ILK-PINCH. This complex is considered to be one of the convergence points of integrin- and growth factor-signaling pathway. Could be implicated in mediating cell architecture, adhesion to integrin substrates and anchorage-dependent growth in epithelial cells. Regulates cell motility by forming a complex with PARVB. Phosphorylates beta-1 and beta-3 integrin subunit on serine and threonine residues, but also AKT1 and GSK3B. {ECO:0000250|UniProtKB:Q13418}.
|
Mus musculus (Mouse)
|
O55225
|
OTOG_MOUSE
|
MGARMPRRCLLLLSCFCLLRVESTAEVQHQASALTWKISAELQQEPAPEPSHTYQEMSLAVEDVTTVMEGQEAEALAASAMSSWERRLHRAKCAPSYLFSCFNGGECVHPALCDCRRFNATGPRCQLVYNVGPERDSICRTWGQHHVETFDGLYYYFSGKGSYTLVGHHEPEGQSFSIQVHNDPQCGSAHYTCPRSVSLFLSGEREICLAKEVTHGGVRVQLPQVVGGVQLQQLAGYVIARHPSAFTLAWDGISAIYIKMSPEFLGWTHGLCGNNNADPQDDLVTSYGKVTDDVGEFVHSWQEQVPNSPPGPVTTSLPRPPCLQQSPASMQGVYERCEVLLRPPFDTCHAYVSPLPFAASCTSDLCQSGGDEATWCRALMEYARACAQAGRPLQGWRTQLSQCTVHCKEKAFIYNECIACCPASCQSRASCVDSEITCVDGCYCPNGLIFEDGGCMSPAECPCEFHGTLHPPGSVVTEDCNACTCTAGKWVCSSSVCPAECSVTGDIHFTTFDGRRYTFPATCQYILAKSRSSGTFTVTLQNAPCGLNQDGACVQSVSVILHQDPRRQVTLTQAGDVLLFDQYKITPPYSDDAFEIRRLSSVFLRVRTNVGVRILYDREGLRLYLQVDQRWVEDTVGLCGTFNGNTQDDFLSPVGVPESTPQLFGNSWKTLSACVPLVPGSLLDPCDVHLQAASYALQSCSVLTGELFAPCSAYLSPIPYFEQCRRDACRCGQPCLCATLAHYARLCRRHGLPVDFRAHLPACALSCEATKEYSPCVTLCAPTCQDLASPDVCGANGGGNFSREECVEGCTCPPDTFLDTQADLCVPRNQCSCHFQGVDYPPGDSDIPSLGHCHCKDGVMSCDSRAPAAACPAGQVFVNCSELHPDPELSRERTCEQQLLNLSVPARGPCLSGCACPQGLLRHGDACFPPEECPCTWKGKEYFPGDQVVSSCHTCVCQRGSFQCTLHPCASTCTAYGDRHYRTFDGLPYDFVGACKVHLVKSTSELSFSVMVEDVNCYGSGVICRKSISINVGSSLIIFDDDSGDPSPESFLDEKQAVHIWRAGFFTLVHFPREHITLLWDQRTTVHVQAGPQWQGQLVGLCGNFDLKTINEMRTPENLELTNPQEFGSSWAAVECPDTPDPRDTCVLNPLREPFARKECGILLSEVFETCHPVVDVTWFYSNCLTDTCGCSRGGDCECFCASVAAYAHQCCQHGVVIDWRTPRICPYDCDFFNKALGKGPYQLSSVAAGGTLVATKAVDSDIALVRAEDLAPGDISSFLLTAALYKAKAHDPDVVSLEAADRPNFFLHTTANGSIGLAKWQRDEAFHQHASFSLHRGTWQAGLVALESLAKPGSFLHSSGLELALRAYEHTEVFRGGALFRLLDAKPLGAAYPTCEWRYDACASPCFQTCRDPRATSCQDVPRVEGCVPVCPTPKVLDEVTQRCVYLEDCVEPAPRGPTETLGNETLVPGQVPPTTSAEQQLPQGLPGASAYSPAPVPVAPPTSAPNPPMAATEGQAPSPGSTQPTLQTPLGLTTSNFPAGHTEATAREEGAASLLTTSHPPGFSSSLPSSLQMPTSGIVSGATETTKVTITFTGSPNTTVASRSPPIPRFPLMTKAVTVPSHDSFPVKTTPLQPSWLWSLSSRPMTSLGATSWPPTSPGSHLSTAVTKVANKTMTSLSVLAQSTSSSSQPLAAVTTAHRAPASPLVTKGLEVVSATEKGEAGHSQLTELPVSPPPSPAPIDLPHPAQHTTTAPGPSALSPGILAAGSPSTGAHRPGATALASLEPTRPPHLLSGLPLDTSLPLAKVGTSAPVATPGSKGYIPTPPPQHQATTLATAMTVSPLTQSLSLTVPLMSAVEEQAHSPSPKPPQGTGMAPDQMLGATLPSFGASSVIAGVPPTVSAAPRKSTTQRAAILSKKVSPPTLISDSVQGGFTELTPIVSHTVTPLATEAEGPRAGTVPLVPTTYSLSRVSARTASREGPLVLLPQLAEAYGTPAGLQPQEDLVRQATTEQSGRSAPAKSIAEESMEAEVNTSATCVPIAEQDCVRHICLEGQLIRVNQTQHCPQGAVRPRCGVLGLAVRVGGDRCCPQWECACRCSIFPDLSFVTFDGSHAALFKEAIYVLSQSPDETISVHVLDCKSANLGHLNWPPFCLVILNVTHLAHHVSIDRFNRKVTVDSQVVWPPMSRYGFRIEDTGHMYIVRTPSHIQIQWLHSSGLMILEASKVSKTQGHGLCGICDGDAANDLTLKDGSVLGEAEDPAPFLDSWQVPSSLTSEGQTRFRPDSCATADCSPCLRMVSNRTFSACHSFVSPESFCELWIRDTKYVQQPCVALTVYVAMCHKFHVCIEWRGSDYCPFLCSSDSTYQACVAACEPPDTCQDGILGPLDPEQCQVLGEGCVCTEGTILHRRHSALCIPEDKCACTDSTGVPRALGETWNSSLSGCCQQQCQAPDTIIPVDLDCPGPRPESCPRFGEVILLQPTEDPCCLGSVCVCNQTLCEGLAPTCRPGHSLITHFQEDSCCPSYSCECDPGLCEAEQVPTCREDQILIEGRLGDSCCTSYFCGCGECSDPMPECQEGEALTVHRNTTELCCPLYQCVCENFRCPQVQCGMGTSLVEVWSPDRCCPYKSCECDCDTIPVPRCHLWEKSQLDEEFMHSVENVCGCAKYECVKAPVCLSRELGVMQPGQTVVELSADGVCHTSRCTDVLDPLTNFYQINITSVLCDMHCEANQEYDHPRDLAACCGSCRNVSCLFTFPNGTTSLFLPGASWIADCARHHCGSTPLGAVLVRSPISCPPFNETECAKVGGSVVPSLEGCCRACKEDGRSCKKVTIRMTIRKNDCRSNTPVNLVSCDGRCPSASIYNHNINTYARFCKCCREVGLQRRSVQLFCATNATWVPYTVQEPTDCACQWS
| null | null |
adult locomotory behavior [GO:0008344]; L-arabinose metabolic process [GO:0046373]; sensory perception of sound [GO:0007605]
|
apical plasma membrane [GO:0016324]; cytosol [GO:0005829]; extracellular matrix [GO:0031012]; extracellular space [GO:0005615]
|
alpha-L-arabinofuranosidase activity [GO:0046556]; structural molecule activity [GO:0005198]
|
PF05270;PF08742;PF01826;PF00094;
|
2.80.10.50;2.10.25.10;
|
Otogelin family
|
PTM: N-glycosylated. Not O-glycosylated. {ECO:0000269|PubMed:9405633}.
|
SUBCELLULAR LOCATION: Apical cell membrane {ECO:0000269|PubMed:11506947, ECO:0000269|PubMed:9405633}; Peripheral membrane protein {ECO:0000269|PubMed:11506947, ECO:0000269|PubMed:9405633}; Extracellular side {ECO:0000269|PubMed:11506947, ECO:0000269|PubMed:9405633}. Secreted, extracellular space {ECO:0000269|PubMed:9405633}. Note=Found in fiber-like structures during the maturation process of the tectorial membrane (PubMed:9405633).
| null | null | null | null | null |
FUNCTION: Glycoprotein specific to acellular membranes of the inner ear. May be required for the anchoring of the otoconial membranes and cupulae to the underlying neuroepithelia in the vestibule. May be involved in the organization and/or stabilization of the fibrillar network that compose the tectorial membrane in the cochlea. May play a role in mechanotransduction processes. {ECO:0000269|PubMed:10655058}.
|
Mus musculus (Mouse)
|
O55229
|
CHKB_MOUSE
|
MAADGTGVVGGGAVGGGLPKDGLQDAKCPEPIPNRRRASSLSRDAQRRAYQWCREYLGGAWRRARPEELSVCPVSGGLSNLLFRCSLPNHVPSVGGEPREVLLRLYGAILQGVDSLVLESVMFAILAERSLGPQLYGVFPEGRLEQYLPSRPLKTQELRDPVLSGAIATRMARFHGMEMPFTKEPRWLFGTMERYLKQIQDLPSTSLPQMNLVEMYSLKDEMNSLRKLLDDTPSPVVFCHNDIQEGNILLLSEPDSDDNLMLVDFEYSSYNYRGFDIGNHFCEWVYDYTYEEWPFYKARPTDYPTREQQLHFIRHYLAEVQKGEILSEEEQKKREEELLLEISRYSLASHFFWGLWSTLQASMSTIEFGYLEYAQSRFQFYFQQKGQLTSSPSS
|
2.7.1.32; 2.7.1.82
| null |
CDP-choline pathway [GO:0006657]; muscle organ development [GO:0007517]; phosphatidylcholine biosynthetic process [GO:0006656]; phosphatidylethanolamine biosynthetic process [GO:0006646]; phosphorylation [GO:0016310]
|
cytoplasm [GO:0005737]
|
ATP binding [GO:0005524]; choline kinase activity [GO:0004103]; ethanolamine kinase activity [GO:0004305]
|
PF01633;
|
3.90.1200.10;
|
Choline/ethanolamine kinase family
| null | null |
CATALYTIC ACTIVITY: Reaction=ATP + choline = ADP + H(+) + phosphocholine; Xref=Rhea:RHEA:12837, ChEBI:CHEBI:15354, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:295975, ChEBI:CHEBI:456216; EC=2.7.1.32; Evidence={ECO:0000250|UniProtKB:Q9Y259}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12838; Evidence={ECO:0000250|UniProtKB:Q9Y259}; CATALYTIC ACTIVITY: Reaction=ATP + ethanolamine = ADP + H(+) + phosphoethanolamine; Xref=Rhea:RHEA:13069, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:57603, ChEBI:CHEBI:58190, ChEBI:CHEBI:456216; EC=2.7.1.82; Evidence={ECO:0000250|UniProtKB:Q9Y259}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13070; Evidence={ECO:0000250|UniProtKB:Q9Y259};
| null |
PATHWAY: Phospholipid metabolism; phosphatidylethanolamine biosynthesis; phosphatidylethanolamine from ethanolamine: step 1/3. {ECO:0000250|UniProtKB:Q9Y259}.
| null | null |
FUNCTION: Has a key role in phospholipid metabolism, and catalyzes the first step of phosphatidylethanolamine and phosphatidylcholine biosynthesis. {ECO:0000250|UniProtKB:Q9Y259}.
|
Mus musculus (Mouse)
|
O55230
|
RA51D_MOUSE
|
MGMLRAGLCPGLTEETVQLLRGRKIKTVADLAAADLEEVAQKCGLSYKALVALRRVLLAQFSAFPLNGADLYEELKTSTAILSTGIGSLDKLLDAGLYTGEVTEIVGGPGSGKTQVCLCVAANVAHSLQQNVLYVDSNGGMTASRLLQLLQARTQDEEKQASALQRIQVVRSFDIFRMLDMLQDLRGTIAQQEATSSGAVKVVIVDSVTAVVAPLLGGQQREGLALMMQLARELKILARDLGVAVVVTNHLTRDWDGRRFKPALGRSWSFVPSTRILLDVTEGAGTLGSSQRTVCLTKSPRQPTGLQEMIDIGTLGTEEQSPELPGKQT
| null | null |
chromosome organization [GO:0051276]; DNA damage response [GO:0006974]; DNA strand invasion [GO:0042148]; double-strand break repair via homologous recombination [GO:0000724]; interstrand cross-link repair [GO:0036297]; reciprocal meiotic recombination [GO:0007131]; regulation of cell cycle [GO:0051726]; telomere maintenance [GO:0000723]; telomere maintenance via recombination [GO:0000722]
|
centrosome [GO:0005813]; chromosome, telomeric region [GO:0000781]; Rad51B-Rad51C-Rad51D-XRCC2 complex [GO:0033063]; replication fork [GO:0005657]
|
ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; ATP-dependent activity, acting on DNA [GO:0008094]; ATP-dependent DNA damage sensor activity [GO:0140664]; four-way junction DNA binding [GO:0000400]; gamma-tubulin binding [GO:0043015]; single-stranded DNA binding [GO:0003697]
|
PF08423;PF21794;
|
3.40.50.300;
|
RecA family, RAD51 subfamily
| null |
SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Chromosome, telomere {ECO:0000269|PubMed:15109494}.
| null | null | null | null | null |
FUNCTION: Involved in the homologous recombination repair (HRR) pathway of double-stranded DNA breaks arising during DNA replication or induced by DNA-damaging agents. Bind to single-stranded DNA (ssDNA) and has DNA-dependent ATPase activity. Part of the RAD51 paralog protein complex BCDX2 which acts in the BRCA1-BRCA2-dependent HR pathway. Upon DNA damage, BCDX2 acts downstream of BRCA2 recruitment and upstream of RAD51 recruitment. BCDX2 binds predominantly to the intersection of the four duplex arms of the Holliday junction and to junction of replication forks. The BCDX2 complex was originally reported to bind single-stranded DNA, single-stranded gaps in duplex DNA and specifically to nicks in duplex DNA. Involved in telomere maintenance. The BCDX2 subcomplex XRCC2:RAD51D can stimulate Holliday junction resolution by BLM (By similarity). {ECO:0000250|UniProtKB:O75771, ECO:0000269|PubMed:15109494}.
|
Mus musculus (Mouse)
|
O55232
|
OREX_RAT
|
MNLPSTKVPWAAVTLLLLLLLPPALLSLGVDAQPLPDCCRQKTCSCRLYELLHGAGNHAAGILTLGKRRPGPPGLQGRLQRLLQANGNHAAGILTMGRRAGAELEPYPCPGRRCPTATATALAPRGGSRV
| null | null |
behavioral fear response [GO:0001662]; eating behavior [GO:0042755]; excitatory postsynaptic potential [GO:0060079]; feeding behavior [GO:0007631]; negative regulation of DNA replication [GO:0008156]; negative regulation of potassium ion transport [GO:0043267]; negative regulation of transmission of nerve impulse [GO:0051970]; neuropeptide signaling pathway [GO:0007218]; phospholipase C-activating G protein-coupled receptor signaling pathway [GO:0007200]; positive regulation of calcium ion transport [GO:0051928]; positive regulation of cold-induced thermogenesis [GO:0120162]; positive regulation of cytosolic calcium ion concentration [GO:0007204]; positive regulation of transmission of nerve impulse [GO:0051971]; protein kinase C-activating G protein-coupled receptor signaling pathway [GO:0007205]; regulation of neurotransmitter secretion [GO:0046928]; response to starvation [GO:0042594]; sleep [GO:0030431]; temperature homeostasis [GO:0001659]
|
perinuclear region of cytoplasm [GO:0048471]; postsynapse [GO:0098794]; rough endoplasmic reticulum [GO:0005791]; secretory granule [GO:0030141]
|
neuropeptide hormone activity [GO:0005184]; type 1 orexin receptor binding [GO:0031771]; type 2 orexin receptor binding [GO:0031772]
|
PF02072;
| null |
Orexin family
|
PTM: Specific enzymatic cleavages at paired basic residues yield the different active peptides. {ECO:0000303|PubMed:9491897}.
|
SUBCELLULAR LOCATION: Rough endoplasmic reticulum {ECO:0000269|PubMed:9419374}. Cytoplasmic vesicle {ECO:0000269|PubMed:9419374}. Synapse {ECO:0000269|PubMed:9419374}. Note=Associated with perikaryal rough endoplasmic reticulum as well as cytoplasmic large granular vesicles at synapses. {ECO:0000269|PubMed:9419374}.
| null | null | null | null | null |
FUNCTION: Neuropeptides that play a significant role in the regulation of food intake and sleep-wakefulness, possibly by coordinating the complex behavioral and physiologic responses of these complementary homeostatic functions (PubMed:11283317, PubMed:11340621, PubMed:9491897). A broader role in the homeostatic regulation of energy metabolism, autonomic function, hormonal balance and the regulation of body fluids, is also suggested (PubMed:9491897). A modulation effect on luteinizing hormone-releasing hormone (LHRH) secretion also suggests a more minor contribution to the regulation of reproductive function (PubMed:11340621, PubMed:9879756). {ECO:0000269|PubMed:9491897, ECO:0000269|PubMed:9879756, ECO:0000303|PubMed:11283317, ECO:0000303|PubMed:11340621}.; FUNCTION: [Orexin-A]: Binds to orexin receptors HCRTR1/OX1R and HCRTR2/OX2R with a high affinity (PubMed:9491897). Stimulates food intake (PubMed:9491897). Modulates pituitary luteinizing hormone secretion in an ovarian steroid-dependent manner (PubMed:9879756). {ECO:0000269|PubMed:9491897, ECO:0000269|PubMed:9879756}.; FUNCTION: [Orexin-B]: Binds to orexin receptor HCRTR2/OX2R only (PubMed:9491897). Stimulates food intake (PubMed:9491897). Modulates pituitary luteinizing hormone secretion in an ovarian steroid-dependent manner (PubMed:9879756). {ECO:0000269|PubMed:9491897, ECO:0000269|PubMed:9879756}.
|
Rattus norvegicus (Rat)
|
O55233
|
CER1_MOUSE
|
MHLLLVQLLVLLPLGKADLCVDGCQSQGSLSFPLLERGRRDLHVANHEEAEDKPDLFVAVPHLMGTSLAGEGQRQRGKMLSRLGRFWKKPETEFYPPRDVESDHVSSGMQAVTQPADGRKVERSPLQEEAKRFWHRFMFRKGPAFQGVILPIKSHEVHWETCRTVPFNQTIAHEDCQKVVVQNNLCFGKCSSIRFPGEGADAHSFCSHCSPTKFTTVHLMLNCTSPTPVVKMVMQVEECQCMVKTERGEERLLLAGSQGSFIPGLPASKTNP
| null | null |
anterior/posterior axis specification [GO:0009948]; anterior/posterior pattern specification [GO:0009952]; bone mineralization [GO:0030282]; cell migration involved in gastrulation [GO:0042074]; cell population proliferation [GO:0008283]; cellular response to cadmium ion [GO:0071276]; determination of dorsal identity [GO:0048263]; determination of heart left/right asymmetry [GO:0061371]; gastrulation [GO:0007369]; growth plate cartilage chondrocyte proliferation [GO:0003419]; negative regulation of activin receptor signaling pathway [GO:0032926]; negative regulation of BMP signaling pathway [GO:0030514]; negative regulation of cell population proliferation [GO:0008285]; negative regulation of mesoderm development [GO:2000381]; nervous system development [GO:0007399]; sequestering of BMP in extracellular matrix [GO:0035582]; signal transduction involved in regulation of gene expression [GO:0023019]; ureteric bud development [GO:0001657]
|
extracellular region [GO:0005576]; extracellular space [GO:0005615]
|
BMP binding [GO:0036122]; cytokine activity [GO:0005125]; morphogen activity [GO:0016015]; protein homodimerization activity [GO:0042803]
|
PF03045;
|
2.10.90.10;
|
DAN family
|
PTM: N-glycosylated. {ECO:0000269|PubMed:9501024}.
|
SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:9431803}.
| null | null | null | null | null |
FUNCTION: Cytokine that may play a role in anterior neural induction and somite formation during embryogenesis in part, through a BMP-inhibitory mechanism. Can regulate Nodal signaling during gastrulation as well as the formation and patterning of the primitive streak. {ECO:0000269|PubMed:12431380, ECO:0000269|PubMed:9431803, ECO:0000269|PubMed:9501024, ECO:0000269|PubMed:9600941}.
|
Mus musculus (Mouse)
|
O55234
|
PSB5_MOUSE
|
MALASVLQRPMPVNQHGFFGLGGGADLLDLGPGSPGDGLSLAAPSWGVPEEPRIEMLHGTTTLAFKFLHGVIVAADSRATAGAYIASQTVKKVIEINPYLLGTMAGGAADCSFWERLLARQCRIYELRNKERISVAAASKLLANMVYQYKGMGLSMGTMICGWDKRGPGLYYVDSEGNRISGTAFSVGSGSVYAYGVMDRGYSYDLKVEEAYDLARRAIYQATYRDAYSGGAVNLYHVREDGWIRVSSDNVADLHDKYSSVSVP
|
3.4.25.1
| null |
proteasome-mediated ubiquitin-dependent protein catabolic process [GO:0043161]; proteolysis [GO:0006508]; response to oxidative stress [GO:0006979]
|
centrosome [GO:0005813]; cytosol [GO:0005829]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; proteasome core complex [GO:0005839]; proteasome core complex, beta-subunit complex [GO:0019774]
|
endopeptidase activity [GO:0004175]; peptidase activity [GO:0008233]; threonine-type endopeptidase activity [GO:0004298]
|
PF00227;
|
3.60.20.10;
|
Peptidase T1B family
| null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P28074}. Nucleus {ECO:0000250|UniProtKB:P28074}. Note=Translocated from the cytoplasm into the nucleus following interaction with AKIRIN2, which bridges the proteasome with the nuclear import receptor IPO9. {ECO:0000250|UniProtKB:P28074}.
|
CATALYTIC ACTIVITY: Reaction=Cleavage of peptide bonds with very broad specificity.; EC=3.4.25.1; Evidence={ECO:0000250|UniProtKB:P28074};
| null | null | null | null |
FUNCTION: Component of the 20S core proteasome complex involved in the proteolytic degradation of most intracellular proteins. This complex plays numerous essential roles within the cell by associating with different regulatory particles. Associated with two 19S regulatory particles, forms the 26S proteasome and thus participates in the ATP-dependent degradation of ubiquitinated proteins. The 26S proteasome plays a key role in the maintenance of protein homeostasis by removing misfolded or damaged proteins that could impair cellular functions, and by removing proteins whose functions are no longer required. Associated with the PA200 or PA28, the 20S proteasome mediates ubiquitin-independent protein degradation. This type of proteolysis is required in several pathways including spermatogenesis (20S-PA200 complex) or generation of a subset of MHC class I-presented antigenic peptides (20S-PA28 complex). Within the 20S core complex, PSMB5 displays a chymotrypsin-like activity. {ECO:0000269|PubMed:16581775, ECO:0000269|PubMed:19183883, ECO:0000269|PubMed:22341445}.
|
Mus musculus (Mouse)
|
O55236
|
MCE1_MOUSE
|
MAYNKIPPRWLNCPRRGQPVAGRFLPLKTMLGPRYDSQVAEENRFHPSMLSNYLKSLKVKMSLLVDLTNTSRFYDRNDIEKEGIKYIKLQCKGHGECPTTENTETFIRLCERFNERSPPELIGVHCTHGFNRTGFLICAFLVEKMDWSIEAAVATFAQARPPGIYKGDYLKELFRRYGDIEEAPPPPVLPDWCFEDEDEEDEDEDGKKDSEPGSSASFSKRRKERLKLGAIFLEGITVKGVTQVTTQPKLGEVQQKCHQFCGWEGSGFPGAQPVSMDKQNIRLLEQKPYKVSWKADGTRYMMLIDGTNEVFMIDRDNSVFHVSNLEFPFRKDLRMHLSNTLLDGEMIIDKVNGQAVPRYLIYDIIKFNAQPVGDCDFNIRLQCIEREIISPRHEKMKTGLIDKTQEPFSVRPKQFFDINISRKLLEGNFAKEVSHEMDGLIFQPIGKYKPGRCDDILKWKPPSLNSVDFRLKITRMGGEGLLPQNVGLLYVGGYERPFAQIKVTKELKQYDNKIIECKFENNSWVFMRQRIDKSFPNAYNTAMAVCNSISNPVTKEMLFEFIDRCAAAAQGQKRKYPLDPDTELMPPPPPKRLHRPT
|
2.7.7.50; 3.6.1.74
| null |
7-methylguanosine mRNA capping [GO:0006370]; dephosphorylation [GO:0016311]
|
nucleus [GO:0005634]
|
ATP binding [GO:0005524]; GTP binding [GO:0005525]; inorganic triphosphate phosphatase activity [GO:0050355]; mRNA 5'-phosphatase activity [GO:0140818]; mRNA guanylyltransferase activity [GO:0004484]; polynucleotide 5'-phosphatase activity [GO:0004651]; protein tyrosine/serine/threonine phosphatase activity [GO:0008138]
|
PF00782;PF03919;PF01331;
|
3.30.1490.430;3.30.470.30;2.40.50.140;3.90.190.10;
|
Non-receptor class of the protein-tyrosine phosphatase family; Eukaryotic GTase family
| null |
SUBCELLULAR LOCATION: Nucleus.
|
CATALYTIC ACTIVITY: Reaction=a 5'-end triphospho-ribonucleoside in mRNA + H2O = a 5'-end diphospho-ribonucleoside in mRNA + H(+) + phosphate; Xref=Rhea:RHEA:67004, Rhea:RHEA-COMP:17164, Rhea:RHEA-COMP:17165, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474, ChEBI:CHEBI:167616, ChEBI:CHEBI:167618; EC=3.6.1.74; Evidence={ECO:0000269|PubMed:21683636}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67005; Evidence={ECO:0000305|PubMed:21683636}; CATALYTIC ACTIVITY: Reaction=a 5'-end diphospho-ribonucleoside in mRNA + GTP + H(+) = a 5'-end (5'-triphosphoguanosine)-ribonucleoside in mRNA + diphosphate; Xref=Rhea:RHEA:67012, Rhea:RHEA-COMP:17165, Rhea:RHEA-COMP:17166, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019, ChEBI:CHEBI:37565, ChEBI:CHEBI:167616, ChEBI:CHEBI:167617; EC=2.7.7.50; Evidence={ECO:0000269|PubMed:21683636}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67013; Evidence={ECO:0000305|PubMed:21683636};
| null | null | null | null |
FUNCTION: Bifunctional mRNA-capping enzyme exhibiting RNA 5'-triphosphate monophosphatase activity in the N-terminal part and mRNA guanylyltransferase activity in the C-terminal part. Catalyzes the first two steps of cap formation: by removing the gamma-phosphate from the 5'-triphosphate end of nascent mRNA to yield a diphosphate end, and by transferring the GMP moiety of GTP to the 5'-diphosphate terminus of RNA via a covalent enzyme-GMP reaction intermediate. {ECO:0000269|PubMed:21683636, ECO:0000269|PubMed:9371772}.
|
Mus musculus (Mouse)
|
O55237
|
CD70_MOUSE
|
MPEEGRPCPWVRWSGTAFQRQWPWLLLVVFITVFCCWFHCSGLLSKQQQRLLEHPEPHTAELQLNLTVPRKDPTLRWGAGPALGRSFTHGPELEEGHLRIHQDGLYRLHIQVTLANCSSPGSTLQHRATLAVGICSPAAHGISLLRGRFGQDCTVALQRLTYLVHGDVLCTNLTLPLLPSRNADETFFGVQWICP
| null | null |
B cell mediated immunity [GO:0019724]; B cell proliferation [GO:0042100]; extrinsic apoptotic signaling pathway [GO:0097191]; T cell mediated immunity [GO:0002456]; tumor necrosis factor-mediated signaling pathway [GO:0033209]
|
extracellular exosome [GO:0070062]; plasma membrane [GO:0005886]
|
cytokine activity [GO:0005125]; protease binding [GO:0002020]; tumor necrosis factor receptor binding [GO:0005164]
|
PF00229;
|
2.60.120.40;
|
Tumor necrosis factor family
|
PTM: N-glycosylated. {ECO:0000269|PubMed:9366422}.
|
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:9366422, ECO:0000269|PubMed:9620608}; Single-pass type II membrane protein {ECO:0000255}.
| null | null | null | null | null |
FUNCTION: Expressed at the plasma membrane of B cells, it is the ligand of the CD27 receptor which is specifically expressed at the surface of T cells. The CD70-CD27 signaling pathway mediates antigen-specific T cell activation and expansion which in turn provides immune surveillance of B cells. {ECO:0000269|PubMed:9366422, ECO:0000269|PubMed:9620608}.
|
Mus musculus (Mouse)
|
O55239
|
NNMT_MOUSE
|
MESGFTSKDTYLSHFNPRDYLEKYYSFGSRHCAENEILRHLLKNLFKIFCLGAVKGELLIDIGSGPTIYQLLSACESFTEIIVSDYTDQNLWELQKWLKKEPGAFDWSPVVTYVCDLEGNRMKGPEKEEKLRRAIKQVLKCDVTQSQPLGGVSLPPADCLLSTLCLDAACPDLPAYRTALRNLGSLLKPGGFLVMVDALKSSYYMIGEQKFSSLPLGWETVRDAVEEAGYTIEQFEVISQNYSSTTSNNEGLFSLVGRKPGRSE
|
2.1.1.1
| null |
animal organ regeneration [GO:0031100]; methylation [GO:0032259]; nicotinamide metabolic process [GO:0006769]; positive regulation of gluconeogenesis [GO:0045722]; positive regulation of protein deacetylation [GO:0090312]; response to organonitrogen compound [GO:0010243]; response to xenobiotic stimulus [GO:0009410]
|
cytosol [GO:0005829]
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nicotinamide N-methyltransferase activity [GO:0008112]
|
PF01234;
|
3.40.50.150;
|
Class I-like SAM-binding methyltransferase superfamily, NNMT/PNMT/TEMT family
|
PTM: Deiminated by PADI1 and PADI2. {ECO:0000250|UniProtKB:P40261}.
|
SUBCELLULAR LOCATION: Cytoplasm.
|
CATALYTIC ACTIVITY: Reaction=nicotinamide + S-adenosyl-L-methionine = 1-methylnicotinamide + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:23884, ChEBI:CHEBI:16797, ChEBI:CHEBI:17154, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789; EC=2.1.1.1; Evidence={ECO:0000269|PubMed:26168293, ECO:0000269|PubMed:29483571}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:23885; Evidence={ECO:0000305|PubMed:26168293, ECO:0000305|PubMed:29483571};
| null |
PATHWAY: Cofactor metabolism. {ECO:0000250|UniProtKB:P40261}.; PATHWAY: Amino-acid degradation. {ECO:0000250|UniProtKB:P40261}.
| null | null |
FUNCTION: Catalyzes the N-methylation of nicotinamide using the universal methyl donor S-adenosyl-L-methionine to form N1-methylnicotinamide and S-adenosyl-L-homocysteine, a predominant nicotinamide/vitamin B3 clearance pathway (PubMed:26168293, PubMed:29483571). Plays a central role in regulating cellular methylation potential, by consuming S-adenosyl-L-methionine and limiting its availability for other methyltransferases (By similarity). Actively mediates genome-wide epigenetic and transcriptional changes through hypomethylation of repressive chromatin marks, such as H3K27me3. In a developmental context, contributes to low levels of the repressive histone marks that characterize pluripotent embryonic stem cell pre-implantation state (By similarity). Acts as a metabolic regulator primarily on white adipose tissue energy expenditure as well as hepatic gluconeogenesis and cholesterol biosynthesis (PubMed:24717514, PubMed:26168293). In white adipocytes, regulates polyamine flux by consuming S-adenosyl-L-methionine which provides for propylamine group in polyamine biosynthesis, whereas by consuming nicotinamide controls NAD(+) levels through the salvage pathway (PubMed:24717514). Via its product N1-methylnicotinamide regulates protein acetylation in hepatocytes, by repressing the ubiquitination and increasing the stability of SIRT1 deacetylase (PubMed:26168293). Can also N-methylate other pyridines structurally related to nicotinamide and play a role in xenobiotic detoxification (By similarity). {ECO:0000250|UniProtKB:P40261, ECO:0000269|PubMed:24717514, ECO:0000269|PubMed:26168293, ECO:0000269|PubMed:29483571}.
|
Mus musculus (Mouse)
|
O55240
|
RDH5_MOUSE
|
MWLPLLLGALLWAVLWLLRDRQSLPASDAFIFITGCDSGFGRLLALQLDQKGFQVLAGCLTPSGAEDLQQMASSRLHTTLLDITDPQNVQQVAKWVKTRVGETGLFGLVNNAGVAGIIGPTPWLTQDDFQRVLSVNTLGPIGVTLALLPLLQQARGRVVNITSVLGRIAANGGGYCVSKFGLEAFSDSLRRDMAPFGVQVSIVEPGFFRTPVTNLESLESTLKACWARLPPAIQAHYGEAFLDTYLRVQRRIMNLICDPELTKVTSCLEHALTARHPRTRYSPGWDAKLLWLPASYLPARVVDAVLTWILPRPAQSVS
|
1.1.1.209; 1.1.1.315; 1.1.1.53
| null |
response to stimulus [GO:0050896]; retinoid metabolic process [GO:0001523]; retinol metabolic process [GO:0042572]; steroid metabolic process [GO:0008202]; visual perception [GO:0007601]
|
cell body [GO:0044297]; endoplasmic reticulum lumen [GO:0005788]; endoplasmic reticulum membrane [GO:0005789]; intracellular membrane-bounded organelle [GO:0043231]
|
11-cis-retinol dehydrogenase [GO:0106429]; androstan-3-alpha,17-beta-diol dehydrogenase activity [GO:0047044]; androsterone dehydrogenase activity [GO:0047023]; NAD-retinol dehydrogenase activity [GO:0004745]; protein homodimerization activity [GO:0042803]
|
PF00106;
|
3.40.50.720;
|
Short-chain dehydrogenases/reductases (SDR) family
| null |
SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:10739682, ECO:0000269|PubMed:11279029}; Multi-pass membrane protein {ECO:0000255}; Lumenal side {ECO:0000269|PubMed:10739682, ECO:0000269|PubMed:11279029, ECO:0000269|PubMed:16223484}.
|
CATALYTIC ACTIVITY: Reaction=11-cis-retinol + NAD(+) = 11-cis-retinal + H(+) + NADH; Xref=Rhea:RHEA:42060, ChEBI:CHEBI:15378, ChEBI:CHEBI:16066, ChEBI:CHEBI:16302, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.315; Evidence={ECO:0000269|PubMed:10588954}; CATALYTIC ACTIVITY: Reaction=9-cis-retinol + NAD(+) = 9-cis-retinal + H(+) + NADH; Xref=Rhea:RHEA:42052, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:78272, ChEBI:CHEBI:78273; Evidence={ECO:0000269|PubMed:10588954, ECO:0000269|PubMed:11279029, ECO:0000269|PubMed:9539749}; CATALYTIC ACTIVITY: Reaction=13-cis-retinol + NAD(+) = 13-cis-retinal + H(+) + NADH; Xref=Rhea:RHEA:42056, ChEBI:CHEBI:15378, ChEBI:CHEBI:45479, ChEBI:CHEBI:45487, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; Evidence={ECO:0000269|PubMed:10588954}; CATALYTIC ACTIVITY: Reaction=androsterone + NAD(+) = 5alpha-androstan-3,17-dione + H(+) + NADH; Xref=Rhea:RHEA:20381, ChEBI:CHEBI:15378, ChEBI:CHEBI:15994, ChEBI:CHEBI:16032, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.209; Evidence={ECO:0000250|UniProtKB:Q92781}; CATALYTIC ACTIVITY: Reaction=5alpha-androstane-3alpha,17beta-diol + NAD(+) = 17beta-hydroxy-5alpha-androstan-3-one + H(+) + NADH; Xref=Rhea:RHEA:42004, ChEBI:CHEBI:15378, ChEBI:CHEBI:16330, ChEBI:CHEBI:36713, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.53; Evidence={ECO:0000250|UniProtKB:Q92781};
| null |
PATHWAY: Cofactor metabolism; retinol metabolism. {ECO:0000303|PubMed:9539749}.
| null | null |
FUNCTION: Catalyzes the oxidation of cis-isomers of retinol, including 11-cis-, 9-cis-, and 13-cis-retinol in an NAD-dependent manner (PubMed:10588954, PubMed:9539749). Has no activity towards all-trans retinal (By similarity). Plays a significant role in 11-cis retinol oxidation in the retinal pigment epithelium cells (RPE). Also recognizes steroids (androsterone, androstanediol) as its substrates (By similarity). {ECO:0000250|UniProtKB:Q27979, ECO:0000250|UniProtKB:Q92781, ECO:0000269|PubMed:10588954, ECO:0000269|PubMed:9539749}.
|
Mus musculus (Mouse)
|
O55241
|
OREX_MOUSE
|
MNFPSTKVPWAAVTLLLLLLLPPALLSLGVDAQPLPDCCRQKTCSCRLYELLHGAGNHAAGILTLGKRRPGPPGLQGRLQRLLQANGNHAAGILTMGRRAGAELEPHPCSGRGCPTVTTTALAPRGGSGV
| null | null |
eating behavior [GO:0042755]; excitatory postsynaptic potential [GO:0060079]; negative regulation of DNA replication [GO:0008156]; negative regulation of potassium ion transport [GO:0043267]; negative regulation of transmission of nerve impulse [GO:0051970]; neuropeptide signaling pathway [GO:0007218]; phospholipase C-activating G protein-coupled receptor signaling pathway [GO:0007200]; positive regulation of calcium ion transport [GO:0051928]; positive regulation of cold-induced thermogenesis [GO:0120162]; positive regulation of cytosolic calcium ion concentration [GO:0007204]; positive regulation of transmission of nerve impulse [GO:0051971]; protein kinase C-activating G protein-coupled receptor signaling pathway [GO:0007205]; regulation of neurotransmitter secretion [GO:0046928]; response to starvation [GO:0042594]; sleep [GO:0030431]; temperature homeostasis [GO:0001659]
|
perinuclear region of cytoplasm [GO:0048471]; postsynapse [GO:0098794]; rough endoplasmic reticulum [GO:0005791]; secretory granule [GO:0030141]
|
neuropeptide hormone activity [GO:0005184]; type 1 orexin receptor binding [GO:0031771]; type 2 orexin receptor binding [GO:0031772]
|
PF02072;
| null |
Orexin family
|
PTM: Specific enzymatic cleavages at paired basic residues yield the different active peptides.
|
SUBCELLULAR LOCATION: Rough endoplasmic reticulum {ECO:0000250|UniProtKB:O55232}. Cytoplasmic vesicle {ECO:0000250|UniProtKB:O55232}. Synapse {ECO:0000250|UniProtKB:O55232}. Note=Associated with perikaryal rough endoplasmic reticulum as well as cytoplasmic large granular vesicles at synapses. {ECO:0000250|UniProtKB:O55232}.
| null | null | null | null | null |
FUNCTION: Neuropeptides that play a significant role in the regulation of food intake and sleep-wakefulness, possibly by coordinating the complex behavioral and physiologic responses of these complementary homeostatic functions. A broader role in the homeostatic regulation of energy metabolism, autonomic function, hormonal balance and the regulation of body fluids, is also suggested. {ECO:0000250|UniProtKB:O55232}.; FUNCTION: [Orexin-A]: Binds to orexin receptors HCRTR1/OX1R and HCRTR2/OX2R with a high affinity (By similarity). Stimulates food intake (By similarity). Modulates pituitary luteinizing hormone secretion in an ovarian steroid-dependent manner (By similarity). {ECO:0000250|UniProtKB:O55232}.; FUNCTION: [Orexin-B]: Binds to orexin receptor HCRTR2/OX2R only (By similarity). Stimulates food intake (By similarity). Modulates pituitary luteinizing hormone secretion in an ovarian steroid-dependent manner (By similarity). {ECO:0000250|UniProtKB:O55232}.
|
Mus musculus (Mouse)
|
O55242
|
SGMR1_MOUSE
|
MPWAAGRRWAWITLILTIIAVLIQAAWLWLGTQNFVFSREEIAQLARQYAGLDHELAFSRLIVELRRLHPGHVLPDEELQWVFVNAGGWMGAMCILHASLSEYVLLFGTALGSHGHSGRYWAEISDTIISGTFHQWKEGTTKSEVFYPGETVVHGPGEATALEWGPNTWMVEYGRGVIPSTLFFALADTFFSTQDYLTLFYTLRAYARGLRLELTTYLFGQDS
| null | null |
ergosterol biosynthetic process [GO:0006696]; lipid transport [GO:0006869]; nervous system development [GO:0007399]; protein homotrimerization [GO:0070207]; regulation of neuron apoptotic process [GO:0043523]
|
anchoring junction [GO:0070161]; cytoplasmic vesicle [GO:0031410]; endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]; growth cone [GO:0030426]; lipid droplet [GO:0005811]; membrane [GO:0016020]; nuclear inner membrane [GO:0005637]; nuclear outer membrane [GO:0005640]; postsynaptic density [GO:0014069]; postsynaptic density membrane [GO:0098839]
|
G protein-coupled opioid receptor activity [GO:0004985]; signaling receptor activity [GO:0038023]
|
PF04622;
| null |
ERG2 family
| null |
SUBCELLULAR LOCATION: Nucleus inner membrane {ECO:0000250|UniProtKB:Q99720}. Nucleus outer membrane {ECO:0000250|UniProtKB:Q99720}. Nucleus envelope {ECO:0000269|PubMed:12730355}. Cytoplasmic vesicle {ECO:0000250|UniProtKB:Q99720}. Endoplasmic reticulum membrane {ECO:0000269|PubMed:12730355}. Membrane {ECO:0000250|UniProtKB:Q99720}; Single-pass membrane protein {ECO:0000250|UniProtKB:Q99720}. Lipid droplet {ECO:0000269|PubMed:12730355}. Cell junction {ECO:0000250|UniProtKB:Q99720}. Cell membrane {ECO:0000250|UniProtKB:Q99720}. Cell projection, growth cone {ECO:0000250|UniProtKB:Q99720}. Postsynaptic density membrane {ECO:0000269|PubMed:20167253}. Note=During interphase, detected at the inner and outer nuclear membrane and the endoplasmic reticulum. Detected on cytoplasmic vesicles during mitosis (By similarity). Targeted to lipid droplets, cholesterol and galactosylceramide-enriched domains of the endoplasmic reticulum (PubMed:12730355). Enriched at cell-cell communication regions, growth cone and postsynaptic structures. Localization is modulated by ligand-binding. In motor neurons it is enriched at cholinergic postsynaptic densities (PubMed:20167253). {ECO:0000250|UniProtKB:Q99720, ECO:0000269|PubMed:12730355, ECO:0000269|PubMed:20167253}.
| null | null | null | null | null |
FUNCTION: Functions in lipid transport from the endoplasmic reticulum and is involved in a wide array of cellular functions probably through regulation of the biogenesis of lipid microdomains at the plasma membrane (PubMed:12730355). Involved in the regulation of different receptors it plays a role in BDNF signaling and EGF signaling. Also regulates ion channels like the potassium channel and could modulate neurotransmitter release. Plays a role in calcium signaling through modulation together with ANK2 of the ITP3R-dependent calcium efflux at the endoplasmic reticulum. Plays a role in several other cell functions including proliferation, survival and death. Originally identified for its ability to bind various psychoactive drugs it is involved in learning processes, memory and mood alteration (PubMed:11149946, PubMed:14622179, PubMed:15571673, PubMed:15777781, PubMed:23332758, PubMed:9425306, PubMed:9603192). Necessary for proper mitochondrial axonal transport in motor neurons, in particular the retrograde movement of mitochondria (PubMed:25678561). Plays a role in protecting cells against oxidative stress-induced cell death via its interaction with RNF112 (PubMed:26792191). {ECO:0000269|PubMed:11149946, ECO:0000269|PubMed:12730355, ECO:0000269|PubMed:14622179, ECO:0000269|PubMed:15571673, ECO:0000269|PubMed:15777781, ECO:0000269|PubMed:23332758, ECO:0000269|PubMed:25678561, ECO:0000269|PubMed:26792191, ECO:0000269|PubMed:9425306, ECO:0000269|PubMed:9603192}.
|
Mus musculus (Mouse)
|
O55245
|
TTHY_CROPO
|
MAFHSMLLVFLAGLVFLTEAAPLVSHGSIDSKCPLMVKVLDAVRGSPAANVAIKVFKKTSDGDWQEFAAGKTTEFGEVHELTSDEKFVEGIYRVEFDTSSYWKALGLSPFHEYADVVFTANDSGHRHYTIAALLSPFSYSTTAVVSDPQE
| null | null |
purine nucleobase metabolic process [GO:0006144]; thyroid hormone transport [GO:0070327]
|
extracellular region [GO:0005576]; extracellular space [GO:0005615]
|
hormone activity [GO:0005179]; identical protein binding [GO:0042802]; thyroid hormone binding [GO:0070324]
|
PF00576;
|
2.60.40.180;
|
Transthyretin family
|
PTM: Sulfonation of the reactive cysteine Cys-33 enhances the stability of the native conformation of TTR, avoiding misassembly of the protein leading to amyloid formation. {ECO:0000250|UniProtKB:P02766}.
|
SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:12228058}.
| null | null | null | null | null |
FUNCTION: Thyroid hormone-binding protein, with a much higher binding affinity for triiodothyronine (T3) than for thyroxine (T4). Probably transports triiodothyronine from the bloodstream to the brain. {ECO:0000269|PubMed:12228058}.
|
Crocodylus porosus (Saltwater crocodile) (Estuarine crocodile)
|
O55528
|
L_SENDO
|
MDGQESTQNPSDILYPECHLNSPIVRGKIAQLHVLLDVNQPYILKDDSIINITKHKIRNGGLSLRQIKIRSLGKALQRTIKDLDRYTFEPYPTYSQELLRLDIPEICDKIRSVFAVSDRLTKELSNGFQDLWLNIFKQLGNIEGREGYDPLQDISTIPEITERYSRNKWYRPFLTWFSIKYDMRWMQKTRPGGPLDTSNSHNLLECKSYTLVTYGDLVMILNKSTLTGYILTPELVLMYCDVVEGRWNMSAAGQLDKRSTGITSKGEELWELVDSLFSSLGEEIYNVIALLEPLSLALIQLSDPVIPLRGAFMRHVLTELQTVLTSKDVYTDPEADAIVESLLAIFHGTSIDEKAEIFSFFRTFGHPSLEAVTAADKVRAHMYAQKAIKLKTLHECHAVFCTIIINGYRERHGGQWPPCDFPDHVCLELRNAQGSNTAISYECAVDNYTSFIGFKFRKFIEPQLDEDLTIYMKDKALSPRKEAWDSVYPDSNLYYKVPESEETRRLIEVFINDENFNPEDIIDYVESGDWLKDEKFNISYSLKEKEIKQEGRLFAKMTYKMRAVQVLAETLLAKGIGELFSENGMVKGEIDLLKRLTTLSVSGVPRTDSVYNNPRSSEKRNESMKKRNSKGYWDEKKRSRHEFKATDSSTDGYETLSCFLTTDLKKYCLNWRFESTALFGQRCNEIFGFKTFFNWMHPVLEKCTIYVGDPYCPVADRMHRQLQDHADSGIFIHNPRGGIEGYCQKLWTLISISAIHLAAVRVGVRVSAMVQGDNQAIAVTSRVPVAQTYKQKKNHVYEEITRYFGALRHVMFDIGHELKLNETIISSKMFVYSKRIYYDGKILPQCLKALTRCVFWSETLVDENRSACSNISTSIAKAIENGYSPILGYCIALYKTCQQVCISLGMTINPTISPTVRDQYFKGKNWLRCAVLIPANVGGFNYMSTSRCFVRNIGDPAVAALADLKRFIRADLLDKQVLYRVMNQEPGDSSFLDWASDPYSCNLPHSQSITTIIKNITARSVLQESPNPLLSGLFTETSGEEDLNLASFLMDRKVILPRVAHEILSNSLTGVREAIAGMLDTTKSLVRASVKRGGLSYGILRRLVNYDLLQYETLTRTLRKPVKDNIEYEYMCSVELAVGLRQKMWIHLTYGRPIHGLETPDPLELLRGTFIEGSEVCKLCRSEGADPIYTWFYLPDNIDLDTLTNGSPAIRIPYFGSATDERSEAQLGYVRNLSKPAKAAIRIAMVYTWAYGTDEISWMEAALIAQTRANLSLENLKLLTPVSTSTNLSHRLKDTATQMKFSSATLVRASRFITISNDNMALKEAGESKDTNLVYQQIMLTGLSLFEFNMRYKKGSLEKPLILHLHLNNGCCIMESPQEANIPPRSTLDLEITQENNKLIYDPDPLRDVDLELFSKVRDVVHTVDMTYWSDDEVIRATSICTAMTIADTMSQLDRDNLKEMIALVNDDDVNSLITEFMVIDVPLFCSTFGGILVNQFAYSLYGLNIRGREEIWGHVVRILKDTSHAVLKVLSNALSHPKIFKRFWNAGVVEPVYGPNLSNQDKTLLALSVCEYSVDLFMHDWQGGVPLEVFICDNDPDVADMRRSSFLARHLAYLCSLAEISRDGPRLESMNSLERLETLKSYLELTFLDDPVLRYSQLTGLVIKVFPSTLTYIRKSSIKVLRTRGIGVPEVLEDWDPEADNALLDGIAAEIQQNIPLGHQTRAPFWGLRVSKSQVLRLRGYEEITRGEVGRSGVGLTLPFDGRYLSHQLRLFGVNSTSCLKALELTYLLSPLVDKDKDRLFLGEGAGAMLSCYDATLGPCINYYNSGVYSCDVNGQRELNIYPAEVALVGKKLNNVTSLGQRVKVLFNGNPGSTWIGNDECEALIWNELQNNSIGLVHCDMEGGDHKDDQVVLHEHYSVIRIAYLVGDRDVVLISKIAPRLGTDWTRQLSLYLRYWDEVNLVVLKTSNPASTEMYLLSRHPKSDIIEDSKTVLASLHPLSKEDSIKIEKWILIEKAKAHEWVTRELREGSSSSGMLRPYHQALQTFGFEPNLYKLSRDFLSTMNIADTHNCMTAFNRVLKDTIFEWARITESDKRLKLTGKYDLYPVRDSGKLKTISRRLVLSWVSLSMSTRLVTGSFPDQKFEARLQLGIVSLSSREIRNLRVITKTILDRFENTIHSITYRFLTKEVKILMKILGAVKMFGARQNEYTTVVDDGSLDDIEPYDSL
|
2.1.1.375; 2.7.7.48; 2.7.7.88; 3.6.1.-
| null |
negative stranded viral RNA replication [GO:0039689]
|
host cell cytoplasm [GO:0030430]; virion component [GO:0044423]
|
ATP binding [GO:0005524]; GTPase activity [GO:0003924]; mRNA 5'-cap (guanine-N7-)-methyltransferase activity [GO:0004482]; RNA-dependent RNA polymerase activity [GO:0003968]
|
PF14318;PF00946;
| null |
Paramyxovirus L protein family
| null |
SUBCELLULAR LOCATION: Virion {ECO:0000305}. Host cytoplasm {ECO:0000250}.
|
CATALYTIC ACTIVITY: Reaction=a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate + RNA(n+1); Xref=Rhea:RHEA:21248, Rhea:RHEA-COMP:14527, Rhea:RHEA-COMP:17342, ChEBI:CHEBI:33019, ChEBI:CHEBI:61557, ChEBI:CHEBI:140395; EC=2.7.7.48; Evidence={ECO:0000255|PROSITE-ProRule:PRU00539}; CATALYTIC ACTIVITY: Reaction=a 5'-end (5'-triphosphoguanosine)-adenylyl-adenylyl-cytidylyl-adenosine in mRNA + 2 S-adenosyl-L-methionine = a 5'-end (N(7)-methyl 5'-triphosphoguanosine)-(2'-O-methyladenylyl)-adenylyl-cytidylyl-adenosine in mRNA + H(+) + 2 S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:65376, Rhea:RHEA-COMP:16797, Rhea:RHEA-COMP:16798, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:156483, ChEBI:CHEBI:156484; EC=2.1.1.375; Evidence={ECO:0000250|UniProtKB:P03523}; CATALYTIC ACTIVITY: Reaction=a 5'-end (5'-triphosphoguanosine)-adenylyl-adenylyl-cytidylyl-adenosine in mRNA + S-adenosyl-L-methionine = a 5'-end (5'-triphosphoguanosine)-(2'-O-methyladenylyl)-adenylyl-cytidylyl-adenosine in mRNA + H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:65380, Rhea:RHEA-COMP:16797, Rhea:RHEA-COMP:16801, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:156482, ChEBI:CHEBI:156484; Evidence={ECO:0000250|UniProtKB:P03523}; CATALYTIC ACTIVITY: Reaction=a 5'-end triphospho-adenylyl-adenylyl-cytidylyl-adenosine in mRNA + GDP + H(+) = a 5'-end (5'-triphosphoguanosine)-adenylyl-adenylyl-cytidylyl-adenosine in mRNA + diphosphate; Xref=Rhea:RHEA:65436, Rhea:RHEA-COMP:16797, Rhea:RHEA-COMP:16799, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019, ChEBI:CHEBI:58189, ChEBI:CHEBI:156484, ChEBI:CHEBI:156503; EC=2.7.7.88; Evidence={ECO:0000250|UniProtKB:P28887}; CATALYTIC ACTIVITY: Reaction=a 5'-end (5'-triphosphoguanosine)-(2'-O-methyladenylyl)-adenylyl-cytidylyl-adenosine in mRNA + S-adenosyl-L-methionine = a 5'-end (N(7)-methyl 5'-triphosphoguanosine)-(2'-O-methyladenylyl)-adenylyl-cytidylyl-adenosine in mRNA + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:65440, Rhea:RHEA-COMP:16798, Rhea:RHEA-COMP:16801, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:156482, ChEBI:CHEBI:156483; Evidence={ECO:0000250|UniProtKB:P03523}; CATALYTIC ACTIVITY: Reaction=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:58189; Evidence={ECO:0000250|UniProtKB:P28887};
| null | null | null | null |
FUNCTION: RNA-directed RNA polymerase that catalyzes the transcription of viral mRNAs, their capping and polyadenylation. The template is composed of the viral RNA tightly encapsidated by the nucleoprotein (N). The viral polymerase binds to the genomic RNA at the 3' leader promoter, and transcribes subsequently all viral mRNAs with a decreasing efficiency. The first gene is the most transcribed, and the last the least transcribed. The viral phosphoprotein acts as a processivity factor. Capping is concommitant with initiation of mRNA transcription. Indeed, a GDP polyribonucleotidyl transferase (PRNTase) adds the cap structure when the nascent RNA chain length has reached few nucleotides. Ribose 2'-O methylation of viral mRNA cap precedes and facilitates subsequent guanine-N-7 methylation, both activities being carried by the viral polymerase. Polyadenylation of mRNAs occur by a stuttering mechanism at a slipery stop site present at the end viral genes. After finishing transcription of a mRNA, the polymerase can resume transcription of the downstream gene. {ECO:0000250|UniProtKB:P03523}.; FUNCTION: RNA-directed RNA polymerase that catalyzes the replication of viral genomic RNA. The template is composed of the viral RNA tightly encapsidated by the nucleoprotein (N). The replicase mode is dependent on intracellular N protein concentration. In this mode, the polymerase replicates the whole viral genome without recognizing transcriptional signals, and the replicated genome is not caped or polyadenylated. {ECO:0000250|UniProtKB:P03523}.
|
Sendai virus (strain Ohita) (SeV)
|
O56075
|
POLG_PEMVM
|
MASITFGNACTVVFGQVRKEEVTAGPVAVNLNEGTRMVVVPTAAQMATPTPSVSIKIINRWSNKAVSSYERQVEDVFANFFAKKERSDELLTRYYGKVVQKGNKLMVKRAPLHVARVLEKQRLQDIEDEKAFLQYRDAGVHVAGSVKFTDTRSRGQTVSFRTEHYKPTGKIVQKKKAQKQRANADVDHLIDEVMKICSADCKQVEFISMGKRRLTAKFKLFGKSVIPCIHLAHEQGRRLRRELDPRIHEQVIAHLVTGRKVRELIKDDMVTYGWSGAILNKNLFKRTPFRWDEVVIRGRLYGKLVDARSKLSECSKDKIHQYSSFEAQFWKGWKNKFDTLHPHNKDHICEPTINNEKCGEIVATIFQAIHPVIKVSCSTCRERLTKASNEELNEYLATNLACHKATFDDMRQQHATVNTVLNKIEQTSLANPNLKDSMEIVRLLQNLNQTQARQLMKVNNTLLKGNVATSEEFSDATTQLLEVTRWYAKHLSLVDEGSISSFRNKATSKSLINPSLLCDNQLDRNGNFVWGERGRHSKRFFENFFEEVVPGGGYKKYQIRNSPNCTRKLAIGNLIVPMSLERARNALIGESVERLPVTEACVSRVNGAFMHVASCVTSDNGSAHFSPLYSPTKRHLVVGTTGDSKYIDLPATESDKMYVAKEGYCYINIFLAMLVNVNEDSAKDFTKMIRDTIVPMLGTWPSMMDVATACYILTVFHPETKSAELPRILVDHTNKTMHVIDSFGSISTGYHILKAGTVSQLIHFASNELVSEMKHYVVGGEAPHARRMRMEKALIQGIFKPKQLVYLIEEDPYILMMSLVSPTLLINLFNVGGLEVAMKHWIKKEMNIGLIFSMLSSLAQKVSRADLVNEQITMIDANAAQFIETLAGIDVENPMRNELVSALTMMLARSDVDSTLNKTGFTGFSDTLLEMREKIIGDELNKVWSELSWWEKFSSIIFSRRARKHIMAPLPNTKLHAIDDRYAISCTWLHGKIKARFNGAKSATLEVCKKVTSILKRNTVDSILYICRKCYSDIFYFVNVMLISSMILSVIYTMHKMVIESRAHKQAMVIMKMREDELVVKQMYDQYCKLANETPTKEEFFQYVCKMNKELGERIAPEFEEGSLVVYQAKTETELGLEKVVAYLALIAMIFDGERSDAVFRALSKLKTVFGTLGETVRYQSLDEIESVADEKKMTIDFELEGSEASSSTVMSAKFSDWWYKQLETNRVVPHYRIGGEFVEFTRKTAAEVVNNMRASNASEFLVRGAVGSGKSTGLPHLLAQKGRVLLLEPTRPLAENVCKQLRQAPFQQNPTLRMRGLTTFGSSNIVIMTSGFALHYYANNPTKLQEYDFVMIDESHTMDASAMAFYCLVREYNFQGKIIKVSATPPGKECEFKTQFDVALLIEEDLSFQQFAQSQGQGGNADMTKHGDNILVYVASYNDVDQLAELLIRGNHFVTKVDGRTMKMGSTEIVSKGTASKKHYIIATNIIENGVTLDVDVVVDFGQKVVAELDGDSRCMRYRKVAVSYGERIQRLGRVGRVKKGTALRIGHTEHGISEIPASISTEAAFLCFAYGLPVITHNVTVSILANCTVQQARTMMLFELSPFFLADLVKYNGSMHPEVHKLLKPYKLRDSEIELCKLAIPNSSIGRWLSVHEYAKLGIKIHAVDSVRIPFAGRGIPDKLYSELWHIIQEHKHEAGFGRLTSASASTIAYTLSTDPEAIPRTIALLDNLIAEEMQKKAHFEALNSTLCSQRFTLKNIVDTVRQRYMKDHSKHNIEVLQSARSQILEFNSATHDFKKVASLLGYGFLDTVQYQSKNELSKRLGLKGRWNKSLVTNDLLVCGMVLFGGVWMVWEYAKSAMNEPVRYQGKRQNQKLKFRDARDRKVGREVYGDDGTIEHFFGEAYTKKGKSKGNHTVKGMGRKTRRFIHMYGFDPTEYSFVRFVDPLTGYAIDENITCDISLVQDEVAEVRKQFINEDEISAQSIAENPGIIAYYMSRNADKALKIDLTPHNPLAVGRGGSSIAGFPEREYELRQTGKPLEVKKSEVPPVSKDVVATEGKSMCRGLRNYNPIATSICKLVNESDGHSETIHGIGFGPVIITNSHLFRRNNGTLQIQTHHGVFRVKNSTQLQVSHMAKKDMIIIKMPCDVPPFPSKLRFRQPEQGEKAVLVGSLFQQKSITSSVSESTMVMPVNDSGYWRHWVSTKDGDCGLPLVSTVDGAILGLHGLTSTKSDRNYFVPFDEQFERDILANLEKLDWKRHWLHSSDLIAWGGMSLKENHPHDCFRTSKLVTDLLGLTKDSVEYQSGQDKWVLAGLENNLKAVAQSESQLVTKHVVKGQCMYFQEYLATHSTAEKFFKPLMGAYQPSKLNKEAFTKDLYKYQNEIIVGEVDKDAFDNAVEAVIYLLDDLGFGECAYVTDEEAILDSLNMKAAVGALYKGKKKEYFESLSEPEKHHIVQASCERLFYGEMGVWNGSLKAELRPKEKVALNKTRTFTAAPIDTLLGGKCCVDDFNNRFYSLNIEGPWTVGMTKFYGGWDKLMRKLPDGWRYCHADGSQFDSSLTPFLLNAVLAVRLMFMEDWWVGEQMLRNFYTEIIYTPILTPDGTIVKKFKGNNSGQPSTVVDNTLMVMIAMFYGMKKLNWTDEQIKERIVFFAXGDDLIIAVQPEHEGILDTLQRSLGELGLKYDFSERCDDRQELWFMSHQGHLVDGMYIPKLEQERIVSILEWDRSTVIEHRAEAICAAMIEAWGYPELLKQIRLFYAWILDHDMFKSLVAEGKLPYIAETALRKLYTDADATDVELEEYILRFTEVDEDEDHNDEVRYQSGENKSKVEVDAAAAKLKEKEKEKHKKTEEGTSEGTSQTKEPDVDTGSQGIVYVPKLAKITKKMRMPMVGGQVILHIPHLLDYKPEQVDLSNTRSSQQQFTAWYNGLKEAYEITDDTSMSVLMNGLMVWCIENGTSPNINGNWTMMDGHEQNEYPLKPVIENAKPTFRQIMHHFSDAAEAYIEMRNAEKPYMPRYGLQRNLRDFSYARIAFDFYEITSRTSAKAREIHMQMKAAALNNVAIKTFGLDGNVGTQDEDTERHTANDVNRNMHSLLGMRQM
|
2.7.7.48; 3.4.-.-; 3.4.22.44; 3.4.22.45; 3.6.4.-
| null |
DNA-templated transcription [GO:0006351]; proteolysis [GO:0006508]; viral RNA genome replication [GO:0039694]; virus-mediated perturbation of host defense response [GO:0019049]
|
helical viral capsid [GO:0019029]; host cell cytoplasmic vesicle [GO:0044161]; host cell nucleus [GO:0042025]
|
ATP binding [GO:0005524]; cysteine-type endopeptidase activity [GO:0004197]; helicase activity [GO:0004386]; hydrolase activity, acting on acid anhydrides, in phosphorus-containing anhydrides [GO:0016818]; RNA binding [GO:0003723]; RNA-dependent RNA polymerase activity [GO:0003968]; serine-type peptidase activity [GO:0008236]; structural molecule activity [GO:0005198]
|
PF00270;PF00271;PF00863;PF00851;PF01577;PF00767;PF08440;PF13608;PF00680;
|
3.30.70.270;3.90.70.150;3.40.50.300;2.40.10.10;
|
Potyviridae genome polyprotein family
|
PTM: [Viral genome-linked protein]: VPg is uridylylated by the polymerase and is covalently attached to the 5'-end of the genomic RNA. This uridylylated form acts as a nucleotide-peptide primer for the polymerase (By similarity). {ECO:0000250|UniProtKB:P09814}.; PTM: [Genome polyprotein]: Potyviral RNA is expressed as two polyproteins which undergo post-translational proteolytic processing. Genome polyprotein is processed by NIa-pro, P1 and HC-pro proteinases resulting in the production of at least ten individual proteins. P3N-PIPO polyprotein is cleaved by P1 and HC-pro proteinases resulting in the production of three individual proteins. The P1 proteinase and the HC-pro cleave only their respective C-termini autocatalytically. 6K1 is essential for proper proteolytic separation of P3 from CI (By similarity). {ECO:0000250}.
|
SUBCELLULAR LOCATION: [6 kDa protein 1]: Host cytoplasmic vesicle. Note=Probably colocalizes with 6K2-induced vesicles associated with host chloroplasts. {ECO:0000250|UniProtKB:P13529}.; SUBCELLULAR LOCATION: [6 kDa protein 2]: Host cytoplasmic vesicle {ECO:0000250|UniProtKB:P09814}. Note=6K-induced vesicles associate with host chloroplasts. {ECO:0000250|UniProtKB:P09814}.; SUBCELLULAR LOCATION: [Viral genome-linked protein]: Host nucleus {ECO:0000250|UniProtKB:P21231}. Note=Binds to host plant eIF4E proteins in the host nucleus. {ECO:0000250|UniProtKB:P21231}.; SUBCELLULAR LOCATION: [Capsid protein]: Virion {ECO:0000305}.
|
CATALYTIC ACTIVITY: Reaction=a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate + RNA(n+1); Xref=Rhea:RHEA:21248, Rhea:RHEA-COMP:14527, Rhea:RHEA-COMP:17342, ChEBI:CHEBI:33019, ChEBI:CHEBI:61557, ChEBI:CHEBI:140395; EC=2.7.7.48; Evidence={ECO:0000255|PROSITE-ProRule:PRU00539}; CATALYTIC ACTIVITY: Reaction=Hydrolyzes glutaminyl bonds, and activity is further restricted by preferences for the amino acids in P6 - P1' that vary with the species of potyvirus, e.g. Glu-Xaa-Xaa-Tyr-Xaa-Gln-|-(Ser or Gly) for the enzyme from tobacco etch virus. The natural substrate is the viral polyprotein, but other proteins and oligopeptides containing the appropriate consensus sequence are also cleaved.; EC=3.4.22.44; Evidence={ECO:0000250|UniProtKB:P04517}; CATALYTIC ACTIVITY: Reaction=Hydrolyzes a Gly-|-Gly bond at its own C-terminus, commonly in the sequence -Tyr-Xaa-Val-Gly-|-Gly, in the processing of the potyviral polyprotein.; EC=3.4.22.45; Evidence={ECO:0000250|UniProtKB:P04517};
| null | null | null | null |
FUNCTION: [Helper component proteinase]: Required for aphid transmission and also has proteolytic activity. Only cleaves a Gly-Gly dipeptide at its own C-terminus. Interacts with virions and aphid stylets. Acts as a suppressor of RNA-mediated gene silencing, also known as post-transcriptional gene silencing (PTGS), a mechanism of plant viral defense that limits the accumulation of viral RNAs. May have RNA-binding activity. {ECO:0000250|UniProtKB:P04517}.; FUNCTION: [Cytoplasmic inclusion protein]: Has helicase activity. It may be involved in replication.; FUNCTION: [6 kDa protein 1]: Indispensable for virus replication. {ECO:0000250|UniProtKB:P13529}.; FUNCTION: [6 kDa protein 2]: Indispensable for virus replication. {ECO:0000250|UniProtKB:P09814}.; FUNCTION: [Viral genome-linked protein]: Mediates the cap-independent, EIF4E-dependent translation of viral genomic RNAs (By similarity). Binds to the cap-binding site of host EIF4E and thus interferes with the host EIF4E-dependent mRNA export and translation (By similarity). VPg-RNA directly binds EIF4E and is a template for transcription (By similarity). Also forms trimeric complexes with EIF4E-EIF4G, which are templates for translation (By similarity). {ECO:0000250|UniProtKB:P18247}.; FUNCTION: [Nuclear inclusion protein A]: Has RNA-binding and proteolytic activities. {ECO:0000250|UniProtKB:P04517}.; FUNCTION: [Nuclear inclusion protein B]: An RNA-dependent RNA polymerase that plays an essential role in the virus replication.; FUNCTION: [Capsid protein]: Involved in aphid transmission, cell-to-cell and systemis movement, encapsidation of the viral RNA and in the regulation of viral RNA amplification. {ECO:0000250|UniProtKB:P04517}.
|
Peanut mottle virus (strain M)
|
O56129
|
CAPSD_PCV2
|
MTYPRRRYRRRRHRPRSHLGQILRRRPWLVHPRHRYRWRRKNGIFNTRLSRTFGYTVKATTVRTPSWAVDMMRFNIDDFVPPGGGTNKISIPFEYYRIRKVKVEFWPCSPITQGDRGVGSTAVILDDNFVTKATALTYDPYVNYSSRHTIPQPFSYHSRYFTPKPVLDSTIDYFQPNNKRTQLWLRLQTSRNVDHVGLGTAFENSIYDQDYNIRVTMYVQFREFNLKDPPLKP
| null | null |
receptor-mediated endocytosis of virus by host cell [GO:0019065]; symbiont-mediated perturbation of host microtubule cytoskeleton [GO:0141028]; viral capsid assembly [GO:0019069]; viral penetration into host nucleus [GO:0075732]; virion attachment to host cell [GO:0019062]
|
host cell [GO:0043657]; host cell cytoplasm [GO:0030430]; host cell endosome [GO:0044174]; host cell nucleus [GO:0042025]; T=1 icosahedral viral capsid [GO:0039615]
|
DNA binding [GO:0003677]
|
PF02443;
|
2.60.120.950;
|
Circoviridae capsid protein family
| null |
SUBCELLULAR LOCATION: Host nucleus {ECO:0000269|PubMed:11414809, ECO:0000269|PubMed:29292065}. Virion {ECO:0000305}.
| null | null | null | null | null |
FUNCTION: Self-assembles to form the virion icosahedral capsid with a T=1 symmetry. This very small capsid (17 - 22 nm in diameter) allows the virus to be very stable in the environment and resistant to some disinfectants, including detergents. Essential for the initial attachment to heparan sulfate moieties and chondroitin sulfate B of the host cell surface proteoglycans. After attachment, the virus is internalized in a clathrin-, caveolae- and dynamin-independent, actin and Rho-GTPase-mediated pathway and traffics to the nucleus. The capsid protein binds and transports the viral genome and Rep across the nuclear envelope (By similarity). {ECO:0000250, ECO:0000269|PubMed:10950986, ECO:0000269|PubMed:16537616, ECO:0000269|PubMed:18952130}.
|
Porcine circovirus 2 (PCV2)
|
O56861
|
ENV_FFV
|
MEQEHVMTLKEWMEWNAHKQLQKLQSTHPELHVDIPEDIPLVPEKVPLKMRMRYRCYTLCATSTRIMFWILFFLLCFSIVTLSTIISILRYQWKEAITHPGPVLSWQVTNSHVTMGGNTSSSSRRRRDIQYHKLPVEVNISGIPQGLFFAPQPKPIFHKERTLGLSQVILIDSDTITQGHIKQQKAYLVSTINEEMEQLQKTVLPFDLPIKDPLTQKEYIEKRCFQKYGHCYVIAFNGNKVWPSQDLIQDQCPLPPRFGNNLKYRNHTIWKYYIPLPFKVSSNWTRVESYGNIRIGSFKVPDEFRQNATHGIFCSDALYSNWYPRDLPSSVQQSFAQAYITKVLMKRKKQPTLRDIAFPKELSPVGSGMLFRPINPYDICNMPRAVLLLNKTYYTFSLWEGDCGYYQHNLTLHPACKNFNRTRQDHPYACRFWRNKYDSESVQCYNNDMCYYRPLYDGTENTEDWGWLAYTDSFPSPICIEEKRIWKKNYTLSSVLAECVNQAMEYGIDEVLSKLDLIFGNLTHQSADEAFIPVNNFTWPRYEKQNKQQKTSCERKKGRRQRRSVSTENLRRIQEAGLGLANAITTVAKISDLNDQKLAKGVHLLRDHVVTLMEANLDDIVSLGEGIQIEHIHNHLTSLKLLTLENRIDWRFINDSWIQEELGVSDNIMKVIRKTARCIPYNVKQTRNLNTSTAWEIYLYYEIIIPTTIYTQNWNIKNLGHLVRNAGYLSKVWIQQPFEVLNQECGTNIYLHMEECVDQDYIICEEVMELPPCGNGTGSDCPVLTKPLTDEYLEIEPLKNGSYLVLSSTTDCGIPAYVPVVITVNDTISCFDKEFKRPLKQELKVTKYAPSVPQLELRVPRLTSLIAKIKGIQIEITSSWETIKEQVARAKAELLRLDLHEGDYPEWLQLLGEATKDVWPTISNFVSGIGNFIKDTAGGIFGTAFSFLGYVKPVLLGFVIIFCIILIIKIIGWLQNTRKKDQ
| null | null | null |
host cell endoplasmic reticulum membrane [GO:0044167]; membrane [GO:0016020]; viral envelope [GO:0019031]; virion membrane [GO:0055036]
| null |
PF03408;
| null | null |
PTM: Envelope glycoproteins are synthesized as an inactive precursor that is processed by host furin or a furin-like protease to yield a functional hetero-oligomeric complex. A 9 kDa protein corresponding to the N-terminus of the leader peptide may arise through low efficient cleavage by host signal peptidase. {ECO:0000269|PubMed:15564468}.; PTM: The transmembrane protein and the surface protein are N-glycosylated. {ECO:0000250}.
|
SUBCELLULAR LOCATION: [Envelope glycoprotein gp130]: Host endoplasmic reticulum membrane. Note=The polyprotein has a highly unusual biosynthesis for a retroviral glycoprotein. It is translated as a full-length precursor protein into the rough endoplasmic reticulum and initially has a type III protein configuration with both its N and C-termini located intracytoplasmically.; SUBCELLULAR LOCATION: [Leader peptide]: Virion membrane {ECO:0000305}; Single-pass type II membrane protein {ECO:0000305}. Host endoplasmic reticulum membrane {ECO:0000305}; Single-pass type II membrane protein {ECO:0000305}. Note=Its N-terminus is located inside the viral particle. {ECO:0000250}.; SUBCELLULAR LOCATION: [Transmembrane protein]: Virion membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. Host endoplasmic reticulum membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}.; SUBCELLULAR LOCATION: [Surface protein]: Virion membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Host endoplasmic reticulum membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Note=The surface protein is not anchored to the viral envelope, but associates with the extravirion surface through its binding to TM. {ECO:0000250}.
| null | null | null | null | null |
FUNCTION: The surface protein (SU) attaches the virus to the host cell by binding to the cell receptor. This interaction triggers the refolding of transmembrane protein (TM) and is thought to activate its fusogenic potential by unmasking its fusion peptide (By similarity). {ECO:0000250}.; FUNCTION: The transmembrane protein (TM) acts as a class I viral fusion protein. Under the current model, the protein has at least 3 conformational states: pre-fusion native state, pre-hairpin intermediate state, and post-fusion hairpin state. During viral and target cell membrane fusion, the coiled coil regions (heptad repeats) assume a trimer-of-hairpins structure, positioning the fusion peptide in close proximity to the C-terminal region of the ectodomain. The formation of this structure appears to drive apposition and subsequent fusion of viral and target cell membranes. Membranes fusion leads to delivery of the nucleocapsid into the cytoplasm (By similarity). {ECO:0000250}.; FUNCTION: The leader peptide is a component of released, infectious virions and is required for particle budding.
|
Feline foamy virus (FFV) (Feline syncytial virus)
|
O57209
|
MCEL_VACCA
|
MDANIVSSSTIATYIDALAKNASELEQRSTAYEINNELELVFIKPPLITLTNVVNISTIQESFIRFTVTNKEGVKIRTKIPLSKVHGLDVKNVQLVDAIDNIVWEKKSLVTENRLHKECLLRLSTEERHIFLDYKKYGSSIRLELVNLIQAKTKNFTIDFKLKYFLGSGAQSKSSLLHAINHPKSRPNTSLEIEFTPRDNEKVPYDELIKELTTLSRHIFMASPENVILSPPINAPIKTFMLPKQDIVGLDLENLYAVTKTDGIPITIRVTSKGLYCYFTHLGYIIRYPVKRIIDSEVVVFGEAVKDKNWTVYLIKLIEPVNAINDRLEESKYVESKLVDICDRIVFKSKKYEGPFTTTSEVVDMLSTYLPKQPEGVILFYSKGPKSNIDFKIKKENTIDQTANVVFRYMSSEPIIFGESSIFVEYKKFSNDKGFPKEYGSGKIVLYNGVNYLNNIYCLEYINTHNEVGIKSVVVPIKFIAEFLVNGEILKPRIDKTMKYINSEDYYGNQHNIIVEHLRDQSIKIGDIFNEDKLSDVGHQYANNDKFRLNPEVSYFTNKRTRGPLGILSNYVKTLLISMYCSKTFLDDSNKRKVLAIDFGNGADLEKYFYGEIALLVATDPDADAIARGNERYNKLNSGIKTKYYKFDYIQETIRSDTFVSSVREVFYFGKFNIIDWQFAIHYSFHPRHYATVMNNLSELTASGGKVLITTMDGDKLSKLTDKKTFIIHKNLPSSENYMSVEKIADDRIVVYNPSTMSTPMTEYIIKKNDIVRVFNEYGFVLVDNVDFATIIERSKKFINGASTMEDRPSTKNFFELNRGAIKCEGLDVEDLLSYYVVYVFSKR
|
2.1.1.56; 2.7.7.50; 3.6.1.74
|
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:P04298};
| null |
virion component [GO:0044423]
|
GTP binding [GO:0005525]; inorganic triphosphate phosphatase activity [GO:0050355]; metal ion binding [GO:0046872]; mRNA 5'-cap (guanine-N7-)-methyltransferase activity [GO:0004482]; mRNA 5'-phosphatase activity [GO:0140818]; mRNA guanylyltransferase activity [GO:0004484]; polynucleotide 5'-phosphatase activity [GO:0004651]; RNA binding [GO:0003723]
|
PF21004;PF21005;PF10640;PF03291;
|
2.40.50.830;3.20.100.20;3.30.470.140;3.40.50.150;
|
DsDNA virus mRNA guanylyltransferase family; Class I-like SAM-binding methyltransferase superfamily, mRNA cap 0 methyltransferase family
| null |
SUBCELLULAR LOCATION: Virion {ECO:0000250|UniProtKB:P04298}. Note=All the enzymes and other proteins required to synthesize early mRNAs are packaged within the virion core along with the DNA genome. {ECO:0000250|UniProtKB:P04298}.
|
CATALYTIC ACTIVITY: Reaction=a 5'-end triphospho-ribonucleoside in mRNA + H2O = a 5'-end diphospho-ribonucleoside in mRNA + H(+) + phosphate; Xref=Rhea:RHEA:67004, Rhea:RHEA-COMP:17164, Rhea:RHEA-COMP:17165, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474, ChEBI:CHEBI:167616, ChEBI:CHEBI:167618; EC=3.6.1.74; Evidence={ECO:0000250|UniProtKB:P04298}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67005; Evidence={ECO:0000250|UniProtKB:P04298}; CATALYTIC ACTIVITY: Reaction=a 5'-end diphospho-ribonucleoside in mRNA + GTP + H(+) = a 5'-end (5'-triphosphoguanosine)-ribonucleoside in mRNA + diphosphate; Xref=Rhea:RHEA:67012, Rhea:RHEA-COMP:17165, Rhea:RHEA-COMP:17166, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019, ChEBI:CHEBI:37565, ChEBI:CHEBI:167616, ChEBI:CHEBI:167617; EC=2.7.7.50; Evidence={ECO:0000250|UniProtKB:P04298}; CATALYTIC ACTIVITY: Reaction=a 5'-end (5'-triphosphoguanosine)-ribonucleoside in mRNA + S-adenosyl-L-methionine = a 5'-end (N(7)-methyl 5'-triphosphoguanosine)-ribonucleoside in mRNA + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:67008, Rhea:RHEA-COMP:17166, Rhea:RHEA-COMP:17167, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:156461, ChEBI:CHEBI:167617; EC=2.1.1.56; Evidence={ECO:0000250|UniProtKB:P04298};
| null | null | null | null |
FUNCTION: Catalytic subunit of the mRNA capping enzyme which catalyzes three enzymatic reactions: the 5' triphosphate end of the pre-mRNA is hydrolyzed to a diphosphate by RNA 5' triphosphatase; the diphosphate RNA end is capped with GMP by RNA guanylyltransferase and the GpppN cap is methylated by RNA (guanine-N7) methyltransferase. Heterodimeric mRNA capping enzyme catalyzes the linkage of a N7-methyl-guanosine moiety to the first transcribed nucleotide (cap 0 structure), whereas the methyltransferase OPG102 is responsible for a second methylation at the 2'-O position of the ribose (cap 1 structure). Also involved in early viral gene transcription termination and intermediate viral gene transcription initiation. Early gene transcription termination requires the termination factor VTF, the DNA-dependent ATPase NPH-I/OPG123 and the RAP94/OPG109 subunit of the viral RNA polymerase, as well as the presence of a specific termination motif. Binds, together with RAP94/OPG109, to the termination motif 5'-UUUUUNU-3' in the nascent early mRNA. {ECO:0000250|UniProtKB:P04298}.
|
Vaccinia virus (strain Ankara) (VACV)
|
O57311
|
ZIC3_XENLA
|
MTMLLDGGPQFPTLGVGGFGTARHHEMSNRDAGMGLNPFTEPSHAAAFKLSPASHDLSSSQSSAFTPQASGYASSLGHHAGQVPSYGGAAFNSTRDFLFRNRNSGIADSSSAGSQHGLFANHGPPGIGEPPGHLIFPGLHEQSSSHTSSNGHVVNGQMHLGLRGDIFGRPDPYRAVPSPRTDHYAAAQFHNYNHMNMSMNVAAHHGQGAFFRYMRQPIKQELSCKWLEESTMNHPQKTCDRTFSSMHELVTHMTMEHVGGPEQNNHICYWEECPRGGKSFKAKYKLVNHIRVHTGEKPFPCPFPGCGKIFARSENLKIHKRTHTGEKPFKCEFEGCDRRFANSSDRKKHMHVHTSDKPYICKVCDKSYTHPSSLRKHMKVHESQGSDSSPAASSGYESATPPAMVSANSEEPSKNSSATHQTNNNSHNTGLLPPNFNEWYV
| null | null |
determination of left/right symmetry [GO:0007368]; embryonic axis specification [GO:0000578]; nervous system development [GO:0007399]; neural crest cell fate commitment [GO:0014034]; positive regulation of DNA-templated transcription [GO:0045893]; positive regulation of transcription by RNA polymerase II [GO:0045944]
|
cytoplasm [GO:0005737]; nucleus [GO:0005634]
|
DNA-binding transcription factor activity [GO:0003700]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; metal ion binding [GO:0046872]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]; sequence-specific DNA binding [GO:0043565]
|
PF00096;PF18366;
|
3.30.160.60;
|
GLI C2H2-type zinc-finger protein family
| null |
SUBCELLULAR LOCATION: Nucleus. Cytoplasm {ECO:0000250}.
| null | null | null | null | null |
FUNCTION: Probably acts as a transcriptional activator. May bind to the minimal GLI-consensus sequence 5'-GGGTGGTC-3'. Can determine the ectodermal cell fate and promote the earliest step of neural and neural crest development. Involved in establishing left-right asymmetry in the embryo. {ECO:0000269|PubMed:11044394, ECO:0000269|PubMed:11869292, ECO:0000269|PubMed:9342348}.
|
Xenopus laevis (African clawed frog)
|
O57321
|
EAA1_AMBTI
|
MTKSNGEDPRAGSRMERFQQGVRQRTLLAKKKVQNITKDDVKGFLKRNGFVLFTVIAVVVGSILGFSVRSYHMTFRELKYFSFPGELLMRMLQMLVLPLIVSSLVTGMAALDSKASGKMGLRAVVYYMTTTVIAVFIGIVIVIIVHPGKGTKEHMHREGKIEPVTAADAFLDLIRNMFPPNMVEACFKQFKTSYEKKIFKVTMPANETAVMTSVLNNVSEAMETLTKMREEMIPVPGAVNGVNALGLVVFSMCFGLVIGNMKEQGKALKDFFDSLNEAIMRLVAVIMWYAPIGILFLIAGKIAEMEDMGVVGGQLGMYTVTVIIGLLIHAVIVLPLLYFAVTRKNPWVFIGGILQALITALGTSSSSATLPITFKCLEENNKVDKRVTRFVLPVGATINMDGTALYEALAAIFIAQVNNYDLNFGQILTISITATAASIGAAGIPQAGLVTMVIVLTSVGLPTDDITLIIAVDWFLDRLRTTTNVLGDSLGAGIVEHLSRHELQSGDAEMGNSVIEENEMKKPYQLVSQENELEKPIDSETKM
| null | null |
chloride transmembrane transport [GO:1902476]; D-aspartate import across plasma membrane [GO:0070779]; L-aspartate import across plasma membrane [GO:0140009]; L-glutamate import across plasma membrane [GO:0098712]; potassium ion transmembrane transport [GO:0071805]
|
plasma membrane [GO:0005886]
|
glutamate:sodium symporter activity [GO:0015501]; high-affinity L-glutamate transmembrane transporter activity [GO:0005314]; metal ion binding [GO:0046872]; neutral L-amino acid transmembrane transporter activity [GO:0015175]
|
PF00375;
|
1.10.3860.10;
|
Dicarboxylate/amino acid:cation symporter (DAACS) (TC 2.A.23) family
| null |
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:17008380, ECO:0000269|PubMed:9425012}; Multi-pass membrane protein.
|
CATALYTIC ACTIVITY: Reaction=H(+)(out) + K(+)(in) + L-glutamate(out) + 3 Na(+)(out) = H(+)(in) + K(+)(out) + L-glutamate(in) + 3 Na(+)(in); Xref=Rhea:RHEA:70699, ChEBI:CHEBI:15378, ChEBI:CHEBI:29101, ChEBI:CHEBI:29103, ChEBI:CHEBI:29985; Evidence={ECO:0000250|UniProtKB:P43003}; CATALYTIC ACTIVITY: Reaction=H(+)(out) + K(+)(in) + L-aspartate(out) + 3 Na(+)(out) = H(+)(in) + K(+)(out) + L-aspartate(in) + 3 Na(+)(in); Xref=Rhea:RHEA:70851, ChEBI:CHEBI:15378, ChEBI:CHEBI:29101, ChEBI:CHEBI:29103, ChEBI:CHEBI:29991; Evidence={ECO:0000250|UniProtKB:P43003}; CATALYTIC ACTIVITY: Reaction=D-aspartate(out) + H(+)(out) + K(+)(in) + 3 Na(+)(out) = D-aspartate(in) + H(+)(in) + K(+)(out) + 3 Na(+)(in); Xref=Rhea:RHEA:71379, ChEBI:CHEBI:15378, ChEBI:CHEBI:29101, ChEBI:CHEBI:29103, ChEBI:CHEBI:29990; Evidence={ECO:0000250|UniProtKB:P43003};
| null | null | null | null |
FUNCTION: Sodium-dependent, high-affinity amino acid transporter that mediates the uptake of L-glutamate and also L-aspartate and D-aspartate (PubMed:17008380, PubMed:9425012). Functions as a symporter that transports one amino acid molecule together with two or three Na(+) ions and one proton, in parallel with the counter-transport of one K(+) ion (PubMed:17008380). Plays a redundant role in the rapid removal of released glutamate from the synaptic cleft, which is essential for terminating the postsynaptic action of glutamate (By similarity). {ECO:0000250|UniProtKB:P56564, ECO:0000269|PubMed:17008380, ECO:0000269|PubMed:9425012}.
|
Ambystoma tigrinum (Eastern tiger salamander)
|
O57341
|
FGF8A_DANRE
|
MRLIPSRLSYLFLHLFAFCYYAQVTIQSPPNFTQHVSEQSKVTDRVSRRLIRTYQLYSRTSGKHVQVLANKKINAMAEDGDVHAKLIVETDTFGSRVRIKGAETGFYICMNRRGKLIGKKNGLGKDCIFTEIVLENNYTALQNVKYEGWYMAFTRKGRPRKGSKTRQHQREVHFMKRLPKGHQIAEHRPFDFINYPFNRRTKRTRYSGER
| null | null |
animal organ morphogenesis [GO:0009887]; anterior/posterior pattern specification [GO:0009952]; brain development [GO:0007420]; cardiac ventricle morphogenesis [GO:0003208]; cardioblast differentiation [GO:0010002]; cartilage development [GO:0051216]; cell fate specification [GO:0001708]; cerebellum development [GO:0021549]; cerebellum formation [GO:0021588]; cilium assembly [GO:0060271]; closure of optic fissure [GO:0061386]; determination of dorsal identity [GO:0048263]; determination of left/right symmetry [GO:0007368]; dorsal/ventral pattern formation [GO:0009953]; ectodermal placode formation [GO:0060788]; embryonic camera-type eye development [GO:0031076]; embryonic heart tube development [GO:0035050]; embryonic neurocranium morphogenesis [GO:0048702]; embryonic pattern specification [GO:0009880]; embryonic retina morphogenesis in camera-type eye [GO:0060059]; endoderm development [GO:0007492]; fibroblast growth factor receptor signaling pathway [GO:0008543]; heart morphogenesis [GO:0003007]; hindbrain development [GO:0030902]; inner ear development [GO:0048839]; Kupffer's vesicle development [GO:0070121]; limb morphogenesis [GO:0035108]; locus ceruleus development [GO:0021703]; mesoderm development [GO:0007498]; midbrain development [GO:0030901]; midbrain-hindbrain boundary development [GO:0030917]; midbrain-hindbrain boundary morphogenesis [GO:0021555]; negative regulation of endodermal cell fate specification [GO:0042664]; neuron differentiation [GO:0030182]; neuron fate specification [GO:0048665]; notochord development [GO:0030903]; oligodendrocyte differentiation [GO:0048709]; otic placode formation [GO:0043049]; otic vesicle development [GO:0071599]; otic vesicle formation [GO:0030916]; paraxial mesoderm development [GO:0048339]; peripheral nervous system development [GO:0007422]; pharyngeal system development [GO:0060037]; positive regulation of cell migration [GO:0030335]; positive regulation of cell population proliferation [GO:0008284]; positive regulation of gene expression [GO:0010628]; positive regulation of protein phosphorylation [GO:0001934]; positive regulation of somitomeric trunk muscle development [GO:0014709]; positive regulation of Wnt signaling pathway [GO:0030177]; regulation of bone remodeling [GO:0046850]; regulation of cell migration [GO:0030334]; retina development in camera-type eye [GO:0060041]; rhombomere 5 development [GO:0021571]; rhombomere 6 development [GO:0021572]; skeletal system morphogenesis [GO:0048705]; somite development [GO:0061053]; somitogenesis [GO:0001756]; striated muscle cell differentiation [GO:0051146]; taste bud formation [GO:0061195]; thyroid gland development [GO:0030878]; ventricular cardiac muscle cell differentiation [GO:0055012]
|
cytoplasm [GO:0005737]; extracellular space [GO:0005615]; lysosome [GO:0005764]
|
growth factor activity [GO:0008083]; type 1 fibroblast growth factor receptor binding [GO:0005105]; type 2 fibroblast growth factor receptor binding [GO:0005111]
|
PF00167;
|
2.80.10.50;
|
Heparin-binding growth factors family
| null |
SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P55075}.
| null | null | null | null | null |
FUNCTION: Plays an important role in the regulation of embryonic development, cell proliferation, cell differentiation and cell migration (By similarity). Required for Kupffer's vesicle ciliogenesis (PubMed:19164561). {ECO:0000250|UniProtKB:P55075, ECO:0000269|PubMed:19164561}.
|
Danio rerio (Zebrafish) (Brachydanio rerio)
|
O57342
|
MAFA_COTJA
|
MASELAMTAELPTSPLAIEYVNDFDLMKFEVKKEPAEAERLCHRLPAGSLSSTPLSTPCSSVPSSPSFCAPSPGGQPSAGPTAAPLGSKPQLEELYWMSGYQHHLNPEALNLTPEDAVEALIGAPHHHHHHHQSYESFRPQPFGGEELPPAAHHHNAHHHHHHHHLRLEERFSDDQLVSMSVRELNRQLRGFSKEEVIRLKQKRRTLKNRGYAQSCRYKRVQQRHILENEKCQLQSQVEQLKQEVSRLAKERDLYKEKYEKLAARGFPRETSPPAAPKTTAADFFM
| null | null |
insulin secretion [GO:0030073]; response to glucose [GO:0009749]
|
nucleus [GO:0005634]
|
DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]
|
PF03131;PF08383;
|
1.20.5.170;
|
BZIP family, Maf subfamily
|
PTM: Phosphorylation at Ser-14 and Ser-65 is required for transcription regulation activity and lens differentiation in neuroretina cells (PubMed:11416124). Phosphorylation at Ser-65 may be required for efficient phosphorylation at Thr-53, Thr57 and Ser-61 by GSK3 (PubMed:18042454). {ECO:0000269|PubMed:11416124, ECO:0000269|PubMed:18042454}.; PTM: Ubiquitinated and degraded by the proteasome, following phosphorylation by GSK3. {ECO:0000269|PubMed:18042454}.
|
SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00978, ECO:0000269|PubMed:11416124}.
| null | null | null | null | null |
FUNCTION: Transcription factor involved in transcription regulation during lens development, including that of crystallin genes (PubMed:15963504, PubMed:18042454, PubMed:9674710). Binds to CRE-type MARE 5'-TGCTGACGTCAGCA-3' and TRE-type MARE 5'-TGCTGACTCAGCA-3' DNA sequences (PubMed:9674710). {ECO:0000269|PubMed:15963504, ECO:0000269|PubMed:18042454, ECO:0000269|PubMed:9674710}.
|
Coturnix japonica (Japanese quail) (Coturnix coturnix japonica)
|
O57383
|
DPOLB_XENLA
|
MSKRKAPQESPNEGITDFLVELANYERNVNRAIHKYNAYRKAASVIAKYPTKIKSGTEAKKLDGVGAKIAEKIDEFLATGKLRKLEKIRQDDTSSSINFLTRVTGIGPAAARKFFDEGIKTLDDLRNNEHKLNHHQKIGLKHFDDFEKRIPRKEMLQMQEIILDKVNNLDPEYIATVCGSFRRGAESSGDMDILLTHPDFTSESAKQPRLLHQVVQCLEDCNFITDTLVKGDTKFMGVCQLPCESDQDYPYRRIDIRLIPKDQYYCGVLYFTGSDIFNKNMRTHALEKGFTLNEYTLRPLGVTGIAGEPLPIDSEKDIFDYIQWKYREPKDRSE
|
2.7.7.7; 4.2.99.-; 4.2.99.18
|
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:P06746}; Note=Binds 2 magnesium ions per subunit. {ECO:0000250|UniProtKB:P06746};
|
base-excision repair [GO:0006284]; DNA damage response [GO:0006974]; DNA replication [GO:0006260]; double-strand break repair via nonhomologous end joining [GO:0006303]
|
cytoplasm [GO:0005737]; nucleus [GO:0005634]
|
class I DNA-(apurinic or apyrimidinic site) endonuclease activity [GO:0140078]; DNA binding [GO:0003677]; DNA-directed DNA polymerase activity [GO:0003887]; metal ion binding [GO:0046872]
|
PF14792;PF14791;PF10391;PF14716;
|
1.10.150.20;3.30.460.10;1.10.150.110;3.30.210.10;
|
DNA polymerase type-X family
|
PTM: Methylation by PRMT6 stimulates the polymerase activity by enhancing DNA binding and processivity. {ECO:0000250}.; PTM: Ubiquitinated: monoubiquitinated by huwe1/arf-bp1. Monoubiquitinated protein is then the target of stub1/chip, which catalyzes polyubiquitination from monoubiquitin, leading to degradation by the proteasome. usp47 mediates the deubiquitination of monoubiquitinated protein, preventing polyubiquitination by STUB1/CHIP and its subsequent degradation (By similarity). {ECO:0000250}.
|
SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P06746}. Cytoplasm {ECO:0000250|UniProtKB:P06746}. Note=Cytoplasmic in normal conditions. Translocates to the nucleus following DNA damage. {ECO:0000250|UniProtKB:P06746}.
|
CATALYTIC ACTIVITY: Reaction=a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1); Xref=Rhea:RHEA:22508, Rhea:RHEA-COMP:17339, Rhea:RHEA-COMP:17340, ChEBI:CHEBI:33019, ChEBI:CHEBI:61560, ChEBI:CHEBI:173112; EC=2.7.7.7; Evidence={ECO:0000250|UniProtKB:P06746}; CATALYTIC ACTIVITY: Reaction=a 5'-end 2'-deoxyribose-2'-deoxyribonucleotide-DNA = (2E,4S)-4-hydroxypenten-2-al-5-phosphate + a 5'-end 5'-phospho-2'-deoxyribonucleoside-DNA + H(+); Xref=Rhea:RHEA:76255, Rhea:RHEA-COMP:13180, Rhea:RHEA-COMP:18657, ChEBI:CHEBI:15378, ChEBI:CHEBI:136412, ChEBI:CHEBI:195194, ChEBI:CHEBI:195195; Evidence={ECO:0000250|UniProtKB:P06746}; CATALYTIC ACTIVITY: Reaction=2'-deoxyribonucleotide-(2'-deoxyribose 5'-phosphate)-2'-deoxyribonucleotide-DNA = a 3'-end 2'-deoxyribonucleotide-(2,3-dehydro-2,3-deoxyribose 5'-phosphate)-DNA + a 5'-end 5'-phospho-2'-deoxyribonucleoside-DNA + H(+); Xref=Rhea:RHEA:66592, Rhea:RHEA-COMP:13180, Rhea:RHEA-COMP:16897, Rhea:RHEA-COMP:17067, ChEBI:CHEBI:15378, ChEBI:CHEBI:136412, ChEBI:CHEBI:157695, ChEBI:CHEBI:167181; EC=4.2.99.18; Evidence={ECO:0000250|UniProtKB:P06746};
| null | null | null | null |
FUNCTION: Repair polymerase that plays a key role in base-excision repair. During this process, the damaged base is excised by specific DNA glycosylases, the DNA backbone is nicked at the abasic site by an apurinic/apyrimidic (AP) endonuclease, and POLB removes 5'-deoxyribose-phosphate from the preincised AP site acting as a 5'-deoxyribose-phosphate lyase (5'-dRP lyase); through its DNA polymerase activity, it adds one nucleotide to the 3' end of the arising single-nucleotide gap. Conducts 'gap-filling' DNA synthesis in a stepwise distributive fashion rather than in a processive fashion as for other DNA polymerases. It is also able to cleave sugar-phosphate bonds 3' to an intact AP site, acting as an AP lyase. {ECO:0000250|UniProtKB:P06746}.
|
Xenopus laevis (African clawed frog)
|
O57385
|
PA2H_DEIAC
|
MRALWIVAVLLVGVEGSLFELGKMIWQETGKNPVKNYGLYGCNCGVGGRGEPLDATDRCCFVHKCCYKKLTDCDSKKDRYSYKWKNKAIVCGKNQPCMQEMCECDKAFAICLRENLDTYNKSFRYHLKPSCKKTSEQC
| null | null |
arachidonic acid secretion [GO:0050482]; lipid catabolic process [GO:0016042]; negative regulation of T cell proliferation [GO:0042130]; phospholipid metabolic process [GO:0006644]
|
extracellular region [GO:0005576]
|
calcium ion binding [GO:0005509]; calcium-dependent phospholipase A2 activity [GO:0047498]; phospholipid binding [GO:0005543]; toxin activity [GO:0090729]
|
PF00068;
|
1.20.90.10;
|
Phospholipase A2 family, Group II subfamily, K49 sub-subfamily
| null |
SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:10930841}.
| null | null | null | null | null |
FUNCTION: Snake venom phospholipase A2 homolog that lacks enzymatic activity (PubMed:10930841). Is myotoxic (By similarity). Has a strong indirect hemolytic activity and anticoagulant activity (PubMed:10930841). A model of myotoxic mechanism has been proposed: an apo Lys49-PLA2 is activated by the entrance of a hydrophobic molecule (e.g. fatty acid) at the hydrophobic channel of the protein leading to a reorientation of a monomer (By similarity). This reorientation causes a transition between 'inactive' to 'active' states, causing alignment of C-terminal and membrane-docking sites (MDoS) side-by-side and putting the membrane-disruption sites (MDiS) in the same plane, exposed to solvent and in a symmetric position for both monomers (By similarity). The MDoS region stabilizes the toxin on membrane by the interaction of charged residues with phospholipid head groups (By similarity). Subsequently, the MDiS region destabilizes the membrane with penetration of hydrophobic residues (By similarity). This insertion causes a disorganization of the membrane, allowing an uncontrolled influx of ions (i.e. calcium and sodium), and eventually triggering irreversible intracellular alterations and cell death (By similarity). {ECO:0000250|UniProtKB:I6L8L6, ECO:0000269|PubMed:10930841}.
|
Deinagkistrodon acutus (Hundred-pace snake) (Agkistrodon acutus)
|
O57406
|
CEL1A_XENLA
|
MNGTMDHPDHPDPDSIKMFVGQVPRSWSEKELRELFEQYGAVYEINVLRDRSQNPPQSKGCCFITFYTRKAALEAQNALHNMKVLPGMHHPIQMKPADSEKNNAVEDRKLFIGMVSKNCNENDIRAMFSPFGQIEECRILRGPDGMSRGCAFVTFTTRSMAQMAIKSMHQAQTMEGCSSPIVVKFADTQKDKEQKRMTQQLQQQMQQLNAASMWGNLTGLNSLAPQYLALLQQTASSGNLNSLSGLHPMGAEYGTGMTSGLNAIQLQNLAALAAAASAAQNTPSAGAALTSSSSPLSILTSSGSSPSSNNSSINTMASLGALQTLAGATAGLNVNSLAGMAAFNGGLGSSLSNGTGSTMEALSQAYSGIQQYAAAALPSLYNQSLLSQQGLGAAGSQKEGPEGANLFIYHLPQEFGDQDLLQMFMPFGNVVSSKVFIDKQTNLSKCFGFVSYDNPVSAQAAIQSMNGFQIGMKRLKVQLKRSKNDSKPY
| null | null |
mRNA splice site recognition [GO:0006376]; regulation of alternative mRNA splicing, via spliceosome [GO:0000381]
|
cytoplasm [GO:0005737]; nucleus [GO:0005634]; ribonucleoprotein complex [GO:1990904]
|
mRNA 3'-UTR binding [GO:0003730]
|
PF00076;
|
3.30.70.330;
|
CELF/BRUNOL family
|
PTM: Phosphorylated during oocyte maturation and dephosphorylated following egg activation. Dephosphorylation is calcium dependent and correlates with the increase in the activity of EDEN-dependent deadenylation. {ECO:0000269|PubMed:12746489}.
|
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:9427761}. Cytoplasm {ECO:0000269|PubMed:9427761}.
| null | null | null | null | null |
FUNCTION: RNA-binding protein implicated in the regulation of several post-transcriptional events. May be involved in pre-mRNA alternative splicing, mRNA translation activation and stability (By similarity). Mediates the rapid and sequence-specific cytoplasmic deadenylation of EDEN-containing maternal mRNAs following fertilization. Binds to AU-rich sequences (AREs) of jun mRNA. Binds to the embryonic deadenylation element (EDEN) motif localized in the 3'-UTR of maternal mRNAs. Binds to RNA containing several repeats of the consensus sequence 5'-UGU-3'. EDEN-dependent deadenylation is enhanced by the presence of an additional cis element composed of three AUU repeats. {ECO:0000250, ECO:0000269|PubMed:11707455, ECO:0000269|PubMed:12799066, ECO:0000269|PubMed:16836486, ECO:0000269|PubMed:16938098, ECO:0000269|PubMed:9819376}.
|
Xenopus laevis (African clawed frog)
|
O57413
|
VM2T3_PROMU
|
MIEVLLVTICLAVFPYQGSSIILESGNVNDYEVVYPRKVSALPKGAVQPKYEDAMQYEFKVNGEAVVLHLEKNKGLFSEDYSETHYSPDGREITTYPSVEDHCYYHGRIHNDADSTASISACDGLKGYFKLQGETYPIEPLELSDSEAHAVFKYENVEKEDEAPKMCGVTQNWESDESIKKASQLYLTPEQQRFPQRYIKLAIVVDHGMYTKYSSNFKKIRKRVHQMVSNINEMCRPLNIAITLALLDVWSEKDFITVQADAPTTAGLFGDWRERVLLKKKNHDHAQLLTDTNFARNTIGWAYVGRMCDEKYSVAVVKDHSSKVFMVAVTMTHELGHNLGMEHDDKDKCKCDTCIMSAVISDKQSKLFSDCSKDYYQTFLTNDNPQCILNAPLRTDTVSTPVSGNEFLEAGEECDCGSPENPCCDAATCKLRPGAQCAEGLCCDQCRFKKKRTICRRARGDNPDDRCTGQSADCPRNGLYG
|
3.4.24.-
|
COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000305|PubMed:12071970, ECO:0000305|PubMed:12077431}; Note=Binds 1 zinc ion per subunit. {ECO:0000269|PubMed:12071970, ECO:0000269|PubMed:12077431};
|
proteolysis [GO:0006508]
|
extracellular region [GO:0005576]; plasma membrane [GO:0005886]
|
metal ion binding [GO:0046872]; metalloendopeptidase activity [GO:0004222]; toxin activity [GO:0090729]
|
PF00200;PF01562;PF01421;
|
3.40.390.10;4.10.70.10;
|
Venom metalloproteinase (M12B) family, P-II subfamily, P-IIa sub-subfamily
|
PTM: The N-terminus is blocked. {ECO:0000269|PubMed:7488093}.
|
SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:7488093, ECO:0000269|PubMed:8193588}.
| null | null | null | null | null |
FUNCTION: [Snake venom metalloproteinase TM-3]: Potent fibrinogenolytic protease which cleaves mainly the Aalpha chain of fibrinogen (FGA) and slightly the Bbeta (FGB) and the gamma (FGG) chains (PubMed:7488093, PubMed:8193588). May possess hemorrhagic activity (PubMed:7488093). Compared to other SVMP, the substrate-binding pocket is relatively shallow (PubMed:12077431). Is less susceptible to tripeptide inhibitors than TM-1 (AC U3KRG1) and TM-2 (PubMed:9703966). {ECO:0000269|PubMed:12077431, ECO:0000269|PubMed:7488093, ECO:0000269|PubMed:8193588, ECO:0000269|PubMed:9703966}.; FUNCTION: [Disintegrin trimucrin]: Inhibits platelet aggregation induced by ADP, thrombin, platelet-activating factor and collagen. Acts by inhibiting fibrinogen interaction with platelet receptors GPIIb/GPIIIa (ITGA2B/ITGB3). {ECO:0000250|UniProtKB:P17349}.
|
Protobothrops mucrosquamatus (Taiwan habu) (Trimeresurus mucrosquamatus)
|
O57437
|
DAZLA_XENLA
|
MSGKEESSNYAATAEEEAVNQGFVLPEGEIMPNTVFVGGIDITMDEIEIRDFFTRFGNVKEVKIITDRTGVSKGYGFISFSDEVDVQKIVKSQISFHGKKLKLGPAIRKICTYVQPRPVVLSHPTPFHHAWNNQNADSYIQHSPIVSPITQYVQACPYPSSPPMAIQQIPVGCQQPGYFQVSPQWPADQRSYMFPTPAFTFNYHCCDMDPNGGEPIPREYPIDQTVSASGANPQKRYVEMSTQTIVSCLFDPANKFHSFVSQEDYLKDNRVHHLRRRESVIKRVSK
| null | null |
3'-UTR-mediated mRNA stabilization [GO:0070935]; germ cell development [GO:0007281]; germ cell migration [GO:0008354]; oogenesis [GO:0048477]; positive regulation of translational initiation [GO:0045948]; spermatogenesis [GO:0007283]
|
cytoplasm [GO:0005737]; mitochondrial cloud [GO:0032019]; pole plasm [GO:0045495]
|
mRNA 3'-UTR binding [GO:0003730]; RNA binding [GO:0003723]; translation activator activity [GO:0008494]
|
PF00076;
|
3.30.70.330;
|
RRM DAZ family
| null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10842082, ECO:0000269|PubMed:11784096, ECO:0000269|PubMed:9486791}.
| null | null | null | null | null |
FUNCTION: RNA-binding protein that is required for primordial germ cell (PGC) differentiation and indirectly necessary for the migration of PGCs through the endoderm. May promote meiotic cell division during spermatogenesis. Shows a preference for G- and U-rich RNAs and probably binds the 3'-UTR of target mRNAs. Stimulates the initiation of translation of mRNAs through the recruitment of poly(A)-binding proteins (PABPs). {ECO:0000269|PubMed:10631166, ECO:0000269|PubMed:16001084, ECO:0000269|PubMed:9486791}.
|
Xenopus laevis (African clawed frog)
|
O57460
|
TLL1_DANRE
|
MDYLYSALTSKMNWIALLLAGLTFCCKVSVHSCLDYDDSYDYYEEEKTETIDYKDPCKAAVFWGDIALDDEDLKMFHIDGTIDLKQQTHGRQGHTSGGLGEHVPTKKRGSLYLLLDRIRRLGFESWPVNSSKDVSSIKTGIRRVNSARNVKSRVPRAATSRAEKIWPGGVIPYVIGGNFTGSQRAMLKQAMRHWEKQTCVTFIEKTDEESYIVFTYRPCGCCSYVGRRGNGPQAISIGKNCDKFGIVVHELGHVIGFWHEHTRPDRDDHVTIIRDNIQPGQEYNFIKMEPGDVNSLGEPYDFDSIMHYARNTFSRGMFLDTILPSRDENGVRPAIGQRTRLSKGDISQAKKLYRCPACGETLQDSVGNFSSPGYPNGYPSYTHCVWRISVTPGEKIVLNFTTMDLYKSSLCWYDYIEVRDGYWRKAPLLGRFCGDKIPEVLVSTDSRMWIEFRSSSNWVGKGFAAVYEAICGGEISKDSGQIQSPNYPDDYRPSKECVWRITVSEGYSVGLSFQVFEIERHDSCAYDYLEVRDGLSENSPLIGRFCGYDKPEDIRSTSNNLWMKFVSDGTVNKAGFAANFFKEEDECLKPDNGGCEQRCVNTLGSFKCACDPGYELAPDKKSCEAACGGLLTKLNGTITTPGWPKEYPPNKNCVWQVVAPTQYRISMQFEAFELEGNEVCKYDYVEVRSGLSSDSKLHGKYCGTEVPEVITSQYNNMRIEFKSDNTVSKKGFKAHFFSDKDECSKDNGGCQHECINTIGSYVCQCRNGFILHENKHDCKEAECEHKIHSTTGTISSPNWPDKYPSRKECTWDITATPGHRVKISFNEFEIEQHQECAYDHLEAFDGDSDKTPILSRLCGNKIPEPLISTGNKMYLRFISDASVQRKGFQATHSTECGGRLKAEARQKNLYSHAQFGDNNYPGHTDCEWLIVAESGYGIELTFTTFEVEEEADCGYDYIELYDGYDTGAHKIGRFCGSGPREELYSAGDAVLIHFHSDDTISKKGFHIRYTSTKFQEALHTRK
|
3.4.24.-
|
COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000255|PROSITE-ProRule:PRU01211}; Note=Binds 1 zinc ion per subunit. {ECO:0000255|PROSITE-ProRule:PRU01211};
|
blood vessel development [GO:0001568]; determination of ventral identity [GO:0048264]; dorsal/ventral pattern formation [GO:0009953]; embryonic caudal fin morphogenesis [GO:0035124]; embryonic hemopoiesis [GO:0035162]; endothelial cell development [GO:0001885]; mesoderm formation [GO:0001707]; positive regulation of BMP signaling pathway [GO:0030513]; post-anal tail morphogenesis [GO:0036342]; protein processing [GO:0016485]; proteolysis [GO:0006508]
|
extracellular region [GO:0005576]; extracellular space [GO:0005615]
|
calcium ion binding [GO:0005509]; metalloendopeptidase activity [GO:0004222]; metallopeptidase activity [GO:0008237]; peptidase activity [GO:0008233]; zinc ion binding [GO:0008270]
|
PF01400;PF00431;PF14670;
|
3.40.390.10;2.10.25.10;2.60.120.290;
| null | null | null | null | null | null | null | null |
FUNCTION: Required for patterning ventral tissues of the tail. May increase bone morphogenetic protein (BMP) activity at the end of gastrulation by proteolytic cleavage of chordin and release of BMP from inactive complexes. {ECO:0000269|PubMed:10375503, ECO:0000269|PubMed:9395394}.
|
Danio rerio (Zebrafish) (Brachydanio rerio)
|
O57472
|
CHRD_DANRE
|
MMEGLLWILLSVIIASVHGSRLKTPALPIQPEREPMISKGLSGCSFGGRFYSLEDTWHPDLGEPFGVMHCVMCHCEPQRSRRGKVFGKVSCRNMKQDCPDPTCDDPVLLPGHCCKTCPKGDSGRKEVESLFDFFQEKDDDLHKSYNDRSYISSEDTSTRDSTTTDFVALLTGVTDSWLPSSSGVARARFTLSRTSLTFSITFQRINRPSLIAFLDTDGNTAFEFRVPQADNDMICGIWKNVPKPHMRQLEAEQLHVSMTTADNRKEELQGRIIKHRALFAETFSAILTSDEVHSGMGGIAMLTLSDTENNLHFILIMQGLVPPGSSKVPVRVKLQYRQHLLREIRANITADDSDFAEVLADLNSRELFWLSRGQLQISVQTEGQTLRHISGFISGRRSCDTLQSVLSSGAALTAGQTGGVGSAVFTLHPNGSLDYQLLVAGLSSAVLSVSIEMKPRRRNKRSVLYELSAVFTDQRAAGSCGRVEARHTHMLLQNELFINIATALQPDGELRGQIRLLPYNGLDARRNELPVPLAGVLVSPPVRTGAAGHAWVSVDPQCHLHYEIIVNGLSKSEDASISAHLHGLAEIGEMDDSSTNHKRLLTGFYGQQAQGVLKDISVELLRHLNEGTAYLQVSTKMNPRGEIRGRIHVPNHCESPAPRAEFLEEPEFEDLLFTREPTELRKDTHTHVHSCFFEGEQHTHGSQWTPQYNTCFTCTCQKKTVICDPVMCPTLSCTHTVQPEDQCCPICEEKKESKETAAVEKVEENPEGCYFEGDQKMHAPGTTWHPFVPPFGYIKCAVCTCKGSTGEVHCEKVTCPPLTCSRPIRRNPSDCCKECPPEETPPLEDEEMMQADGTRLCKFGKNYYQNSEHWHPSVPLVGEMKCITCWCDHGVTKCQRKQCPLLSCRNPIRTEGKCCPECIEDFMEKEEMAKMAEKKKSWRH
| null | null |
anterior/posterior axis specification [GO:0009948]; caudal fin morphogenesis [GO:0035143]; determination of heart left/right asymmetry [GO:0061371]; determination of left/right symmetry [GO:0007368]; determination of ventral identity [GO:0048264]; dorsal convergence [GO:0060030]; dorsal/ventral pattern formation [GO:0009953]; embryonic heart tube morphogenesis [GO:0003143]; embryonic hemopoiesis [GO:0035162]; heart looping [GO:0001947]; Kupffer's vesicle development [GO:0070121]; negative regulation of BMP signaling pathway [GO:0030514]; otic placode formation [GO:0043049]; regulation of BMP signaling pathway [GO:0030510]; somitogenesis [GO:0001756]; specification of animal organ position [GO:0010159]
|
extracellular space [GO:0005615]
|
BMP binding [GO:0036122]
|
PF07452;PF00093;
|
6.20.200.20;
|
Chordin family
|
PTM: Cleaved by tolloid proteases; cleavage participates in dorsoventral patterning during early development. {ECO:0000250}.
|
SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
| null | null | null | null | null |
FUNCTION: Dorsalizing factor. Key developmental protein that dorsalizes early vertebrate embryonic tissues by binding to ventralizing TGF-beta family bone morphogenetic proteins (BMPs) and sequestering them in latent complexes (By similarity). {ECO:0000250, ECO:0000269|PubMed:9441687}.
|
Danio rerio (Zebrafish) (Brachydanio rerio)
|
O57473
|
WEE2B_XENLA
|
MRMAMSCGGRLVQRLDFSSSEEEDGLSNRINEAPQKGSPVSSWRTNNCPFPITPQRNERGLSPTQELSPSSDYSPDPSDKGVGGECPGTPLHYSTWKKLKLCDTPYTPKSLLYKTLPSPGSRVHCRGQRLLRFVAGTGAETEDPTLVNVNPFTPQSYRQTHFQPNGKRKERPEDDCSSDSQMKFTDKEHPAVFQSKRFVLRETNMESRYKTEFLEIEKIGAGEFGSVFKCVKRLDGCFYVIKRSKKPLAGSTDEQLALREVYAHAVLGHHPHVVRYYSAWAEDDHMIIQNEYCNGGSLQDLIMENNKKGQFVPEQELKEILLQVSMGLKYIHGSGLVHMDIKPSNIFICRKQTEVGEDESDGEDDVASASVLYKIGDLGHVTSILNPQVEEGDSRFLANEILQEDYRQLPKADIFALGLTIALAAGAAPLPCNEDGWHHIRKGNLPHIPQPLTPAFLALLKLLVHPDPATRPPATSLAKNSVLRRCVGKAAELQKQLNVEKFKTAMLERELQAAKLAQDECLDLPPVSGFSCRGRKRLVGAKNARSLSFTCGGY
|
2.7.10.2
| null |
meiotic cell cycle [GO:0051321]; mitotic cell cycle [GO:0000278]; negative regulation of G2/MI transition of meiotic cell cycle [GO:0110031]; phosphorylation [GO:0016310]; regulation of meiosis I [GO:0060631]
|
cytoplasm [GO:0005737]; nucleus [GO:0005634]
|
ATP binding [GO:0005524]; magnesium ion binding [GO:0000287]; non-membrane spanning protein tyrosine kinase activity [GO:0004715]
|
PF00069;
|
1.10.510.10;
|
Protein kinase superfamily, Ser/Thr protein kinase family, WEE1 subfamily
|
PTM: Ubiquitinated and degraded at the onset of G2/M phase. {ECO:0000269|PubMed:12679038}.; PTM: Phosphorylated during M and G1 phases. Interacts with cdca3 when phosphorylated at Ser-38. {ECO:0000269|PubMed:12679038}.
|
SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
|
CATALYTIC ACTIVITY: Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-[protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858, ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=2.7.10.2; Evidence={ECO:0000255|PROSITE-ProRule:PRU10027, ECO:0000269|PubMed:9486797};
| null | null | null | null |
FUNCTION: Oocyte and early embryo-specific protein tyrosine kinase that phosphorylates and inhibits cdk1 and acts as a regulator of meiosis in oocytes. Required to ensure the meiotic cell cycle in oocytes by phosphorylating cdk1 at 'Tyr-15', leading to inhibit cdk1 activity and prevent meiosis. {ECO:0000269|PubMed:9486797}.
|
Xenopus laevis (African clawed frog)
|
O57474
|
CXA1_DANRE
|
MGDWSALGRLLDKVQAYSTAGGKVWLSVLFIFRILVLGTAVESAWGDEQSAFKCNTQQPGCENVCYDKSFPISHVRFWVLQIIFVSTPTLLYLAHVFYLMRKEEKLNRKEEELKAVQNDGGDVELHLKKIELKKFKHGLEEHGKVKMKGSLLRTYIFSIIFKSICEVVFLVIQWYLYGFSLSAVYTCERTPCPHRVDCFLSRPTEKTIFIIFMLVVSLFSLLLNIIELFYVLFKRIKDRVKSRQNTQFPTGTLSPTPKELSTTKYAYYNGCSSPTAPLSPMSPPGYKLATGERTNSCRNYNKQANEQNWANYSTEQNRLGQNGSTISNSHAQAFDYPDDTHEHKKLTPGHELQPLALIDARPCSRASSRMSSRARPDDLDV
| null | null |
bone growth [GO:0098868]; bone morphogenesis [GO:0060349]; caudal fin morphogenesis [GO:0035143]; cell communication [GO:0007154]; cell communication by electrical coupling [GO:0010644]; cell population proliferation [GO:0008283]; cell-cell signaling [GO:0007267]; embryonic heart tube development [GO:0035050]; embryonic hemopoiesis [GO:0035162]; embryonic skeletal joint morphogenesis [GO:0060272]; fin development [GO:0033333]; fin morphogenesis [GO:0033334]; fin regeneration [GO:0031101]; heart contraction [GO:0060047]; heart development [GO:0007507]; Kupffer's vesicle development [GO:0070121]; medial fin development [GO:0033338]; microtubule-based transport [GO:0099111]
|
apical plasma membrane [GO:0016324]; connexin complex [GO:0005922]; gap junction [GO:0005921]; intercalated disc [GO:0014704]; mitochondrion [GO:0005739]; plasma membrane [GO:0005886]
|
gap junction channel activity [GO:0005243]; gap junction hemi-channel activity [GO:0055077]; voltage-gated channel activity [GO:0022832]
|
PF00029;PF03508;
|
1.20.5.1130;1.20.1440.80;
|
Connexin family, Alpha-type (group II) subfamily
| null |
SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P17302}; Multi-pass membrane protein {ECO:0000255}. Cell junction, gap junction {ECO:0000250|UniProtKB:P17302}. Note=Localizes at the intercalated disk (ICD) in cardiomyocytes and proper localization at ICD is dependent on TMEM65. {ECO:0000250|UniProtKB:P23242}.
| null | null | null | null | null |
FUNCTION: One gap junction consists of a cluster of closely packed pairs of transmembrane channels, the connexons, through which materials of low MW diffuse from one cell to a neighboring cell. Plays an essential role in gap junction communication in the ventricles (By similarity). {ECO:0000250|UniProtKB:P23242, ECO:0000269|PubMed:15649473}.; FUNCTION: Plays a role in regulation of fin bone size and growth. {ECO:0000269|PubMed:15649473}.
|
Danio rerio (Zebrafish) (Brachydanio rerio)
|
O57479
|
G3P_COLLI
|
MVKVGVNGFGRIGRLVTRAAILSAKVQVVAINDPFIDLNYMVYMFKYDSTHGHFRGTVKAENGKLVINGNAITIFQERDPSNIKWADAGAEYVVESTGVFTTMEKAGAHLKGGAKRVIISAPSADAPMFVMGVNHEKYDKSLKIVSNASCTTNCLAPLAKVIHDNFGIVEGLMTTVHAITATQKTVDGPSGKLWRDGRGAAQNIIPASTGAAKAVGKVIPELNGKLTGMAFRVPTPNVSVVDLTCRLEKPAKYDDIKRVVKAAADGPLKGILAYTEDQVVSCDFNGDSHSSTFDAGAGIALNDHFVKLVSWYDNEYGYSNRVVDLMVHMASKE
|
1.2.1.12; 2.6.99.-
| null |
glucose metabolic process [GO:0006006]; glycolytic process [GO:0006096]; microtubule cytoskeleton organization [GO:0000226]; neuron apoptotic process [GO:0051402]; peptidyl-cysteine S-trans-nitrosylation [GO:0035606]; positive regulation of canonical NF-kappaB signal transduction [GO:0043123]; positive regulation of type I interferon production [GO:0032481]; protein stabilization [GO:0050821]
|
cytoplasm [GO:0005737]; cytosol [GO:0005829]; microtubule cytoskeleton [GO:0015630]; nucleus [GO:0005634]
|
glyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity [GO:0004365]; microtubule binding [GO:0008017]; NAD binding [GO:0051287]; NADP binding [GO:0050661]; peptidyl-cysteine S-nitrosylase activity [GO:0035605]
|
PF02800;PF00044;
|
3.40.50.720;
|
Glyceraldehyde-3-phosphate dehydrogenase family
|
PTM: S-nitrosylation of Cys-150 leads to translocation to the nucleus. {ECO:0000250|UniProtKB:P04797}.
|
SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250|UniProtKB:P04797}. Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:P04797}. Nucleus {ECO:0000250|UniProtKB:P04797}.
|
CATALYTIC ACTIVITY: Reaction=D-glyceraldehyde 3-phosphate + NAD(+) + phosphate = (2R)-3-phospho-glyceroyl phosphate + H(+) + NADH; Xref=Rhea:RHEA:10300, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474, ChEBI:CHEBI:57540, ChEBI:CHEBI:57604, ChEBI:CHEBI:57945, ChEBI:CHEBI:59776; EC=1.2.1.12; Evidence={ECO:0000250|UniProtKB:P04406, ECO:0000255|PROSITE-ProRule:PRU10009}; CATALYTIC ACTIVITY: Reaction=L-cysteinyl-[protein] + S-nitroso-L-cysteinyl-[GAPDH] = L-cysteinyl-[GAPDH] + S-nitroso-L-cysteinyl-[protein]; Xref=Rhea:RHEA:66684, Rhea:RHEA-COMP:10131, Rhea:RHEA-COMP:17089, Rhea:RHEA-COMP:17090, Rhea:RHEA-COMP:17091, ChEBI:CHEBI:29950, ChEBI:CHEBI:149494; Evidence={ECO:0000250|UniProtKB:P04797}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66685; Evidence={ECO:0000250|UniProtKB:P04797};
| null |
PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 1/5.
| null | null |
FUNCTION: Has both glyceraldehyde-3-phosphate dehydrogenase and nitrosylase activities, thereby playing a role in glycolysis and nuclear functions, respectively. Glyceraldehyde-3-phosphate dehydrogenase is a key enzyme in glycolysis that catalyzes the first step of the pathway by converting D-glyceraldehyde 3-phosphate (G3P) into 3-phospho-D-glyceroyl phosphate (By similarity). Participates in nuclear events including transcription, RNA transport, DNA replication and apoptosis. Nuclear functions are probably due to the nitrosylase activity that mediates cysteine S-nitrosylation of nuclear target proteins such as SIRT1, HDAC2 and PRKDC (By similarity). {ECO:0000250|UniProtKB:P04406, ECO:0000250|UniProtKB:P04797}.
|
Columba livia (Rock dove)
|
O57521
|
HS90B_DANRE
|
MPEEMRQEEEAETFAFQAEIAQLMSLIINTFYSNKEIFLRELVSNASDALDKIRYESLTDPTKLDSGKDLKIDIIPNVQERTLTLIDTGIGMTKADLINNLGTIAKSGTKAFMEALQAGADISMIGQFGVGFYSAYLVAEKVTVITKHNDDEQYAWESSAGGSFTVKVDHGEPIGRGTKVILHLKEDQTEYIEEKRVKEVVKKHSQFIGYPITLYVEKERDKEISDDEAEEEKAEKEEKEEEGEDKPKIEDVGSDDEEDTKDKDKKKKKKIKEKYIDQEELNKTKPIWTRNPDDISNEEYGEFYKSLTNDWEDHLAVKHFSVEGQLEFRALLFIPRRAPFDLFENKKKKNNIKLYVRRVFIMDNCEELIPEYLNFIRGVVDSEDLPLNISREMLQQSKILKVIRKNIVKKCLELFAELAEDKDNYKKFYDAFSKNLKLGIHEDSQNRKKLSELLRYQSSQSGDEMTSLTEYVSRMKENQKSIYYITGESKDQVAHSAFVERVCKRGFEVLYMTEPIDEYCVQQLKDFDGKSLVSVTKEGLELPEDEDEKKKMEEDKAKFENLCKLMKEILDKKVEKVTVSNRLVSSPCCIVTSTYGWTANMERIMKAQALRDNSTMGYMMAKKHLEINPDHPIMETLRQKAEADKNDKAVKDLVILLFETALLSSGFSLDDPQTHSNRIYRMIKLGLGIDEDEDVPVEEPSSAAAPEDIPPLEGDDDASRMEEVD
| null | null |
blood vessel development [GO:0001568]; cellular response to heat [GO:0034605]; leukocyte migration [GO:0050900]; muscle organ development [GO:0007517]; negative regulation of proteasomal ubiquitin-dependent protein catabolic process [GO:0032435]; negative regulation of transforming growth factor beta activation [GO:1901389]; positive regulation of transforming growth factor beta receptor signaling pathway [GO:0030511]; protein folding [GO:0006457]; protein stabilization [GO:0050821]; regulation of cell cycle [GO:0051726]; response to estrogen [GO:0043627]
|
aryl hydrocarbon receptor complex [GO:0034751]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; dynein axonemal particle [GO:0120293]; extracellular region [GO:0005576]; nucleus [GO:0005634]; perinuclear region of cytoplasm [GO:0048471]; plasma membrane [GO:0005886]; protein-containing complex [GO:0032991]
|
ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; ATP-dependent protein folding chaperone [GO:0140662]; disordered domain specific binding [GO:0097718]; protein dimerization activity [GO:0046983]; unfolded protein binding [GO:0051082]
|
PF13589;PF00183;
|
3.30.230.80;3.40.50.11260;1.20.120.790;3.30.565.10;
|
Heat shock protein 90 family
| null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P08238}. Dynein axonemal particle {ECO:0000250|UniProtKB:Q6AZV1}.
| null | null | null | null | null |
FUNCTION: Molecular chaperone that promotes the maturation, structural maintenance and proper regulation of specific target proteins involved for instance in cell cycle control and signal transduction. Undergoes a functional cycle linked to its ATPase activity. This cycle probably induces conformational changes in the client proteins, thereby causing their activation. Interacts dynamically with various co-chaperones that modulate its substrate recognition, ATPase cycle and chaperone function. Engages with a range of client protein classes via its interaction with various co-chaperone proteins or complexes, that act as adapters, simultaneously able to interact with the specific client and the central chaperone itself. Recruitment of ATP and co-chaperone followed by client protein forms a functional chaperone. After the completion of the chaperoning process, properly folded client protein and co-chaperone leave HSP90 in an ADP-bound partially open conformation and finally, ADP is released from HSP90 which acquires an open conformation for the next cycle (By similarity). Not required for myofibril formation in skeletal muscles (PubMed:10364427, PubMed:17586488). {ECO:0000250|UniProtKB:P08238, ECO:0000269|PubMed:10364427, ECO:0000269|PubMed:17586488}.
|
Danio rerio (Zebrafish) (Brachydanio rerio)
|
O57526
|
IF23B_XENLA
|
MNKLYIGNLSENVSPPDLESLFKESKIPFTGQFLVKSGYAFVDCPDETWAMKAIDTLSGKVELHGKVIEVEHSVPKRQRSRKLQIRNIPPHLQWEVLDSLLAQYGTVENCEQVNTDSETAVVNVTYANKEHARQGLEKLNGYQLENYSLKVTYIPDEMATPQSPSQQLQQPQQQHPQGRRGFGQRGPARQGSPGAAARPKPQSEVPLRMLVPTQFVGAIIGKEGATIRNITKQTQSKIDIHRKENAGAAEKPITIHSTPEGCSAACKIIMEIMQKEAQDTKFTEEIPLKILAHNNFVGRLIGKEGRNLKKIEQDTDTKITISPLQDLTLYNPERTITVKGSIETCAKAEEEVMKKIRESYENDIAAMNLQAHLIPGLNLNALGLFPPSSSGMPPPSAGVSSPTTSASYPPFGQQPESETVHLFIPALAVGAIIGKQGQHIKQLSRFAGASIKIAPAEGPDAKLRMVIITGPPEAQFKAQGRIYGKLKEENFFGPKEEVKLEAHIKVPSYAAGRVIGKGGKTVNELQNLTSAEVVVPRDQTPDENDQVVVKITGHFYASQLAQRKIQEILAQVRRQQQQQQKTAQSGQPQPRRK
| null | null |
mRNA transport [GO:0051028]; nervous system development [GO:0007399]; regulation of translation [GO:0006417]
|
cytosol [GO:0005829]; endoplasmic reticulum [GO:0005783]; nucleus [GO:0005634]
|
DNA binding [GO:0003677]; mRNA 3'-UTR binding [GO:0003730]
|
PF00013;PF00076;
|
3.30.310.210;3.30.70.330;3.30.1370.10;
|
RRM IMP/VICKZ family
| null |
SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Endoplasmic reticulum. Note=Accumulates along the vegetal cortex in oocytes as oogenesis progresses ('late pathway' for RNA localization). Colocalizes with Vg1 RNA along the vegetal cortex (By similarity). {ECO:0000250}.
| null | null | null | null | null |
FUNCTION: RNA-binding protein that acts as a regulator of mRNA transport and localization. Binds to the RNA sequence motif 5'-UUCAC-3'. Preferentially binds to N6-methyladenosine (m6A)-containing mRNAs and increases their stability (By similarity). Mediates the specific association of Vg1 RNA to microtubules. May regulate mRNA translation (By similarity). Binds specifically to the vegetal localization elements (VLE or VgLE) in the 3'-UTR of Vg1 and VegT mRNAs. Binds to the Vg1 and VegT mRNAs in both the nucleus and the cytoplasm. May regulate mRNA translation (By similarity). Acts as a transcription regulator (PubMed:12957389, PubMed:1577195). Binds to the 5'-[TA]GGTTACT-3' motif within element 3 of the TFIIIA gene promoter (PubMed:12957389, PubMed:1577195). {ECO:0000250|UniProtKB:O00425, ECO:0000250|UniProtKB:O73932, ECO:0000269|PubMed:12957389, ECO:0000269|PubMed:1577195}.
|
Xenopus laevis (African clawed frog)
|
O57539
|
NCOA3_XENLA
|
MSGLGENSLDPLASETRKRKPSSCDTPGPGLTCSGEKRRREQESKYIEELADLISANLSDIDNFNVKPDKCAILKETVRQIRQIKEQGKASSNDDDVQKADVSSTGQGVIDKDSLGPLLLQALDGFLYVVNREGSIVFVSENVTQYLQYKQEDLVNTSVYSILHEEDRKDFLKNLPKSTVNGVPWFSETPRQKSHTFNCRMLVKTSHDHLEDGSNLDARQRYETMQCFALSQPRAMIEEGEDLQSCMICVARRITTAERAFSANPESFITRHDLTGKVVNIDANSLRSSMRPGFEDTIRRCIQRFLFHSEGQPWTYKRHYQEAYVHGLSETPLYRFSLADGTMVTAQTKSKLFRNPVTNDPHGFVSTHFLQREQNGYRPNPNPMAQGIRPQMNPNLPNTMNSMPPQAMQQQNRNYGMGDPNSMAQMQGMRYKSPGNMAPVNQAPGVQQSPYQNNSNYGLNMNSPPHGSPGMNANQPNLMVSPRNRASPKMASNQFSPVPGMNSPMGSSGNAGGGSFSSSSLSALHAISEGVGSSLLSSLSSPGQKVENNSNMNMPQQGKICNQDCKSPSGLYCEQGQVESSVCQSSGREHLGEKDVKENIFEGSESQRSQAESKGHKKLLQLLTCFTEERGQSLMSSSSMDCKDSSNVTSPSGVSSSTSIGVSSTSNLHGSMLQEKHRILHKLLQNGNSPAEVAKITAEATGKDVFQETVSSAPCTEATVKREQLSPKKKENNALLRHLLDKDDWKDPLAKDIKPKVEHMDIKMGSCSSSNVPTSSQDKEVKIKTEPGEEVPGDLDNLDAILGDLAGSDFYSNSMSSRASDLGPKQPVFQDSPTLAMRSPDSMQGSRPPFNRAMSLDSRSSTPPVRNVNSFPMLPKQGMIGSPRMMDGQDNFGVMMGSGPNRSMNQHPGGDWAMQNSAVNRLEPPNVGSVGRPGPDYSSAMTRPAMGGNMPGLLTRSNSIPGSRPVMQQQQHILPMRPNDMAMSMGSNPYGQQAPSNPPGSWPDAIMMNQGRGGAQNRQLGRNSLDDLLCPPSTVEGQTDEIALLDQLHTLLSNTDATGLEEIDRALGIPDLVSQGQALEPQPDSYQPQGSPVMIDQKPPMYGQHYAGQGAAMSAGGFNNMQGQHPPFNTVMGQMNQQQGMHPLQGMHPRANLIRPRNNIPKQLRMQLQQRLQGQQFLNQNRQALEMKVDPMNPGGAGVMRPVMQTPVSQQGFLNAQMVAQKNRELISHQIRQHRMAMMMQQQQGQPQAFSPPPNVTASASMDNPLGGPPMPQAPPQQFSYPPNYGINQQTDPTFGRVSSPPNAMMSSRMAPSQNPHPQTTQMYPSPDMKGWPSGNMARPNSFPQQQYSHQTNPATYNMMHMNGNGNHMGQMNINSLPMSGMPMGPDQKYC
|
2.3.1.48
| null |
cellular response to hormone stimulus [GO:0032870]; positive regulation of transcription by RNA polymerase II [GO:0045944]
|
cytoplasm [GO:0005737]; nucleus [GO:0005634]
|
histone acetyltransferase activity [GO:0004402]; nuclear receptor binding [GO:0016922]; nuclear receptor coactivator activity [GO:0030374]; protein dimerization activity [GO:0046983]
|
PF07469;PF16279;PF16665;PF08815;PF00989;PF14598;PF08832;
|
6.10.140.410;4.10.280.10;3.30.450.20;
|
SRC/p160 nuclear receptor coactivator family
|
PTM: Phosphorylated and acetylated. {ECO:0000250}.
|
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000255|PROSITE-ProRule:PRU00981}. Note=Mainly cytoplasmic and weakly nuclear. {ECO:0000250}.
|
CATALYTIC ACTIVITY: Reaction=acetyl-CoA + L-lysyl-[protein] = CoA + H(+) + N(6)-acetyl-L-lysyl-[protein]; Xref=Rhea:RHEA:45948, Rhea:RHEA-COMP:9752, Rhea:RHEA-COMP:10731, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:61930; EC=2.3.1.48;
| null | null | null | null |
FUNCTION: Nuclear receptor coactivator that directly binds nuclear receptors and stimulates the transcriptional activities in a hormone-dependent fashion. Plays a central role in creating a multisubunit coactivator complex, probably via remodeling of chromatin. Involved in the coactivation of different nuclear receptors, such as retinoids (RAR and RXR), thyroid hormone (TR) and orphan nuclear receptor (hepatocyte nuclear receptor 4 (HNF4) and constitutive androstane receptor (CAR)). Displays histone acetyltransferase activity.
|
Xenopus laevis (African clawed frog)
|
O57579
|
AMPN_CHICK
|
MAAGFFISKSVGIVGIVLALGAVATIIALSVVYAQEKNKSSGGSGGSDTTSTTTASTTTTSTTTASTTAAPNNPWNRWRLPTALKPESYEVTLQPFLTPDDNNMYIFKGNSSVVFLCEEATDLILIHSNKLNYTLQGGFHASLHAVNGSTPPTISNTWLETNTQYLVLQLAGPLQQGQHYRLFSIFTGELADDLAGFYRSEYTEGNVTKVVATTQMQAPDARKAFPCFDEPAMKAVFTVTMIHPSDHTAISNMPVHSTYQLQMDGQSWNVTQFDPTPRMSTYLLAFIVSQFDYVENNTGKVQIRIWGRPAAIAEGQGEYALEKTGPILSFFERHYNTAYPLPKSDQVGLPDFNAGAMENWGLVTYRENSLLYDNAYSSIGNKERVVTVIAHELAHQWFGNLVTLRWWNDLWLNEGFASYVEYLGADSAEPTWDIKDLMVLNELYTVMATDALTTSHPLTFREDEINTPAQISEVFDSIAYSKGASVLRMLSDFLTEDVFKEGLQSYLHDFSYNNTVYTDLWDHLQEAVNKNSVPLPDSIGAIMDRWTLQMGFPVVTVNTLTGSVQQSHFLLDSNSTVERPSVFNYTWIVPITWMTPSRTGDRYWLVDVSATNSDFSVGSSTWLLLNLNVSGYFRVNYNQENWDQLLQQLSNNHQAIPVINRAQIIDDAFNLARAQQVSVTLALNTTRFLSGETAYMPWQAALNNLQYFQLMFDRSEVFGAMTKYIQKQVTPLFEYYRTATNNWTAIPSALMDQYNEINAISTACSYGIAECQQLATALYQQWRQNVSNNPIAPNLRSAIYCSAVATGGEEVWDFIWERFLEAPVVSEADKLRTALTCSTETWILQRYLQYTIDPTKIRKQDATSTINSIASNVVGQPLAWDFIRSNWRTLFGQYGGGSFSFSRLISAVTQRFNTEFELKQLEQFKADNQDIGFGSGTRALEQALERTRTNINWVKENKEVVHAWFRAETASS
|
3.4.11.20
|
COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000269|PubMed:8288037}; Note=Binds 1 zinc ion per subunit. {ECO:0000269|PubMed:8288037};
|
peptide catabolic process [GO:0043171]; proteolysis [GO:0006508]
|
cytoplasm [GO:0005737]; extracellular space [GO:0005615]; plasma membrane [GO:0005886]
|
metalloaminopeptidase activity [GO:0070006]; peptide binding [GO:0042277]; zinc ion binding [GO:0008270]
|
PF11838;PF01433;PF17900;
|
1.25.50.20;2.60.40.1910;1.10.390.10;2.60.40.1730;
|
Peptidase M1 family
| null |
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|Ref.4}; Single-pass type II membrane protein {ECO:0000250|UniProtKB:P15144}. Note=Also found as a soluble form. {ECO:0000269|Ref.4}.
|
CATALYTIC ACTIVITY: Reaction=Differs from other aminopeptidases in broad specificity for amino acids in the P1 position and the ability to hydrolyze peptides of four or five residues that contain Pro in the P1' position.; EC=3.4.11.20; Evidence={ECO:0000269|PubMed:7684960, ECO:0000269|PubMed:8205380};
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.58 mM for Leu-Pro-Leu-Arg-PheNH2 {ECO:0000269|PubMed:7684960, ECO:0000269|PubMed:8205380}; KM=1.23 mM for fMet-Leu-Phe {ECO:0000269|PubMed:7684960, ECO:0000269|PubMed:8205380}; KM=1.53 mM for fMet-Ala-Gly-Ser-Glu {ECO:0000269|PubMed:7684960, ECO:0000269|PubMed:8205380}; KM=1.72 mM for fMet-Nle-Leu-Phe-Nle-Tyr-Lys {ECO:0000269|PubMed:7684960, ECO:0000269|PubMed:8205380};
| null | null | null |
FUNCTION: Broad specificity aminopeptidase. Degrades a variety of peptides possessing various N-terminal amino acids including hydrophobic, basic and acidic amino acids. Preferentially hydrolyzes small peptides consisting of 4 or 5 amino acids. Hydrolyzes the N-terminal Xaa-Pro bonds in the chicken brain peptide Leu-Pro-Leu-Arg-PheNH2, the substance P fragment Arg-Pro-Lys-Pro and the bradykinin fragment Arg-Pro-Pro-Gly-Phe. Hydrolyzes the N-formylated peptides fMet-Leu-Phe, fMet-Ala-Gly-Ser-Glu and fMet-Nle-Leu-Phe-Nle-Tyr-Lys, but does not hydrolyze peptides with acetylation or pyroglutamic acid at N-terminus. Does not hydrolyze large peptides such as complete substance P, bradykinin or schistoFLRFamide. {ECO:0000269|PubMed:7684960, ECO:0000269|PubMed:8205380, ECO:0000269|Ref.4}.
|
Gallus gallus (Chicken)
|
O57598
|
ATOH7_CHICK
|
MKTCQSSHLDSGVESDIQCRSGSGCVVKCSTERMESAAKRRLAANARERRRMQGLNTAFDRLRKVVPQWGQDKKLSKYETLQMALSYIMALTRILAEAERYSTEREWINLHCEHFHPESYHHYTGQKVATDSDPYAQRIFSYHPEHFQIAN
| null | null |
axon development [GO:0061564]; circadian rhythm [GO:0007623]; entrainment of circadian clock by photoperiod [GO:0043153]; neural retina development [GO:0003407]; neuron differentiation [GO:0030182]; neuron fate commitment [GO:0048663]; optic nerve development [GO:0021554]; positive regulation of retinal ganglion cell axon guidance [GO:1902336]; positive regulation of transcription by RNA polymerase II [GO:0045944]; regulation of transcription by RNA polymerase II [GO:0006357]; response to auditory stimulus [GO:0010996]; sensory organ development [GO:0007423]
|
axon [GO:0030424]; nucleus [GO:0005634]; perikaryon [GO:0043204]
|
DNA-binding transcription factor activity [GO:0003700]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; E-box binding [GO:0070888]; protein dimerization activity [GO:0046983]; transcription cis-regulatory region binding [GO:0000976]
|
PF00010;
|
4.10.280.10;
| null | null |
SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q8N100}. Perikaryon {ECO:0000250|UniProtKB:Q9Z2E5}. Cell projection, axon {ECO:0000250|UniProtKB:Q9Z2E5}.
| null | null | null | null | null |
FUNCTION: Transcription factor that binds to DNA at the consensus sequence 5'-CAG[GC]TG-3' (By similarity). Positively regulates the determination of retinal ganglion cell fate and formation of the optic nerve and retino-hypothalamic tract (PubMed:11124117, PubMed:15342472, PubMed:16260616). Required for retinal circadian rhythm photoentrainment (By similarity). Plays a role in brainstem auditory signaling and binaural processing (By similarity). During retinal neurogenesis, activates its own transcription, as well as the transcription of CHRNB3 and BRN3 (PubMed:11172005). {ECO:0000250|UniProtKB:Q9Z2E5, ECO:0000269|PubMed:11124117, ECO:0000269|PubMed:11172005, ECO:0000269|PubMed:15342472, ECO:0000269|PubMed:16260616}.
|
Gallus gallus (Chicken)
|
O57604
|
PODXL_CHICK
|
MRAPLLLPLLPLLLFGVSSGNNDKTTHSTTVSPETTKQITTITVTTSQVQGSISASKPSSTAPTAVMSFTKAQEAATSSKQHDSSTSSIPPPSTSITPSIITTSPQGKTPSTPALTHTPDQNTKTTGRQDDTSHVSVASTSASQQVSSSASAAVPTTTSAVTSSATQQKVSPTDSSEILLKPSASPNSTQVTSPSRTPKGFLSTVTTSPHIADNGSTALNQLKSTVSSSEVPVSSFLDKDHSVSSSTSATNQHLSLSSHRPTSPVPKFECSTPHSGSVPSTSSKTSLSSPSSSTKNATVTTTMTTAKAAYTSQGDGSVTHKSGVTAQSPTSAPLPTPTLKDHMKSKSPDQTHSNVSPPNEVICEDQIGEVRPILNLKEEKTCDDWKKASNEAFFEVFCSGRRHAFNSTRDRCTVKLASSNHRRWAVHVIVHRVLDPAAVFEELKEKRNELEKLGITNVTYLNQEMEEEIKDQSSTPLIITIVTLAGSLLLIAAIYGCCHQRFSQKKSQQRLTEELQTMENGYHDNPTLEVMETGSEMQEKKVNLNGELGDSWIVPLDTIMKEDLEEEDTHL
| null | null |
cell adhesion [GO:0007155]; cell migration [GO:0016477]; epithelial tube formation [GO:0072175]; negative regulation of cell-cell adhesion [GO:0022408]; positive regulation of cell migration [GO:0030335]; positive regulation of cell-cell adhesion mediated by integrin [GO:0033634]; regulation of microvillus assembly [GO:0032534]
|
apical plasma membrane [GO:0016324]; cytoplasm [GO:0005737]; filopodium [GO:0030175]; lamellipodium [GO:0030027]; membrane raft [GO:0045121]; microvillus membrane [GO:0031528]; plasma membrane [GO:0005886]; ruffle [GO:0001726]
| null |
PF06365;
| null |
Podocalyxin family
|
PTM: N- and O-linked glycosylated. Sialoglycoprotein (By similarity). {ECO:0000250}.
|
SUBCELLULAR LOCATION: Apical cell membrane {ECO:0000269|PubMed:17311105}. Cell projection, microvillus {ECO:0000250}. Membrane raft {ECO:0000250}. Cell projection, lamellipodium {ECO:0000250}. Cell projection, filopodium {ECO:0000250}. Cell projection, ruffle {ECO:0000250}. Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. Note=In single attached epithelial cells is restricted to a preapical pole on the free plasma membrane whereas other apical and basolateral proteins are not yet polarized. Colocalizes with NHERF2 at the apical plasma membrane during epithelial polarization. Colocalizes with NHERF1 at the trans-Golgi network (transiently). Its association with the membrane raft is transient. Forms granular, punctuated pattern, forming patches, preferentially adopting a polar distribution, located on the migrating poles of the cell or forming clusters along the terminal ends of filipodia establishing contact with the endothelial cells. Colocalizes with the submembrane actin of lamellipodia, particularly associated with ruffles. Colocalizes with vinculin at protrusions of cells. Colocalizes with ITGB1. Colocalizes with actin filaments, ezrin and NHERF1 in a punctate pattern at the apical cell surface where microvilli form. Colocalizes with EZR and NHERF2 at the apical cell membrane of glomerular epithelium cells (By similarity). Colocalizes with NHERF1 at the apical cell membrane. Colocalizes with PARD3, PRKCI, EXOC5, OCLN, RAB11A and RAB8A in apical membrane initiation sites (AMIS) during the generation of apical surface and luminogenesis (By similarity). {ECO:0000250}.
| null | null | null | null | null |
FUNCTION: Involved in the regulation of both adhesion and cell morphology and cancer progression. Functions as an anti-adhesive molecule that maintains an open filtration pathway between neighboring foot processes in the podocyte by charge repulsion. Acts as a pro-adhesive molecule, enhancing the adherence of cells to immobilized ligands, increasing the rate of migration and cell-cell contacts in an integrin-dependent manner. Involved in the formation of a preapical plasma membrane subdomain to set up initial epithelial polarization and the apical lumen formation during renal tubulogenesis. Plays a role in cancer development and aggressiveness by inducing cell migration and invasion through its interaction with the actin-binding protein EZR. Affects EZR-dependent signaling events, leading to increased activities of the MAPK and PI3K pathways in cancer cells (By similarity). Induces the formation of apical actin-dependent microvilli. {ECO:0000250, ECO:0000269|PubMed:17311105}.
|
Gallus gallus (Chicken)
|
O57672
|
G3P_MELGA
|
AEYVVESTGVFTTMEKAGAHLKGGAKRVIISAPSADAPMFVMGVNHEKYDKSLKIVSNALCTTNCLAPLAKVIHDNFGIVEGLMTTVHAITATQKTVDGPFGKLWRDGRGAAQNIIPASTGAAKAVGKVIPELNGKLTGMAFHVPTPNVSVVDLTCRLEKPAKYDDIKRVVKAAADGPLKGILGYTEDQVVSCDFNGDSHSSTFDAGAGIALNDHFVKLVSWYDNEFGYSNRVV
|
1.2.1.12; 2.6.99.-
| null |
glycolytic process [GO:0006096]; microtubule cytoskeleton organization [GO:0000226]; neuron apoptotic process [GO:0051402]; peptidyl-cysteine S-trans-nitrosylation [GO:0035606]; positive regulation of canonical NF-kappaB signal transduction [GO:0043123]; positive regulation of type I interferon production [GO:0032481]; protein stabilization [GO:0050821]
|
cytoplasm [GO:0005737]; cytosol [GO:0005829]; microtubule cytoskeleton [GO:0015630]; nucleus [GO:0005634]
|
glyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity [GO:0004365]; microtubule binding [GO:0008017]; NAD binding [GO:0051287]; peptidyl-cysteine S-nitrosylase activity [GO:0035605]
|
PF02800;
|
3.40.50.720;
|
Glyceraldehyde-3-phosphate dehydrogenase family
|
PTM: S-nitrosylation of Cys-61 leads to translocation to the nucleus. {ECO:0000250|UniProtKB:P04797}.
|
SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250|UniProtKB:P04797}. Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:P04797}. Nucleus {ECO:0000250|UniProtKB:P04797}.
|
CATALYTIC ACTIVITY: Reaction=D-glyceraldehyde 3-phosphate + NAD(+) + phosphate = (2R)-3-phospho-glyceroyl phosphate + H(+) + NADH; Xref=Rhea:RHEA:10300, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474, ChEBI:CHEBI:57540, ChEBI:CHEBI:57604, ChEBI:CHEBI:57945, ChEBI:CHEBI:59776; EC=1.2.1.12; Evidence={ECO:0000250|UniProtKB:P04406, ECO:0000255|PROSITE-ProRule:PRU10009}; CATALYTIC ACTIVITY: Reaction=L-cysteinyl-[protein] + S-nitroso-L-cysteinyl-[GAPDH] = L-cysteinyl-[GAPDH] + S-nitroso-L-cysteinyl-[protein]; Xref=Rhea:RHEA:66684, Rhea:RHEA-COMP:10131, Rhea:RHEA-COMP:17089, Rhea:RHEA-COMP:17090, Rhea:RHEA-COMP:17091, ChEBI:CHEBI:29950, ChEBI:CHEBI:149494; Evidence={ECO:0000250|UniProtKB:P04797}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66685; Evidence={ECO:0000250|UniProtKB:P04797};
| null |
PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 1/5.
| null | null |
FUNCTION: Has both glyceraldehyde-3-phosphate dehydrogenase and nitrosylase activities, thereby playing a role in glycolysis and nuclear functions, respectively. Glyceraldehyde-3-phosphate dehydrogenase is a key enzyme in glycolysis that catalyzes the first step of the pathway by converting D-glyceraldehyde 3-phosphate (G3P) into 3-phospho-D-glyceroyl phosphate (By similarity). Participates in nuclear events including transcription, RNA transport, DNA replication and apoptosis. Nuclear functions are probably due to the nitrosylase activity that mediates cysteine S-nitrosylation of nuclear target proteins such as SIRT1, HDAC2 and PRKDC (By similarity). {ECO:0000250|UniProtKB:P04406, ECO:0000250|UniProtKB:P04797}.
|
Meleagris gallopavo (Wild turkey)
|
O57693
|
GAPN_THETE
|
MRAGLLEGVIKEKGGVPVYPSYLAGEWGGSGQEIEVKSPIDLATIAKVISPSREEVERTLDVLFKRGRWSARDMPGTERLAVLRKAADIIERNLDVFAEVLVMNAGKPKSAAVGEVKAAVDRLRLAELDLKKIGGDYIPGDWTYDTLETEGLVRREPLGVVAAITPFNYPLFDAVNKITYSFIYGNAVVVKPSISDPLPAAMAVKALLDAGFPPDAIALLNLPGKEAEKIVADDRVAAVSFTGSTEVGERVVKVGGVKQYVMELGGGDPAIVLEDADLDLAADKIARGIYSYAGQRCDAIKLVLAERPVYGKLVEEVAKRLSSLRVGDPRDPTVDVGPLISPSAVDEMMAAIEDAVEKGGRVLAGGRRLGPTYVQPTLVEAPADRVKDMVLYKREVFAPVASAVEVKDLDQAIELANGRPYGLDAAVFGRDVVKIRRAVRLLEVGAIYINDMPRHGIGYYPFGGRKKSGVFREGIGYAVEAVTAYKTIVFNYKGKGVWKYE
|
1.2.1.90
| null |
metabolic process [GO:0008152]
| null |
glyceraldehyde-3-phosphate dehydrogenase (NADP+) (non-phosphorylating) activity [GO:0008886]; lactaldehyde dehydrogenase activity [GO:0008911]; NAD binding [GO:0051287]; NADP binding [GO:0050661]
|
PF00171;
| null |
Aldehyde dehydrogenase family
| null | null |
CATALYTIC ACTIVITY: Reaction=D-glyceraldehyde 3-phosphate + H2O + NADP(+) = (2R)-3-phosphoglycerate + 2 H(+) + NADPH; Xref=Rhea:RHEA:14669, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58272, ChEBI:CHEBI:58349, ChEBI:CHEBI:59776; EC=1.2.1.90; Evidence={ECO:0000269|PubMed:3121324, ECO:0000269|PubMed:9497334}; CATALYTIC ACTIVITY: Reaction=D-glyceraldehyde 3-phosphate + H2O + NAD(+) = (2R)-3-phosphoglycerate + 2 H(+) + NADH; Xref=Rhea:RHEA:42760, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:58272, ChEBI:CHEBI:59776; EC=1.2.1.90; Evidence={ECO:0000269|PubMed:3121324, ECO:0000269|PubMed:9497334};
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.4 mM for NAD (with G1P as effector) {ECO:0000269|PubMed:9497334}; KM=1.3 mM for NAD (with AMP as effector) {ECO:0000269|PubMed:9497334}; KM=1.7 mM for NAD (with ADP as effector) {ECO:0000269|PubMed:9497334}; KM=3.1 mM for NAD {ECO:0000269|PubMed:3121324}; Vmax=32.5 umol/min/mg enzyme with NAD as substrate (with AMP as effector) {ECO:0000269|PubMed:9497334}; Vmax=35 umol/min/mg enzyme with NAD as substrate (with G1P as effector) {ECO:0000269|PubMed:9497334}; Vmax=36 umol/min/mg enzyme with NAD as substrate (with ADP as effector) {ECO:0000269|PubMed:9497334}; Vmax=36 umol/min/mg enzyme with NAD as substrate {ECO:0000269|PubMed:3121324, ECO:0000269|PubMed:9497334}; Vmax=14 umol/min/mg enzyme with NADP as substrate {ECO:0000269|PubMed:15288789, ECO:0000269|PubMed:3121324, ECO:0000269|PubMed:9497334}; Vmax=31 umol/min/mg enzyme with NADP as substrate (with F6P as effector) {ECO:0000269|PubMed:15288789}; Vmax=33 umol/min/mg enzyme with NADP as substrate (with ADP as effector) {ECO:0000269|PubMed:15288789}; Vmax=39 umol/min/mg enzyme with NADP as substrate (with AMP as effector) {ECO:0000269|PubMed:15288789}; Vmax=43 umol/min/mg enzyme with NADP as substrate (with G1P as effector) {ECO:0000269|PubMed:15288789}; Note=Km applies to a data set exhibiting Michaelis-Menten kinetics. When an enzyme does not exhibit Michaelis-Menten kinetics the binding affinity is simply expressed as S0.5 which corresponds to the observed substrate concentration for 0.5 x Vmax. S0.5 is 20 mM for NADP alone, 0.1 mM for NADP with G1P as effector, 0.2 mM for NADP with F6P as effector, 0.15 mM for NADP with AMP as effector and 0.2 mM for NADP with ADP as effector.;
| null | null |
BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 96 degrees Celsius. High thermostability. {ECO:0000269|PubMed:3121324, ECO:0000269|PubMed:9497334};
|
FUNCTION: Catalyzes the irreversible NAD(P)-dependent non-phosphorylating oxidation of glyceraldehyde-3-phosphate (GAP) to 3-phosphoglycerate (3PG). It is highly specific for D-GAP. {ECO:0000269|PubMed:3121324, ECO:0000269|PubMed:9497334}.
|
Thermoproteus tenax
|
O57712
|
NSUN6_PYRHO
|
MAMNYLEAFPKELREYYKNLFGKEEANKIMKKLREPVEHYYIRVNTLKISREKLIGELKKEGLKPLRSPYLPEGLYFVREGPNFSDDFEPKLPVVVANKYAAESVYQGAMLYAPGVLKADKNIKEGDEVQIRDPKGLLVGIGIARMDYKEMTEATRGLAVEVTLPKFKLPSLSELKAFEKGYFYPQGLPSMVTARVLEPKEDDVIIDMAAAPGGKTTHIAQLLENKGEIIAIDKSKNRLRKMEENIKRLGVKNVKLVQMDARKLPDLGIKADKILLDAPCTALGVRPKLWEERTLKHIEATARYQRAFIWAAIKSLRRGGVLVYSTCTLSYEENEGNVKFMIRKGMKLEEQSIFIGSPGIGMNKVQRFYPHKHLTQGFFIAKLRKVKDI
|
2.1.1.-
| null |
RNA methylation [GO:0001510]; tRNA modification [GO:0006400]
| null |
tRNA (cytidine-5-)-methyltransferase activity [GO:0016428]; tRNA binding [GO:0000049]
|
PF01189;PF01472;
|
2.30.130.10;3.40.50.150;
|
Class I-like SAM-binding methyltransferase superfamily, RsmB/NOP family
| null | null |
CATALYTIC ACTIVITY: Reaction=cytidine(72) in tRNA + S-adenosyl-L-methionine = 5-methylcytidine(72) in tRNA + H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:61988, Rhea:RHEA-COMP:15996, Rhea:RHEA-COMP:15997, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:74483, ChEBI:CHEBI:82748; Evidence={ECO:0000269|PubMed:30541086}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:61989; Evidence={ECO:0000305|PubMed:30541086}; CATALYTIC ACTIVITY: Reaction=cytidine(72) in tRNA(Thr) + S-adenosyl-L-methionine = 5-methylcytidine(72) in tRNA(Thr) + H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:21124, Rhea:RHEA-COMP:15877, Rhea:RHEA-COMP:15878, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:74483, ChEBI:CHEBI:82748; Evidence={ECO:0000269|PubMed:30541086}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:21125; Evidence={ECO:0000305|PubMed:30541086}; CATALYTIC ACTIVITY: Reaction=cytidine(72) in tRNA(Cys) + S-adenosyl-L-methionine = 5-methylcytidine(72) in tRNA(Cys) + H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:61584, Rhea:RHEA-COMP:15875, Rhea:RHEA-COMP:15876, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:74483, ChEBI:CHEBI:82748; Evidence={ECO:0000269|PubMed:30541086}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:61585; Evidence={ECO:0000305|PubMed:30541086};
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.38 uM for tRNA(Cys)(GCA) {ECO:0000269|PubMed:30541086}; KM=0.43 uM for tRNA(Thr)(CGU) {ECO:0000269|PubMed:30541086}; KM=0.63 uM for tRNA(Thr)(GGU) {ECO:0000269|PubMed:30541086}; KM=0.59 uM for tRNA(Thr)(GGU) {ECO:0000269|PubMed:30541086}; KM=0.83 uM for tRNA(Ser)(UGA) {ECO:0000269|PubMed:30541086}; KM=0.76 uM for tRNA(Ser)(CGA) {ECO:0000269|PubMed:30541086}; KM=0.64 uM for tRNA(Ser)(GGA) {ECO:0000269|PubMed:30541086}; KM=0.56 uM for tRNA(Ser)(GCU) {ECO:0000269|PubMed:30541086}; KM=0.7 uM for tRNA(Asn)(GUU) {ECO:0000269|PubMed:30541086}; KM=0.3 uM for tRNA(Asp)(GUC) {ECO:0000269|PubMed:30541086}; KM=0.52 uM for tRNA(Arg)(GCG) {ECO:0000269|PubMed:30541086}; Note=kcat is 3.04 min(-1) with tRNA(Cys)(GCA) as substrate. kcat is 4.30 min(-1) with tRNA(Thr)(CGU) as substrate. kcat is 4.34 min(-1) with tRNA(Thr)(GGU) as substrate. kcat is 4.43 min(-1) with tRNA(Thr)(GGU) as substrate. kcat is 2.23 min(-1) with tRNA(Ser)(UGA) as substrate. kcat is 1.50 min(-1) with tRNA(Ser)(CGA) as substrate. kcat is 1.19 min(-1) with tRNA(Ser)(GGA) as substrate. kcat is 0.37 min(-1) with tRNA(Ser)(GCU) as substrate. kcat is 1.76 min(-1) with tRNA(Asn)(GUU) as substrate. kcat is 3.71 min(-1) with tRNA(Asp)(GUC) as substrate. kcat is 0.67 min(-1) with tRNA(Arg)(GCG) as substrate. {ECO:0000269|PubMed:30541086};
| null | null |
BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Methyltransferase activity is much more higher at 65 degrees Celsius than at 55 and 37 degrees Celsius. {ECO:0000269|PubMed:30541086};
|
FUNCTION: S-adenosyl-L-methionine-dependent methyltransferase that specifically methylates the C5 position of cytosine 72 in several tRNAs. This modification appears to slightly promote the thermal stability of P.horikoshii tRNAs, but does not affect their amino acid accepting activity. Four elements in the acceptor stems of tRNAs are essential for substrate recognition by this enzyme: the target site C72, the 3'-CCA terminus, U73 or G73, and the second base pair C2:G71. {ECO:0000269|PubMed:30541086}.
|
Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3)
|
O57767
|
NADA_PYRHO
|
MDLVEEILRLKEERNAIILAHNYQLPEVQDIADFIGDSLELARRATRVDADVIVFAGVDFMAETAKILNPDKVVLIPSREATCAMANMLKVEHILEAKRKYPNAPVVLYVNSTAEAKAYADVTVTSANAVEVVKKLDSDVVIFGPDKNLAHYVAKMTGKKIIPVPSKGHCYVHQKFTLDDVERAKKLHPNAKLMIHPECIPEVQEKADIIASTGGMIKRACEWDEWVVFTEREMVYRLRKLYPQKKFYPAREDAFCIGMKAITLKNIYESLKDMKYKVEVPEEIARKARKAIERMLEMSK
|
2.5.1.72
|
COFACTOR: Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; Evidence={ECO:0000255|HAMAP-Rule:MF_00568, ECO:0000269|PubMed:27224840, ECO:0000269|PubMed:27404889, ECO:0000269|PubMed:31390192}; Note=Binds 1 [4Fe-4S] cluster per subunit. {ECO:0000255|HAMAP-Rule:MF_00568, ECO:0000269|PubMed:27224840, ECO:0000269|PubMed:27404889, ECO:0000269|PubMed:31390192};
|
'de novo' NAD biosynthetic process from aspartate [GO:0034628]
|
cytosol [GO:0005829]
|
4 iron, 4 sulfur cluster binding [GO:0051539]; metal ion binding [GO:0046872]; quinolinate synthetase A activity [GO:0008987]
|
PF02445;
|
3.40.50.10800;
|
Quinolinate synthase family, Type 2 subfamily
| null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00568}.
|
CATALYTIC ACTIVITY: Reaction=dihydroxyacetone phosphate + iminosuccinate = H(+) + 2 H2O + phosphate + quinolinate; Xref=Rhea:RHEA:25888, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29959, ChEBI:CHEBI:43474, ChEBI:CHEBI:57642, ChEBI:CHEBI:77875; EC=2.5.1.72; Evidence={ECO:0000255|HAMAP-Rule:MF_00568, ECO:0000269|PubMed:15937336, ECO:0000269|PubMed:27224840}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:25889; Evidence={ECO:0000255|HAMAP-Rule:MF_00568, ECO:0000269|PubMed:15937336};
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.24 mM for dihydroxyacetone phosphate {ECO:0000269|PubMed:27224840};
|
PATHWAY: Cofactor biosynthesis; NAD(+) biosynthesis; quinolinate from iminoaspartate: step 1/1. {ECO:0000255|HAMAP-Rule:MF_00568, ECO:0000305|PubMed:15937336}.
| null | null |
FUNCTION: Catalyzes the condensation of iminoaspartate with dihydroxyacetone phosphate to form quinolinate. {ECO:0000255|HAMAP-Rule:MF_00568, ECO:0000269|PubMed:15937336, ECO:0000269|PubMed:27224840}.
|
Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3)
|
O57878
|
BARAC_PYRHO
|
MVSMTKWDEIRKYTSKKIEKNLEIVKLDEKYIPRASGFKYYPMVIERSSGSRIWDKDGNEYIDFLTSAAVFNVGHTHPGVVKAVEEQIKKFFNYTMGYLYVEPPVRLAELLVEITPGNFEKKVTYGFSGSDAVDSSIKAARAYTKRVNIISFLHSYHGMTYGALSATGILDPKLKKLLHPMGNFHHVEFPDPYRNSWGIDGYEDPSELANRALDEIERKIKELNEDVAGIIIEPIQGDAGVVIPPEEFVRDLKKLTEEYGIVFIDEEVQTGMGRTGRWWGIEHFGVTPDLIVSAKALGGGMPISAVVGKAEIMDSVPVPFFVFTHIGHAVNASAAIATINVIKEEKLVERSEKLGEYMLKRLRELQETYPIIGDVRGKGLLIGVDIVKEGTREPDRSLAQKISWRAWEKGLIMITFGKHGNVLRIAPPLNIPQEDLDKGVEIIEESIKDAVEGKIPDEVLKFLRAW
|
5.1.1.10
|
COFACTOR: Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; Evidence={ECO:0000269|PubMed:25963389, ECO:0000269|PubMed:28343923};
| null | null |
identical protein binding [GO:0042802]; methionine racemase activity [GO:0018111]; pyridoxal phosphate binding [GO:0030170]; threonine racemase activity [GO:0018114]; transaminase activity [GO:0008483]
|
PF00202;
|
3.90.1150.10;3.40.640.10;
|
Class-III pyridoxal-phosphate-dependent aminotransferase family
| null | null |
CATALYTIC ACTIVITY: Reaction=an L-alpha-amino acid = a D-alpha-amino acid; Xref=Rhea:RHEA:18317, ChEBI:CHEBI:59869, ChEBI:CHEBI:59871; EC=5.1.1.10; Evidence={ECO:0000269|PubMed:25963389, ECO:0000269|PubMed:28343923}; CATALYTIC ACTIVITY: Reaction=L-phenylalanine = D-phenylalanine; Xref=Rhea:RHEA:59804, ChEBI:CHEBI:57981, ChEBI:CHEBI:58095; Evidence={ECO:0000269|PubMed:28343923}; CATALYTIC ACTIVITY: Reaction=L-leucine = D-leucine; Xref=Rhea:RHEA:59396, ChEBI:CHEBI:57427, ChEBI:CHEBI:143079; Evidence={ECO:0000269|PubMed:28343923}; CATALYTIC ACTIVITY: Reaction=L-methionine = D-methionine; Xref=Rhea:RHEA:12492, ChEBI:CHEBI:57844, ChEBI:CHEBI:57932; Evidence={ECO:0000269|PubMed:28343923}; CATALYTIC ACTIVITY: Reaction=L-tyrosine = D-tyrosine; Xref=Rhea:RHEA:59808, ChEBI:CHEBI:58315, ChEBI:CHEBI:58570; Evidence={ECO:0000269|PubMed:28343923}; CATALYTIC ACTIVITY: Reaction=L-isoleucine = D-allo-isoleucine; Xref=Rhea:RHEA:45560, ChEBI:CHEBI:58045, ChEBI:CHEBI:85306; Evidence={ECO:0000269|PubMed:28343923}; CATALYTIC ACTIVITY: Reaction=L-threonine = D-threonine; Xref=Rhea:RHEA:13913, ChEBI:CHEBI:57757, ChEBI:CHEBI:57926; Evidence={ECO:0000269|PubMed:28343923}; CATALYTIC ACTIVITY: Reaction=L-tryptophan = D-tryptophan; Xref=Rhea:RHEA:60516, ChEBI:CHEBI:57719, ChEBI:CHEBI:57912; Evidence={ECO:0000269|PubMed:28343923};
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=3.94 mM for L-Ile {ECO:0000269|PubMed:28343923}; KM=9.54 mM for D-Ile {ECO:0000269|PubMed:28343923}; KM=4.95 mM for L-Leu {ECO:0000269|PubMed:28343923}; KM=4.19 mM for D-Leu {ECO:0000269|PubMed:28343923}; KM=4.28 mM for L-Met {ECO:0000269|PubMed:28343923}; KM=7.86 mM for D-Met {ECO:0000269|PubMed:28343923}; KM=8.23 mM for L-Phe {ECO:0000269|PubMed:28343923}; KM=2.78 mM for D-Phe {ECO:0000269|PubMed:28343923}; KM=2.23 mM for L-Tyr {ECO:0000269|PubMed:28343923}; KM=2.77 mM for D-Tyr {ECO:0000269|PubMed:28343923}; KM=5.84 mM for L-Trp {ECO:0000269|PubMed:28343923}; KM=1.68 mM for D-Trp {ECO:0000269|PubMed:28343923}; Vmax=14.3 umol/min/mg enzyme with L-Ile as substrate {ECO:0000269|PubMed:28343923}; Vmax=25.9 umol/min/mg enzyme with D-Ile as substrate {ECO:0000269|PubMed:28343923}; Vmax=38.9 umol/min/mg enzyme with L-Leu as substrate {ECO:0000269|PubMed:28343923}; Vmax=50.9 umol/min/mg enzyme with D-Leu as substrate {ECO:0000269|PubMed:28343923}; Vmax=23.3 umol/min/mg enzyme with L-Met as substrate {ECO:0000269|PubMed:28343923}; Vmax=65.7 umol/min/mg enzyme with D-Met as substrate {ECO:0000269|PubMed:28343923}; Vmax=59.9 umol/min/mg enzyme with L-Phe as substrate {ECO:0000269|PubMed:28343923}; Vmax=36.4 umol/min/mg enzyme with D-Phe as substrate {ECO:0000269|PubMed:28343923}; Vmax=16.8 umol/min/mg enzyme with L-Tyr as substrate {ECO:0000269|PubMed:28343923}; Vmax=10.4 umol/min/mg enzyme with D-Tyr as substrate {ECO:0000269|PubMed:28343923}; Vmax=9.23 umol/min/mg enzyme with L-Trp as substrate {ECO:0000269|PubMed:28343923}; Vmax=1.45 umol/min/mg enzyme with D-Trp as substrate {ECO:0000269|PubMed:28343923};
| null |
BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 6.5-7.5. {ECO:0000269|PubMed:28343923};
|
BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Shows extremely high thermostability. Retains full activity after incubation at 80 degrees Celsius for at least 2 hours. {ECO:0000269|PubMed:28343923};
|
FUNCTION: Amino-acid racemase able to utilize a broad range of substrates (PubMed:25963389). Can use Met, Leu, Phe, Ala, Ser, Ile, Val, Trp, Tyr and Thr (PubMed:25963389, PubMed:28343923). Is mostly active with Phe, Leu, Met and Tyr, followed by Ile, Thr and Trp. Has weaker activity with Val, Ser and Ala (PubMed:28343923). Shows no activity toward Pro, Asp, Glu, Arg, His, Gln and Asn (PubMed:25963389, PubMed:28343923). {ECO:0000269|PubMed:25963389, ECO:0000269|PubMed:28343923}.
|
Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3)
|
O58038
|
TTUA_PYRHO
|
MKCKFCSREAYIKIHYPKMYLCEEHFKEYFERKVSRTIERYKLLTKDERILVAVSGGKDSAVTAYVLKKLGYNIECLHINLGISGYSEKSEEYAKKQCKLIGAPLHIVRIKEILGYGIGEVKTRRPPCSYCGLTKRYIMNKFAYDNGFDAIATGHNLDDEASFLLNNILHWNTEYLAKGGPILPQQGKFIKKVKPLYEVTEREVVAYALAVGLEYIVEECPYARGATTLDMKGVLNELEEKRPGTKFNFVRGYLKKKKLFEPEIKEKEIKECKICRMPSSGDICAFCKFWGLKKEINFKVSSTDEEPFGP
|
2.8.1.-
|
COFACTOR: Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; Evidence={ECO:0000269|PubMed:28655838}; Note=Binds 1 [4Fe-4S] cluster per subunit. The cluster is chelated by three Cys residues, the fourth Fe with a free coordination site may bind a small ligand, such as exogenous sulfide, thus acting as a sulfur carrier. {ECO:0000269|PubMed:28655838}; COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:28655838};
|
tRNA wobble position uridine thiolation [GO:0002143]
|
cytosolic tRNA wobble base thiouridylase complex [GO:0002144]
|
4 iron, 4 sulfur cluster binding [GO:0051539]; ATP binding [GO:0005524]; metal ion binding [GO:0046872]; transferase activity [GO:0016740]; tRNA binding [GO:0000049]
|
PF01171;
|
3.40.50.620;
|
TtcA family, TtuA subfamily
| null | null |
CATALYTIC ACTIVITY: Reaction=5-methyluridine(54) in tRNA + ATP + hydrogen sulfide = 5-methyl-2-thiouridine(54) in tRNA + AMP + diphosphate; Xref=Rhea:RHEA:55188, Rhea:RHEA-COMP:10167, Rhea:RHEA-COMP:13344, ChEBI:CHEBI:29919, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:74447, ChEBI:CHEBI:136799, ChEBI:CHEBI:456215; Evidence={ECO:0000269|PubMed:28655838};
| null |
PATHWAY: tRNA modification. {ECO:0000269|PubMed:28655838}.
| null | null |
FUNCTION: Catalyzes the ATP-dependent 2-thiolation of 5-methyluridine residue at position 54 in the T loop of tRNAs, leading to 5-methyl-2-thiouridine (m(5)s(2)U or s(2)T) (PubMed:28655838). This modification allows thermal stabilization of tRNAs in thermophilic microorganisms, and is required for cell growth at high temperatures (By similarity). Can use free sulfide as sulfur source in vitro, which may be also the sulfur source in vivo (PubMed:28655838). {ECO:0000250|UniProtKB:Q72LF3, ECO:0000269|PubMed:28655838}.
|
Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3)
|
O58308
|
NCPPR_PYRHO
|
MGENMKKKVVIIGGGAAGMSAASRVKRLKPEWDVKVFEATEWVSHAPCGIPYVVEGLSTPDKLMYYPPEVFIKKRGIDLHLNAEVIEVDTGYVRVRENGGEKSYEWDYLVFANGASPQVPAIEGVNLKGVFTADLPPDALAIREYMEKYKVENVVIIGGGYIGIEMAEAFAAQGKNVTMIVRGERVLRRSFDKEVTDILEEKLKKHVNLRLQEITMKIEGEERVEKVVTDAGEYKAELVILATGIKPNIELAKQLGVRIGETGAIWTNEKMQTSVENVYAAGDVAETRHVITGRRVWVPLAPAGNKMGYVAGSNIAGKELHFPGVLGTAVTKFMDVEIGKTGLTEMEALKEGYDVRTAFIKASTRPHYYPGGREIWLKGVVDNETNRLLGVQVVGSDILPRIDTAAAMLMAGFTTKDAFFTDLAYAPPFAPVWDPLIVLARVLKF
|
1.8.1.-; 1.8.1.14
|
COFACTOR: Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000269|PubMed:15720393, ECO:0000269|PubMed:23530771}; Note=Binds 1 FAD per subunit. {ECO:0000269|PubMed:23530771};
| null | null |
CoA-disulfide reductase (NADP) activity [GO:0050451]; flavin adenine dinucleotide binding [GO:0050660]; NADP binding [GO:0050661]; protein disulfide isomerase activity [GO:0003756]
|
PF07992;PF02852;
|
3.50.50.60;
|
Class-III pyridine nucleotide-disulfide oxidoreductase family
| null | null |
CATALYTIC ACTIVITY: Reaction=2 CoA + NADP(+) = CoA-disulfide + H(+) + NADPH; Xref=Rhea:RHEA:14705, ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:62209; EC=1.8.1.14; Evidence={ECO:0000269|PubMed:15720393}; CATALYTIC ACTIVITY: Reaction=2 CoA + NAD(+) = CoA-disulfide + H(+) + NADH; Xref=Rhea:RHEA:14701, ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:62209; Evidence={ECO:0000269|PubMed:15720393};
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=73 uM for NADH {ECO:0000269|PubMed:15720393}; KM=20.5 uM for CoA persulfide (in the presence of NADH) {ECO:0000269|PubMed:23530771}; KM=56.2 uM for CoA persulfide (in the presence of NADPH) {ECO:0000269|PubMed:23530771}; KM=13.9 uM for NADH (in the presence of CoA persulfide) {ECO:0000269|PubMed:23530771}; KM=12.7 uM for NADPH (in the presence of CoA persulfide) {ECO:0000269|PubMed:23530771}; KM=94.9 uM for CoA polysulfide (in the presence of NADH) {ECO:0000269|PubMed:23530771}; KM=125 uM for NADH (in the presence of CoA polysulfide) {ECO:0000269|PubMed:23530771}; KM=14.1 uM for NADPH (in the presence of CoA polysulfide) {ECO:0000269|PubMed:23530771}; KM=12.3 uM for polysulfide (in the presence of NADH) {ECO:0000269|PubMed:23530771}; KM=25.1 uM for TNB persulfide (in the presence of NADH) {ECO:0000269|PubMed:23530771}; KM=129 uM for DTNB (in the presence of NADH) {ECO:0000269|PubMed:23530771}; Note=kcat is 1.11 sec(-1) with CoA persulfide as substrate (in the presence of NADH). kcat is 1.50 sec(-1) with CoA persulfide as substrate (in the presence of NADPH). kcat is 1.07 sec(-1) with NADH as substrate (in the presence of CoA persulfide). kcat is 2.08 sec(-1) with NADPH as substrate (in the presence of CoA persulfide). kcat is 6.56 sec(-1) with CoA polysulfide as substrate (in the presence of NADH). kcat is 8.86 sec(-1) with NADH as substrate (in the presence of CoA polysulfide). kcat is 16.1 sec(-1) with NADPH as substrate (in the presence of CoA polysulfide). kcat is 1.04 sec(-1) with polysulfide as substrate (in the presence of NADH). kcat is 3.37 sec(-1) with TNB persulfide as substrate (in the presence of NADH). kcat is 0.69 sec(-1) with DTNB as substrate (in the presence of NADH). {ECO:0000269|PubMed:23530771};
| null | null |
BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 85 degrees Celsius. Thermostable. {ECO:0000269|PubMed:15720393};
|
FUNCTION: Catalyzes the NAD(P)H-dependent reduction of polysulfide, CoA-polysulfides, and CoA persulfide, as well as the reduction of a range of other small persulfides, including TNB and glutathione persulfides. The likely in vivo substrates are di-, poly-, and persulfide derivatives of coenzyme A, although polysulfide itself is also efficiently reduced (PubMed:23530771). Shows coenzyme A disulfide reductase (CoADR) activity with both NADH and NADPH, with a preference for NADPH (PubMed:15720393). May also play a role in the reduction of elemental sulfur (PubMed:23530771). {ECO:0000269|PubMed:15720393, ECO:0000269|PubMed:23530771}.
|
Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3)
|
O58328
|
GLKA_PYRHO
|
MITMTNWESLYEKALDKVEASIRKVRGVLLAYNTNIDAIKYLKREDLEKRIEKVGKEEVLRYSEELPKEIETIPQLLGSILWSIKRGKAAELLVVSREVREYMRKWGWDELRMGGQVGIMANLLGGVYGIPVIAHVPQLSELQASLFLDGPIYVPTFERGELRLIHPREFRKGEEDCIHYIYEFPRNFKVLDFEAPRENRFIGAADDYNPILYVREEWIERFEEIAKRSELAIISGLHPLTQENHGKPIKLVREHLKILNDLGIRAHLEFAFTPDEVVRLEIVKLLKHFYSVGLNEVELASVVSVMGEKELAERIISKDPADPIAVIEGLLKLIKETGVKRIHFHTYGYYLALTREKGEHVRDALLFSALAAATKAMKGNIEKLSDIREGLAVPIGEQGLEVEKILEKEFSLRDGIGSIEDYQLTFIPTKVVKKPKSTVGIGDTISSSAFVSEFSLH
|
2.7.1.-; 2.7.1.147
|
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255|HAMAP-Rule:MF_00809}; Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000255|HAMAP-Rule:MF_00809};
|
glucose metabolic process [GO:0006006]; glycolytic process [GO:0006096]
|
cytoplasm [GO:0005737]
|
ADP-specific glucokinase activity [GO:0043843]; glucokinase activity [GO:0004340]; magnesium ion binding [GO:0000287]
|
PF04587;
|
3.30.1110.20;3.40.1190.20;
|
ADP-dependent glucokinase family
| null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00809}.
|
CATALYTIC ACTIVITY: Reaction=ADP + D-glucose = AMP + D-glucose 6-phosphate + H(+); Xref=Rhea:RHEA:11460, ChEBI:CHEBI:4167, ChEBI:CHEBI:15378, ChEBI:CHEBI:61548, ChEBI:CHEBI:456215, ChEBI:CHEBI:456216; EC=2.7.1.147; Evidence={ECO:0000255|HAMAP-Rule:MF_00809, ECO:0000269|PubMed:29784881}; CATALYTIC ACTIVITY: Reaction=ADP + D-glucosamine = AMP + D-glucosamine 6-phosphate + H(+); Xref=Rhea:RHEA:62084, ChEBI:CHEBI:15378, ChEBI:CHEBI:58723, ChEBI:CHEBI:58725, ChEBI:CHEBI:456215, ChEBI:CHEBI:456216; Evidence={ECO:0000255|HAMAP-Rule:MF_00809};
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.64 mM for glucose {ECO:0000269|PubMed:29784881}; KM=0.13 mM for ADP {ECO:0000269|PubMed:29784881};
|
PATHWAY: Carbohydrate degradation; glycolysis. {ECO:0000255|HAMAP-Rule:MF_00809}.
| null | null |
FUNCTION: Catalyzes the ADP-dependent phosphorylation of D-glucose to D-glucose 6-phosphate and glucosamine to glucosamine 6-phosphate. {ECO:0000255|HAMAP-Rule:MF_00809, ECO:0000269|PubMed:29784881}.
|
Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3)
|
O58389
|
TDH_PYRHO
|
MSEKMVAIMKTKPGYGAELVEVDVPKPGPGEVLIKVLATSICGTDLHIYEWNEWAQSRIKPPQIMGHEVAGEVVEIGPGVEGIEVGDYVSVETHIVCGKCYACRRGQYHVCQNTKIFGVDTDGVFAEYAVVPAQNIWKNPKSIPPEYATLQEPLGNAVDTVLAGPISGKSVLITGAGPLGLLGIAVAKASGAYPVIVSEPSDFRRELAKKVGADYVINPFEEDVVKEVMDITDGNGVDVFLEFSGAPKALEQGLQAVTPAGRVSLLGLYPGKVTIDFNNLIIFKALTIYGITGRHLWETWYTVSRLLQSGKLNLDPIITHKYKGFDKYEEAFELMRAGKTGKVVFMLK
|
1.1.1.103
|
COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000255|HAMAP-Rule:MF_00627, ECO:0000269|PubMed:15902509, ECO:0000269|PubMed:16233775}; Note=Binds 2 Zn(2+) ions per subunit. Contains one structural ion and one catalytic ion that seems to be less tightly bound at the site (PubMed:16233775). Zn(2+) can be replaced by Mn(2+) or Co(2+) to some extent (PubMed:15902509). {ECO:0000255|HAMAP-Rule:MF_00627, ECO:0000269|PubMed:15902509, ECO:0000305|PubMed:16233775};
|
L-threonine catabolic process to glycine [GO:0019518]; protein homotetramerization [GO:0051289]; threonine metabolic process [GO:0006566]
|
cytoplasm [GO:0005737]
|
amino acid binding [GO:0016597]; L-threonine 3-dehydrogenase activity [GO:0008743]; NAD+ binding [GO:0070403]; NADP+ binding [GO:0070401]; zinc ion binding [GO:0008270]
|
PF08240;PF00107;
|
3.90.180.10;3.40.50.720;
|
Zinc-containing alcohol dehydrogenase family
| null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00627}.
|
CATALYTIC ACTIVITY: Reaction=L-threonine + NAD(+) = (2S)-2-amino-3-oxobutanoate + H(+) + NADH; Xref=Rhea:RHEA:13161, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57926, ChEBI:CHEBI:57945, ChEBI:CHEBI:78948; EC=1.1.1.103; Evidence={ECO:0000255|HAMAP-Rule:MF_00627, ECO:0000269|PubMed:15902509, ECO:0000269|PubMed:16233775};
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.2 mM for L-threonine (at 50 degrees Celsius) {ECO:0000269|PubMed:15902509}; KM=0.024 mM for NAD(+) (at 50 degrees Celsius) {ECO:0000269|PubMed:15902509}; KM=0.013 mM for L-threonine (in the presence of NAD(+) as cosubstrate, at 65 degrees Celsius) {ECO:0000269|PubMed:16233775}; KM=0.01 mM for NAD(+) (at 65 degrees Celsius) {ECO:0000269|PubMed:16233775}; KM=0.447 mM for L-threonine (in the presence of NAD(+) as cosubstrate, at 65 degrees Celsius) {ECO:0000269|PubMed:16233775}; KM=0.689 mM for NADP(+) (at 65 degrees Celsius) {ECO:0000269|PubMed:16233775}; Vmax=1.75 mmol/min/mg enzyme for the NAD(+) oxidation of L-threonine (at 65 degrees Celsius) {ECO:0000269|PubMed:16233775}; Vmax=1.32 mmol/min/mg enzyme for the NADP(+) oxidation of L-threonine (at 65 degrees Celsius) {ECO:0000269|PubMed:16233775};
|
PATHWAY: Amino-acid degradation; L-threonine degradation via oxydo-reductase pathway; glycine from L-threonine: step 1/2. {ECO:0000255|HAMAP-Rule:MF_00627, ECO:0000305|PubMed:16233775}.
|
BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is around 10. Below and above pH 10, the marked decrease of activity is observed: the relative activities are 50, 22 and 55% at pH 9.5, 9.2 and 12, respectively. Is stable over a wide pH range: upon heating at 50 degrees Celsius for 20 minutes, the enzyme does not lose activity at pH 4.5-10.0. {ECO:0000269|PubMed:15902509};
|
BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 70 degrees Celsius. Extremely thermostable, the activity is not lost after incubation at 100 degrees Celsius for 20 minutes. {ECO:0000269|PubMed:15902509, ECO:0000269|PubMed:16233775};
|
FUNCTION: Catalyzes the NAD(+)-dependent oxidation of L-threonine to 2-amino-3-ketobutyrate (PubMed:15902509, PubMed:16233775). Is much less efficient when using NADP(+) instead of NAD(+) (PubMed:16233775). To a lesser extent, also catalyzes the oxidation of L-serine and DL-threo-3-phenylserine, but not that of L-allo-threonine, D-threonine and D-allo-threonine and many other L-amino acids (PubMed:15902509). {ECO:0000269|PubMed:15902509, ECO:0000269|PubMed:16233775}.
|
Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3)
|
O58440
|
NOB1_PYRHO
|
MLRNLKKTLVLDSSVFIQGIDIEGYTTPSVVEEIKDRESKIFLESLISAGKVKIAEPSKESIDRIIQVAKETGEVNELSKADIEVLALAYELKGEIFSDDYNVQNIASLLGLRFRTLKRGIKKVIKWRYVCIGCGRKFSTLPPGGVCPDCGSKVKLIPRKR
|
3.1.-.-
|
COFACTOR: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000269|PubMed:22156373}; Note=Manganese; magnesium does not support nuclease activity. {ECO:0000269|PubMed:22156373}; COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000269|PubMed:22156373}; Note=Binds 1 zinc ion per subunit. {ECO:0000269|PubMed:22156373};
|
maturation of SSU-rRNA [GO:0030490]
|
preribosome, small subunit precursor [GO:0030688]
|
magnesium ion binding [GO:0000287]; RNA endonuclease activity [GO:0004521]; rRNA binding [GO:0019843]
|
PF17146;
|
2.20.28.10;3.40.50.1010;
|
PINc/VapC protein family
| null | null | null | null | null | null | null |
FUNCTION: Toxic component of a type II toxin-antitoxin (TA) system (Potential). Processes pre-16S-rRNA at its 3' end (the D-site) to yield the mature 3' end. {ECO:0000269|PubMed:22156373, ECO:0000305}.
|
Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3)
|
O58478
|
ASRAC_PYRHO
|
MPFLPFSYYPFSLEVILMEYPKIVVKPPGPRAKELIEREKKVLSTGIGVKLFPLVPKRGFGPFIEDVDGNVFIDFLAGAAAASTGYAHPKLVKAVKEQVELIQHSMIGYTHSERAIRVAEKLVEISPIENSKVIFGLSGSDAVDMAIKVSKFSTRRPWILAFIGAYHGQTLGATSVASFQVSQKRGYSPLMPNVFWIPYPNPFRNIWGINGYEEPDELINRVLDYLEYYVFSHVVPPDEVAALFAEPIQGDAGIVVPPENFFKELKKLLEEYGILLVMDEVQTGIGRTGKWFASEWFNVKPDMIIFGKGVASGMGLSGVIGRKEIMDITSGSALLTPAANPVISAAAEATLEIIEEENLLKNALEVGEFIMGRLKEIKERFEIIGDVRGKGLMIGVEIVKENGRPDPEMTGKICWRAFELGLILPSYGMFGNVIRITPPLVLTKEVAEKALEIIERAIKDTLTGKVERKVVTWH
|
5.1.1.-; 5.1.1.1
|
COFACTOR: Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; Evidence={ECO:0000269|PubMed:30038603};
| null | null |
alanine racemase activity [GO:0008784]; identical protein binding [GO:0042802]; pyridoxal phosphate binding [GO:0030170]; serine racemase activity [GO:0030378]; transaminase activity [GO:0008483]
|
PF00202;
|
3.90.1150.10;3.40.640.10;
|
Class-III pyridoxal-phosphate-dependent aminotransferase family
| null | null |
CATALYTIC ACTIVITY: Reaction=L-alanine = D-alanine; Xref=Rhea:RHEA:20249, ChEBI:CHEBI:57416, ChEBI:CHEBI:57972; EC=5.1.1.1; Evidence={ECO:0000269|PubMed:30038603}; CATALYTIC ACTIVITY: Reaction=L-serine = D-serine; Xref=Rhea:RHEA:10980, ChEBI:CHEBI:33384, ChEBI:CHEBI:35247; Evidence={ECO:0000269|PubMed:30038603};
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=3.3 mM for L-alanine {ECO:0000269|PubMed:30038603}; KM=4.5 mM for L-serine {ECO:0000269|PubMed:30038603}; KM=5.5 mM for D-alanine {ECO:0000269|PubMed:30038603}; KM=5.9 mM for D-serine {ECO:0000269|PubMed:30038603}; Vmax=28.2 umol/min/mg enzyme with L-alanine as substrate {ECO:0000269|PubMed:30038603}; Vmax=31.4 umol/min/mg enzyme with L-serine as substrate {ECO:0000269|PubMed:30038603}; Vmax=49.5 umol/min/mg enzyme with D-alanine as substrate {ECO:0000269|PubMed:30038603}; Vmax=41.2 umol/min/mg enzyme with D-serine as substrate {ECO:0000269|PubMed:30038603};
| null |
BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 6.5-7.0. {ECO:0000269|PubMed:30038603};
|
BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Highly stable at high temperatures. {ECO:0000269|PubMed:30038603};
|
FUNCTION: Catalyzes the interconversion of L-alanine and D-alanine, and L-serine and D-serine. Has weak activity with valine and threonine. {ECO:0000269|PubMed:30038603}.
|
Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3)
|
O58523
|
TYW2_PYRHO
|
MRTQGIKPRIREILSKELPEELVKLLPKRWVRIGDVLLLPLRPELEPYKHRIAEVYAEVLGVKTVLRKGHIHGETRKPDYELLYGSDTVTVHVENGIKYKLDVAKIMFSPANVKERVRMAKVAKPDELVVDMFAGIGHLSLPIAVYGKAKVIAIEKDPYTFKFLVENIHLNKVEDRMSAYNMDNRDFPGENIADRILMGYVVRTHEFIPKALSIAKDGAIIHYHNTVPEKLMPREPFETFKRITKEYGYDVEKLNELKIKRYAPGVWHVVLDLRVFKS
|
2.5.1.114
| null |
tRNA methylation [GO:0030488]; tRNA modification [GO:0006400]; wybutosine biosynthetic process [GO:0031591]
|
cytoplasm [GO:0005737]
|
transferase activity, transferring alkyl or aryl (other than methyl) groups [GO:0016765]; tRNA 4-demethylwyosine alpha-amino-alpha-carboxypropyltransferase activity [GO:0102522]; tRNA methyltransferase activity [GO:0008175]
|
PF02475;
|
3.30.300.110;3.40.50.150;
|
Class I-like SAM-binding methyltransferase superfamily, TRM5/TYW2 family
| null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01922}.
|
CATALYTIC ACTIVITY: Reaction=4-demethylwyosine(37) in tRNA(Phe) + S-adenosyl-L-methionine = 4-demethyl-7-[(3S)-3-amino-3-carboxypropyl]wyosine(37) in tRNA(Phe) + H(+) + S-methyl-5'-thioadenosine; Xref=Rhea:RHEA:36355, Rhea:RHEA-COMP:10164, Rhea:RHEA-COMP:10378, ChEBI:CHEBI:15378, ChEBI:CHEBI:17509, ChEBI:CHEBI:59789, ChEBI:CHEBI:64315, ChEBI:CHEBI:73550; EC=2.5.1.114; Evidence={ECO:0000255|HAMAP-Rule:MF_01922, ECO:0000269|PubMed:19717466};
| null | null | null | null |
FUNCTION: S-adenosyl-L-methionine-dependent transferase that acts as a component of the wyosine derivatives biosynthesis pathway. Catalyzes the transfer of the alpha-amino-alpha-carboxypropyl (acp) group from S-adenosyl-L-methionine to 4-demethylwyosine (imG-14), forming 7-aminocarboxypropyl-demethylwyosine (wybutosine-86) at position 37 of tRNA(Phe). {ECO:0000255|HAMAP-Rule:MF_01922, ECO:0000269|PubMed:19717466}.
|
Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3)
|
O58679
|
MFNA_PYRHO
|
MKFPRIGLPKEKVIELINEKTKKDLTFSSGKILGSMCTMPHDLAIEVYTKYIDRNLGDPGLHPGTRKIEEEVIEMISDLLHLEKGHGHIVSGGTEANILAVRAFRNLSDVEKPELILPKSAHFSFIKAGEMLGVKLVWAELNPDYTVDVRDVEAKISDNTIGIVGIAGTTGLGVVDDIPALSDLARDYGIPLHVDAAFGGFVIPFAKELGYELPDFDFKLKGVQSITIDPHKMGMAPIPAGGIVFRRKKYLKAISVLAPYLAGGKVWQATITGTRPGASVIAVWALIKHLGFEGYMRIVERAMKLSRWFAEEIKKINNAWLVREPMLNIVSFQTKNLKKVERELKSRGWGISAHRGYIRIVFMPHVTREMIEEFLKDLKEVLS
|
4.1.1.11; 4.1.1.15
|
COFACTOR: Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; Evidence={ECO:0000255|HAMAP-Rule:MF_01610, ECO:0000269|PubMed:19129626};
|
carboxylic acid metabolic process [GO:0019752]; coenzyme A biosynthetic process [GO:0015937]; sphingolipid catabolic process [GO:0030149]
| null |
aspartate 1-decarboxylase activity [GO:0004068]; glutamate decarboxylase activity [GO:0004351]; pyridoxal phosphate binding [GO:0030170]; sphinganine-1-phosphate aldolase activity [GO:0008117]; sulfinoalanine decarboxylase activity [GO:0004782]
|
PF00282;
|
3.90.1150.10;3.40.640.10;
|
Group II decarboxylase family, MfnA subfamily
| null | null |
CATALYTIC ACTIVITY: Reaction=H(+) + L-aspartate = beta-alanine + CO2; Xref=Rhea:RHEA:19497, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:29991, ChEBI:CHEBI:57966; EC=4.1.1.11; Evidence={ECO:0000255|HAMAP-Rule:MF_01610, ECO:0000269|PubMed:19129626}; CATALYTIC ACTIVITY: Reaction=H(+) + L-glutamate = 4-aminobutanoate + CO2; Xref=Rhea:RHEA:17785, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:29985, ChEBI:CHEBI:59888; EC=4.1.1.15; Evidence={ECO:0000269|PubMed:19129626}; CATALYTIC ACTIVITY: Reaction=H(+) + L-cysteate = CO2 + taurine; Xref=Rhea:RHEA:25221, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:58090, ChEBI:CHEBI:507393; Evidence={ECO:0000269|PubMed:19129626}; CATALYTIC ACTIVITY: Reaction=3-sulfino-L-alanine + H(+) = CO2 + hypotaurine; Xref=Rhea:RHEA:16877, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57853, ChEBI:CHEBI:61085; Evidence={ECO:0000269|PubMed:19129626};
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=1.2 mM for L-aspartate {ECO:0000269|PubMed:19129626}; KM=3.9 mM for L-glutamate {ECO:0000269|PubMed:19129626}; KM=2.2 mM for cysteate {ECO:0000269|PubMed:19129626}; KM=32.6 mM for cysteine sulfite {ECO:0000269|PubMed:19129626}; Note=kcat is 0.34 sec(-1) with L-aspartate as substrate. kcat is 0.26 sec(-1) with L-glutamate as substrate. kcat is 0.65 sec(-1) with cysteate as substrate. kcat is 0.03 sec(-1) with cysteine sulfite as substrate. {ECO:0000269|PubMed:19129626};
|
PATHWAY: Cofactor biosynthesis; coenzyme A biosynthesis. {ECO:0000255|HAMAP-Rule:MF_01610}.
|
BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8.0 with glutamate as substrate. {ECO:0000269|PubMed:19129626};
|
BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is higher than 97 degrees Celsius with glutamate as substrate. {ECO:0000269|PubMed:19129626};
|
FUNCTION: Catalyzes the decarboxylation of L-aspartate to produce beta-alanine, and the decarboxylation of L-glutamate to produce 4-aminobutanoate. Can also use cysteate and, to a lesser extent, cysteine sulfite (3-sulfino-L-alanine), but not L-tyrosine. Specific activities toward L-aspartate and cysteate are higher than toward L-glutamate. {ECO:0000269|PubMed:19129626}.
|
Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3)
|
O58801
|
NADK_PYRHO
|
MKFGIVARRDKEEALKLAYRVYDFLKVHGYEVVVDKETYEHFPHFKEGDVIPLDEFDVDFIVAIGGDGTILRIEHMTKKDIPILSINMGTLGFLTEVEPSDTFFALNRLIEGEYYIDERIKVRTYIDGENRVPDALNEVAILTGIPGKIIHMKYYVDGGLADEVRADGLVVSTPTGSTGYAMSAGGPFIDPRLDVILIAPLLPLPKTSVPMVIPGSSRIDIRMLTDREIILAIDGQYYEHLPPNVEITVVKSPRKTKFIRFTREIYPKYTIRIKERH
|
2.7.1.23
|
COFACTOR: Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240; Evidence={ECO:0000255|HAMAP-Rule:MF_00361, ECO:0000269|PubMed:16085824};
|
NAD metabolic process [GO:0019674]; NADP biosynthetic process [GO:0006741]; phosphorylation [GO:0016310]
|
cytoplasm [GO:0005737]
|
ATP binding [GO:0005524]; metal ion binding [GO:0046872]; NAD binding [GO:0051287]; NAD+ kinase activity [GO:0003951]
|
PF01513;PF20143;
| null |
NAD kinase family
| null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00361}.
|
CATALYTIC ACTIVITY: Reaction=ATP + NAD(+) = ADP + H(+) + NADP(+); Xref=Rhea:RHEA:18629, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:57540, ChEBI:CHEBI:58349, ChEBI:CHEBI:456216; EC=2.7.1.23; Evidence={ECO:0000255|HAMAP-Rule:MF_00361, ECO:0000269|PubMed:16085824};
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.29 mM for ATP (at pH 6 and 70 degrees Celsius) {ECO:0000269|PubMed:16085824}; KM=0.3 mM for NAD (with poly(P) as phosphoryl donor at pH 6.8 and 70 degrees Celsius) {ECO:0000269|PubMed:16085824}; KM=0.4 mM for NAD (with ATP as phosphoryl donor at pH 6.8 and 70 degrees Celsius) {ECO:0000269|PubMed:16085824};
| null |
BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 6.8. At 70 degrees Celsius for 60 minutes, the enzyme does not lose activity in a pH range of 4.0 to 10.5. {ECO:0000269|PubMed:16085824};
|
BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Extremely high thermostability. Upon heating at 95 degrees Celsius for 10 minutes the kinase activity is not lost, but about 80% of the activity is lost upon incubation at 100 degrees Celsius for 10 minutes. {ECO:0000269|PubMed:16085824};
|
FUNCTION: Involved in the regulation of the intracellular balance of NAD and NADP, and is a key enzyme in the biosynthesis of NADP. Catalyzes specifically the phosphorylation on 2'-hydroxyl of the adenosine moiety of NAD to yield NADP. It can use ATP and other nucleoside triphosphates (GTP,UTP) as well as inorganic polyphosphate (poly(P)) as a source of phosphorus. NAD is the preferred substrate for the kinase, but NADH can also be used as phosphoryl acceptor. {ECO:0000255|HAMAP-Rule:MF_00361, ECO:0000269|PubMed:16085824}.
|
Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3)
|
O58832
|
DPH2_PYRHO
|
MLHEIPKSEILKELKRIGAKRVLIQSPEGLRREAEELAGFLEENNIEVFLHGEINYGACDPADREAKLVGCDALIHLGHSYMKLPLEVPTIFVPAFARVSVVEALKENIGEIKKLGRKIIVTTTAQHIHQLKEAKEFLESEGFEVSIGRGDSRISWPGQVLGCNYSVAKVRGEGILFIGSGIFHPLGLAVATRKKVLAIDPYTKAFSWIDPERFIRKRWAQIAKAMDAKKFGVIVSIKKGQLRLAEAKRIVKLLKKHGREARLIVMNDVNYHKLEGFPFEAYVVVACPRVPLDDYGAWRKPVLTPKEVEILLGLREEYEFDEILGGPRESDEPFGISIHSTR
|
2.5.1.108
|
COFACTOR: Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; Evidence={ECO:0000269|PubMed:20559380}; Note=Binds 1 [4Fe-4S] cluster per subunit. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine. {ECO:0000269|PubMed:20559380};
|
protein histidyl modification to diphthamide [GO:0017183]; S-adenosylmethionine catabolic process [GO:0050843]
| null |
2-(3-amino-3-carboxypropyl)histidine synthase activity [GO:0090560]; 4 iron, 4 sulfur cluster binding [GO:0051539]; metal ion binding [GO:0046872]; transferase activity, transferring alkyl or aryl (other than methyl) groups [GO:0016765]
|
PF01866;
|
3.40.50.11840;3.40.50.11850;3.40.50.11860;
|
DPH1/DPH2 family
| null | null |
CATALYTIC ACTIVITY: Reaction=L-histidyl-[translation elongation factor 2] + S-adenosyl-L-methionine = 2-[(3S)-amino-3-carboxypropyl]-L-histidyl-[translation elongation factor 2] + H(+) + S-methyl-5'-thioadenosine; Xref=Rhea:RHEA:36783, Rhea:RHEA-COMP:9748, Rhea:RHEA-COMP:9749, ChEBI:CHEBI:15378, ChEBI:CHEBI:17509, ChEBI:CHEBI:29979, ChEBI:CHEBI:59789, ChEBI:CHEBI:73995; EC=2.5.1.108; Evidence={ECO:0000269|PubMed:20559380};
| null |
PATHWAY: Protein modification; peptidyl-diphthamide biosynthesis. {ECO:0000269|PubMed:20559380}.
| null | null |
FUNCTION: Catalyzes the first step of diphthamide biosynthesis, i.e. the transfer of the 3-amino-3-carboxypropyl group from S-adenosyl-L-methionine (SAM) to the C2 position of the imidazole ring of the target histidine residue in translation elongation factor 2 (EF-2). {ECO:0000269|PubMed:20559380}.
|
Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3)
|
O58843
|
ATGT_PYRHO
|
MSRGDKMLKFEIKARDGAGRIGKLEVNGKKIETPAIMPVVNPKQMVVEPKELEKMGFEIIITNSYIIYKDEELRRKALELGIHRMLDYNGIIEVDSGSFQLMKYGSIEVSNREIIEFQHRIGVDIGTFLDIPTPPDAPREQAVKELEITLSRAREAEEIKEIPMNATIQGSTYTDLRRYAARRLSSMNFEIHPIGGVVPLLESYRFRDVVDIVISSKMALRPDRPVHLFGAGHPIVFALAVAMGVDLFDSASYALYAKDDRYMTPEGTKRLDELDYFPCSCPVCSKYTPQELREMPKEERTRLLALHNLWVIKEEIKRVKQAIKEGELWRLVDERARSHPKLYSAYKRLLEHYTFLEEFEPITKKSALFKISNESLRWPVVRRAKERAKSINERFGELVEHPIFGRVSRYLSLTYPFAQSEAEDDFKIEKPTKEDAIKYVMAIAEYQFGEGASRAFDDAKVELSKTGMPRQVKVNGKRLATVRADDGLLTLGIEGAKRLHRVLPYPRMRVVVNKEAEPFARKGKDVFAKFVIFADPGIRPYDEVLVVNENDELLATGQALLSGREMIVFQYGRAVKVRKGVE
|
2.4.2.48
|
COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000269|PubMed:12054814, ECO:0000269|PubMed:12732145}; Note=Binds 1 zinc ion per subunit. {ECO:0000269|PubMed:12054814, ECO:0000269|PubMed:12732145};
|
queuosine biosynthetic process [GO:0008616]; tRNA wobble guanine modification [GO:0002099]
|
cytosol [GO:0005829]
|
metal ion binding [GO:0046872]; pentosyltransferase activity [GO:0016763]; RNA binding [GO:0003723]
|
PF01472;PF01702;PF14809;PF14810;
|
3.90.1020.10;3.10.450.90;2.30.130.10;3.20.20.105;
|
Archaeosine tRNA-ribosyltransferase family
| null | null |
CATALYTIC ACTIVITY: Reaction=7-cyano-7-deazaguanine + guanosine(15) in tRNA = 7-cyano-7-carbaguanosine(15) in tRNA + guanine; Xref=Rhea:RHEA:43164, Rhea:RHEA-COMP:10371, Rhea:RHEA-COMP:10372, ChEBI:CHEBI:16235, ChEBI:CHEBI:45075, ChEBI:CHEBI:74269, ChEBI:CHEBI:82850; EC=2.4.2.48;
| null |
PATHWAY: tRNA modification; archaeosine-tRNA biosynthesis.
| null | null |
FUNCTION: Exchanges the guanine residue with 7-cyano-7-deazaguanine (preQ0) at position 15 in the dihydrouridine loop (D-loop) of archaeal tRNAs. {ECO:0000269|PubMed:12054814}.
|
Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3)
|
O58966
|
TDXH_PYRHO
|
MVVIGEKFPEVEVKTTHGVIKLPDYFTKQGKWFILFSHPADFTPVCTTEFYGMQKRVEEFRKLGVEPIGLSVDQVFSHIKWIEWIKDNLSVEIDFPVIADDRGELAEKLGMIPSGATITARAVFVVDDKGIIRAIVYYPAEVGRDWDEILRLVKALKISTEKGVALPHKWPNNELIGDKVIVPPASTIEEKKQREEAKAKGEIECYDWWFCYKKLE
|
1.11.1.24
| null |
cell redox homeostasis [GO:0045454]; cellular response to oxygen levels [GO:0071453]; cellular response to stress [GO:0033554]; hydrogen peroxide catabolic process [GO:0042744]; response to oxidative stress [GO:0006979]
|
cytosol [GO:0005829]
|
antioxidant activity [GO:0016209]; peroxiredoxin activity [GO:0051920]; thioredoxin peroxidase activity [GO:0008379]
|
PF10417;PF00578;
|
3.40.30.10;
|
Peroxiredoxin family, Prx6 subfamily
| null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00401}.
|
CATALYTIC ACTIVITY: Reaction=[thioredoxin]-dithiol + a hydroperoxide = [thioredoxin]-disulfide + an alcohol + H2O; Xref=Rhea:RHEA:62620, Rhea:RHEA-COMP:10698, Rhea:RHEA-COMP:10700, ChEBI:CHEBI:15377, ChEBI:CHEBI:29950, ChEBI:CHEBI:30879, ChEBI:CHEBI:35924, ChEBI:CHEBI:50058; EC=1.11.1.24; Evidence={ECO:0000255|HAMAP-Rule:MF_00401, ECO:0000269|PubMed:12944367, ECO:0000269|PubMed:15625325};
| null | null |
BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 4.8. {ECO:0000269|PubMed:15625325};
|
BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Thermostable. Retains full activity after 20 minutes at 90 degrees Celsius and 75 % of its initial activity after 20 minutes at 100 degrees Celsius. {ECO:0000269|PubMed:15625325};
|
FUNCTION: Thiol-specific peroxidase that catalyzes the reduction of hydrogen peroxide and organic hydroperoxides to water and alcohols, respectively. Plays a role in cell protection against oxidative stress by detoxifying peroxides. {ECO:0000255|HAMAP-Rule:MF_00401, ECO:0000269|PubMed:12944367, ECO:0000269|PubMed:15625325}.
|
Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3)
|
O59010
|
GLT_PYRHO
|
MGLYRKYIEYPVLQKILIGLILGAIVGLILGHYGYADAVKTYVKPFGDLFVRLLKMLVMPIVFASLVVGAASISPARLGRVGVKIVVYYLLTSAFAVTLGIIMARLFNPGAGIHLAVGGQQFQPKQAPPLVKILLDIVPTNPFGALANGQVLPTIFFAIILGIAITYLMNSENEKVRKSAETLLDAINGLAEAMYKIVNGVMQYAPIGVFALIAYVMAEQGVKVVGELAKVTAAVYVGLTLQILLVYFVLLKIYGIDPISFIKKAKDAMLTAFVTRSSSGTLPVTMRVAKEMGISEGIYSFTLPLGATINMDGTALYQGVCTFFIANALGSHLTVGQQLTIVLTAVLASIGTAGVPGAGAIMLAMVLESVGLPLTDPNVAAAYAMILGIDAILDMGRTMVNVTGDLTGTAIVAKTEGELEKGVIA
| null | null |
chloride transmembrane transport [GO:1902476]; L-aspartate import across plasma membrane [GO:0140009]; L-aspartate transmembrane transport [GO:0070778]; protein homotrimerization [GO:0070207]
|
plasma membrane [GO:0005886]
|
amino acid:sodium symporter activity [GO:0005283]; chloride transmembrane transporter activity [GO:0015108]; identical protein binding [GO:0042802]; L-aspartate transmembrane transporter activity [GO:0015183]; metal ion binding [GO:0046872]
|
PF00375;
|
1.10.3860.10;
|
Dicarboxylate/amino acid:cation symporter (DAACS) (TC 2.A.23) family
| null |
SUBCELLULAR LOCATION: Cell membrane {ECO:0000305|PubMed:15483603, ECO:0000305|PubMed:17230192, ECO:0000305|PubMed:17435767, ECO:0000305|PubMed:19380583, ECO:0000305|PubMed:28137870, ECO:0000305|Ref.11}; Multi-pass membrane protein {ECO:0000269|PubMed:15483603, ECO:0000269|PubMed:17230192, ECO:0000269|PubMed:19924125, ECO:0000269|PubMed:22343718, ECO:0000269|PubMed:23563139, ECO:0000269|PubMed:24842876, ECO:0000269|PubMed:28137870, ECO:0000269|Ref.11}.
| null |
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=120 nM for L-aspartate transport {ECO:0000269|PubMed:19380583}; Vmax=3.7 nmol/min/mg enzyme {ECO:0000269|PubMed:19380583};
| null | null | null |
FUNCTION: Sodium-dependent, high-affinity amino acid transporter that mediates aspartate uptake (PubMed:17230192, PubMed:17435767, PubMed:19380583, Ref.11). Has only very low glutamate transport activity (PubMed:17230192, PubMed:19380583). Functions as a symporter that transports one amino acid molecule together with two or three Na(+) ions, resulting in electrogenic transport (PubMed:17435767, PubMed:19380583, Ref.11). Na(+) binding enhances the affinity for aspartate (PubMed:19380583, Ref.11). Mediates Cl(-) flux that is not coupled to amino acid transport; this avoids the accumulation of negative charges due to aspartate and Na(+) symport (PubMed:17435767). In contrast to mammalian homologs, transport does not depend on pH or K(+) ions (PubMed:19380583). {ECO:0000269|PubMed:17230192, ECO:0000269|PubMed:17435767, ECO:0000269|PubMed:19380583, ECO:0000269|Ref.11}.
|
Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3)
|
O59179
|
STOPP_PYRHO
|
MRRILLSMIVLIFLASPILAKNIVYVAQIKGQITSYTYDQFDRYITIAEQDNAEAIIIELDTPGGRADAMMNIVQRIQQSKIPVIIYVYPPGASAASAGTYIALGSHLIAMAPGTSIGACRPILGYSQNGSIIEAPPKITNYFIAYIKSLAQESGRNATIAEEFITKDLSLTPEEALKYGVIEVVARDINELLKKSNGMKTKIPVNGRYVTLNFTNVEVRYLAPSFKDKLISYITDPNVAYLLLTLGIWALIIGFLTPGWHVPETVGAIMIILAIIGFGYFGYNSAGILLIIVAMLFFIAEALTPTFGLFTVAGLITFIIGGILLFGGGEEYLVRKEVFSQLRILIITVGAILAAFFAFGMAAVIRAHKKKARTGKEEMIGLIGTVVEELNPEGMIKVRGELWKARSKFNGKIEKGEKVRVVDMDGLTLIVVRERKEGGEK
|
3.4.21.-
| null |
proteolysis [GO:0006508]
|
plasma membrane [GO:0005886]
|
serine-type peptidase activity [GO:0008236]
|
PF00574;PF01957;
|
2.40.50.140;
|
Peptidase S14 family
| null |
SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
| null | null | null |
BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 5-6. {ECO:0000269|PubMed:15611110};
|
BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is above 90 degrees Celsius. {ECO:0000269|PubMed:15611110};
|
FUNCTION: Protease that cleaves its substrates preferentially near hydrophobic or aromatic amino acid residues. Can degrade casein and the stomatin homolog PH1511 (in vitro). {ECO:0000269|PubMed:15611110, ECO:0000269|PubMed:16574150, ECO:0000269|PubMed:24121343}.
|
Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3)
|
O59196
|
TET_PYRHO
|
MEVRNMVDYELLKKVVEAPGVSGYEFLGIRDVVIEEIKDYVDEVKVDKLGNVIAHKKGEGPKVMIAAHMDQIGLMVTHIEKNGFLRVAPIGGVDPKTLIAQRFKVWIDKGKFIYGVGASVPPHIQKPEDRKKAPDWDQIFIDIGAESKEEAEDMGVKIGTVITWDGRLERLGKHRFVSIAFDDRIAVYTILEVAKQLKDAKADVYFVATVQEEVGLRGARTSAFGIEPDYGFAIDVTIAADIPGTPEHKQVTHLGKGTAIKIMDRSVICHPTIVRWLEELAKKHEIPYQLEILLGGGTDAGAIHLTKAGVPTGALSVPARYIHSNTEVVDERDVDATVELMTKALENIHELKI
|
3.4.11.-
|
COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000269|PubMed:15375159, ECO:0000269|PubMed:15713475, ECO:0000269|PubMed:15736957}; Name=Co(2+); Xref=ChEBI:CHEBI:48828; Evidence={ECO:0000269|PubMed:15375159, ECO:0000269|PubMed:15713475, ECO:0000269|PubMed:15736957}; Note=Binds 2 Zn(2+) ions per subunit. Can also use Co(2+). {ECO:0000269|PubMed:15375159, ECO:0000269|PubMed:15713475, ECO:0000269|PubMed:15736957};
|
proteolysis [GO:0006508]
| null |
aminopeptidase activity [GO:0004177]; metal ion binding [GO:0046872]; metallopeptidase activity [GO:0008237]
|
PF05343;
|
2.40.30.40;3.40.630.10;
|
Peptidase M42 family
| null | null | null | null | null |
BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.5 with Leu-pNA as substrate. Strong activity is still detectable at pH 6 and 9. {ECO:0000269|PubMed:15736957};
|
BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 100 degrees Celsius over a broad pH array. At temperatures lower than 70 degrees Celsius, less than 10% of the maximum activity is detected. Highly thermostable. Shows half-lives of 24.8 minutes and 10.03 hours when incubated at 100 and 80 degrees Celsius, respectively. {ECO:0000269|PubMed:15736957};
|
FUNCTION: Functions as an aminopeptidase, with a clear preference for leucine as the N-terminal amino acid. However, can also cleave moderately long polypeptide substrates of various compositions in a fairly unspecific manner. Has neither carboxypeptidase nor endoproteolytic activities, and it is devoid of N-terminal deblocking activity. Is involved in protein degradation, performing degradation of oligopeptides produced by the proteasome into single amino acids. {ECO:0000269|PubMed:15375159, ECO:0000269|PubMed:15713475, ECO:0000269|PubMed:15736957}.
|
Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3)
|
O59245
|
RTCB_PYRHO
|
MVVPLKRIDKIRWEIPKFDKRMRVPGRVYADEVLLEKMKNDRTLEQATNVAMLPGIYKYSIVMPDGHQGYGFPIGGVAAFDVKEGVISPGGIGYDINCLAPGTRVLTEHGYWLKIEEMPEKFKLQRLRVYNIEEGHNDFSKVVFVAEREVGSEEKAIRIVTESGKVIEGSEDHPVLTPEGYVYLRNVKEGDYILVYPFEGVPYEEKKGVILDESAFEGEDPQVVKFLRERNLIPLQWKDPKVGILARILGFALANGYISENDNLTFHGKEEVLREVRKDLEELGIEAIVAEEDKLKVTSREFAFLLEKLGMAHDSIPEWIIEGPLWIKRNFLAGLFGANGSIVEFKGDVPLPITLTHSRELLNDVSRILEGFKVRAKIKMGKNGSYQLVIEDEDSIRNFLGRINYEYDPEKKARGLIAYAYLKFKELMKGNLMTFEEFARDRGYEGGFVAEKVIEVKSVKPEYDKFYDIGVYHSAHNFIANGIVVHNCGVRLIRTNLTEKEVRPRIKQLVDTLFKNVPSGVGSQGRIKLHWTQIDDVLVDGAKWAVDNGYGWERDLERLEEGGRMEGADPEAVSQRAKQRGAPQLGSLGSGNHFLEVQVVDKIFDPEVAKAYGLFEGQVVVMVHTGSRGLGHQVASDYLRIMERAIRKYRIPWPDRELVSVPFQSEEGQRYFSAMKAAANFAWANRQMITHWVRESFQEVFKQDPEGDLGMDIVYDVAHNIGKVEEHEVDGKRVKVIVHRKGATRAFPPGHEAVPRLYRDVGQPVLIPGSMGTASYILAGTEGAMKETFGSTCHGAGRVLSRKAATRQYRGDRIRQELLNRGIYVRAASMRVVAEEAPGAYKNVDNVVKVVSEAGIAKLVARMRPIGVAKG
|
3.1.-.-; 6.5.1.8
|
COFACTOR: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000269|PubMed:22320833, ECO:0000269|PubMed:22949672, ECO:0000269|PubMed:23560983}; Note=Binds 2 manganese ions per subunit. {ECO:0000269|PubMed:22949672, ECO:0000269|PubMed:23560983};
|
intein-mediated protein splicing [GO:0016539]; intron homing [GO:0006314]; RNA splicing, via endonucleolytic cleavage and ligation [GO:0000394]; tRNA exon ligation utilizing 2',3' cyclic phosphate of 5'-exon as source of linkage phosphate [GO:0000971]
|
tRNA-splicing ligase complex [GO:0072669]
|
DNA binding [GO:0003677]; endonuclease activity [GO:0004519]; GMP binding [GO:0019002]; GTP binding [GO:0005525]; manganese ion binding [GO:0030145]; RNA ligase (ATP) activity [GO:0003972]
|
PF14890;PF14528;PF01139;
|
3.10.28.10;3.90.1860.10;
|
RtcB family
|
PTM: This protein undergoes a protein self splicing that involves a post-translational excision of the intervening region (intein) followed by peptide ligation. {ECO:0000305}.
| null |
CATALYTIC ACTIVITY: Reaction=a 3'-end 3'-phospho-ribonucleotide-RNA + a 5'-end dephospho-ribonucleoside-RNA + GTP = a ribonucleotidyl-ribonucleotide-RNA + diphosphate + GMP; Xref=Rhea:RHEA:68076, Rhea:RHEA-COMP:10463, Rhea:RHEA-COMP:13936, Rhea:RHEA-COMP:17355, ChEBI:CHEBI:33019, ChEBI:CHEBI:37565, ChEBI:CHEBI:58115, ChEBI:CHEBI:83062, ChEBI:CHEBI:138284, ChEBI:CHEBI:173118; EC=6.5.1.8; Evidence={ECO:0000269|PubMed:22320833, ECO:0000269|PubMed:22949672}; CATALYTIC ACTIVITY: Reaction=a 3'-end 2',3'-cyclophospho-ribonucleotide-RNA + a 5'-end dephospho-ribonucleoside-RNA + GTP + H2O = a ribonucleotidyl-ribonucleotide-RNA + diphosphate + GMP + H(+); Xref=Rhea:RHEA:68080, Rhea:RHEA-COMP:10464, Rhea:RHEA-COMP:13936, Rhea:RHEA-COMP:17355, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019, ChEBI:CHEBI:37565, ChEBI:CHEBI:58115, ChEBI:CHEBI:83064, ChEBI:CHEBI:138284, ChEBI:CHEBI:173118; EC=6.5.1.8; Evidence={ECO:0000269|PubMed:22320833};
| null | null | null | null |
FUNCTION: Essential for tRNA splicing and maturation (Probable). Acts by directly joining spliced tRNA halves to mature-sized tRNAs (PubMed:22320833, PubMed:22949672). Joins RNA with 2',3'-cyclic-phosphate or 3'-phosphate ends to RNA with 5'-hydroxy ends (PubMed:22320833, PubMed:22949672). {ECO:0000269|PubMed:22320833, ECO:0000269|PubMed:22949672, ECO:0000305|PubMed:22320833}.
|
Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3)
|
O59248
|
RNP4_PYRHO
|
MVDIVKRRDWEKKEKKKIAIERIDTLFTLAERVARYSPDLAKRYVELALEIQKKAKVKIPRKWKRRYCKRCHTFLIPGVNARVRLRTKRMPHVVITCLECGYIMRYPYLREVKQKRKKAT
|
3.1.26.5
|
COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000255|HAMAP-Rule:MF_00757, ECO:0000269|PubMed:16142906, ECO:0000269|PubMed:18929577}; Note=Binds 1 zinc ion per subunit. {ECO:0000255|HAMAP-Rule:MF_00757, ECO:0000269|PubMed:16142906, ECO:0000269|PubMed:18929577};
|
tRNA 5'-leader removal [GO:0001682]
|
cytoplasm [GO:0005737]; ribonuclease P complex [GO:0030677]
|
ribonuclease P activity [GO:0004526]; zinc ion binding [GO:0008270]
|
PF04032;
|
6.20.50.20;1.20.5.420;
|
Eukaryotic/archaeal RNase P protein component 4 family
| null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00757}.
|
CATALYTIC ACTIVITY: Reaction=Endonucleolytic cleavage of RNA, removing 5'-extranucleotides from tRNA precursor.; EC=3.1.26.5; Evidence={ECO:0000255|HAMAP-Rule:MF_00757};
| null | null | null |
BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 70 degrees Celsius. {ECO:0000269|PubMed:12810070, ECO:0000269|PubMed:16574071};
|
FUNCTION: Part of ribonuclease P, a protein complex that generates mature tRNA molecules by cleaving their 5'-ends. Binds RNase P RNA. {ECO:0000255|HAMAP-Rule:MF_00757, ECO:0000269|PubMed:12810070, ECO:0000269|PubMed:16142906, ECO:0000269|PubMed:16574071, ECO:0000269|PubMed:16829535, ECO:0000269|PubMed:18929577}.
|
Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3)
|
O59272
|
D89S1_PYRHO
|
MKVQYECLTCMANQCQRIVEMATQDMDIRRRAMILAAKLLAKEYNENAIPAIAGSLIFLELYKFLGNDDPFIEYKLKSEEMARKVADIIKRKLKLDFELAVKLAIIGNVIDFSVGFSPEDLEEEVEKMLKDKLYIDDSKELFEEVKRAENILYITDNVGEHYFDAILIEKIREISNAEVYIAGKEGPIINDATVEDLKRAGLEKLGKVISTGTRIVGVPLKLVSREFMEAFNKADVIIAKGQGNFETLSEINDSRIFFLLKAKCPAVARELKVPKGALVCMRNKFKL
|
3.1.3.-
|
COFACTOR: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000269|PubMed:27322068}; Name=Ni(2+); Xref=ChEBI:CHEBI:49786; Evidence={ECO:0000269|PubMed:27322068}; Note=Phosphatase activity is strongly promoted by several divalent cation ions but it is suggested that Mn(2+) and possibly Ni(2+) represent biologically relevant metal ion cofactors for damage-control phosphatase activity (PubMed:27322068). {ECO:0000269|PubMed:27322068}; COFACTOR: Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135; Evidence={ECO:0000269|PubMed:27322068}; Note=The [2Fe-2S] cluster does not seem to be directly involved in catalysis (PubMed:27322068). {ECO:0000269|PubMed:27322068};
| null | null |
hydrolase activity [GO:0016787]; metal ion binding [GO:0046872]
|
PF01937;
|
1.10.8.380;1.10.285.20;3.40.50.10880;
|
Damage-control phosphatase family, Nucleotides phosphatase I subfamily
| null | null | null |
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=110 uM for p-nitrophenylphosphate {ECO:0000269|PubMed:27322068}; KM=600 uM for 8-oxo-2'-deoxyguanosine-5'-triphosphate {ECO:0000269|PubMed:27322068}; KM=420 uM for adenosine-5'-diphosphate {ECO:0000269|PubMed:27322068}; KM=1.9 uM for Zn(2+) {ECO:0000269|PubMed:27322068}; KM=4.6 uM for Ni(2+) {ECO:0000269|PubMed:27322068}; Note=kcat is 1.00 sec(-1) with p-nitrophenylphosphate as substrate. kcat is 0.20 sec(-1) with adenosine-5'-diphosphate as substrate. kcat is 0.12 sec(-1) with 8-oxo-2'-deoxyguanosine-5'-triphosphatee as substrate. {ECO:0000269|PubMed:27322068};
| null | null | null |
FUNCTION: Metal-dependent phosphatase with probable damage-control functions (PubMed:27322068). Shows phosphatase activity against p-nitrophenyl phosphate (pNPP), but natural substrates have not been identified yet (PubMed:27322068). Low phosphatase activity against 8-oxo nucleotides suggests that it could hydrolyze oxidatively damaged purine nucleotides or their biosynthetic intermediates (PubMed:27322068). {ECO:0000269|PubMed:27322068}.
|
Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3)
|
O59425
|
RNP1_PYRHO
|
MRRNSKERKNRATRRSQGSYQEIIGRTWIFRGAHRGRVTRRNIIWHELIGLRVRIVGSTHPAFVGIEGYVIDETRNMLVIAGDRIWKVPKDVCIFEFEADDGTKIKIPGERLVGRPEMRLKKRWKKW
|
3.1.26.5
| null |
tRNA 5'-leader removal [GO:0001682]
|
cytoplasm [GO:0005737]; ribonuclease P complex [GO:0030677]
|
ribonuclease P activity [GO:0004526]; RNA binding [GO:0003723]
|
PF01868;
|
2.30.30.210;
|
Eukaryotic/archaeal RNase P protein component 1 family
| null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00754}.
|
CATALYTIC ACTIVITY: Reaction=Endonucleolytic cleavage of RNA, removing 5'-extranucleotides from tRNA precursor.; EC=3.1.26.5; Evidence={ECO:0000255|HAMAP-Rule:MF_00754};
| null | null | null |
BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 70 degrees Celsius. {ECO:0000269|PubMed:12810070, ECO:0000269|PubMed:16574071};
|
FUNCTION: Part of ribonuclease P (RNase P), a protein complex that generates mature tRNA molecules by cleaving their 5'-ends. Binds RNase P RNA. {ECO:0000269|PubMed:12810070, ECO:0000269|PubMed:16574071, ECO:0000269|PubMed:16829535, ECO:0000269|PubMed:18929577}.
|
Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3)
|
O59543
|
RNP3_PYRHO
|
MVGGGGVKFIEMDIRDKEAYELAKEWFDEVVVSIKFNEEVDKEKLREARKEYGKVAILLSNPKPSLVRDTVQKFKSYLIYVESNDLRVIRYSIEKGVDAIISPWVNRKDPGIDHVLAKLMVKKNVALGFSLRPLLYSNPYERANLLRFMMKAWKLVEKYKVRRFLTSSAQEKWDVRYPRDLISLGVVIGMEIPQAKASISMYPEIILKRLKY
|
3.1.26.5
| null |
tRNA 5'-leader removal [GO:0001682]
|
cytoplasm [GO:0005737]; ribonuclease P complex [GO:0030677]
|
ribonuclease P activity [GO:0004526]
|
PF01876;
|
3.20.20.140;
|
Eukaryotic/archaeal RNase P protein component 3 family
| null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00756}.
|
CATALYTIC ACTIVITY: Reaction=Endonucleolytic cleavage of RNA, removing 5'-extranucleotides from tRNA precursor.; EC=3.1.26.5; Evidence={ECO:0000255|HAMAP-Rule:MF_00756};
| null | null | null |
BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 70 degrees Celsius. {ECO:0000269|PubMed:12810070, ECO:0000269|PubMed:16574071};
|
FUNCTION: Part of ribonuclease P, a protein complex that generates mature tRNA molecules by cleaving their 5'-ends. Not absolutely essential for activity in vitro, however it strongly stimulates activity. Binds RNase P RNA. {ECO:0000255|HAMAP-Rule:MF_00756, ECO:0000269|PubMed:12810070, ECO:0000269|PubMed:16574071, ECO:0000269|PubMed:16829535}.
|
Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3)
|
O59651
|
KATG2_HALMA
|
MAETPNSDMSGATGGRSKRPKSNQDWWPSKLNLEILDQNARDVGPVEDDFDYAEEFQKLDLEAVKSDLEELMTSSQDWWPADYGHYGPLFIRMAWHSAGTYRTADGRGGAAGGRQRFAPINSWPDNANLDKARRLLLPIKQKYGQKISWADLMILAGNVAIESMGFKTFGYAGGREDAFEEDKAVNWGPEDEFETQERFDEPGEIQEGLGASVMGLIYVNPEGPDGNPDPEASAKNIRQTFDRMAMNDKETAALIAGGHTFGKVHGADDPEENLGPEPEAAPIEQQGLGWQNKNGNSKGGEMITSGIEGPWTQSPTEWDMGYINNLLDYEWEPEKGPGGAWQWAPKSEELKNSVPDAHDPDEKQTPMMLTTDIALKRDPDYREVMETFQENPMEFGMNFAKAWYKLTHRDMGPPERFLGPEVPDEEMIWQDPLPDADYDLIGDEEIAELKEEILDSDLSVSQLVKTAWASASTYRDSDKRGGANGARLRLEPQKNWEVNEPEQLETVLGTLENIQTEFNDSRSDGTQVSLADLIVLGGNAAVEQAAANAGYDVEIPFEPGRVDAGPEHTDAPSFDALKPKVDGVRNYIQDDITRPAEEVLVDNADLLNLTASELTALIGGMRSIGANYQDTDLGVFTDEPETLTNDFFVNLLDMGTEWEPAADSEHRYKGLDRDTGEVKWEATRIDLIFGSNDRLRAISEVYGSADAEKKLVHDFVDTWSKVMKLDRFDLE
|
1.11.1.21
|
COFACTOR: Name=heme b; Xref=ChEBI:CHEBI:60344; Note=Binds 1 heme b (iron(II)-protoporphyrin IX) group per subunit.;
|
cellular response to hydrogen peroxide [GO:0070301]; hydrogen peroxide catabolic process [GO:0042744]
|
cytosol [GO:0005829]
|
catalase activity [GO:0004096]; heme binding [GO:0020037]; metal ion binding [GO:0046872]
|
PF00141;
|
1.10.520.10;1.10.420.10;
|
Peroxidase family, Peroxidase/catalase subfamily
|
PTM: Formation of the three residue Trp-Tyr-Met cross-link is important for the catalase, but not the peroxidase activity of the enzyme. {ECO:0000255|HAMAP-Rule:MF_01961}.
| null |
CATALYTIC ACTIVITY: Reaction=AH2 + H2O2 = A + 2 H2O; Xref=Rhea:RHEA:30275, ChEBI:CHEBI:13193, ChEBI:CHEBI:15377, ChEBI:CHEBI:16240, ChEBI:CHEBI:17499; EC=1.11.1.21; Evidence={ECO:0000255|HAMAP-Rule:MF_01961}; CATALYTIC ACTIVITY: Reaction=2 H2O2 = 2 H2O + O2; Xref=Rhea:RHEA:20309, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240; EC=1.11.1.21; Evidence={ECO:0000255|HAMAP-Rule:MF_01961};
| null | null | null | null |
FUNCTION: Bifunctional enzyme with both catalase and broad-spectrum peroxidase activity. {ECO:0000255|HAMAP-Rule:MF_01961}.
|
Haloarcula marismortui (strain ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809) (Halobacterium marismortui)
|
O59666
|
ATU2_SCHPO
|
MYTTTLSVQGMTCTSCVASIQSMLEGVEGIEQFTISLLLERAIAVHDPSIISPDQIAEKIEDCGFDASVISSTEGEHGVMANYLLLSPMQAEQWTKVHNHINELQGVLSVNCSSSPDAAIRVIYDSEITGPRSIMKEILSMGVKCTFQPVDSSTSRILSLQRGSQIRVWKIRFIISISFSLAVMFLPQIFDSCDSMRAAFLVPHYFGICAGHIISLVLSLPVQFGVGRVYYSAAYHALKRGTANMDVLVSLGSTVAFAASIFFMILYSARHADNPAPIFFDTADMLLTFVTLGRYLESKAKGSTSAALSQLLSLAPSSATIIEDNEQIEILADLIERGDLILVKPGEIIPVDGTVVEGSSYVDESSVSGEPVPVHKTIDDELLSGTANGNGRLLVKATKSPRESQLAVIVDLVQRAQISHAPIQQFADRVAGIFVPVIVALSISTFTFWFLFTKYSSKYPSVFDDPMGKFAVCLKLTISVVVVACPCALGLSTPTAVMVGTGVGALNGIIIKGGEILERLNQVDTVVFDKTGTLTVGKLSVTDISIVDNLEELLDIPKNIFWAFVKASESSSEHPIGKAITEKASEFTDVSEIGIESFNAVPGEGVDVVLRWKERTFHALLGNSLLLEHNNVSIPDDFDSKLKLSSSSGLTCVRIAIDGQFVGFLGCMDQVRPDSYQTVSALKQLGKKVCLLTGDQKATARRVAQGLEIDFSDVYAEAVPSQKAEIIQKLKDQKHCVAMVGDGINDSPSLVLADVGIAPINGSGIALESADVILVRKGVLLDTAVSFDLSRVIVKRIKMNLVWACIYNFVMIPIAMGFFLPWGIYLNPMWASAAMMFSSLSVLASSLLLRRWKKPKSLIFSEADDVETESSTNSSVLQKVYTATRSIFGRNKSSNKYQPVANEV
|
7.2.2.8
| null |
copper ion export [GO:0060003]; copper ion homeostasis [GO:0055070]; copper ion import [GO:0015677]; intracellular copper ion homeostasis [GO:0006878]
|
Golgi apparatus [GO:0005794]; Golgi membrane [GO:0000139]; membrane [GO:0016020]; plasma membrane [GO:0005886]; trans-Golgi network [GO:0005802]
|
ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; copper ion binding [GO:0005507]; P-type divalent copper transporter activity [GO:0043682]; P-type monovalent copper transporter activity [GO:0140581]
|
PF00122;PF00403;PF00702;
|
3.30.70.100;3.40.1110.10;2.70.150.10;3.40.50.1000;
|
Cation transport ATPase (P-type) (TC 3.A.3) family, Type IB subfamily
| null |
SUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network membrane {ECO:0000269|PubMed:16823372}; Multi-pass membrane protein {ECO:0000269|PubMed:16823372}.
|
CATALYTIC ACTIVITY: Reaction=ATP + Cu(+)(in) + H2O = ADP + Cu(+)(out) + H(+) + phosphate; Xref=Rhea:RHEA:25792, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:49552, ChEBI:CHEBI:456216; EC=7.2.2.8;
| null | null | null | null |
FUNCTION: Probably involved in copper transport and in the regulation of cellular copper level. Retrieves copper from the metallochaperone atx1 and incorporates it into trans-Golgi vesicles (By similarity). {ECO:0000250}.
|
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
|
O59676
|
PDP1_SCHPO
|
MNNARTNAKRRRLSSKQGGLSISEGKESNIPSVVEESKDNLEQASADDRLNFGDRILVKAPGYPWWPALLLRRKETKDSLNTNSSFNVLYKVLFFPDFNFAWVKRNSVKPLLDSEIAKFLGSSKRKSKELIEAYEASKTPPDLKEESSTDEEMDSLSAAEEKPNFLQKRKYHWETSLDESDAESISSGSLMSITSISEMYGPTVASTSRSSTQLSDQRYPLSSNFDHRGEAKGKGKQPLKNPQERGRISPSSPLNDQTKALMQRLLFFRHKLQKAFLSPDHLIVEEDFYNASKYLNAISDIPFLNYELITSTKLAKVLKRIAFLEHLENDELYDIRQKCKNLLYSWAMFLPNEPSIKGM
| null | null |
chromatin remodeling [GO:0006338]; DNA damage response [GO:0006974]; regulation of transcription by RNA polymerase II [GO:0006357]
|
NuA3 histone acetyltransferase complex [GO:0033100]; nucleus [GO:0005634]
|
double-stranded DNA binding [GO:0003690]; H4K20me3 modified histone binding [GO:1990889]; histone binding [GO:0042393]; methylated histone binding [GO:0035064]
|
PF00855;
|
2.30.30.140;
| null | null |
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10759889, ECO:0000269|PubMed:16823372}.
| null | null | null | null | null |
FUNCTION: Necessary for DNA damage checkpoint activation. Required for the association of set9 with chromatin and subsequent methylation of H4K20. Associates with H4K20me1 to increase the concentration of set9 on chromatin to perform H4K20me3. H4K20me3 is mainly enriched at heterochromatin and is required for proper heterochromatin assembly. {ECO:0000269|PubMed:19250904}.
|
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
|
O59701
|
CYSK_SCHPO
|
MATSGIQTKVPGIVSGFIGAIGRTPLIRLNTLSNETGCNILAKAEFQNPGGSVKDRAAYYVVRDAEKKGKLSRGGTIVEGTAGNTGIGLAHIARARGYKCVIYMPNTQSQAKIDTLKFLGAEVHPVPVAPFSNPLNYNHQARRHAESTPNASWTDQFDNVANLLSHYETTGPEIWDQTKGTVDGFTCSTGTGGTFAGVTKYLKEKSDGRVASFVADPPGSVLYSHIKTKGKHPDNKGSSFTEGIGQGRITGNVQPVYDLIDDAMKIPDEKSINMFFRLLDQEGLFLGGSSCLNVVAAVEMAKILGPGKTVVTILCDSGHKYATRLFSRSFLESKKLFDVIEPQYKKYIVLP
|
2.5.1.-; 2.5.1.47
|
COFACTOR: Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; Evidence={ECO:0000250|UniProtKB:P0ABK5};
|
cysteine biosynthetic process from serine [GO:0006535]
|
cytoplasm [GO:0005737]; mitochondrion [GO:0005739]
|
cysteine synthase activity [GO:0004124]
|
PF00291;
|
3.40.50.1100;
|
Cysteine synthase/cystathionine beta-synthase family
| null |
SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:14981292}.
|
CATALYTIC ACTIVITY: Reaction=hydrogen sulfide + O-succinyl-L-serine = L-cysteine + succinate; Xref=Rhea:RHEA:53816, ChEBI:CHEBI:29919, ChEBI:CHEBI:30031, ChEBI:CHEBI:35235, ChEBI:CHEBI:136856; Evidence={ECO:0000269|PubMed:28581482}; CATALYTIC ACTIVITY: Reaction=hydrogen sulfide + O-acetyl-L-serine = acetate + L-cysteine; Xref=Rhea:RHEA:14829, ChEBI:CHEBI:29919, ChEBI:CHEBI:30089, ChEBI:CHEBI:35235, ChEBI:CHEBI:58340; EC=2.5.1.47; Evidence={ECO:0000269|PubMed:17482430, ECO:0000269|PubMed:28581482};
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.24 mM for O-succinyl-L-serine {ECO:0000269|PubMed:28581482}; KM=0.33 mM for O-acetyl-L-serine {ECO:0000269|PubMed:28581482}; KM=0.34 mM for Na(2)S {ECO:0000269|PubMed:28581482}; Note=kcat is 2.8 sec(-1) with O-succinyl-L-serine as substrate. kcat is 1.5 sec(-1) with O-acetyl-L-serine as substrate. {ECO:0000269|PubMed:28581482};
|
PATHWAY: Amino-acid biosynthesis; L-cysteine biosynthesis; L-cysteine from L-serine: step 2/2. {ECO:0000305|PubMed:14981292, ECO:0000305|PubMed:28581482}.
| null | null |
FUNCTION: Catalyzes the conversion of O-succinyl-L-serine into cysteine, the last step in the cysteine biosynthesis pathway (PubMed:28581482). Can also use O-acetyl-L-serine (PubMed:17482430, PubMed:28581482). {ECO:0000269|PubMed:28581482, ECO:0000305|PubMed:17482430}.
|
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
|
O59702
|
CLR6_SCHPO
|
MGFGKKKVSYFYDEDVGNYHYGPQHPMKPHRVRMVHNLVVNYNLYEKLNVITPVRATRNDMTRCHTDEYIEFLWRVTPDTMEKFQPHQLKFNVGDDCPVFDGLYEFCSISAGGSIGAAQELNSGNAEIAINWAGGLHHAKKREASGFCYVNDIALAALELLKYHQRVLYIDIDVHHGDGVEEFFYTTDRVMTCSFHKFGEYFPGTGHIKDTGIGTGKNYAVNVPLRDGIDDESYESVFKPVISHIMQWFRPEAVILQCGTDSLAGDRLGCFNLSMKGHSMCVDFVKSFNLPMICVGGGGYTVRNVARVWTYETGLLAGEELDENLPYNDYLQYYGPDYKLNVLSNNMENHNTRQYLDSITSEIIENLRNLSFAPSVQMHKTPGDFTFENAEKQNIAKEEIMDERV
|
3.5.1.98
| null |
epigenetic regulation of gene expression [GO:0040029]; negative regulation of transcription by RNA polymerase II [GO:0000122]; transcription initiation-coupled chromatin remodeling [GO:0045815]
|
chromatin [GO:0000785]; Clr6 histone deacetylase complex I'' [GO:1990483]; cytosol [GO:0005829]; nucleus [GO:0005634]; NuRD complex [GO:0016581]; Rpd3L complex [GO:0033698]; Rpd3L-Expanded complex [GO:0070210]; Rpd3S complex [GO:0032221]
|
histone deacetylase activity [GO:0004407]; histone H3K14 deacetylase activity [GO:0031078]; histone H3K9 deacetylase activity [GO:0032129]; histone H4K16 deacetylase activity [GO:0034739]; protein lysine deacetylase activity [GO:0033558]
|
PF00850;
|
3.40.800.20;
|
Histone deacetylase family, HD type 1 subfamily
| null |
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12773392}.
|
CATALYTIC ACTIVITY: Reaction=H2O + N(6)-acetyl-L-lysyl-[histone] = acetate + L-lysyl-[histone]; Xref=Rhea:RHEA:58196, Rhea:RHEA-COMP:9845, Rhea:RHEA-COMP:11338, ChEBI:CHEBI:15377, ChEBI:CHEBI:29969, ChEBI:CHEBI:30089, ChEBI:CHEBI:61930; EC=3.5.1.98;
| null | null | null | null |
FUNCTION: Responsible for the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4). Histone deacetylation gives a tag for epigenetic repression and plays an important role in transcriptional regulation, cell cycle progression and developmental events. Histone deacetylases act via the formation of large multiprotein complexes. Has a role in chromatin assembly and chromosome segregation. {ECO:0000269|PubMed:12773392}.
|
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
|
O59703
|
GGPPS_SCHPO
|
MVNDFNEKNGIKKRLLDFFPVVLEGIREILESMQYFPEETEKLLYSIKRNTLGGKNNRGLAVLQSLTSLINRELEEAEFRDAALLGWLIEILQGCFLMADDIMDQSIKRRGLDCWYLVVGVRRAINESQLLEACIPLLIRKYFRNMPYYVDLLDTFREVTFLTELGQQEDLLSSRDGEASLRSFDLMKYDFIITYKTSFYSFYLPIKCALLLSRNSNQKAYDTTIKLSKLLGYYFQVQDDYLDCFGDYTVLGKVGMDIQDNKCTWLVCYAEKFASADQLNLLRAHYGKAGSENIAVIKQLYHELQIPELYHKFEDDMVDSISKEIDLIDESTGLKKCIFTKFFQLIYKRSR
|
2.5.1.-; 2.5.1.1; 2.5.1.10; 2.5.1.29
|
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; Note=Binds 2 Mg(2+) ions per subunit. {ECO:0000250};
|
ergosterol biosynthetic process [GO:0006696]; farnesyl diphosphate biosynthetic process [GO:0045337]; geranyl diphosphate biosynthetic process [GO:0033384]; geranylgeranyl diphosphate biosynthetic process [GO:0033386]; protein transport [GO:0015031]
|
cytoplasm [GO:0005737]; cytosol [GO:0005829]; endoplasmic reticulum [GO:0005783]; nucleus [GO:0005634]
|
dimethylallyltranstransferase activity [GO:0004161]; farnesyltranstransferase activity [GO:0004311]; geranyltranstransferase activity [GO:0004337]; metal ion binding [GO:0046872]
|
PF00348;
|
1.10.600.10;
|
FPP/GGPP synthase family
| null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus {ECO:0000269|PubMed:16823372}.
|
CATALYTIC ACTIVITY: Reaction=dimethylallyl diphosphate + isopentenyl diphosphate = (2E)-geranyl diphosphate + diphosphate; Xref=Rhea:RHEA:22408, ChEBI:CHEBI:33019, ChEBI:CHEBI:57623, ChEBI:CHEBI:58057, ChEBI:CHEBI:128769; EC=2.5.1.1; CATALYTIC ACTIVITY: Reaction=(2E)-geranyl diphosphate + isopentenyl diphosphate = (2E,6E)-farnesyl diphosphate + diphosphate; Xref=Rhea:RHEA:19361, ChEBI:CHEBI:33019, ChEBI:CHEBI:58057, ChEBI:CHEBI:128769, ChEBI:CHEBI:175763; EC=2.5.1.10; CATALYTIC ACTIVITY: Reaction=(2E,6E)-farnesyl diphosphate + isopentenyl diphosphate = (2E,6E,10E)-geranylgeranyl diphosphate + diphosphate; Xref=Rhea:RHEA:17653, ChEBI:CHEBI:33019, ChEBI:CHEBI:58756, ChEBI:CHEBI:128769, ChEBI:CHEBI:175763; EC=2.5.1.29;
| null |
PATHWAY: Isoprenoid biosynthesis; farnesyl diphosphate biosynthesis; farnesyl diphosphate from geranyl diphosphate and isopentenyl diphosphate: step 1/1.; PATHWAY: Isoprenoid biosynthesis; geranyl diphosphate biosynthesis; geranyl diphosphate from dimethylallyl diphosphate and isopentenyl diphosphate: step 1/1.; PATHWAY: Isoprenoid biosynthesis; geranylgeranyl diphosphate biosynthesis; geranylgeranyl diphosphate from farnesyl diphosphate and isopentenyl diphosphate: step 1/1.
| null | null |
FUNCTION: Catalyzes the trans-addition of the 3 molecules of IPP onto DMAPP to form geranylgeranyl pyrophosphate. Required for the membrane attachment of ypt7 and rhb1. May be involved in vesicle trafficking and protein sorting. Required for forespore membrane formation. {ECO:0000269|PubMed:17596513}.
|
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
|
O59726
|
FNX2_SCHPO
|
MSNPRTKSPNTNRGQGLRSERSALLNDSLSSLNGNSSYDSIKDSSKNNKDVAEVNEYPRRPESSVSVVSNSPHRQDAATTNTVSTVSVSKVLPALLLGVVLAALDNTIVASTYTKIGAEFGKFSQVSWTATAYMISCTAFQPLFGKFCDIYGRKKTLLAAYCVFGIGCFLCGTSRSLWQLVAARAIAGIGGGGMNSTVSILMSDIVPLKQRGTYQGIINVFFAIGSSLGGPVGGYFADQYTWRIGFLIQVPLIAIAFLCVYFTLNLPHHNHVSFMTRFRKIDLKGLILLIIGVTTMTCAFTLGGNVREWNDPVVISLLIASSISYLSFVYVEAFVAFEPLAPMDVLTERTCLSSYLCNFFHSVANFGWIYGMPLFFQSIKNEGAEKSGIRLIPMIIGSSLGSLLGGAVISLTGNYKKITVGSYFFGSVAALFMLRYGYSNFNWEYAVYPFSGGLGNGIAVTTTLVAIIHASPSAFQASAIATSYLFRSNGCVLGVSISSSIVQTVLGIKLRKSLDFDVDELLHHLRKDISYVHRLPEEIRQTVLDALLGSIHYSFLFVSFMFFCAFVCSMFIKNRNL
| null | null |
asparagine transmembrane import into vacuole [GO:1990591]; basic amino acid transport [GO:0015802]; isoleucine transmembrane transport [GO:1903714]; L-lysine transmembrane import into vacuole [GO:0090517]; transmembrane transport [GO:0055085]
|
cytoplasm [GO:0005737]; fungal-type vacuole [GO:0000324]; fungal-type vacuole membrane [GO:0000329]
|
basic amino acid transmembrane transporter activity [GO:0015174]; L-asparagine transmembrane transporter activity [GO:0015182]; L-isoleucine transmembrane transporter activity [GO:0015188]; L-lysine transmembrane transporter activity [GO:0015189]
|
PF07690;
|
1.20.1250.20;
|
Major facilitator superfamily
| null |
SUBCELLULAR LOCATION: Vacuole {ECO:0000269|PubMed:10759889, ECO:0000269|PubMed:16823372}. Membrane {ECO:0000269|PubMed:10759889, ECO:0000269|PubMed:16823372}; Multi-pass membrane protein {ECO:0000269|PubMed:10759889, ECO:0000269|PubMed:16823372}.
| null | null | null | null | null |
FUNCTION: MFS-type transporter involved in vacuolar amino acid uptake. {ECO:0000269|PubMed:18503766}.
|
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
|
O59734
|
RUXF_SCHPO
|
MSFVPVNPKPFLQGLIGKPVLVRLKWGQEYKGTLQSVDSYMNLQLLNAEELVDGVKTGDLGEILIRCNNVLWVGESTV
| null | null |
mRNA 5'-splice site recognition [GO:0000395]; mRNA splicing, via spliceosome [GO:0000398]; spliceosomal snRNP assembly [GO:0000387]
|
catalytic step 2 spliceosome [GO:0071013]; cytosol [GO:0005829]; nucleus [GO:0005634]; pICln-Sm protein complex [GO:0034715]; post-mRNA release spliceosomal complex [GO:0071014]; spliceosomal complex [GO:0005681]; U1 snRNP [GO:0005685]; U2 snRNP [GO:0005686]; U4/U6 x U5 tri-snRNP complex [GO:0046540]
|
RNA binding [GO:0003723]
|
PF01423;
|
2.30.30.100;
|
SnRNP Sm proteins family, SmF/LSm6 subfamily
| null |
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16823372}. Cytoplasm {ECO:0000269|PubMed:16823372}.
| null | null | null | null | null |
FUNCTION: Plays a role in pre-mRNA splicing as a core component of the spliceosomal U1, U2, U4 and U5 small nuclear ribonucleoproteins (snRNPs), the building blocks of the spliceosome (By similarity). {ECO:0000250|UniProtKB:P62306}.
|
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
|
O59740
|
MOD5P_SCHPO
|
MSALSESPAIPSFWRPETSEISKKPRPNTTVGFQFDNRNVGTSAPSTPAIRRNNTDSFERGLSLPLPSSKQDTGSSVLDPDGDAYVNRYARPVTAGSIYIPSNYHKSFSPNTFSGFNVKRSASKSPKRSANGSTSEDISIEGSPSETAKGARSSFNSNFRTFDIGSERRRRILEASQDSSRPGRYSYRTKSASPALIDTSTLDSRLNFTMGRLERSIAQLSKNTMRAVSHLENPPKDITLPKLNVKNSAWPLQPYSPPANETPASSSSSAKARPVSVPDMSSPVPASSVEYESLKAAVTYSPSQNPKKVAETDSESRKSSFQSSYNDADRPFQVGAQTQSTPNRISRSDSPIVYDVDTHSEDNASTASSEAISQSMRSFQPQPNTGSPFPRFTSTNTEDEQESDIPQSDANDSTVNLNQPNYANLTPTPQVSPKRPTYSRSSPLPSASVPALGDGSPDPPAAPSIQNSLSVHESEMPPHVTRDYTQPAASATPVPKEKPSEKSEKPPKKKGSKLEKFCCILM
| null | null |
maintenance of protein location in cell cortex of cell tip [GO:0097248]
|
cell cortex of cell tip [GO:0051285]; cell division site [GO:0032153]; cell tip [GO:0051286]; cytoplasmic side of plasma membrane [GO:0009898]; plasma membrane of cell tip [GO:0031520]
|
protein-membrane adaptor activity [GO:0043495]
| null | null | null | null |
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:12789340}; Peripheral membrane protein {ECO:0000269|PubMed:12789340}; Cytoplasmic side {ECO:0000269|PubMed:12789340}. Note=localizes to the cell tips.
| null | null | null | null | null |
FUNCTION: With tea1, acts in a positive-feedback loop in the microtubule-mediated regulation of cell polarity. Involved in the anchoring of tea1 at the cortex as well as the correct localization of tea3. {ECO:0000269|PubMed:12789340, ECO:0000269|PubMed:16222337}.
|
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
|
O59747
|
PDF1_SCHPO
|
MLSCSSFLIFFLFSWVLLPMKSFAIPIISLDKVRLAINDGASEQLPVVIWHGLGDTPTSFTLTEVSQRVQKLTKGAVYAIRVGDNEFEDIKAGYLGKLEDQLDEVCDLIGNEDSLSNGFYALGLSQGGLFLRALAQTCDAAKIRSLITLGSPHSGINTIPGCSPTNLICKAVVHSILGLGIWHSWIQNHVVQAQYYRTEKQYDKYLENNKFLTHLNNEVLHDNYTRNIEKLKELDNLVAVSFERDDIVEPPYSTGFGWINETTGENIEMEDFVLYESLGLKDLVNQGKLETISFPGRHLQMRWGDFDALVLKYFKDEKEEKTELEESTRPSNFLSTYFVSPLVSAIDGTVDYLHGKSLFPEKRNFKELTMRKRSIVTPEDSEEVYPYISEFVAASNVSEEKGPKSFANLAFITIFSHFFYHIDDMWRSTLGLFSLIPQIIGIIYLTVMFTGRELDTFMQFGGQVVNEFINYVVKVSLKYPRPADIEYGVGYGMPSSHSQFMGFFSAYMIAWDYKYRRSQCFSMLSFAKYAIYLTLSTFVCSSRYLLDFHYLTQVVYGYMIGFGVGLFWVYLVGKLRSLGVTKWLLSLPPLQFFYIKDTIPHSKDNHKRQWLESKQFKNQKSN
|
3.1.2.22; 3.6.1.43
| null |
lipid biosynthetic process [GO:0008610]; membrane lipid biosynthetic process [GO:0046467]; protein N-linked glycosylation [GO:0006487]
|
endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]; intracellular membrane-bounded organelle [GO:0043231]; vacuole [GO:0005773]
|
dolichyldiphosphatase activity [GO:0047874]; palmitoyl-(protein) hydrolase activity [GO:0008474]
|
PF02089;PF01569;
|
3.40.50.1820;1.20.144.10;
|
Palmitoyl-protein thioesterase family; Dolichyldiphosphatase family
|
PTM: Proteolytically cleaved, possibly by krp1. {ECO:0000269|PubMed:15075260}.
|
SUBCELLULAR LOCATION: Vacuole {ECO:0000255}. Endoplasmic reticulum membrane {ECO:0000255}; Multi-pass membrane protein {ECO:0000255}.
|
CATALYTIC ACTIVITY: Reaction=H2O + S-hexadecanoyl-L-cysteinyl-[protein] = H(+) + hexadecanoate + L-cysteinyl-[protein]; Xref=Rhea:RHEA:19233, Rhea:RHEA-COMP:10131, Rhea:RHEA-COMP:11032, ChEBI:CHEBI:7896, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29950, ChEBI:CHEBI:74151; EC=3.1.2.22; CATALYTIC ACTIVITY: Reaction=a dolichyl diphosphate + H2O = a dolichyl phosphate + H(+) + phosphate; Xref=Rhea:RHEA:14385, Rhea:RHEA-COMP:9517, Rhea:RHEA-COMP:9529, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474, ChEBI:CHEBI:57497, ChEBI:CHEBI:57683; EC=3.6.1.43; Evidence={ECO:0000250|UniProtKB:P53223};
| null | null | null | null |
FUNCTION: Essential protein. Removes thioester-linked fatty acyl groups such as palmitate from modified cysteine residues in proteins or peptides during vacuolar degradation. Required for efficient N-glycosylation. Necessary for maintaining optimal levels of dolichol-linked oligosaccharides. {ECO:0000250|UniProtKB:P45478, ECO:0000250|UniProtKB:P53223, ECO:0000269|PubMed:15075260}.
|
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
|
O59748
|
CTK2_SCHPO
|
MAENENHVLSIRMSHPYYSEKEISRILSTRDPKENNLRMQAFAWISTLSKTLKFPVRTSGLAMLLYSRFQLFFPVNEIPLLECATACLVVASKIEDTAKKFRDILLAHYLQKHPGSEVDAHSQVCYKLIEENKKRILGLERMTLELICFDFRVRHPHNYMVKFAKSLKFSSSTASIAWNVCTDAYKTYTMLKYPAHIVAVASISIACKLQQLPQPIIPRSFFAPPALTEAVIADILDLYMHYQPHTCIGNMYTTEKLLGLCVDFQRAQKNSGRPQKPPQIDPHSSSLADEYRESNKRLQESKESCARFILDCDRKYFNTEFEKRMLEERRNKGTV
| null | null |
mRNA processing [GO:0006397]; positive regulation of DNA-templated transcription, elongation [GO:0032786]; positive regulation of transcription by RNA polymerase II [GO:0045944]; regulation of transcription by RNA polymerase II [GO:0006357]
|
CTDK-1 complex [GO:0070692]; cyclin/CDK positive transcription elongation factor complex [GO:0008024]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; nuclear cyclin-dependent protein kinase holoenzyme complex [GO:0019908]; nucleus [GO:0005634]
|
cyclin-dependent protein serine/threonine kinase activator activity [GO:0061575]
|
PF00134;
|
1.10.472.10;
|
Cyclin family
| null |
SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Note=Nuclear localization is dependent on ctk1/lsk1.
| null | null | null | null | null |
FUNCTION: Cyclin subunit of the CTDK-I complex, which hyperphosphorylates the C-terminal heptapeptide repeat domain (CTD) of the largest RNA polymerase II subunit. As part of the CTDK-I complex, involved in RNA polymerase II transcriptional elongation and pre-mRNA 3'-end processing. Together with ctk3, required for ctk1/lsk1 CTD kinase activation (By similarity). Together with ctk1/lsk1, required for the regulation of cytokinesis by phosphorylating 'Ser-2' residues found in the heptad repeats of the CTD. {ECO:0000250, ECO:0000269|PubMed:17502918}.
|
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
|
O59751
|
KLP6_SCHPO
|
MKEGSSISVAVRVRPFTEREKGLLAETPKSKEFLGDGSLAVSNTSSNTFCTNGIRKIVRVLDDNVLIFDPPEENPLAKVQKSLLPAGKRFRDVRYAFDRLFGEEASQEDVYKGTTEPLLDSVLQGYNATVFAYGATGCGKTHTISGRPDDPGIIFLTMRALLDRVEGLKRTMNVDISVSYLEIYNEKIRDLLVQDPLSMEKPKSLNICEDAEQNVSVPGLSYFTPTNLEEVMEIIIRGNSNRTMSPTEANAVSSRSHAVLQIYITQTPKSGEKQEESESQNSHKVRSVFSFIDLAGSERASATKNRGKRLVEGANINRSLLALGNCINSLCEPRRRQHVPYRDSKLTRLLKFSLGGNCRTCMIVCISPSSEHYDETHNTLKYGNRAKNIKTKVSRNVVSVDRHVSEYVRTIYELRQKVSILQKRIAEESKQLALNKEVRKISSREIKMLDARSMLKNSFDGSRDLQKSLIEHVRTLRRIEDEITLTKMWISIAKESDAMSGHNIKSVETRLAKLYDQRSLITAKVNPEEICKTFQNSISHIVSSFKGEGADMYADMLQDDVDLLKSIIENQILDAKHESETFSSTSRKLIQNLFLLFPLLPGNAIDVNESLARAFDQLVGIVPSEPTIQVPNLIEKGKAPLLSMFEIPRSPSRFKARSPSKAARVLKKPLKKRVRFSEVPTTSSVPPVEIKNKDSKPKVEKSLDKHNMNNDRSFLVPSRDARNSLTSLSLHSNVAKNKSSHSSKWPTHTLSPIITTALKQPVRRISLVSQPLQKTGGTENTPNA
| null | null |
cell division [GO:0051301]; deactivation of mitotic spindle assembly checkpoint [GO:1902426]; microtubule depolymerization [GO:0007019]; microtubule-based movement [GO:0007018]; mitotic chromosome movement towards spindle pole [GO:0007079]; mitotic metaphase chromosome recapture [GO:1990942]; mitotic sister chromatid biorientation [GO:1990758]; mitotic sister chromatid segregation [GO:0000070]; mitotic spindle elongation [GO:0000022]; mitotic spindle formation (spindle phase one) [GO:0061804]; mitotic spindle organization [GO:0007052]; plus-end specific microtubule depolymerization [GO:0070462]; protein transport along microtubule to kinetochore [GO:0140210]
|
cortical microtubule [GO:0055028]; cytoplasm [GO:0005737]; cytoplasmic microtubule plus-end [GO:1904511]; cytosol [GO:0005829]; kinesin complex [GO:0005871]; kinesin I complex [GO:0016938]; kinetochore [GO:0000776]; microtubule cytoskeleton [GO:0015630]; mitotic spindle [GO:0072686]; mitotic spindle astral microtubule [GO:0061673]; mitotic spindle midzone [GO:1990023]; mitotic spindle pole body [GO:0044732]; nucleus [GO:0005634]; plus-end kinesin complex [GO:0005873]; post-anaphase microtubule array [GO:1990295]
|
ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; microtubule binding [GO:0008017]; plus-end-directed microtubule motor activity [GO:0008574]
|
PF00225;
|
3.40.850.10;
|
TRAFAC class myosin-kinesin ATPase superfamily, Kinesin family, Kinesin II subfamily
| null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11967147}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:11967147}. Chromosome, centromere, kinetochore {ECO:0000269|PubMed:11967147}. Cytoplasm, cytoskeleton, spindle {ECO:0000269|PubMed:11967147}. Note=Cytoplasmic microtubules in interphase, mitotic kinetochores in metaphase and spindle midzone in anaphase and telophase.
| null | null | null | null | null |
FUNCTION: Has a role in establishing metaphase during mitosis. Required for chromosome segregation where it generates tension during kinetochore capturing. {ECO:0000269|PubMed:11967147}.
|
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
|
O59755
|
CUT12_SCHPO
|
MSETLNTPPTYAWVLKAFSSKLAGTVTKPVTKMSSYIEDAESDAELPQDAKEDLRPTETLTPLKSKAAQNGILKTPGTLQIKKTVNFKDISKDAATWNRPTKNNFLFTRLDDENPLMGHEEFKSPLLQSTPKPNINNPDNENKSKHDEFDNRYNININESYKNETKSNQRLGEDVPSKKKYPHSMDAEISKFKWDSNNNNDWSSLMKDCFRDVVNNNRKMKEIIKDVMIDTSQAFPSESLDEPDYTINLDAPRSSSGKYWKQKFSMLDSAHSDLELELTSIRERLESLILEKQEEINFWKQRCRALETEKIHNHQGQQSKYKGKEFVGNRFSQMRELYTAKPSPITTKVVSRPSQSDVREPQEQVPSKNLHRGADMSHLAAQMLTHSSKKSHTTNLIPSEGIISSTPISAASKVRMNLMQSNQTPTPAPFSIAAKKSHLPSKLSFPQDGGSLSSATTLQQLPKARVTPNVLSSLSSNLGKTNPTSVYQSKANVTTSADVEKPQVKVATSSRVDYDLKSPNQRTANAKKRLEERRRRRKLKLQELQLNS
| null | null |
cell division [GO:0051301]; G2/M transition of mitotic cell cycle [GO:0000086]; mitotic spindle pole body insertion into the nuclear envelope [GO:0140480]; negative regulation of G2/M transition of mitotic cell cycle [GO:0010972]; positive regulation of mitotic spindle formation (spindle phase one) [GO:0110161]
|
cytoplasm [GO:0005737]; inner plaque of mitotic spindle pole body [GO:0061497]; meiotic spindle pole body [GO:0035974]; microtubule cytoskeleton [GO:0015630]; mitotic spindle pole body [GO:0044732]; nucleus [GO:0005634]
|
protein kinase activator activity [GO:0030295]; signaling adaptor activity [GO:0035591]
|
PF11500;
| null | null | null |
SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, spindle pole body {ECO:0000269|PubMed:9531532}.
| null | null | null | null | null |
FUNCTION: Required for bipolar spindle formation. May act as a regulator of the p34cdc2/cyclin B kinase. Required for full activation of the plo1 kinase. However, in cut12.1 cells at restrictive temperature the H1 kinase does rise concomitant with entry into mitosis, indicating that cut12 is not required for activation of p34cdc2/cyclin B. The cut12.s11 allele may promote cdc2-independent phosphorylation of SPB proteins thereby overcoming the requirement for cdc25 in cell cycle progression. {ECO:0000269|PubMed:12815070, ECO:0000269|PubMed:9531532}.
|
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
|
O59757
|
SPC7_SCHPO
|
MPTSPRRNSIATTDNVIGRNKSRKRPHSLGGPGALQELKEHTNPAKGILKSYSSFSVDPAFTGDEDFNDIHTQINNTVIGISSNVMAASKRLQMEDLQQLSRETSRKSLNRRVSFASHARVRWYPKDHQSDSEKSTSNHSTPERTFASDAKNHSPKGPTTTSFSRNETQSSPHSHSASIISDGSDMDIASPIRSTESDMVSEALNAGHPPPSLYPENDDLSIQNPTKALPEAEKALDVHDATREQVNDREETNMDLTIQFQEADSFLSHSESIKGLSSSEQGTVYSLKASHDPSNQTQLSSPNKSSSPTSIEISDFSKNNENHDQSENKEEEEDMMLTRPIEIPQHFSPIARPLTSQEAIVDMDITSNNINLSPVSHFSNGLDLQNLEEAPMNLTRPINANPHLTNHSPNDLTNGEEEMDTTSAFNIENSHLTLLSPIRPSSRSMEEQIMDLTQPISSTNAPTHLNEDDLNQFTSNISSSSKPRKDNNKTANSSKPIPDSEDFMDITRPFNILSPSKEALSEEQPMELTSTVFPCENSTSHLEVEEAAMDETVAFQIRGNNVELPSADKENAEREEIPSYSDKSENFNTTSFTNHERSPNGNNNLKFSKDPNSSSPSRHVVATPTDKLGTRKRRLRYSTSSFDQSTLRRNRLATIRNARKSISTLNDRELLPVNFFEKKVNSGLYKSVERSENYRLGATPLTAEKPFTTEKPLSSLPEEVSRQPTDDKGEQVSNADVDSGLSKTERLTIQQTNEIKHVPTNTTSSVKLPQQPSNEDEKERITTADYADSTSLERLESQEPNRNELVQVGSSNAGNTTSVGMNEHEKSPVKLSKGVSNVDTSLGASTINTNILNQDSGPNEEIPVGNEPEFDTMPTLPNVEPISLSDFLKMTGIEFLDNLTIAKRRETLLPNAEENKKCSIQELLESFYIQFPLLELYKFSCQQLQDYIAEGKDFVTKIEEETLKENPLLFYEYRKASSDMRVLMDSQFLMMKTFARLQAKGDWYEWREGLMQGIKHELNLNLTGMQRSLTHLMDVANVIHPYAQEIQERYNGSITTVQTLKKQKEFANQYDSTLLAQAQEKLEKLKVEVERRRRLLSEKEERRKELAIKIEQVTNSCSDLELRTNAEQDFYAKNQDFEFDEIKRYEEQLLNLKNELGWTIVSLTAGGIKLATNNTALSPYSAEVTVEILRQNFQVNVDIACKFPNESNACSSNVLEHVASSFSKWHSKVFSRNLRLLKKYLNDVSICWEQIVYLVQDFQRLWYHWPFLSVENDDKSIIINVELYLRSVSSKVKVVFGLPIDTIYQTTEVGKFYASTSVAVKQMYAESEGDSYVSEVLNTLSEVVHCTSTYALSSACLTVWNKYS
| null | null |
attachment of mitotic spindle microtubules to kinetochore [GO:0051315]; cell division [GO:0051301]; deactivation of mitotic spindle assembly checkpoint [GO:1902426]; homologous chromosome orientation in meiotic metaphase I [GO:0031619]; meiotic centromeric cohesion protection in anaphase I [GO:1990813]; mitotic sister chromatid biorientation [GO:1990758]; mitotic spindle assembly checkpoint signaling [GO:0007094]; positive regulation of meiosis I spindle assembly checkpoint [GO:1905326]; protein localization to kinetochore [GO:0034501]; spindle attachment to meiosis I kinetochore [GO:0051455]
|
condensed chromosome, centromeric region [GO:0000779]; cytoplasm [GO:0005737]; kinetochore [GO:0000776]; Knl1/Spc105 complex [GO:0180019]; nucleus [GO:0005634]; outer kinetochore [GO:0000940]; spindle pole body [GO:0005816]
|
kinetochore adaptor activity [GO:0140483]; microtubule plus-end binding [GO:0051010]; signaling adaptor activity [GO:0035591]
|
PF18210;PF08317;
| null | null | null |
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16823372}. Chromosome, centromere, kinetochore {ECO:0000269|PubMed:16823372}. Cytoplasm, cytoskeleton, microtubule organizing center, spindle pole body {ECO:0000269|PubMed:16823372}.
| null | null | null | null | null |
FUNCTION: Acts as a component of the NMS (Ndc80-MIND-Spc7) super complex which has a role in kinetochore function during late meiotic prophase and throughout the mitotic cell cycle.
|
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
|
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