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
|
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
O64644
|
SAP18_ARATH
|
MAEAARRQGGGRPLPPPPRGVNQQPPRPKPEPVDREKTCPLLLRVFTKSGGHHTSEDYAVRGKEPKDEVQIYTWKDASLRELTDLVKEVSVAARRRNARLSFAFVYPNNKGGYNVREVGETMAYPNRKQPDDSKTLSELPFEIGDYLDVAIY
| null | null |
response to abscisic acid [GO:0009737]; response to salt stress [GO:0009651]
|
cytosol [GO:0005829]; nucleolus [GO:0005730]
|
transcription corepressor activity [GO:0003714]
|
PF06487;
|
3.10.20.550;
|
SAP18 family
| null | null | null | null | null | null | null |
FUNCTION: Links the histone deacetylase complex to transcriptional repressors bound to chromatin. Involved in the tethering of the SIN3 complex to core histone proteins. {ECO:0000269|PubMed:16429262}.
|
Arabidopsis thaliana (Mouse-ear cress)
|
O64645
|
SOC1_ARATH
|
MVRGKTQMKRIENATSRQVTFSKRRNGLLKKAFELSVLCDAEVSLIIFSPKGKLYEFASSNMQDTIDRYLRHTKDRVSTKPVSEENMQHLKYEAANMMKKIEQLEASKRKLLGEGIGTCSIEELQQIEQQLEKSVKCIRARKTQVFKEQIEQLKQKEKALAAENEKLSEKWGSHESEVWSNKNQESTGRGDEESSPSSEVETQLFIGLPCSSRK
| null | null |
cell differentiation [GO:0030154]; flower development [GO:0009908]; maintenance of inflorescence meristem identity [GO:0010077]; positive regulation of DNA-templated transcription [GO:0045893]; positive regulation of flower development [GO:0009911]; positive regulation of transcription by RNA polymerase II [GO:0045944]; response to cold [GO:0009409]; response to gibberellin [GO:0009739]
|
cytoplasm [GO:0005737]; nucleus [GO:0005634]
|
DNA-binding transcription factor activity [GO:0003700]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; protein dimerization activity [GO:0046983]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]
|
PF01486;PF00319;
|
3.40.1810.10;
| null | null |
SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00251, ECO:0000269|PubMed:18466303, ECO:0000269|PubMed:31540691}. Cytoplasm {ECO:0000269|PubMed:18466303}. Note=Translocation from the cytoplasm to the nucleus in the presence of AGL24.
| null | null | null | null | null |
FUNCTION: Transcription activator active in flowering time control. May integrate signals from the photoperiod, vernalization and autonomous floral induction pathways. Can modulate class B and C homeotic genes expression. When associated with AGL24, mediates effect of gibberellins on flowering under short-day conditions, and regulates the expression of LEAFY (LFY), which links floral induction and floral development. {ECO:0000269|PubMed:10995392, ECO:0000269|PubMed:18339670, ECO:0000269|PubMed:18466303, ECO:0000269|PubMed:19656343}.
|
Arabidopsis thaliana (Mouse-ear cress)
|
O64647
|
TCP9_ARATH
|
MATIQKLEEVAGKDQTLRAVDLTIINGVRNVETSRPFQVNPTVSLEPKAEPVMPSFSMSLAPPSSTGPPLKRASTKDRHTKVEGRGRRIRMPATCAARIFQLTRELGHKSDGETIRWLLENAEPAIIAATGTGTVPAIAMSVNGTLKIPTTTNADSDMGENLMKKKRKRPSNSEYIDISDAVSASSGLAPIATTTTIQPPQALASSTVAQQLLPQGMYPMWAIPSNAMIPTVGAFFLIPQIAGPSNQPQLLAFPAAAASPSSYVAAVQQASTMARPPPLQVVPSSGFVSVSDVSGSNLSRATSVMAPSSSSGVTTGSSSSIATTTTHTLRDFSLEIYEKQELHQFMSTTTARSSNH
| null | null |
negative regulation of leaf senescence [GO:1900056]; regulation of cell size [GO:0008361]; regulation of DNA-templated transcription [GO:0006355]; root development [GO:0048364]
|
nucleus [GO:0005634]
|
DNA-binding transcription factor activity [GO:0003700]; transcription cis-regulatory region binding [GO:0000976]
|
PF03634;
| null | null | null |
SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
| null | null | null | null | null | null |
Arabidopsis thaliana (Mouse-ear cress)
|
O64682
|
PID_ARATH
|
MLRESDGEMSLGTTNSPISSGTESCSSFSRLSFDAPPSTIPEEESFLSLKPHRSSDFAYAEIRRRKKQGLTFRDFRLMRRIGAGDIGTVYLCRLAGDEEESRSSYFAMKVVDKEALALKKKMHRAEMEKTILKMLDHPFLPTLYAEFEASHFSCIVMEYCSGGDLHSLRHRQPHRRFSLSSARFYAAEVLVALEYLHMLGIIYRDLKPENILVRSDGHIMLSDFDLSLCSDSIAAVESSSSSPENQQLRSPRRFTRLARLFQRVLRSKKVQTLEPTRLFVAEPVTARSGSFVGTHEYVAPEVASGGSHGNAVDWWAFGVFLYEMIYGKTPFVAPTNDVILRNIVKRQLSFPTDSPATMFELHARNLISGLLNKDPTKRLGSRRGAAEVKVHPFFKGLNFALIRTLTPPEIPSSVVKKPMKSATFSGRSSNKPAAFDYF
|
2.7.11.1
| null |
auxin polar transport [GO:0009926]; auxin-activated signaling pathway [GO:0009734]; cotyledon development [GO:0048825]; phosphorylation [GO:0016310]; phyllome development [GO:0048827]; positive gravitropism [GO:0009958]; response to auxin [GO:0009733]; root hair elongation [GO:0048767]; root hair initiation [GO:0048766]
|
cell surface [GO:0009986]; cytosol [GO:0005829]; nucleus [GO:0005634]; plasma membrane [GO:0005886]
|
ATP binding [GO:0005524]; kinase activity [GO:0016301]; protein kinase activity [GO:0004672]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674]
|
PF00069;
|
1.10.510.10;
|
Protein kinase superfamily, Ser/Thr protein kinase family
|
PTM: Autophosphorylated. Phosphorylated by PDK1.
|
SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:16731587, ECO:0000269|PubMed:17889649, ECO:0000269|PubMed:20040538}. Note=Targeted to the cell periphery.
|
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-protein kinase involved in the regulation of auxin signaling. Acts as a positive regulator of cellular auxin efflux and regulates organ development by enhancing polar auxin transport. Phosphorylates conserved serine residues in the PIN auxin efflux carriers. Phosphorylation of PIN proteins is required and sufficient for apical-basal PIN polarity that enables directional intercellular auxin fluxes, which mediate differential growth, tissue patterning and organogenesis. Acts in association with PIN1 to control the establishment of bilateral symmetry and promotion of cotyledon outgrowth. Regulates root gravitropism through modulation of PIN2-dependent basipetal auxin transport. Required for polarization of PIN3-dependent auxin transport for hypocotyl gravitropic response. The protein kinase activity of PID is essential for its auxin efflux regulatory function. PID kinase and PP2A phosphatase activities antagonistically regulate phosphorylation of PIN proteins, affecting PIN sorting. {ECO:0000269|PubMed:10693763, ECO:0000269|PubMed:11641228, ECO:0000269|PubMed:15371311, ECO:0000269|PubMed:15514156, ECO:0000269|PubMed:16107478, ECO:0000269|PubMed:16601102, ECO:0000269|PubMed:16731587, ECO:0000269|PubMed:17889649, ECO:0000269|PubMed:19075219, ECO:0000269|PubMed:19363095, ECO:0000269|PubMed:20040538, ECO:0000269|PubMed:20080776, ECO:0000269|PubMed:20407025, ECO:0000269|PubMed:21423279, ECO:0000269|PubMed:21569134}.
|
Arabidopsis thaliana (Mouse-ear cress)
|
O64722
|
ZHD3_ARATH
|
MEIASQEDPIPINTSYGNSGGGHGNMNHHHHANSAPSSLNITTSNPLLVSSNSNGLGKNHDHSHHHHVGYNIMVTNIKKEKPVVIKYKECLKNHAATMGGNAIDGCGEFMPSGEEGSIEALTCSVCNCHRNFHRRETEGEEKTFFSPYLNHHQPPPQQRKLMFHHKMIKSPLPQQMIMPIGVTTAGSNSESEDLMEEEGGGSLTFRQPPPPPSPYSYGHNQKKRFRTKFTQEQKEKMISFAERVGWKIQRQEESVVQQLCQEIGIRRRVLKVWMHNNKQNLSKKSNNVSNNVDLSAGNNDITENLASTNP
| null | null |
glucosinolate metabolic process [GO:0019760]; regulation of developmental process [GO:0050793]
|
nucleus [GO:0005634]
|
DNA binding [GO:0003677]; DNA-binding transcription factor activity [GO:0003700]; metal ion binding [GO:0046872]; protein homodimerization activity [GO:0042803]; transcription cis-regulatory region binding [GO:0000976]
|
PF04770;
|
1.10.10.60;
| null | null |
SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00108}. Note=Interactions with MIF proteins prevent nuclear subcellular location and leads to a scattered repartition throughout the cytoplasm. {ECO:0000250}.
| null | null | null | null | null |
FUNCTION: Putative transcription factor. {ECO:0000250}.
|
Arabidopsis thaliana (Mouse-ear cress)
|
O64728
|
STI_ARATH
|
MSGSRVSDLSKLHLKKELTQIRKAGRVLRDPGTTSSWKSPLDSSRSVALLETPASRNGGSSSQFPIRGESSTNRRGKEKKVFLYNWKTQKSSSEKSGLAKNGKEEEEEEEDASSWTQASVNDDDDVSDARNGGDSYRREIQSASMGFRCRDTNLASQGVSKMRKSNVGSCKKKSKKKISSSRLDCLSKYQPRDDIVARNCNAGSDDTEEELSNSEDLRKVTGASPLLLKLKQKNWSRSSSRLLRANNRKEDSSCTYNSTPALSTSSYNMYAVRNPSTVGSWDGTTTSVNDGDDELDDNLDLPGRQGCGIPCYWTKKAMKHRGGCRSCCSPSFSDTLRRTGSSILCGSQSVYRRHNRHSSGGYSKQKIACRSAQGVLPLLSYGGDGRGGSSLGTGLSDDELSTNYGELDLEAQSRLDGRRWSTSYRSQDGLEAVALDGEEEEGSTPETIRSFSQKYRPMFFEELIGQSIVVQSLMNAVKRSRIAPVYLFQGPRGTGKTSTARIFSAALNCVATEEMKPCGYCKECNDFMSGKSKDFWELDGANKKGADKVRYLLKNLPTILPRNSSMYKVFVIDECHLLPSKTWLSFLKFLENPLQKVVFIFITTDLENVPRTIQSRCQKFLFDKLKDSDIVVRLKKIASDENLDVDLHALDLIAMNADGSLRDAETMLEQLSLLGKRITTALVNELVGVVSDEKLLELLELALSSDTAETVKRARELLDLGADPIVLMSQLASLIMDIIAGTYKVVDEKYSNAFFDGRNLTEADMEGLKHALKLLSEAEKQLRVSNDRSTWFTATLLQLGSMPSPGTTHTGSSRRQSSRATDDDPASVSREVMAYKQRIGGLHFSKSASPASVIKRNGNHSHEAKPFSRVIDNNCYKSSSSSQMIESEGSIASHENSIASTMMLNQRSSEKLNDIWRKCIERCHSKTLRQLLYTHGKLISISEVEGILVAYIAFGENDIKLRAERFLSSITNSIEMVLRRSVEVRIILLPETELLVVPHQTRKPEMTNKSGHLNNIAGLNAETDVEVGSSVESRSKLPMQRIESIIREQRLETAWLQTADKDTPGSIIRVKPERNQILPQEDTYRQTNVASAISSSGLTTHQWVDELNNEVKLLKIGDNGELQENLTGTRGQHCPLSPSLLHDTNFGNNKDNLGGYESGSGRVGCNILFCWNTKKTQRRSKSKQVKGTPVRSRRNRKSRFSLFNGCAKPRKAEGNIRR
| null | null |
DNA repair [GO:0006281]; DNA-templated DNA replication [GO:0006261]; trichome branching [GO:0010091]; trichome differentiation [GO:0010026]
|
DNA polymerase III complex [GO:0009360]; DNA replication factor C complex [GO:0005663]; nucleus [GO:0005634]; plasma membrane [GO:0005886]
|
ATP binding [GO:0005524]; DNA binding [GO:0003677]; DNA clamp loader activity [GO:0003689]; DNA-directed DNA polymerase activity [GO:0003887]
|
PF13177;PF12169;
|
1.10.8.60;1.20.272.10;3.40.50.300;
|
DnaX/STICHEL family
| null |
SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
| null | null | null | null | null |
FUNCTION: Acts as a key regulator of trichome branching through an endoreduplication-independent pathway. {ECO:0000269|PubMed:10572032, ECO:0000269|PubMed:12586888, ECO:0000269|PubMed:18477400, ECO:0000269|PubMed:22210898, ECO:0000269|PubMed:9367433}.
|
Arabidopsis thaliana (Mouse-ear cress)
|
O64743
|
BBE15_ARATH
|
MAFAISKRNATLFLVTLLLISVPLSSSTLQQDFVKCLVDNSDVSFPITASFFSPDQNATLFKEELESTAQNLRYLTPSNPKPVFIFEPLYETHVQAAVVCAKKLQLHLRLRSGGHDYEGLSFVAEDETPFVIVDLSKLRQVDVDLDSNSAWAHAGATIGEVYYRIQEKSQTHGFPAGLCSSLGIGGHLVGGAYGSMMRKFGLGADNVLDARIVDANGQILDRAAMGEDVFWAIRGGGGGSFGVILAWKIKLVPVPATVTVFTVTKTLEQDGTKVLYKWEQIADKLDDDLFIRVIISPASKTTKPGNRTISMSYQAQFLGDSNRLLQVMQKSFPELGLTKKDCTEMSWIKSVMYIAGFPNSAAPEALLAGKSLFKNHFKAKSDFVKEPIPVEGLEGLWERFLEEDSPLTIWNPYGGMMSRISESEIPFPHRNGTLFKIQWLSTWQDGKVSEERHMKWIREMYSYMEQYVSKNPRQAYVNYRDLDLGTNEGETDAREWGAKYYKGNFERLVKIKGEFDPDNFFRHEQSVPTKIG
|
1.1.99.-
|
COFACTOR: Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000269|PubMed:26037923}; Note=Binds 1 FAD per subunit in a bicovalent manner. {ECO:0000269|PubMed:26037923};
|
embryo development ending in seed dormancy [GO:0009793]; polar nucleus fusion [GO:0010197]
|
extracellular region [GO:0005576]; plant-type cell wall [GO:0009505]; plasmodesma [GO:0009506]
|
cinnamyl-alcohol dehydrogenase activity [GO:0045551]; coniferyl-alcohol dehydrogenase activity [GO:0050268]; FAD binding [GO:0071949]; sinapyl alcohol dehydrogenase activity [GO:0052747]
|
PF08031;PF01565;
|
3.30.465.10;3.40.462.20;3.30.43.10;
|
Oxygen-dependent FAD-linked oxidoreductase family
|
PTM: The FAD cofactor is bound via a bicovalent 6-S-cysteinyl, 8alpha-N1-histidyl FAD linkage. {ECO:0000269|PubMed:26037923}.
|
SUBCELLULAR LOCATION: Secreted, cell wall {ECO:0000303|PubMed:26037923}.
|
CATALYTIC ACTIVITY: Reaction=(E)-4-coumaroyl alcohol + A = (E)-4-coumaraldehyde + AH2; Xref=Rhea:RHEA:76451, ChEBI:CHEBI:13193, ChEBI:CHEBI:17499, ChEBI:CHEBI:28353, ChEBI:CHEBI:64555; Evidence={ECO:0000269|PubMed:26037923}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:76452; Evidence={ECO:0000305|PubMed:26037923}; CATALYTIC ACTIVITY: Reaction=(E)-coniferol + A = (E)-coniferaldehyde + AH2; Xref=Rhea:RHEA:76455, ChEBI:CHEBI:13193, ChEBI:CHEBI:16547, ChEBI:CHEBI:17499, ChEBI:CHEBI:17745; Evidence={ECO:0000269|PubMed:26037923}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:76456; Evidence={ECO:0000305|PubMed:26037923}; CATALYTIC ACTIVITY: Reaction=(E)-sinapyl alcohol + A = (E)-sinapaldehyde + AH2; Xref=Rhea:RHEA:76459, ChEBI:CHEBI:13193, ChEBI:CHEBI:17499, ChEBI:CHEBI:27949, ChEBI:CHEBI:64557; Evidence={ECO:0000269|PubMed:26037923}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:76460; Evidence={ECO:0000305|PubMed:26037923}; CATALYTIC ACTIVITY: Reaction=4-O-(beta-D-glucosyl)-(E)-coniferol + A = 4-O-(beta-D-glucosyl)-4-(E)-coniferyl aldehyde + AH2; Xref=Rhea:RHEA:76463, ChEBI:CHEBI:13193, ChEBI:CHEBI:16220, ChEBI:CHEBI:17499, ChEBI:CHEBI:136949; Evidence={ECO:0000269|PubMed:26037923}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:76464; Evidence={ECO:0000305|PubMed:26037923};
| null | null | null | null |
FUNCTION: Required for endosperm development and polar nuclei fusion (PubMed:15634699). Mediates oxidation of p-hydroxylated derivatives of cinnamyl alcohol (i.e. the monolignols p-coumaryl-, coniferyl-, and sinapyl alcohol) to their corresponding aldehydes. Can also use the beta-O-glycosylated form of coniferyl alcohol (coniferin) as substrate, but is much less efficient towards cinnamyl alcohol. The electron acceptor required for these reactions is not known, but does not seem to be dioxygen (PubMed:26037923). {ECO:0000269|PubMed:15634699, ECO:0000269|PubMed:26037923}.
|
Arabidopsis thaliana (Mouse-ear cress)
|
O64750
|
PSA2_ARATH
|
MAASSSHLFALPSPASPFLSAPNRNRVRVLAKSCPENQSFDSNDSDSSSETTHKAQGDQKSVSRRQWMTACVCASAALISNSYTFVSVQSAAALDKKPGGSCRNCQGSGAVLCDMCGGTGKWKALNRKRAKDVYEFTECPNCYGRGKLVCPVCLGTGLPNNKGLLRRPGARELLEKMYNGRLLPDS
| null |
COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250|UniProtKB:Q6A662}; Note=Binds 2 Zn(2+) ions per monomer. {ECO:0000250|UniProtKB:Q6A662};
|
megagametogenesis [GO:0009561]; photosystem I assembly [GO:0048564]; thylakoid membrane organization [GO:0010027]
|
chloroplast [GO:0009507]; chloroplast thylakoid [GO:0009534]; chloroplast thylakoid lumen [GO:0009543]; chloroplast thylakoid membrane [GO:0009535]; endoplasmic reticulum [GO:0005783]; nucleus [GO:0005634]
|
metal ion binding [GO:0046872]; protein-disulfide reductase (NAD(P)) activity [GO:0047134]
| null |
2.10.230.10;
|
DnaJ family
| null |
SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid lumen {ECO:0000269|PubMed:27047527}.
| null | null | null | null | null |
FUNCTION: Involved in female gametophyte development. Required for embryo sac development (PubMed:15634699). Nuclear genome-encoded factor required for the accumulation of photosystem I (PSI) during plant development (PubMed:25228689). Required for light acclimation and chloroplast development (PubMed:27047527). {ECO:0000269|PubMed:15634699, ECO:0000269|PubMed:25228689, ECO:0000269|PubMed:27047527}.
|
Arabidopsis thaliana (Mouse-ear cress)
|
O64752
|
JMJ15_ARATH
|
MEPFSAAQNKEDKDTSVEPPRRRCHRKNKGTNVEPPSSPYHPKVLARWDPANEKRPDIGEAPVFHPTSEEFEDTLAYIEKIRPLAESFGICRIVPPSNWSPPCRLKGDSIWKNKNFPTRVQFVDLLQNRGPVKKKTPKGRKRKRGKYSRTVAPKKRNGSVSKSVSTPKATEEENFGFESGPEFTLEKFEKYAQDFKDSYFERKDNVGDPSVEEIEGEYWRIIEKETNEVKVLYGTDLENPILGSGFSKGVKIPTRRNDMDKYISSGWNLNNLARLQGSLLSFEDCEISGVQVPWLYVGMCFSTFCWHVEDNHLYSLNYHHFGEPKVWYGVPGSHATGLEKAMRKHLPDLFDEQPDLLHELVTQFSPTILKNEGVPVYRAVQNAGEYVLTFPRAYHSGFNCGFNCAEAVNVAPVDWLAHGQNAVEIYSQETRKTSLSHDKILLGAAFEAVKSLSAHGEDNTKRFSWKRFCGKDGIITKAIEARLRMEEKRIEALGNGFSLVKMDKDFDSNCERECISCFSDLHLSATGCKNCSSLEEYGCTKHDICSCEGKDRFIFLRYTIDELSSLVRALEGESDDLKAWLSKVMEGCSETQKGESSGIIVKEKQVQEECFDLNGECNKSSEICEDASIMDLAAYHVEPINLGFLVVGKLWCNKHAIFPKGFKSRVKFYNVQDPMRISYYVSEIVDAGLLGPLFKVTLEESQDESFSYASPQKCWEMVLLRVKEEIMRRSNQKQDVHMLESIDGLKMFGFRSPFIVQATEALDPNHGQVEYWNHKNEKDSLEMKDCFMSNSSQSLSKARLFGVDLN
|
1.14.11.-
|
COFACTOR: Name=Fe(2+); Xref=ChEBI:CHEBI:29033; Evidence={ECO:0000250|UniProtKB:Q8GUI6}; Note=Binds 1 Fe(2+) ion per subunit. {ECO:0000250|UniProtKB:Q8GUI6};
|
embryo development ending in seed dormancy [GO:0009793]; negative regulation of DNA-templated transcription [GO:0045892]; negative regulation of gene expression, epigenetic [GO:0045814]; pollen development [GO:0009555]; positive regulation of response to salt stress [GO:1901002]; regulation of DNA-templated transcription [GO:0006355]; regulation of flower development [GO:0009909]; response to salt [GO:1902074]
|
chromatin [GO:0000785]; nucleus [GO:0005634]
|
histone H3K4me/H3K4me2/H3K4me3 demethylase activity [GO:0034647]; metal ion binding [GO:0046872]
|
PF05965;PF05964;PF02373;PF02375;PF02928;
|
3.30.160.360;2.60.120.650;
|
JARID1 histone demethylase family
| null |
SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00537, ECO:0000255|PROSITE-ProRule:PRU00768}.
|
CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + N(6),N(6),N(6)-trimethyl-L-lysyl(4)-[histone H3] + O2 = CO2 + formaldehyde + N(6),N(6)-dimethyl-L-lysyl(4)-[histone H3] + succinate; Xref=Rhea:RHEA:60212, Rhea:RHEA-COMP:15537, Rhea:RHEA-COMP:15540, ChEBI:CHEBI:15379, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, ChEBI:CHEBI:16842, ChEBI:CHEBI:30031, ChEBI:CHEBI:61961, ChEBI:CHEBI:61976; Evidence={ECO:0000269|PubMed:22555401}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60213; Evidence={ECO:0000269|PubMed:22555401};
| null | null | null | null |
FUNCTION: Histone demethylase that demethylates 'Lys-4' (H3K4me) of histone H3 with a specific activity for H3K4me3 (PubMed:22555401). No activity on H3K4me2, H3K4me1, H3K9me3/2, H3K27me3/2 and H3K36me3/2 (PubMed:22555401). Involved in the control of flowering time by demethylating H3K4me3 at the FLC locus and repressing its expression (PubMed:22555401). The repression of FLC level and reduction in H3K4me3 at the FLC locus results in induction of the flowering activator FT, which is a downstream target of FLC (PubMed:22555401). Promotes salt tolerance by down-regulating the expression of several transcriptions factors involved in stress responses via H3K4me3 and H3K4me2 demethylation (PubMed:25009544). {ECO:0000269|PubMed:22555401, ECO:0000269|PubMed:25009544}.
|
Arabidopsis thaliana (Mouse-ear cress)
|
O64763
|
ATL9_ARATH
|
MAILDTKSSRWIPHNLLFLLLLLLLQSVPYGFGQTQTTPPGTTKTKPNDPVVVVITVLFLVIFFMVFGSIFCRRSNAQFSRSSIFRSTDADAESQVVRIRRLTARGLDAEAIETFPTFLYSEVKAVRIGKGGVECAVCLCEFEDDETLRLMPPCCHVFHADCVDVWLSEHSTCPLCRADLVLNQQGDDDDSTESYSGTDPGTISSSTDPERGMVLESSDAHLLDAVTWSNSNITPRSKSTGLSSWQITGILFPRSHSTGHSLIQPAGNLDRFTLRLPDDVRRQLMKTSRTMGHVALLPQARSSRSGYRSGSVGSERSAFPYGRKSNNNNRRLHSLSFSFSFRSGSVRSTFSGDAPKNLPTSIEAGERSFERLRPDERV
|
2.3.2.27
| null |
defense response to fungus [GO:0050832]; protein ubiquitination [GO:0016567]; response to chitin [GO:0010200]
|
membrane [GO:0016020]
|
metal ion binding [GO:0046872]; ubiquitin-protein transferase activity [GO:0004842]
|
PF13639;
|
3.30.40.10;
|
RING-type zinc finger family, ATL subfamily
| null |
SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}.
|
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; Evidence={ECO:0000269|PubMed:15644464};
| null |
PATHWAY: Protein modification; protein ubiquitination.
| null | null |
FUNCTION: E3 ubiquitin-protein ligase able to catalyze polyubiquitination with ubiquitin-conjugating enzyme E2 UBC8 in vitro. May be involved in the early steps of the plant defense signaling pathway. {ECO:0000269|PubMed:15644464, ECO:0000269|PubMed:15923325}.
|
Arabidopsis thaliana (Mouse-ear cress)
|
O64765
|
UAP2_ARATH
|
MKEPTTEIEIETSAVATILPPPLPPTASPHQALVERLKDYGQEDVFSLWDELSPEERDLLLRDIENLDLPRIDRIIRCSLHSQGLPVAAIEPVPENCVSTVEERTKEDREKWWKMGLKAIYEGKLGVVLLSGGQGTRLGSSDPKGCYNIGLPSGKSLFQIQAERILCVQRLASQAMSEASPTRPVTIQWYIMTSPFTHEPTQKFFKSHKYFGLEPDQVTFFQQGTLPCISKDGKFIMETPFSLSKAPDGNGGVYTALKSSRLLEDMASRGIKYVDCYGVDNVLVRVADPTFLGYFIDKSAASAAKVVRKAYPQEKVGVFVRRGKGGPLTVVEYTELDQSMASATNQQTGRLQYCWSNVCLHMFTLDFLNQVANGLEKDSVYHLAEKKIPSINGDIVGLKLEQFIFDCFPYAPSTALFEVLREEEFAPVKNANGSNYDTPESARLLVLRLHTRWVIAAGGFLTHSVPLYATGVEVSPLCSYAGENLEAICRGRTFHAPCEISL
|
2.7.7.23; 2.7.7.83; 2.7.7.9
|
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:20557289}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000269|PubMed:20557289};
|
embryo development ending in seed dormancy [GO:0009793]; embryo sac development [GO:0009553]; pollen development [GO:0009555]; UDP-glucose metabolic process [GO:0006011]; UDP-N-acetylgalactosamine metabolic process [GO:0019276]; UDP-N-acetylglucosamine biosynthetic process [GO:0006048]; UDP-N-acetylglucosamine metabolic process [GO:0006047]
|
cytoplasm [GO:0005737]
|
UDP-N-acetylgalactosamine diphosphorylase activity [GO:0052630]; UDP-N-acetylglucosamine diphosphorylase activity [GO:0003977]; UTP:glucose-1-phosphate uridylyltransferase activity [GO:0003983]
|
PF01704;
| null |
UDPGP type 1 family
| null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
|
CATALYTIC ACTIVITY: Reaction=H(+) + N-acetyl-alpha-D-glucosamine 1-phosphate + UTP = diphosphate + UDP-N-acetyl-alpha-D-glucosamine; Xref=Rhea:RHEA:13509, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019, ChEBI:CHEBI:46398, ChEBI:CHEBI:57705, ChEBI:CHEBI:57776; EC=2.7.7.23; Evidence={ECO:0000269|PubMed:20557289}; CATALYTIC ACTIVITY: Reaction=H(+) + N-acetyl-alpha-D-galactosamine 1-phosphate + UTP = diphosphate + UDP-N-acetyl-alpha-D-galactosamine; Xref=Rhea:RHEA:34363, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019, ChEBI:CHEBI:46398, ChEBI:CHEBI:61970, ChEBI:CHEBI:67138; EC=2.7.7.83; Evidence={ECO:0000269|PubMed:20557289}; CATALYTIC ACTIVITY: Reaction=alpha-D-glucose 1-phosphate + H(+) + UTP = diphosphate + UDP-alpha-D-glucose; Xref=Rhea:RHEA:19889, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019, ChEBI:CHEBI:46398, ChEBI:CHEBI:58601, ChEBI:CHEBI:58885; EC=2.7.7.9; Evidence={ECO:0000269|PubMed:20557289};
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=180 uM for GlcNAc-1-P {ECO:0000269|PubMed:20557289}; KM=203 uM for UTP {ECO:0000269|PubMed:20557289}; KM=65 uM for UDP-GlcNAc {ECO:0000269|PubMed:20557289}; KM=808 uM for UDP-GalNAc {ECO:0000269|PubMed:20557289};
|
PATHWAY: Nucleotide-sugar biosynthesis; UDP-N-acetyl-alpha-D-glucosamine biosynthesis; UDP-N-acetyl-alpha-D-glucosamine from N-acetyl-alpha-D-glucosamine 1-phosphate: step 1/1.
| null | null |
FUNCTION: Uridylyltransferase involved in the biosynthesis of UDP-glucosamine, an essential precursor for glycoprotein and glycolipid synthesis. Can use UDP-glucosamine, the 4-epimer UDP-galactosamine and UDP-glucose as substrates (PubMed:20557289). Acts redundantly with GLCNAC1PUT1. Required for gametogenesis and embryo development (PubMed:25231969). {ECO:0000269|PubMed:20557289, ECO:0000269|PubMed:25231969}.
|
Arabidopsis thaliana (Mouse-ear cress)
|
O64768
|
RAF24_ARATH
|
MDQAKGYEHVRYTAPDPRDEGLGSINQRFSHDSSTNVNTYVRPPDYGVSTPARPVLNYSIQTGEEFAFEFMRDRVIMKPQFIPNVYGEHSGMPVSVNLSALGMVHPMSESGPNATVLNIEEKRQSFEHERKPPSRIEDKTYHELVQSAPVISSKNDTGQRRHSLVSSRASDSSLNRAKFLCSFGGKVIPRPRDQKLRYVGGETRIIRISKTISFQELMHKMKEIFPEARTIKYQLPGEDLDALVSVSSDEDLQNMMEECIVFGNGGSEKPRMFLFSSSDIEEAQFVMEHAEGDSEVQYVVAVNGMDLSSRRSSLGLSPPGNNLDELLHGNFDRKIDRAATEPAVASLTPLAGNESLPASQTSQPVTGFSTGNEPFSQPYLGQQLQFPGLGNHQIYTSGHMASIGYIDEKRSAPLHVQPQPHYIPYSVNPETPLESLVPHYPQKPEQGFLREEQIFHVQDPETSSKEAKMRRDDSFQKVNDHPISTVESNLSAKEPKMRRESSTPRVNEYPVSSMPSDLIVPDDLPKEEAPIVTQTSSSTPDPSSSTLSEKSLRKSEDHVENNLSAKEPKMRKEHSTTRVNEYSVSSVSSDSMVPDQALKEEAPISMKISNSTPDPKSLVYPEKSLRTSQEKTGAFDTTNEGMKKNQDNQFCLLGGFSVSGHGTSNNSSSNVSNFDQPVTQQRVFHSERTVRDPTETNRLSKSDDSLASQFVMAQTTSDAFLPISESSETSHEANMESQNVHPTAPVIPAPDSIWTAEGSMSQSEKKNVETNTPEHVSQTETSAKAVPQGHNEKGDIVVDINDRFPREFLADILKTKESLNFPGLGPLHADGAGVSLNIQNNDPKTWSYFRNLAQDEFERKDLSLMDQDHPGFPTSMTNTNGVPIDYSYPPLQSEKVASSQIHPQIHFDGNIKPDVSTITIPDLNTVDTQEDYSQSQIKGAESTDATLNAGVPLIDFMAADSGMRSLQVIKNDDLEELKELGSGTFGTVYHGKWRGTDVAIKRIKRSCFIGRSSEQERLTSEFWHEAEILSKLHHPNVMAFYGVVKDGPGGTLATVTEYMVNGSLRHVLLSNRHLDRRKRLIIAMDAAFGMEYLHSKSIVHFDLKCDNLLVNLKDPARPICKVGDFGLSKIKRNTLVTGGVRGTLPWMAPELLSGSSSKVSEKVDVFSFGIVLWEILTGEEPYANMHYGAIIGGIVNNTLRPTVPNYCDPEWRMLMEQCWAPDPFVRPAFPEIARRLRTMSSSAVHTKPHAVNHQIHK
|
2.7.11.1
| null |
cellular response to auxin stimulus [GO:0071365]; phosphorylation [GO:0016310]; regulation of auxin mediated signaling pathway [GO:0010928]; response to auxin [GO:0009733]; signal transduction [GO:0007165]
|
cytoplasm [GO:0005737]
|
ATP binding [GO:0005524]; protein serine/threonine kinase activity [GO:0004674]; protein serine/threonine/tyrosine kinase activity [GO:0004712]
|
PF00564;PF07714;
|
1.10.510.10;
|
Protein kinase superfamily, Ser/Thr protein kinase family
|
PTM: Hyperphosphorylated in response to auxin in an ABP1- and TMK1-dependent manner. {ECO:0000269|PubMed:38128538}.
|
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:38128538}. Note=Broadly distributed to both membrane-associated and intracellular punctate structures. {ECO:0000269|PubMed:38128538}.
|
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:0000255|PROSITE-ProRule:PRU10027}; 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:0000255|PROSITE-ProRule:PRU10027};
| null | null | null | null |
FUNCTION: RAF-like protein kinase acting, together with RAF20, as a central mediator of a fast response pathway to auxin involving proteins phosphorylation, and leading to rapid cellular responses including membrane depolarization and cytoplasmic streaming (PubMed:38128538). Required for general growth and developmental process (PubMed:38128538). {ECO:0000269|PubMed:38128538}.
|
Arabidopsis thaliana (Mouse-ear cress)
|
O64782
|
SD129_ARATH
|
MGMVLFACLLLLIIFPTCGYAAINTSSPLSIRQTLSSPGGFYELGFFSPNNTQNQYVGIWFKKIVPRVVVWVANRDTPVTSSAANLTISSNGSLILLDGKQDVIWSTGKAFTSNKCHAELLDTGNFVVIDDVSGNKLWQSFEHLGNTMLPQSSLMYDTSNGKKRVLTTWKSNSDPSPGEFSLEITPQIPTQGLIRRGSVPYWRCGPWAKTRFSGISGIDASYVSPFSVVQDTAAGTGSFSYSTLRNYNLSYVTLTPEGKMKILWDDGNNWKLHLSLPENPCDLYGRCGPYGLCVRSDPPKCECLKGFVPKSDEEWGKGNWTSGCVRRTKLSCQAKSSMKTQGKDTDIFYRMTDVKTPDLHQFASFLNAEQCYQGCLGNCSCTAFAYISGIGCLVWNGELADTVQFLSSGEFLFIRLASSELAGSSRRKIIVGTTVSLSIFLILVFAAIMLWRYRAKQNDAWKNGFERQDVSGVNFFEMHTIRTATNNFSPSNKLGQGGFGPVYKGKLVDGKEIGVKRLASSSGQGTEEFMNEITLISKLQHRNLVRLLGYCIDGEEKLLIYEFMVNKSLDIFIFDPCLKFELDWPKRFNIIQGIARGLLYLHRDSRLRVIHRDLKVSNILLDDRMNPKISDFGLARMFQGTQYQDNTRRVVGTLGYMSPEYAWAGLFSEKSDIYSFGVLMLEIISGKRISRFIYGDESKGLLAYTWDSWCETGGSNLLDRDLTDTCQAFEVARCVQIGLLCVQHEAVDRPNTLQVLSMLTSATDLPVPKQPIFAVHTLNDMPMLQANSQDFLSVNEMTESMIQGR
|
2.7.12.1
| null |
detection of lipopolysaccharide [GO:0032497]; innate immune response [GO:0045087]; lipopolysaccharide-mediated signaling pathway [GO:0031663]; pattern recognition receptor signaling pathway [GO:0002221]; protein autophosphorylation [GO:0046777]; recognition of pollen [GO:0048544]
|
plasma membrane [GO:0005886]
|
ATP binding [GO:0005524]; calmodulin binding [GO:0005516]; carbohydrate binding [GO:0030246]; pattern recognition receptor activity [GO:0038187]; protein kinase activity [GO:0004672]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674]; protein serine/threonine/tyrosine kinase activity [GO:0004712]; protein tyrosine kinase activity [GO:0004713]; ubiquitin protein ligase binding [GO:0031625]
|
PF01453;PF11883;PF08276;PF07714;PF00954;
|
2.90.10.10;1.10.510.10;
|
Protein kinase superfamily, Ser/Thr protein kinase family
|
PTM: Autophosphorylated at Tyr-600 (PubMed:31922267). Autophosphorylation at Tyr-600 is required for downstream phosphorylation of the receptor-like cytoplasmic kinase PBL34, PBL35 and PBL36, and activation of plant immunity (PubMed:31922267). {ECO:0000269|PubMed:31922267}.
|
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:25729922, ECO:0000269|PubMed:31922267}; Single-pass type I membrane protein {ECO:0000255}.
|
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=2.7.12.1; Evidence={ECO:0000269|PubMed:31922267}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17990; Evidence={ECO:0000269|PubMed:31922267}; 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=2.7.12.1; Evidence={ECO:0000269|PubMed:31922267}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:46609; Evidence={ECO:0000269|PubMed:31922267}; 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=2.7.12.1; Evidence={ECO:0000269|PubMed:31922267}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:10597; Evidence={ECO:0000269|PubMed:31922267};
| null | null | null | null |
FUNCTION: S-domain receptor protein kinase involved in lipopolysaccharide (LPS) sensing (PubMed:25729922, PubMed:29431629, PubMed:31922267). Specifically detects LPS of Pseudomonas and Xanthomonas species (PubMed:25729922). LPS are major components of the outer membrane of Gram-negative bacteria and are important microbe-associated molecular patterns (MAMPs) that trigger biphasic production of reactive oxygen species (ROS) and immune responses in plants (PubMed:25729922, PubMed:29431629). Seems to be only partially associated with the second LPS-triggered ROS burst (PubMed:29431629). Mediates defense signaling in response to the medium-chain 3-hydroxy fatty acid 3-OH-C10:0, a pathogen-associated molecular pattern (PAMP) which induces autophosphorylation at Tyr-600 (PubMed:31922267). Autophosphorylation at Tyr-600 is required for downstream phosphorylation of the receptor-like cytoplasmic kinase PBL34, PBL35 and PBL36, and activation of plant immunity (PubMed:31922267). {ECO:0000269|PubMed:25729922, ECO:0000269|PubMed:29431629, ECO:0000269|PubMed:31922267}.; FUNCTION: (Microbial infection) Targeted by the bacterial type III effector protein tyrosine phosphatase HopAO1 from Pseudomonas syringae (PubMed:31922267). HopAO1 dephosphorylates Tyr-600, which suppresses the immune response (PubMed:31922267). {ECO:0000269|PubMed:31922267}.
|
Arabidopsis thaliana (Mouse-ear cress)
|
O64816
|
CSK2P_ARATH
|
MALRPCTGFTISSLRNASAANNNLFSLLSFSSSSPAKRNLLLSSLQDNLRRFASSASLYRQHLRNQQQQHQQQQQSRVKEKSETLAQKIGKSIRRAGAPSKARVYADVNVVRPKDYWDYESLAVQWGVQDDYEVVRKVGRGKYSEVFEGIHATDNEKCVIKILKPVKKKKIKREIKILQNLCGGPNIVKLLDIVRDQQSKTPSLIFEHVNNKDFKVLYPTLSDYDVRYYIFELLKALDFCHSRGIMHRDVKPHNVMIDHEQRKLRLIDWGLAEFYHPGKEYNVRVASRYFKGPELLVDLQDYDYSLDLWSLGCMFAGMIFRKEPFFYGHDNYDQLVKIAKVLGTDELNAYLNKYRIELDPNLTSLVGRHSRKPWTKFINSENQHLAVPEAVDFVDKLLRYDHQERPTAKEAMAHPYFYPIRNAESSRTPRSQ
|
2.7.11.1
| null |
cellular response to abscisic acid stimulus [GO:0071215]; chloroplast-nucleus signaling pathway [GO:0010019]; DNA damage response [GO:0006974]; negative regulation of seed germination [GO:0010187]; phosphorylation [GO:0016310]; regulation of cell cycle [GO:0051726]; regulation of growth [GO:0040008]; regulation of photoperiodism, flowering [GO:2000028]; regulation of transcription by RNA polymerase I [GO:0006356]; regulation of transcription by RNA polymerase III [GO:0006359]
|
chloroplast [GO:0009507]; cytosol [GO:0005829]; nucleus [GO:0005634]; protein kinase CK2 complex [GO:0005956]
|
ATP binding [GO:0005524]; kinase activity [GO:0016301]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674]
|
PF00069;
|
1.10.510.10;
|
Protein kinase superfamily, Ser/Thr protein kinase family, CK2 subfamily
| null |
SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000269|PubMed:16926165}.
|
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: Casein kinases are operationally defined by their preferential utilization of acidic proteins such as caseins as substrates. The alpha chain contains the catalytic site (By similarity). Involved in the regulation of various developmental processes (PubMed:26025542). Involved in the regulation of plant growth and flowering time (PubMed:26883224). Involved in retrograde signaling in plant responses to abscisic acid (ABA) and heat stress. May act as an enhancing factor in abiotic stress signaling through modulation of the expression of some molecular players in retrograde signaling (PubMed:24803505). Phosphorylates RuBisCo activase (RCA) at Thr-78 (PubMed:27064346). {ECO:0000250|UniProtKB:Q08467, ECO:0000269|PubMed:24803505, ECO:0000269|PubMed:26025542, ECO:0000269|PubMed:26883224, ECO:0000269|PubMed:27064346}.
|
Arabidopsis thaliana (Mouse-ear cress)
|
O64817
|
CSK23_ARATH
|
MSKARVYTDVNVVRPKEYWDYESLVVQWGHQDDYEVVRKVGRGKYSEVFEGKNVNTNERCVIKILKPVKKKKIKREIKILQNLCGGPNIVKLYDIVRDEHSKTPSLVFEFVNSVDFKVLYPTLTDYDIRYYIYELLKALDFCHSQGIMHRDVKPHNVMIDHQLRKLRLIDWGLAEFYHPGKEYNVRVASRYFKGPELLVDLQDYDYSLDMWSLGCMFAGMIFRKEPFFYGHDNHDQLVKIAKVLGTNELDHYLNKYQLDLDPQLEALVGRHVPKPWSKFINADNQHLVSPEAIDFLDKLLQYDHQDRLTAREAMDHPYFAQVKAAESSRLRTQ
|
2.7.11.1
| null |
chromatin organization [GO:0006325]; circadian rhythm [GO:0007623]; DNA repair [GO:0006281]; phosphorylation [GO:0016310]; regulation of cell cycle [GO:0051726]; regulation of circadian rhythm [GO:0042752]; response to gamma radiation [GO:0010332]; response to UV-C [GO:0010225]
|
cytoplasm [GO:0005737]; cytosol [GO:0005829]; nucleolus [GO:0005730]; nucleus [GO:0005634]; protein kinase CK2 complex [GO:0005956]
|
ATP binding [GO:0005524]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674]
|
PF00069;
|
1.10.510.10;
|
Protein kinase superfamily, Ser/Thr protein kinase family, CK2 subfamily
| null |
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16926165, ECO:0000269|PubMed:21735091}. Nucleus, nucleolus {ECO:0000269|PubMed:16926165}. Cytoplasm {ECO:0000269|PubMed:21735091}.
|
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: Casein kinases are operationally defined by their preferential utilization of acidic proteins such as caseins as substrates. The alpha chain contains the catalytic site. The tetrameric holoenzyme CK2 is composed of two alpha and two beta subunits (By similarity). Acts as a circadian clock component that maintains the correct period length through phosphorylation of CCA1 (PubMed:21900482). {ECO:0000250|UniProtKB:Q08467, ECO:0000269|PubMed:21900482}.
|
Arabidopsis thaliana (Mouse-ear cress)
|
O64825
|
LYK4_ARATH
|
MISFSFHLLVFILLSLSSFATAQQPYVGISTTDCSVSDNTTSVFGYSCNGLNKTCQAYVIFRSTPSFSTVTSISSLFSVDPSLVSSLNDASPSTSFPSGQQVIIPLTCSCTGDDSQSNITYTIQPNDSYFAIANDTLQGLSTCQALAKQNNVSSQSLFPGMRIVVPIRCACPTAKQINEDGVKYLMSYTVVFEDTIAIISDRFGVETSKTLKANEMSFENSEVFPFTTILIPLVNPPANTNSLIPPPPPPPPQSVSPPPLSPDGRKSKKKTWVYALAGVLGGALVLSVIGAAIFCLSKKKTKTQTQEETGNLDSFMGKKPPMSDQEFDPLDGLSGMVVESLKVYKFHELQSATSDFTSSSSIGGSGYIGKINGDGAMIKKIEGNASEEVNLLSKLNHLNIIRLSGFCFHEGDWYLVYEHASNGSLSEWIHTTKSLLSLTQKLQIALDIATGLNYLHNFADPPYVHRDLNSNNVFLDLEFRAKIGSLGSARSTTEDFVLTKHVEGTRGYLAPEYLEHGLVSTKLDVYAFGVVLLEIVTGKEASELKKEIDEGKAIDEILIHGRLLPEGLTSFVERLVVDCLKKDHLNRPSMDENVMSLSKILAATQNWEESSY
|
2.7.11.1
| null |
cellular response to chitin [GO:0071323]; cellular response to molecule of bacterial origin [GO:0071219]; innate immune response [GO:0045087]; phosphorylation [GO:0016310]
|
plasma membrane [GO:0005886]
|
ATP binding [GO:0005524]; chitin binding [GO:0008061]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674]
|
PF01476;PF07714;
|
3.10.350.10;1.10.510.10;
|
Protein kinase superfamily, Ser/Thr protein kinase family
|
PTM: Autophosphorylated; induced by chitin and derivatives. {ECO:0000250}.
|
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:22744984}; Single-pass membrane protein {ECO:0000269|PubMed:22744984}.
|
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: Lysin motif (LysM) receptor kinase that functions as a cell surface receptor in chitin elicitor (chitooligosaccharides) signaling leading to innate immunity. Recognizes microbe-derived N-acetylglucosamine (NAG)-containing ligands. Involved in the resistance to the pathogenic fungus Alternaria brassicicola and to the bacterial pathogen the bacterial pathogen Pseudomonas syringae pv tomato DC3000, probably by sensing microbe-associated molecular pattern (MAMP) and pathogen-associated molecular patterns (PAMP). May play a role in detecting peptidoglycans (e.g. PGNs) during bacterial growth. {ECO:0000269|PubMed:22744984}.
|
Arabidopsis thaliana (Mouse-ear cress)
|
O64827
|
SUVR5_ARATH
|
MEVKMDELVLDVDVEEATGSELLVKSEPEADLNAVKSSTDLVTVTGPIGKNGEGESSPSEPKWLQQDEPIALWVKWRGKWQAGIRCAKADWPLTTLRGKPTHDRKKYCVIFFPHTKNYSWADMQLVRSINEFPDPIAYKSHKIGLKLVKDLTAARRYIMRKLTVGMFNIVDQFPSEVVSEAARDIIIWKEFAMEATRSTSYHDLGIMLVKLHSMILQRYMDPIWLENSFPLWVQKCNNAVNAESIELLNEEFDNCIKWNEVKSLSESPMQPMLLSEWKTWKHDIAKWFSISRRGVGEIAQPDSKSVFNSDVQASRKRPKLEIRRAETTNATHMESDTSPQGLSAIDSEFFSSRGNTNSPETMKEENPVMNTPENGLDLWDGIVVEAGGSQFMKTKETNGLSHPQDQHINESVLKKPFGSGNKSQQCIAFIESKGRQCVRWANEGDVYCCVHLASRFTTKSMKNEGSPAVEAPMCGGVTVLGTKCKHRSLPGFLYCKKHRPHTGMVKPDDSSSFLVKRKVSEIMSTLETNQCQDLVPFGEPEGPSFEKQEPHGATSFTEMFEHCSQEDNLCIGSCSENSYISCSEFSTKHSLYCEQHLPNWLKRARNGKSRIISKEVFVDLLRGCLSREEKLALHQACDIFYKLFKSVLSLRNSVPMEVQIDWAKTEASRNADAGVGEFLMKLVSNERERLTRIWGFATGADEEDVSLSEYPNRLLAITNTCDDDDDKEKWSFSGFACAICLDSFVRRKLLEIHVEERHHVQFAEKCMLLQCIPCGSHFGDKEQLLVHVQAVHPSECKSLTVASECNLTNGEFSQKPEAGSSQIVVSQNNENTSGVHKFVCKFCGLKFNLLPDLGRHHQAEHMGPSLVGSRGPKKGIRFNTYRMKSGRLSRPNKFKKSLGAVSYRIRNRAGVNMKRRMQGSKSLGTEGNTEAGVSPPLDDSRNFDGVTDAHCSVVSDILLSKVQKAKHRPNNLDILSAARSACCRVSVETSLEAKFGDLPDRIYLKAAKLCGEQGVQVQWHQEGYICSNGCKPVKDPNLLHPLIPRQENDRFGIAVDAGQHSNIELEVDECHCIMEAHHFSKRPFGNTAVLCKDISFGKESVPICVVDDDLWNSEKPYEMPWECFTYVTNSILHPSMDLVKENLQLRCSCRSSVCSPVTCDHVYLFGNDFEDARDIYGKSMRCRFPYDGKQRIILEEGYPVYECNKFCGCSRTCQNRVLQNGIRAKLEVFRTESKGWGLRACEHILRGTFVCEYIGEVLDQQEANKRRNQYGNGDCSYILDIDANINDIGRLMEEELDYAIDATTHGNISRFINHSCSPNLVNHQVIVESMESPLAHIGLYASMDIAAGEEITRDYGRRPVPSEQENEHPCHCKATNCRGLLS
|
2.1.1.-
| null |
chromatin remodeling [GO:0006338]; methylation [GO:0032259]; negative regulation of gene expression, epigenetic [GO:0045814]
|
chromosome [GO:0005694]; nucleus [GO:0005634]
|
DNA-binding transcription factor activity [GO:0003700]; histone H3 methyltransferase activity [GO:0140938]; sequence-specific DNA binding [GO:0043565]; zinc ion binding [GO:0008270]
|
PF05033;PF00856;PF18868;
|
3.30.160.60;2.170.270.10;
|
Class V-like SAM-binding methyltransferase superfamily
| null |
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:17224141}. Chromosome {ECO:0000250|UniProtKB:Q5DW34}. Note=Associates with euchromatic regions. {ECO:0000250|UniProtKB:Q5DW34}.
|
CATALYTIC ACTIVITY: Reaction=L-lysyl-[histone] + S-adenosyl-L-methionine = H(+) + N(6)-methyl-L-lysyl-[histone] + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:10024, Rhea:RHEA-COMP:9845, Rhea:RHEA-COMP:9846, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:61929; Evidence={ECO:0000269|PubMed:17224141};
| null | null | null | null |
FUNCTION: Histone methyltransferase that functions together with its binding partner LDL1/SWP1 as one of the regulators of flower timing in Arabidopsis (PubMed:17224141). Mediates H3K9me2 deposition and regulates gene expression in a DNA methylation-independent manner. Binds DNA through its zinc fingers and represses the expression of a subset of stimulus response genes. May represent a novel mechanism for plants to regulate their chromatin and transcriptional state, which may allow for the adaptability and modulation necessary to rapidly respond to environment or developmental cues (PubMed:23071452). {ECO:0000269|PubMed:17224141, ECO:0000269|PubMed:23071452}.
|
Arabidopsis thaliana (Mouse-ear cress)
|
O64879
|
BGL15_ARATH
|
MRGNYLSLLVVLIVLASNDVLANNNSSTPKLRRSDFPEDFIFGSATSAYQVEGGAHEDGRGPSIWDTFSEKYPEKIKDGSNGSVADNSYHLYKEDVALLHQIGFNAYRFSISWSRILPRGNLKGGINQAGIDYYNNLINELLSKGIKPFATMFHWDTPQALEDAYGGFRGAEIVNDFRDYADICFKNFGDRVKHWMTLNEPLTVVQQGYVAGVMAPGRCSKFTNPNCTDGNGATEPYIVGHNLILSHGAAVQVYREKYKASQQGQVGIALNAGWNLPYTESPKDRLAAARAMAFTFDYFMEPLVTGKYPVDMVNNVKGRLPIFTAQQSKMLKGSYDFIGINYYSSTYAKDVPCSTKDVTMFSDPCASVTGERDGVPIGPKAASDWLLIYPKGIRDLVLYAKYKFKDPVMYITENGRDEFSTNKIFLKDGDRIDYYARHLEMVQDAISVGANVKGFFAWSLLDNFEWAMGYTVRFGLVYVDFKDGCKRYPKKSAEWFRKLLNEKKND
|
3.2.1.21
| null |
carbohydrate metabolic process [GO:0005975]; kaempferol O-glucoside metabolic process [GO:0033329]; quercetin O-glucoside metabolic process [GO:0033302]
|
apoplast [GO:0048046]; Golgi apparatus [GO:0005794]; plant-type cell wall [GO:0009505]; plasmodesma [GO:0009506]
|
beta-glucosidase activity [GO:0008422]; scopolin beta-glucosidase activity [GO:0102483]
|
PF00232;
|
3.20.20.80;
|
Glycosyl hydrolase 1 family
| null |
SUBCELLULAR LOCATION: Secreted, extracellular space, apoplast {ECO:0000305|PubMed:25468534}.
|
CATALYTIC ACTIVITY: Reaction=Hydrolysis of terminal, non-reducing beta-D-glucosyl residues with release of beta-D-glucose.; EC=3.2.1.21; Evidence={ECO:0000269|PubMed:25468534};
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=51 uM for kaempferol 3-O-beta-glucoside-7-O-alpha-rhamnoside {ECO:0000269|PubMed:25468534}; KM=36 uM for quercetin 3-O-beta-glucoside-7-O-alpha-rhamnoside {ECO:0000269|PubMed:25468534}; KM=60 uM for kaempferol 3-O-beta-glucoside {ECO:0000269|PubMed:25468534}; KM=52 uM for quercetin 3-O-beta-glucoside {ECO:0000269|PubMed:25468534}; KM=2592 uM for p-nitrophenyl beta-D-glucoside {ECO:0000269|PubMed:25468534}; Vmax=1.08 umol/min/mg enzyme with kaempferol 3-O-beta-glucoside-7-O-alpha-rhamnoside as substrate {ECO:0000269|PubMed:25468534}; Vmax=0.89 umol/min/mg enzyme with quercetin 3-O-beta-glucoside-7-O-alpha-rhamnoside as substrate {ECO:0000269|PubMed:25468534}; Vmax=0.76 umol/min/mg enzyme with kaempferol 3-O-beta-glucoside as substrate {ECO:0000269|PubMed:25468534}; Vmax=0.47 umol/min/mg enzyme with quercetin 3-O-beta-glucoside as substrate {ECO:0000269|PubMed:25468534}; Vmax=3.37 umol/min/mg enzyme with p-nitrophenyl beta-D-glucoside as substrate {ECO:0000269|PubMed:25468534}; Note=kcat is 1.30 sec(-1) with kaempferol 3-O-beta-glucoside-7-O-alpha-rhamnoside as substrate. kcat is 1.10 sec(-1) with quercetin 3-O-beta-glucoside-7-O-alpha-rhamnoside as substrate. kcat is 0.92 sec(-1) with kaempferol 3-O-beta-glucoside as substrate. kcat is 0.57 sec(-1) with quercetin 3-O-beta-glucoside as substrate. kcat is 4.08 sec(-1) with p-nitrophenyl beta-D-glucoside as substrate. {ECO:0000269|PubMed:25468534};
| null |
BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 5.0. {ECO:0000269|PubMed:25468534};
| null |
FUNCTION: Beta-glucosidase involved in the rapid degradation of flavonol 3-O-beta-glucoside-7-O-alpha-rhamnosides during abiotic stress recovery. No activity with quercetin 3-O-alpha-rhamnoside, quercetin 3-O-beta-galactoside and rutin. {ECO:0000269|PubMed:25468534}.
|
Arabidopsis thaliana (Mouse-ear cress)
|
O64883
|
BGL26_ARATH
|
MAHLQRTFPTEMSKGRASFPKGFLFGTASSSYQYEGAVNEGARGQSVWDHFSNRFPHRISDSSDGNVAVDFYHRYKEDIKRMKDINMDSFRLSIAWPRVLPYGKRDRGVSEEGIKFYNDVIDELLANEITPLVTIFHWDIPQDLEDEYGGFLSEQIIDDFRDYASLCFERFGDRVSLWCTMNEPWVYSVAGYDTGRKAPGRCSKYVNGASVAGMSGYEAYIVSHNMLLAHAEAVEVFRKCDHIKNGQIGIAHNPLWYEPYDPSDPDDVEGCNRAMDFMLGWHQHPTACGDYPETMKKSVGDRLPSFTPEQSKKLIGSCDYVGINYYSSLFVKSIKHVDPTQPTWRTDQGVDWMKTNIDGKQIAKQGGSEWSFTYPTGLRNILKYVKKTYGNPPILITENGYGEVAEQSQSLYMYNPSIDTERLEYIEGHIHAIHQAIHEDGVRVEGYYVWSLLDNFEWNSGYGVRYGLYYIDYKDGLRRYPKMSALWLKEFLRFDQEDDSSTSKKEEKKESYGKQLLHSVQDSQFVHSIKDSGALPAVLGSLFVVSATVGTSLFFKGANN
|
3.2.1.21
| null |
carbohydrate metabolic process [GO:0005975]; defense response by callose deposition in cell wall [GO:0052544]; defense response to bacterium [GO:0042742]; defense response to fungus [GO:0050832]; glucosinolate metabolic process [GO:0019760]; indole glucosinolate catabolic process [GO:0042344]; induced systemic resistance [GO:0009682]; response to bacterium [GO:0009617]; response to salt stress [GO:0009651]
|
chloroplast envelope [GO:0009941]; membrane [GO:0016020]; peroxisome [GO:0005777]
|
beta-glucosidase activity [GO:0008422]; scopolin beta-glucosidase activity [GO:0102483]; thioglucosidase activity [GO:0019137]
|
PF00232;
|
3.20.20.80;
|
Glycosyl hydrolase 1 family
| null |
SUBCELLULAR LOCATION: Peroxisome {ECO:0000269|PubMed:16293760}.
|
CATALYTIC ACTIVITY: Reaction=Hydrolysis of terminal, non-reducing beta-D-glucosyl residues with release of beta-D-glucose.; EC=3.2.1.21; Evidence={ECO:0000269|PubMed:19095900};
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=722 uM for indol-3-yl-methylglucosinolate {ECO:0000269|PubMed:19095900}; KM=150 uM for 4-methyl-umbelliferyl-beta-D-glucoside {ECO:0000269|PubMed:19095900}; Vmax=7.5 umol/min/mg enzyme with indol-3-yl-methylglucosinolate as substrate {ECO:0000269|PubMed:19095900}; Vmax=0.76 umol/min/mg enzyme with 4-methyl-umbelliferyl-beta-D-glucoside as substrate {ECO:0000269|PubMed:19095900};
| null |
BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 6.0. {ECO:0000269|PubMed:19095900};
| null |
FUNCTION: Possesses beta-glucosidase activity toward 4-methyl-umbelliferyl-beta-D-glucoside in vitro. Possesses myrosinase activity toward indol-3-yl-methylglucosinolate (I3M) and 4-methoxy-indol-3-yl-methylglucosinolate (4MO-I3M) in vivo (PubMed:19095900). Component of an inducible preinvasion resistance mechanism that prevents penetration of the nonhost fungal species B.graminis and E.pisi (PubMed:16293760). Involved in indole glucosinolate (IGS) activation during pattern-triggered immunity (PTI). Functions as a myrosinase for the breakdown of flg22-triggered IGS. Required for both callose deposition and glucosinolate activation during pathogen-triggered resistance (PubMed:19095898). During fungal attack, required for IGS activation that mediates broad-spectrum antifungal defense (PubMed:19095900). {ECO:0000269|PubMed:16293760, ECO:0000269|PubMed:19095898, ECO:0000269|PubMed:19095900}.
|
Arabidopsis thaliana (Mouse-ear cress)
|
O64884
|
OFT20_ARATH
|
MALSKNSNSNSFNKKKVSYISVPSQIINSLSSSSLQSLLVSPKKSSRSTNRFSFSYRNPRIWFFTLFLVSLFGMLKLGFNVDPISLPFSRYPCSTTQQPLSFDGEQNAASHLGLAQEPILSTGSSNSNAIIQLNGGKNETLLTEGDFWKQPDGLGFKPCLGFTSQYRKDSNSILKNRWKYLLVVVSGGMNQQRNQIVDAVVIARILGASLVVPVLQVNVIWGDESEFADIFDLEHFKDVLADDVHIVSSLPSTHVMTRPVEEKRTPLHASPQWIRAHYLKRINRERVLLLRGLDSRLSKDLPSDLQKLRCKVAFQALRFSPRILELGNKLASRMRNQGQYLSLHLRMEKDVWVRTGCLPGLTPEYDEIVNSERERHPELLTGRSNMTYHERKLAGLCPLTALEVTRLLKALEAPKDARIYWAGGEPLGGKEVLEPLTKEFPQFYNKHDLALPGELEPFANKASVMAAIDYIVCEKSDVFIPSHGGNMGHALQGQRAYAGHKKYITPNKRQMLPYFMNSSLPESDFNRIVKDLHRESLGQPELRMSKAGKDVTKHPVPECMCSDRQQQEQQSDA
|
2.4.1.-
| null |
cell wall organization [GO:0071555]; fucose metabolic process [GO:0006004]
|
Golgi membrane [GO:0000139]
|
glycosyltransferase activity [GO:0016757]
|
PF10250;
| null |
Glycosyltransferase GT106 family
| null |
SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000269|Ref.11}; Single-pass type II membrane protein {ECO:0000305|Ref.11}.
| null | null |
PATHWAY: Glycan metabolism. {ECO:0000305}.
| null | null |
FUNCTION: May play a role in the biosynthesis of matrix polysaccharides and contribute to the biomechanics and development of the plant cell wall. {ECO:0000269|Ref.11}.
|
Arabidopsis thaliana (Mouse-ear cress)
|
O64903
|
NDK2_ARATH
|
MVGATVVSKWTPLCVASPPERNSASLNPHCSPARVNFRTALAAFRPQFRLFSRNSASRRRLRASSSAESGIFLPHLVASMEDVEETYIMVKPDGIQRGLVGEIISRFEKKGFKLIGLKMFQCPKELAEEHYKDLSAKSFFPNLIEYITSGPVVCMAWEGVGVVASARKLIGKTDPLQAEPGTIRGDLAVQTGRNIVHGSDSPENGKREIGLWFKEGELCKWDSALATWLRE
|
2.7.4.6
|
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
|
auxin-activated signaling pathway [GO:0009734]; CTP biosynthetic process [GO:0006241]; GTP biosynthetic process [GO:0006183]; phosphorylation [GO:0016310]; red, far-red light phototransduction [GO:0009585]; response to hydrogen peroxide [GO:0042542]; response to UV [GO:0009411]; UTP biosynthetic process [GO:0006228]
|
chloroplast [GO:0009507]; chloroplast envelope [GO:0009941]; chloroplast stroma [GO:0009570]; cytoplasm [GO:0005737]; nucleus [GO:0005634]; plastid [GO:0009536]; thylakoid [GO:0009579]
|
ATP binding [GO:0005524]; metal ion binding [GO:0046872]; nucleoside diphosphate kinase activity [GO:0004550]
|
PF00334;
|
3.30.70.141;
|
NDK family
|
PTM: Autophosphorylated. {ECO:0000269|PubMed:12506203}.
|
SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000269|PubMed:18431481}.
|
CATALYTIC ACTIVITY: Reaction=a 2'-deoxyribonucleoside 5'-diphosphate + ATP = a 2'-deoxyribonucleoside 5'-triphosphate + ADP; Xref=Rhea:RHEA:44640, ChEBI:CHEBI:30616, ChEBI:CHEBI:61560, ChEBI:CHEBI:73316, ChEBI:CHEBI:456216; EC=2.7.4.6; CATALYTIC ACTIVITY: Reaction=a ribonucleoside 5'-diphosphate + ATP = a ribonucleoside 5'-triphosphate + ADP; Xref=Rhea:RHEA:18113, ChEBI:CHEBI:30616, ChEBI:CHEBI:57930, ChEBI:CHEBI:61557, ChEBI:CHEBI:456216; EC=2.7.4.6;
| null | null | null | null |
FUNCTION: Major role in the synthesis of nucleoside triphosphates other than ATP. The ATP gamma phosphate is transferred to the NDP beta phosphate via a ping-pong mechanism, using a phosphorylated active-site intermediate. May activate MPK3 and MPK6. May be involved in the regulation of cellular redox state and hydrogen peroxide-mediated MAP kinase signaling. {ECO:0000269|PubMed:12506203}.
|
Arabidopsis thaliana (Mouse-ear cress)
|
O64948
|
LONP2_ARATH
|
MAETVELPSRLAILPFRNKVLLPGAIIRIRCTSHSSVTLVEQELWQKEEKGLIGILPVRDDAEGSSIGTMINPGAGSDSGERSLKFLVGTTDAQKSDAKDQQDLQWHTRGVAARALHLSRGVEKPSGRVTYVVVLEGLSRFNVQELGKRGPYSVARITSLEMTKAELEQVKQDPDFVALSRQFKTTAMELVSVLEQKQKTGGRTKVLLETVPIHKLADIFVASFEMSFEEQLSMLDSVDLKVRLSKATELVDRHLQSIRVAEKITQKVEGQLSKSQKEYLLRQQMRAIKEELGDNDDDEDDVAALERKMQAAGMPSNIWKHAQRELRRLKKMQPQQPGYNSSRVYLELLADLPWDKASEEHELDLKAAKERLDSDHYGLAKVKQRIIEYLAVRKLKPDARGPVLCFVGPPGVGKTSLASSIAAALGRKFVRLSLGGVKDEADIRGHRRTYIGSMPGRLIDGLKRVGVCNPVMLLDEIDKTGSDVRGDPASALLEVLDPEQNKSFNDHYLNVPYDLSKVVFVATANRVQPIPPPLLDRMELIELPGYTQEEKLKIAMRHLIPRVLDQHGLSSEFLKIPEAMVKNIIQRYTREAGVRSLERNLAALARAAAVMVAEHEQSLPLSKDVQKLTSPLLNGRMAEGGEVEMEVIPMGVNDHEIGGTFQSPSALVVDETMLEKILGPPRFDDSEAADRVASAGVSVGLVWTTFGGEVQFVEATSMVGKGEMHLTGQLGDVIKESAQLALTWVRARASDFKLALAGDMNVLDGRDIHIHFPAGAVPKDGPSAGVTLVTALVSLFSQKRVRADTAMTGEMTLRGLVLPVGGIKDKILAAHRYGIKRVILPQRNSKDLVEVPAAVLSSLEVILAKRMEDVLENAFEGGCPWRNNYSKL
|
3.4.21.53
| null |
lateral root development [GO:0048527]; protein import into peroxisome matrix, docking [GO:0016560]; protein processing [GO:0016485]; protein quality control for misfolded or incompletely synthesized proteins [GO:0006515]; protein targeting to peroxisome [GO:0006625]
|
intracellular organelle lumen [GO:0070013]; peroxisomal matrix [GO:0005782]; peroxisome [GO:0005777]
|
ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; ATP-dependent peptidase activity [GO:0004176]; serine-type endopeptidase activity [GO:0004252]
|
PF00004;PF05362;PF02190;
|
1.10.8.60;1.20.5.5270;1.20.58.1480;3.30.230.10;2.30.130.40;3.40.50.300;
|
Peptidase S16 family
| null |
SUBCELLULAR LOCATION: Peroxisome matrix {ECO:0000255|HAMAP-Rule:MF_03121, ECO:0000269|PubMed:19329564}.
|
CATALYTIC ACTIVITY: Reaction=Hydrolysis of proteins in presence of ATP.; EC=3.4.21.53; Evidence={ECO:0000255|HAMAP-Rule:MF_03121};
| null | null | null | null |
FUNCTION: ATP-dependent serine protease that mediates the selective degradation of misfolded and unassembled polypeptides in the peroxisomal matrix (By similarity). Necessary for type 2 peroxisome targeting signal (PTS2)-containing protein processing and facilitates peroxisome matrix protein import. {ECO:0000255|HAMAP-Rule:MF_03121, ECO:0000269|PubMed:19748917}.
|
Arabidopsis thaliana (Mouse-ear cress)
|
O64961
|
TPS9_SOLLC
|
MAASSADKCRPLANFHPSVWGYHFLSYTHEITNQEKVEVDEYKETIRKMLVETCDNSTQKLVLIDAMQRLGVAYHFDNEIETSIQNIFDASSKQNDNDNNLYVVSLRFRLVRQQGHYMSSDVFKQFTNQDGKFKETLTNDVQGLLSLYEASHLRVRNEEILEEALTFTTTHLESIVSNLSNNNNSLKVEVGEALTQPIRMTLPRMGARKYISIYENNDAHHHLLLKFAKLDFNMLQKFHQRELSDLTRWWKDLDFANKYPYARDRLVECYFWILGVYFEPKYSRARKMMTKVLNLTSIIDDTFDAYATFDELVTFNDAIQRWDANAIDSIQPYMRPAYQALLDIYSEMEQVLSKEGKLDRVYYAKNEMKKLVRAYFKETQWLNDCDHIPKYEEQVENAIVSAGYMMISTTCLVGIEEFISHETFEWLMNESVIVRASALIARAMNDIVGHEDEQERGHVASLIECYMKDYGASKQETYIKFLKEVTNAWKDINKQFFRPTEVPMFVLERVLNLTRVADTLYKEKDTYTNAKGKLKNMINSILIESVKI
|
4.2.3.-; 4.2.3.113; 4.2.3.15; 4.2.3.60
|
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000305|PubMed:9482865}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000305|PubMed:9482865}; Note=Binds 3 Mg(2+) or Mn(2+) ions per subunit. {ECO:0000305|PubMed:9482865};
|
diterpenoid biosynthetic process [GO:0016102]; terpenoid biosynthetic process [GO:0016114]
|
cytoplasm [GO:0005737]
|
germacrene C synthase activity [GO:0102904]; magnesium ion binding [GO:0000287]; myrcene synthase activity [GO:0050551]; terpene synthase activity [GO:0010333]
|
PF01397;PF03936;
|
1.10.600.10;1.50.10.130;
|
Terpene synthase family, Tpsa subfamily
| null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
|
CATALYTIC ACTIVITY: Reaction=(2E,6E)-farnesyl diphosphate = diphosphate + germacrene C; Xref=Rhea:RHEA:28302, ChEBI:CHEBI:33019, ChEBI:CHEBI:61478, ChEBI:CHEBI:175763; EC=4.2.3.60; Evidence={ECO:0000269|PubMed:21818683, ECO:0000269|PubMed:9482865}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:28303; Evidence={ECO:0000269|PubMed:21818683, ECO:0000269|PubMed:9482865}; CATALYTIC ACTIVITY: Reaction=(2E)-geranyl diphosphate = diphosphate + terpinolene; Xref=Rhea:RHEA:25500, ChEBI:CHEBI:9457, ChEBI:CHEBI:33019, ChEBI:CHEBI:58057; EC=4.2.3.113; Evidence={ECO:0000269|PubMed:21818683}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:25501; Evidence={ECO:0000269|PubMed:21818683}; CATALYTIC ACTIVITY: Reaction=(2E)-geranyl diphosphate = diphosphate + limonene; Xref=Rhea:RHEA:68640, ChEBI:CHEBI:15384, ChEBI:CHEBI:33019, ChEBI:CHEBI:58057; Evidence={ECO:0000269|PubMed:21818683}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68641; Evidence={ECO:0000269|PubMed:21818683}; CATALYTIC ACTIVITY: Reaction=(2E)-geranyl diphosphate = beta-myrcene + diphosphate; Xref=Rhea:RHEA:16965, ChEBI:CHEBI:17221, ChEBI:CHEBI:33019, ChEBI:CHEBI:58057; EC=4.2.3.15; Evidence={ECO:0000269|PubMed:21818683}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16966; Evidence={ECO:0000269|PubMed:21818683}; CATALYTIC ACTIVITY: Reaction=(2Z,6Z)-farnesyl diphosphate = diphosphate + germacrene C; Xref=Rhea:RHEA:68772, ChEBI:CHEBI:33019, ChEBI:CHEBI:60374, ChEBI:CHEBI:61478; Evidence={ECO:0000269|PubMed:21818683}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68773; Evidence={ECO:0000269|PubMed:21818683};
| null |
PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis. {ECO:0000269|PubMed:21818683, ECO:0000269|PubMed:9482865}.
| null | null |
FUNCTION: Involved in the biosynthesis of germacrene C, one of the most abundant sesquiterpene in the leaf oil of tomato (PubMed:11090225). Produces mainly germacrene C, but also smaller amounts of germacrene A, B and D when used with farnesyl diphosphate (FPP) as substrate; able to use both (2E,6E)-farnesyl diphosphate ((EE)-FPP) and (2Z,6Z)-farnesyl diphosphate ((ZZ)-FPP) (PubMed:21818683, PubMed:9482865). No or low activity with geranylgeranyl diphosphate (GGPP) (PubMed:9482865). Can act with a low efficiency as a monoterpene synthase with geranyl diphosphate (GPP) as substrate, thus producing beta-myrcene, limonene and terpinolene (PubMed:21818683, PubMed:9482865). {ECO:0000269|PubMed:11090225, ECO:0000269|PubMed:21818683, ECO:0000269|PubMed:9482865}.
|
Solanum lycopersicum (Tomato) (Lycopersicon esculentum)
|
O64973
|
RPS5_ARATH
|
MGGCFSVSLPCDQVVSQFSQLLCVRGSYIHNLSKNLASLQKAMRMLKARQYDVIRRLETEEFTGRQQRLSQVQVWLTSVLIIQNQFNDLLRSNEVELQRLCLCGFCSKDLKLSYRYGKRVIMMLKEVESLSSQGFFDVVSEATPFADVDEIPFQPTIVGQEIMLEKAWNRLMEDGSGILGLYGMGGVGKTTLLTKINNKFSKIDDRFDVVIWVVVSRSSTVRKIQRDIAEKVGLGGMEWSEKNDNQIAVDIHNVLRRRKFVLLLDDIWEKVNLKAVGVPYPSKDNGCKVAFTTRSRDVCGRMGVDDPMEVSCLQPEESWDLFQMKVGKNTLGSHPDIPGLARKVARKCRGLPLALNVIGEAMACKRTVHEWCHAIDVLTSSAIDFSGMEDEILHVLKYSYDNLNGELMKSCFLYCSLFPEDYLIDKEGLVDYWISEGFINEKEGRERNINQGYEIIGTLVRACLLLEEERNKSNVKMHDVVREMALWISSDLGKQKEKCIVRAGVGLREVPKVKDWNTVRKISLMNNEIEEIFDSHECAALTTLFLQKNDVVKISAEFFRCMPHLVVLDLSENQSLNELPEEISELASLRYFNLSYTCIHQLPVGLWTLKKLIHLNLEHMSSLGSILGISNLWNLRTLGLRDSRLLLDMSLVKELQLLEHLEVITLDISSSLVAEPLLCSQRLVECIKEVDFKYLKEESVRVLTLPTMGNLRKLGIKRCGMREIKIERTTSSSSRNKSPTTPCFSNLSRVFIAKCHGLKDLTWLLFAPNLTFLEVGFSKEVEDIISEEKAEEHSATIVPFRKLETLHLFELRGLKRIYAKALHFPCLKVIHVEKCEKLRKLPLDSKSGIAGEELVIYYGEREWIERVEWEDQATQLRFLPSSRWRWRET
| null | null |
cell death [GO:0008219]; defense response [GO:0006952]; defense response to bacterium [GO:0042742]; plant-type hypersensitive response [GO:0009626]
|
plasma membrane [GO:0005886]
|
ADP binding [GO:0043531]; ATP binding [GO:0005524]; identical protein binding [GO:0042802]; nucleotide binding [GO:0000166]; signaling receptor activity [GO:0038023]
|
PF13855;PF00931;
|
1.10.8.430;3.40.50.300;3.80.10.10;1.10.10.10;
|
Disease resistance NB-LRR family
| null |
SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor {ECO:0000269|PubMed:22046960, ECO:0000269|PubMed:22331412}.
| null | null | null | null | null |
FUNCTION: Disease resistance (R) protein that specifically recognizes the avrPphB type III effector avirulence protein from Pseudomonas syringae. Also confers resistance against Hyaloperonospora parasitica (downy mildew). Resistance proteins guard the plant against pathogens that contain an appropriate avirulence protein via an indirect interaction with this avirulence protein. That triggers a defense system including the hypersensitive response, which restricts the pathogen growth. Requires PBS1 to trigger the defense reaction against avrPphB. In case of infection by Pseudomonas syringae, AvrPphB triggers RPS5-mediated defense mechanism via the cleavage of PBS1, suggesting that the cleavage of PBS1 could trigger an exchange of ADP for ATP, thereby activating RPS5. May function as a fine-tuned sensor of alterations in the structure of the effector target PBS1. {ECO:0000269|PubMed:12947197, ECO:0000269|PubMed:17277084, ECO:0000269|PubMed:22372664, ECO:0000269|PubMed:9724691}.
|
Arabidopsis thaliana (Mouse-ear cress)
|
O64989
|
C90B1_ARATH
|
MFETEHHTLLPLLLLPSLLSLLLFLILLKRRNRKTRFNLPPGKSGWPFLGETIGYLKPYTATTLGDFMQQHVSKYGKIYRSNLFGEPTIVSADAGLNRFILQNEGRLFECSYPRSIGGILGKWSMLVLVGDMHRDMRSISLNFLSHARLRTILLKDVERHTLFVLDSWQQNSIFSAQDEAKKFTFNLMAKHIMSMDPGEEETEQLKKEYVTFMKGVVSAPLNLPGTAYHKALQSRATILKFIERKMEERKLDIKEEDQEEEEVKTEDEAEMSKSDHVRKQRTDDDLLGWVLKHSNLSTEQILDLILSLLFAGHETSSVAIALAIFFLQACPKAVEELREEHLEIARAKKELGESELNWDDYKKMDFTQCVINETLRLGNVVRFLHRKALKDVRYKGYDIPSGWKVLPVISAVHLDNSRYDQPNLFNPWRWQQQNNGASSSGSGSFSTWGNNYMPFGGGPRLCAGSELAKLEMAVFIHHLVLKFNWELAEDDKPFAFPFVDFPNGLPIRVSRIL
|
1.14.14.178
|
COFACTOR: Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250|UniProtKB:P04798};
|
brassinosteroid biosynthetic process [GO:0016132]; jasmonic acid mediated signaling pathway [GO:0009867]; leaf development [GO:0048366]; leaf shaping [GO:0010358]; response to brassinosteroid [GO:0009741]; response to jasmonic acid [GO:0009753]; sterol metabolic process [GO:0016125]; unidimensional cell growth [GO:0009826]
|
endoplasmic reticulum [GO:0005783]; membrane [GO:0016020]
|
fatty acid alpha-hydroxylase activity [GO:0080132]; heme binding [GO:0020037]; iron ion binding [GO:0005506]; oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen [GO:0016705]; steroid 22-alpha hydroxylase activity [GO:0010012]
|
PF00067;
|
1.10.630.10;
|
Cytochrome P450 family
| null |
SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass membrane protein {ECO:0000255}.
|
CATALYTIC ACTIVITY: Reaction=a C27-steroid + O2 + reduced [NADPH--hemoprotein reductase] = a (22S)-22-hydroxy C27-steroid + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:70059, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:188919, ChEBI:CHEBI:188920; EC=1.14.14.178; Evidence={ECO:0000269|PubMed:16460510}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:70060; Evidence={ECO:0000269|PubMed:16460510}; CATALYTIC ACTIVITY: Reaction=a C28-steroid + O2 + reduced [NADPH--hemoprotein reductase] = a (22S)-22-hydroxy C28-steroid + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:70063, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:188921, ChEBI:CHEBI:188922; EC=1.14.14.178; Evidence={ECO:0000269|PubMed:16460510, ECO:0000269|PubMed:9490746}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:70064; Evidence={ECO:0000269|PubMed:16460510, ECO:0000269|PubMed:9490746}; CATALYTIC ACTIVITY: Reaction=a C29-steroid + O2 + reduced [NADPH--hemoprotein reductase] = a (22S)-22-hydroxy C29-steroid + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:70067, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:188923, ChEBI:CHEBI:188924; EC=1.14.14.178; Evidence={ECO:0000269|PubMed:16460510}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:70068; Evidence={ECO:0000269|PubMed:16460510}; CATALYTIC ACTIVITY: Reaction=cholesterol + O2 + reduced [NADPH--hemoprotein reductase] = (22S)-22-hydroxycholesterol + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:69839, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:1301, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16113, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210; Evidence={ECO:0000269|PubMed:16460510}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:69840; Evidence={ECO:0000269|PubMed:16460510}; CATALYTIC ACTIVITY: Reaction=cholestanol + O2 + reduced [NADPH--hemoprotein reductase] = (22S)-22-hydroxycholestanol + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:69871, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:86570, ChEBI:CHEBI:188465; Evidence={ECO:0000269|PubMed:16460510}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:69872; Evidence={ECO:0000269|PubMed:16460510}; CATALYTIC ACTIVITY: Reaction=campestanol + O2 + reduced [NADPH--hemoprotein reductase] = 6-deoxycathasterone + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:69831, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:20714, ChEBI:CHEBI:36799, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210; Evidence={ECO:0000269|PubMed:16460510, ECO:0000269|PubMed:9490746}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:69832; Evidence={ECO:0000269|PubMed:16460510, ECO:0000269|PubMed:9490746}; CATALYTIC ACTIVITY: Reaction=campesterol + O2 + reduced [NADPH--hemoprotein reductase] = (22S)-22-hydroxycampesterol + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:69835, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:28623, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:72331; Evidence={ECO:0000269|PubMed:16460510}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:69836; Evidence={ECO:0000269|PubMed:16460510}; CATALYTIC ACTIVITY: Reaction=6-oxocampestanol + O2 + reduced [NADPH--hemoprotein reductase] = cathasterone + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:70003, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:20747, ChEBI:CHEBI:23057, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210; Evidence={ECO:0000269|PubMed:16460510, ECO:0000269|PubMed:9490746}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:70004; Evidence={ECO:0000269|PubMed:16460510, ECO:0000269|PubMed:9490746}; CATALYTIC ACTIVITY: Reaction=O2 + reduced [NADPH--hemoprotein reductase] + sitosterol = (22S)-22-hydroxysitosterol + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:70071, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:27693, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:187980; Evidence={ECO:0000269|PubMed:16460510}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:70072; Evidence={ECO:0000269|PubMed:16460510};
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.35 uM for campesterol (at pH 7.25 and 30 degrees Celsius) {ECO:0000269|PubMed:16460510}; KM=3 uM for campestanol (at pH 7.25 and 30 degrees Celsius) {ECO:0000269|PubMed:16460510}; Note=kcat is 1.8 min(-1) for campesterol (at pH 7.25 and 30 degrees Celsius) (PubMed:16460510). kcat is 0.049 min(-1) for campestanol (at pH 7.25 and 30 degrees Celsius) (PubMed:16460510). {ECO:0000269|PubMed:16460510};
|
PATHWAY: Plant hormone biosynthesis; brassinosteroid biosynthesis. {ECO:0000269|PubMed:16460510, ECO:0000269|PubMed:9490746}.
| null | null |
FUNCTION: Catalyzes the C22-alpha-hydroxylation step in brassinosteroids biosynthesis (PubMed:16460510, PubMed:9490746). Converts campesterol (CR) to (22S)-22-hydroxycampesterol (22-OHCR, 22-hydroxyCR), campestanol (CN) to 6-deoxycathasterone (6-deoxoCT), and 6-oxocampestanol (6-oxoCN) to cathasterone (CT) (PubMed:16460510, PubMed:9490746). Can also use cholesterol and cholestanol as substrates (PubMed:16460510, PubMed:9490746). {ECO:0000269|PubMed:16460510, ECO:0000269|PubMed:9490746}.
|
Arabidopsis thaliana (Mouse-ear cress)
|
O65020
|
ETO1_ARATH
|
MRSLKLAEGCKGTQVYALNPSAPTPPPPPGNSSTGGGGGGGSGGGTGGVGDKLLQHLSDHLRVNSVRSKSSRTYPPPTQPNAVVSPEFLLPCGLPVTDLLEPQIDPCLKFVDLVEKMAQVYRRIENCSQFEKSGAYLEQCAIFRGISDPKLFRRSLRSSRQHAVDVHAKVVLASWLRFERREDELIGTTSMDCCGRNLECPKATLVSGYDPESVYDPCVCSGASRSEMMNEDECSTSQEVDYDMSFCIGDEEVRCVRYKIASLSRPFKAMLYGGFREMKRATINFTQNGISVEGMRAAEIFSRTNRLDNFPPNVVLELLKLANRFCCDELKSACDSHLAHLVNSLDEAMLLIEYGLEEAAYLLVAACLQVFLRELPSSMHNPNVIKIFCSAEGRERLASLGHASFTLYFFLSQIAMEDDMKSNTTVMLLERLVECAVDSWEKQLAYHQLGVVMLERKEYKDAQRWFNAAVEAGHLYSLVGVARTKFKRDHRYSAYKIINSLISDHKATGWMHQERSLYCSGKEKLLDLDTATEFDPTLTFPYKFRAVALVEENQFGAAIAELNKILGFKASPDCLEMRAWISIGMEDYEGALKDIRALLTLEPNFMMFNWKIHGDHMVELLRPLAQQWSQADCWMQLYDRWSSVDDIGSLAVVHHMLANDPGKSLLRFRQSLLLLRLNCQKAAMRSLRLARNHSKSEHERLVYEGWILYDTGHREEALAKAEESISIQRSFEAFFLKAYALADSTLDPDSSNYVIQLLQEALKCPSDGLRKGQALNNLGSVYVDCEKLDLAADCYTNALTIKHTRAHQGLARVYHLKNQRKAAYDEMTKLIEKAQNNASAYEKRSEYCDREMAQSDLCLATQLDPLRTYPYRYRAAVLMDDHKESEAIDELSRAISFKPDLQLLHLRAAFYDSMGEGASAIKDCEAALCIDPGHADTLELYHKAREPNDQK
| null | null |
ethylene-activated signaling pathway [GO:0009873]; negative regulation of ethylene-activated signaling pathway [GO:0010105]; protein ubiquitination [GO:0016567]
| null | null |
PF13181;
|
1.25.40.10;
|
ETO1 family
| null | null | null | null |
PATHWAY: Protein modification; protein ubiquitination.
| null | null |
FUNCTION: Essential regulator of the ethylene pathway, which acts by regulating the stability of 1-aminocyclopropane-1-carboxylate synthase (ACS) enzymes. May act as a substrate-specific adapter that connects ACS enzymes, such as ACS5, to ubiquitin ligase complexes, leading to proteasomal degradation of ACS enzymes. {ECO:0000269|PubMed:15118728, ECO:0000269|PubMed:16091151, ECO:0000269|PubMed:18808454}.
|
Arabidopsis thaliana (Mouse-ear cress)
|
O65039
|
CYSEP_RICCO
|
MQKFILLALSLALVLAITESFDFHEKELESEESLWGLYERWRSHHTVSRSLHEKQKRFNVFKHNAMHVHNANKMDKPYKLKLNKFADMTNHEFRNTYSGSKVKHHRMFRGGPRGNGTFMYEKVDTVPASVDWRKKGAVTSVKDQGQCGSCWAFSTIVAVEGINQIKTNKLVSLSEQELVDCDTDQNQGCNGGLMDYAFEFIKQRGGITTEANYPYEAYDGTCDVSKENAPAVSIDGHENVPENDENALLKAVANQPVSVAIDAGGSDFQFYSEGVFTGSCGTELDHGVAIVGYGTTIDGTKYWTVKNSWGPEWGEKGYIRMERGISDKEGLCGIAMEASYPIKKSSNNPSGIKSSPKDEL
|
3.4.22.-
| null |
proteolysis involved in protein catabolic process [GO:0051603]
|
cytoplasmic vesicle [GO:0031410]; extracellular space [GO:0005615]; lysosome [GO:0005764]
|
cysteine-type endopeptidase activity [GO:0004197]
|
PF08246;PF00112;
|
3.90.70.10;
|
Peptidase C1 family
|
PTM: The potential N-glycosylation site at Asn-115 is not glycosylated.
|
SUBCELLULAR LOCATION: Cytoplasmic vesicle {ECO:0000269|PubMed:11296243}. Note=The pro-endopeptidase accumulates in the ricinosomes.
| null | null | null | null | null |
FUNCTION: Involved in programmed cell death. Shows a pronounced preference for hydrophobic residues in the P2 position and no obvious preference in the P1 position of the cleavage site. Accepts proline at the P1 and P1' positions.
|
Ricinus communis (Castor bean)
|
O65041
|
UBA3_ARATH
|
MADLDVPPQVPQSKTRDLDKLLLRHGNLVDPGFVPGPGLRDDIRDYVRILVIGAGGLGCELLKDLALSGFRNLEVIDMDRIEVTNLNRQFLFRIEDVGKPKAEVAAKRVMERVSGVEIVPHFSRIEDKEIEFYNDFNIIALGLDSIEARKYINGVACGFLEYNEDDTPKRETIKPMVDGGTEGFKGHARVILPGVTPCFECTIYLFPPQVKFPLCTLAETPRNAAHCIEYAHLIQWETVHRGKTFDPDEPEHMKWVYDEAIRRAELFGIPGVTYSLTQGVVKNIIPAIASTNAIISAACALETLKIVSACSKTLVNYLTYNGGEGLYTEVTKFERDTECLVCGPGILIELDTSVTLSKFIEMLEDHPKLLLSKASVKQGENTLYMQAPPVLEEFHRPKLSKPLYDLMGRVQKDTIHVFGQRALKNNEKESCTTKVRVVFKGADGVADMDTAIGA
|
6.2.1.64
| null |
protein neddylation [GO:0045116]
|
cytosol [GO:0005829]; nucleus [GO:0005634]
|
ATP binding [GO:0005524]; NEDD8 activating enzyme activity [GO:0019781]; protein heterodimerization activity [GO:0046982]
|
PF08825;PF00899;
|
3.40.50.720;1.10.10.520;3.10.290.20;
|
Ubiquitin-activating E1 family, UBA3 subfamily
| null |
SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
|
CATALYTIC ACTIVITY: Reaction=ATP + [NEDD8 protein] + [E1 NEDD8-activating enzyme]-L-cysteine = AMP + diphosphate + [E1 NEDD8-activating enzyme]-S-[NEDD8 protein]-yl-L-cysteine.; EC=6.2.1.64;
| null |
PATHWAY: Protein modification; protein neddylation.
| null | null |
FUNCTION: Catalytic subunit of the dimeric ECR1-AXR1 E1 enzyme. E1 activates NEDD8/RUB1 by first adenylating its C-terminal glycine residue with ATP, thereafter linking this residue to the side chain of the catalytic cysteine, yielding a NEDD8-ECR1 thioester and free AMP. E1 finally transfers NEDD8 to the catalytic cysteine of RCE1 (By similarity). {ECO:0000250, ECO:0000269|PubMed:10611386, ECO:0000269|PubMed:9624055}.
|
Arabidopsis thaliana (Mouse-ear cress)
|
O65201
|
ACOX2_ARATH
|
MESRREKNPMTEEESDGLIAARRIQRLSLHLSPSLTPSPSLPLVQTETCSARSKKLDVNGEALSLYMRGKHIDIQEKIFDFFNSRPDLQTPIEISKDDHRELCMNQLIGLVREAGVRPFRYVADDPEKYFAIMEAVGSVDMSLGIKMGVQYSLWGGSVINLGTKKHRDKYFDGIDNLDYTGCFAMTELHHGSNVQGLQTTATFDPLKDEFVIDTPNDGAIKWWIGNAAVHGKFATVFARLILPTHDSKGVSDMGVHAFIVPIRDMKTHQTLPGVEIQDCGHKVGLNGVDNGALRFRSVRIPRDNLLNRFGDVSRDGTYTSSLPTINKRFGATLGELVGGRVGLAYASVGVLKISATIAIRYSLLRQQFGPPKQPEVSILDYQSQQHKLMPMLASTYAYHFATVYLVEKYSEMKKTHDEQLVADVHALSAGLKSYVTSYTAKALSVCREACGGHGYAAVNRFGSLRNDHDIFQTFEGDNTVLLQQVAADLLKRYKEKFQGGTLTVTWSYLRESMNTYLSQPNPVTARWEGEDHLRDPKFQLDAFRYRTSRLLQNVAARLQKHSKTLGGFGAWNRCLNHLLTLAESHIETVILAKFIEAVKNCPDPSAKAALKLACDLYALDRIWKDIGTYRNVDYVAPNKAKAIHKLTEYLSFQVRNVAKELVDAFELPDHVTRAPIAMQSDAYSQYTQVVGF
|
1.3.3.6
|
COFACTOR: Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250|UniProtKB:O65202}; Note=Binds 1 FAD per subunit. {ECO:0000250|UniProtKB:O65202};
|
fatty acid beta-oxidation [GO:0006635]; fatty acid beta-oxidation using acyl-CoA oxidase [GO:0033540]; lipid homeostasis [GO:0055088]; long-chain fatty acid metabolic process [GO:0001676]
|
peroxisome [GO:0005777]
|
acyl-CoA oxidase activity [GO:0003997]; FAD binding [GO:0071949]; fatty acid binding [GO:0005504]
|
PF01756;PF00441;PF02770;
|
2.40.110.10;1.20.140.10;
|
Acyl-CoA oxidase family
| null |
SUBCELLULAR LOCATION: Peroxisome {ECO:0000255}.
|
CATALYTIC ACTIVITY: Reaction=a 2,3-saturated acyl-CoA + O2 = a (2E)-enoyl-CoA + H2O2; Xref=Rhea:RHEA:38959, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:58856, ChEBI:CHEBI:65111; EC=1.3.3.6; Evidence={ECO:0000269|PubMed:10571860}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38960; Evidence={ECO:0000269|PubMed:10571860};
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=4.4 uM for C18:1-CoA {ECO:0000269|PubMed:10571860};
| null | null | null |
FUNCTION: Catalyzes the desaturation of long-chain acyl-CoAs to 2-trans-enoyl-CoAs. Active on substrates longer than C14 and mostly with C18-CoA. Activity on long-chain mono-unsaturated substrates is double than with the corresponding saturated substrates. {ECO:0000269|PubMed:10571860}.
|
Arabidopsis thaliana (Mouse-ear cress)
|
O65202
|
ACOX1_ARATH
|
MEGIDHLADERNKAEFDVEDMKIVWAGSRHAFEVSDRIARLVASDPVFEKSNRARLSRKELFKSTLRKCAHAFKRIIELRLNEEEAGRLRHFIDQPAYVDLHWGMFVPAIKGQGTEEQQKKWLSLANKMQIIGCYAQTELGHGSNVQGLETTATFDPKTDEFVIHTPTQTASKWWPGGLGKVSTHAVVYARLITNGKDYGIHGFIVQLRSLEDHSPLPNITVGDIGTKMGNGAYNSMDNGFLMFDHVRIPRDQMLMRLSKVTREGEYVPSDVPKQLVYGTMVYVRQTIVADASNALSRAVCIATRYSAVRRQFGAHNGGIETQVIDYKTQQNRLFPLLASAYAFRFVGEWLKWLYTDVTERLAASDFATLPEAHACTAGLKSLTTTATADGIEECRKLCGGHGYLWCSGLPELFAVYVPACTYEGDNVVLQLQVARFLMKTVAQLGSGKVPVGTTAYMGRAAHLLQCRSGVQKAEDWLNPDVVLEAFEARALRMAVTCAKNLSKFENQEQGFQELLADLVEAAIAHCQLIVVSKFIAKLEQDIGGKGVKKQLNNLCYIYALYLLHKHLGDFLSTNCITPKQASLANDQLRSLYTQVRPNAVALVDAFNYTDHYLNSVLGRYDGNVYPKLFEEALKDPLNDSVVPDGYQEYLRPVLQQQLRTARL
|
1.3.3.6
|
COFACTOR: Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000269|PubMed:15581893}; Note=Binds 1 FAD per subunit. {ECO:0000269|PubMed:15581893};
|
ascaroside biosynthetic process [GO:1904070]; fatty acid beta-oxidation [GO:0006635]; fatty acid beta-oxidation using acyl-CoA oxidase [GO:0033540]; jasmonic acid biosynthetic process [GO:0009695]; lipid homeostasis [GO:0055088]; long-chain fatty acid metabolic process [GO:0001676]; response to fungus [GO:0009620]; response to wounding [GO:0009611]; very long-chain fatty acid metabolic process [GO:0000038]
|
cytosol [GO:0005829]; peroxisome [GO:0005777]; plasmodesma [GO:0009506]
|
acyl-CoA oxidase activity [GO:0003997]; FAD binding [GO:0071949]; fatty acid binding [GO:0005504]; palmitoyl-CoA oxidase activity [GO:0016401]
|
PF01756;PF02770;PF14749;
|
1.10.540.10;2.40.110.10;1.20.140.10;
|
Acyl-CoA oxidase family
| null |
SUBCELLULAR LOCATION: Peroxisome {ECO:0000255}.
|
CATALYTIC ACTIVITY: Reaction=a 2,3-saturated acyl-CoA + O2 = a (2E)-enoyl-CoA + H2O2; Xref=Rhea:RHEA:38959, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:58856, ChEBI:CHEBI:65111; EC=1.3.3.6; Evidence={ECO:0000269|PubMed:10571860}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38960; Evidence={ECO:0000269|PubMed:10571860};
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=5.3 uM for C14-CoA;
| null | null | null |
FUNCTION: Catalyzes the desaturation of both long- and medium-chain acyl-CoAs to 2-trans-enoyl-CoAs. Most active with C14-CoA. Activity on long-chain mono-unsaturated substrates is 40% higher than with the corresponding saturated substrates. Seems to be an important factor in the general metabolism of root tips. May be involved in the biosynthesis of jasmonic acid. {ECO:0000269|PubMed:10571860}.
|
Arabidopsis thaliana (Mouse-ear cress)
|
O65258
|
BAM2_ARATH
|
MAIRLNHSVIPVSVKLGAPTRVSARSSLPFSVGDWRGVSTFSGARPLVLAKVKLRAESTEEDRVPIDDDDDSTDQLVDEEIVHFEERDFAGTACVPVYVMLPLGVIDMNSEVVEPEELLDQLRTLKSVNVDGVMVDCWWGIVESHTPQVYNWSGYKKLFQMIRELGLKIQVVMSFHECGGNVGDDVHIQIPEWVREIGQSNPDIYFTDSAGRRNTECLTWGIDKQRVLRGRTALEVYFDYMRSFRVEFDEFFEEKIIPEIEVGLGPCGELRYPSYPAQFGWKYPGIGEFQCYDKYLMNSLKEAAEVRGHSFWGRGPDNTETYNSTPHGTGFFRDGGDYDSYYGRFFLNWYSRVLIDHGDRVLAMANLAFEGTCIAAKLSGIHWWYKTASHAAELTAGFYNSSNRDGYGPIAAMFKKHDAALNFTCVELRTLDQHEDFPEALADPEGLVWQVLNAAWDASIPVASENALPCYDREGYNKILENAKPLTDPDGRHLSCFTYLRLNPTLMESQNFKEFERFLKRMHGEAVPDLGLAPGTQETNPE
|
3.2.1.2
| null |
polysaccharide catabolic process [GO:0000272]
|
chloroplast [GO:0009507]; chloroplast stroma [GO:0009570]
|
amylopectin maltohydrolase activity [GO:0102229]; beta-amylase activity [GO:0016161]
|
PF01373;
|
3.20.20.80;
|
Glycosyl hydrolase 14 family
| null |
SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000269|PubMed:18390594, ECO:0000269|PubMed:18431481}.
|
CATALYTIC ACTIVITY: Reaction=Hydrolysis of (1->4)-alpha-D-glucosidic linkages in polysaccharides so as to remove successive maltose units from the non-reducing ends of the chains.; EC=3.2.1.2;
| null | null |
BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 6. {ECO:0000269|PubMed:18390594, ECO:0000269|PubMed:19664588};
| null |
FUNCTION: Low beta-amylase activity. Interacts poorly with starch or other alpha-1,4-glucan. {ECO:0000269|PubMed:18390594, ECO:0000269|PubMed:19664588}.
|
Arabidopsis thaliana (Mouse-ear cress)
|
O65272
|
KEA2_ARATH
|
MDFASSVQRQSMFHGGADFASYCLPNRMISAKLCPKGLGGTRFWDPMIDSKVRSAIRSKRNVSYRSSLTLNADFNGRFYGHLLPAKPQNVPLGFRLLCQSSDSVGDLVGNDRNLEFAEGSDDREVTFSKEEKDTREQDSAPSLEELRDLLNKATKELEVASLNSTMFEEKAQRISEVAIALKDEAASAWNDVNQTLNVVQEAVDEESVAKEAVQKATMALSLAEARLQVALESLEAEGYNTSEESEVRDGVKDKEEALLSAKADIKECQENLASCEEQLRRLQVKKDELQKEVDRLNEAAERAQISALKAEEDVANIMVLAEQAVAFELEATQRVNDAEIALQRAEKTLFGSQTQETTQGKVLDGKNTIVGEDEVLSEIVDVSHQAERDLVVVGVSSDVGTQSYESDNENGKPTADFAKEAEGEAEKSKNVVLTKKQEVQKDLPRESSSHNGTKTSLKKSSRFFPASFFSSNGDGTATVFESLVESAKQQWPKLILGFTLLGAGVAIYSNGVGRNNQLPQQPNIVSTSAEDVSSSTKPLIRQMQKLPKRIKKLLEMFPQQEVNEEEASLLDVLWLLLASVIFVPLFQKIPGGSPVLGYLAAGILIGPYGLSIIRNVHGTKAIAEFGVVFLLFNIGLELSVERLSSMKKYVFGLGSAQVLVTAAVIGLITHYVAGQAGPAAIVIGNGLALSSTAVVLQVLQERGESTSRHGRATFSVLLFQDLAVVVLLILIPLISPNSSKGGIGFQAIAEALGLAAIKAAVAITGIIAGGRLLLRPIYKQIAENRNAEIFSANTLLVILGTSLLTARAGLSMALGAFLAGLLLAETEFSLQVESDIAPYRGLLLGLFFMTVGMSIDPKLLLANFPLIMGTLGLLLVGKTILVVIIGKLFGISIISAVRVGLLLAPGGEFAFVAFGEAVNQGIMTPQLSSLLFLVVGISMALTPWLAAGGQLIASRFELQDVRSLLPVESETDDLQGHIIICGFGRIGQIIAQLLSERLIPFVALDVSSDRVAIGRSLDLPVYFGDAGSREVLHKIGADRACAAAIALDTPGANYRCVWALSKYFPNVKTFVRAHDVDHGLNLEKAGATAVVPETLEPSLQLAAAVLAQAKLPTSEIATTINEFRSRHLSELAELCEASGSSLGYGFSRSTSKPKPPSPSETSDDNQIIEGTLAI
| null | null |
abscisic acid-activated signaling pathway [GO:0009738]; calcium-mediated signaling [GO:0019722]; plastid gene expression [GO:0140899]; plastid rRNA transcription [GO:0042794]; potassium ion transport [GO:0006813]; primary root development [GO:0080022]; reactive nitrogen species metabolic process [GO:2001057]; regulation of cellular hyperosmotic salinity response [GO:1900069]; regulation of pH [GO:0006885]; regulation of photosynthesis [GO:0010109]; regulation of reactive oxygen species metabolic process [GO:2000377]; regulation of response to water deprivation [GO:2000070]; regulation of seedling development [GO:1900140]; response to abscisic acid [GO:0009737]; response to absence of light [GO:0009646]; response to sucrose [GO:0009744]
|
chloroplast [GO:0009507]; chloroplast inner membrane [GO:0009706]; membrane [GO:0016020]
|
potassium ion transmembrane transporter activity [GO:0015079]; potassium:proton antiporter activity [GO:0015386]; proton transmembrane transporter activity [GO:0015078]
|
PF00999;PF02254;
|
1.20.1530.20;3.40.50.720;
|
Monovalent cation:proton antiporter 2 (CPA2) transporter (TC 2.A.37) family, KEA (TC 2.A.37.1) subfamily
|
PTM: Acetylated at Lys-170 by the stromal acetyltransferase enzyme NSI. {ECO:0000269|PubMed:29967049, ECO:0000269|PubMed:31865509}.
|
SUBCELLULAR LOCATION: Plastid, chloroplast inner membrane {ECO:0000269|PubMed:18431481, ECO:0000269|PubMed:22551943, ECO:0000269|PubMed:24794527, ECO:0000269|PubMed:33485149}; Multi-pass membrane protein {ECO:0000255}. Plastid inner membrane {ECO:0000269|PubMed:33485149}; Multi-pass membrane protein {ECO:0000255}. Note=Specifically localized to the two caps of the dividing organelle separated by the fission plane (at protein level) (PubMed:27443603). Present both in photosynthetic chloroplasts of shoots and in non-photosynthetic plastids in roots (PubMed:33485149). {ECO:0000269|PubMed:27443603, ECO:0000269|PubMed:33485149}.
|
CATALYTIC ACTIVITY: Reaction=H(+)(out) + K(+)(in) = H(+)(in) + K(+)(out); Xref=Rhea:RHEA:29467, ChEBI:CHEBI:15378, ChEBI:CHEBI:29103; Evidence={ECO:0000269|PubMed:24278440, ECO:0000269|PubMed:31296940, ECO:0000269|PubMed:33111995};
| null | null |
BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 5.8. {ECO:0000269|PubMed:24278440};
| null |
FUNCTION: Electroneutral K(+)/H(+) efflux antiporter modulating monovalent cation and pH homeostasis in plastids, especially during plastid division and thylakoid membrane formation (PubMed:22551943, PubMed:24278440, PubMed:27443603, PubMed:31296940, PubMed:33111995). Transports K(+) and Cs(+) preferentially relative to Na(+) or Li(+) (PubMed:22551943). May function in osmotic adjustment (PubMed:24278440). Collaboratively with KEA1, adjusts alkaline stromal pH upon light to dark transitions in plastids (PubMed:33111995). Together with KEA1, critical for chloroplast development, including chloroplast RNA-metabolism (e.g. rRNA maturation, polysome loading and RNA-protein interactions) and plastid gene expression (PGE), ion homeostasis, and photosynthesis (PubMed:27443603, PubMed:34235544). Contributes, during early seedling development, to the regulation of photosynthesis and abscisic acid- (ABA-) mediated primary root growth in a sucrose-dependent manner (PubMed:35193734). Involved in the regulation of reactive oxygen and nitrogen species (ROS and RNS) metabolism (PubMed:33485149). Required in roots for rapid hyperosmotic-induced Ca(2+) responses and for osmo-sensory potentiation in hyperosmotic conditions (PubMed:27528686). May counteract resilience to drought and salt stress, involving photorespiratory pathway and stomata closure (PubMed:33485149, PubMed:34235544). {ECO:0000269|PubMed:22551943, ECO:0000269|PubMed:24278440, ECO:0000269|PubMed:27443603, ECO:0000269|PubMed:27528686, ECO:0000269|PubMed:31296940, ECO:0000269|PubMed:33111995, ECO:0000269|PubMed:33485149, ECO:0000269|PubMed:34235544, ECO:0000269|PubMed:35193734}.
|
Arabidopsis thaliana (Mouse-ear cress)
|
O65282
|
CH20_ARATH
|
MAATQLTASPVTMSARSLASLDGLRASSVKFSSLKPGTLRQSQFRRLVVKAASVVAPKYTSIKPLGDRVLVKIKEAEEKTLGGILLPSTAQSKPQGGEVVAVGEGRTIGKNKIDITVPTGAQIIYSKYAGTEVEFNDVKHLILKEDDIVGILETEDIKDLKPLNDRVFIKVAEAEEKTAGGLLLTETTKEKPSIGTVIAVGPGSLDEEGKITPLPVSTGSTVLYSKYAGNDFKGKDGSNYIALRASDVMAILS
| null | null |
chaperone cofactor-dependent protein refolding [GO:0051085]; negative regulation of abscisic acid-activated signaling pathway [GO:0009788]; positive regulation of superoxide dismutase activity [GO:1901671]; protein heterotetramerization [GO:0051290]; response to cold [GO:0009409]
|
apoplast [GO:0048046]; chloroplast [GO:0009507]; chloroplast envelope [GO:0009941]; chloroplast stroma [GO:0009570]; chloroplast thylakoid membrane [GO:0009535]; mitochondrial matrix [GO:0005759]; mitochondrion [GO:0005739]; plastid [GO:0009536]; thylakoid [GO:0009579]
|
ATP binding [GO:0005524]; copper ion binding [GO:0005507]; protein folding chaperone [GO:0044183]; protein-folding chaperone binding [GO:0051087]; unfolded protein binding [GO:0051082]
|
PF00166;
|
2.30.33.40;
|
GroES chaperonin family
| null |
SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000269|PubMed:10205903}.
| null | null | null | null | null |
FUNCTION: Seems to function only as a co-chaperone, along with CPN60, and in certain cases is essential for the discharge of biologically active proteins from CPN60 (PubMed:17178727, PubMed:23057508). Required to activate the iron superoxide dismutases (FeSOD) (PubMed:23057508). {ECO:0000269|PubMed:17178727, ECO:0000269|PubMed:23057508}.; FUNCTION: Involved in abscisic acid (ABA) signaling, independently of its co-chaperone role. Acts as a negative regulator of the CHLH-WRKY40 coupled ABA signaling pathway, downstream of CHLH and upstream of WRKY40. {ECO:0000269|PubMed:23783410}.
|
Arabidopsis thaliana (Mouse-ear cress)
|
O65312
|
MEDEA_ARATH
|
MEKENHEDDGEGLPPELNQIKEQIEKERFLHIKRKFELRYIPSVATHASHHQSFDLNQPAAEDDNGGDNKSLLSRMQNPLRHFSASSDYNSYEDQGYVLDEDQDYALEEDVPLFLDEDVPLLPSVKLPIVEKLPRSITWVFTKSSQLMAESDSVIGKRQIYYLNGEALELSSEEDEEDEEEDEEEIKKEKCEFSEDVDRFIWTVGQDYGLDDLVVRRALAKYLEVDVSDILERYNELKLKNDGTAGEASDLTSKTITTAFQDFADRRHCRRCMIFDCHMHEKYEPESRSSEDKSSLFEDEDRQPCSEHCYLKVRSVTEADHVMDNDNSISNKIVVSDPNNTMWTPVEKDLYLKGIEIFGRNSCDVALNILRGLKTCLEIYNYMREQDQCTMSLDLNKTTQRHNQVTKKVSRKSSRSVRKKSRLRKYARYPPALKKTTSGEAKFYKHYTPCTCKSKCGQQCPCLTHENCCEKYCGCSKDCNNRFGGCNCAIGQCTNRQCPCFAANRECDPDLCRSCPLSCGDGTLGETPVQIQCKNMQFLLQTNKKILIGKSDVHGWGAFTWDSLKKNEYLGEYTGELITHDEANERGRIEDRIGSSYLFTLNDQLEIDARRKGNEFKFLNHSARPNCYAKLMIVRGDQRIGLFAERAIEEGEELFFDYCYGPEHADWSRGREPRKTGASKRSKEARPAR
|
2.1.1.356
| null |
heterochromatin formation [GO:0031507]; methylation [GO:0032259]; negative regulation of DNA-templated transcription [GO:0045892]; regulation of endosperm development [GO:2000014]; response to absence of light [GO:0009646]; seed morphogenesis [GO:0048317]
|
nucleus [GO:0005634]; PcG protein complex [GO:0031519]
|
chromatin binding [GO:0003682]; histone H3K27 trimethyltransferase activity [GO:0140951]; sequence-specific DNA binding [GO:0043565]
|
PF18264;PF00856;
|
2.170.270.10;
|
Class V-like SAM-binding methyltransferase superfamily, Histone-lysine methyltransferase family, EZ subfamily
| null |
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11114524}. Note=Excluded from the nucleolus.
|
CATALYTIC ACTIVITY: Reaction=L-lysyl(27)-[histone H3] + 3 S-adenosyl-L-methionine = 3 H(+) + N(6),N(6),N(6)-trimethyl-L-lysyl(27)-[histone H3] + 3 S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:60292, Rhea:RHEA-COMP:15535, Rhea:RHEA-COMP:15548, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:61961; EC=2.1.1.356; Evidence={ECO:0000255|PROSITE-ProRule:PRU00909};
| null | null | null | null |
FUNCTION: Polycomb group (PcG) protein. Catalytic subunit of some PcG multiprotein complex, which methylates 'Lys-27' of histone H3, leading to transcriptional repression of the affected target genes. Required to prevent the proliferation of the central cell of the female gametophyte by repressing target genes before fertilization. After fertilization, it probably also regulates the embryo and endosperm proliferation and anteroposterior organization during seed development. PcG proteins act by forming multiprotein complexes, which are required to maintain the transcriptionally repressive state of homeotic genes throughout development. PcG proteins are not required to initiate repression, but to maintain it during later stages of development. Interacts with the promoter and repress the transcription of genes such as PHE1 and PHE2, that are paternally active and maternally silenced genes. {ECO:0000269|PubMed:10097185, ECO:0000269|PubMed:11250158, ECO:0000269|PubMed:12815071, ECO:0000269|PubMed:15151989, ECO:0000269|PubMed:15619622, ECO:0000269|PubMed:9545225}.
|
Arabidopsis thaliana (Mouse-ear cress)
|
O65351
|
SBT17_ARATH
|
MSSSFLSSTAFFLLLCLGFCHVSSSSSDQGTYIVHMAKSQMPSSFDLHSNWYDSSLRSISDSAELLYTYENAIHGFSTRLTQEEADSLMTQPGVISVLPEHRYELHTTRTPLFLGLDEHTADLFPEAGSYSDVVVGVLDTGVWPESKSYSDEGFGPIPSSWKGGCEAGTNFTASLCNRKLIGARFFARGYESTMGPIDESKESRSPRDDDGHGTHTSSTAAGSVVEGASLLGYASGTARGMAPRARVAVYKVCWLGGCFSSDILAAIDKAIADNVNVLSMSLGGGMSDYYRDGVAIGAFAAMERGILVSCSAGNAGPSSSSLSNVAPWITTVGAGTLDRDFPALAILGNGKNFTGVSLFKGEALPDKLLPFIYAGNASNATNGNLCMTGTLIPEKVKGKIVMCDRGINARVQKGDVVKAAGGVGMILANTAANGEELVADAHLLPATTVGEKAGDIIRHYVTTDPNPTASISILGTVVGVKPSPVVAAFSSRGPNSITPNILKPDLIAPGVNILAAWTGAAGPTGLASDSRRVEFNIISGTSMSCPHVSGLAALLKSVHPEWSPAAIRSALMTTAYKTYKDGKPLLDIATGKPSTPFDHGAGHVSPTTATNPGLIYDLTTEDYLGFLCALNYTSPQIRSVSRRNYTCDPSKSYSVADLNYPSFAVNVDGVGAYKYTRTVTSVGGAGTYSVKVTSETTGVKISVEPAVLNFKEANEKKSYTVTFTVDSSKPSGSNSFGSIEWSDGKHVVGSPVAISWT
|
3.4.21.-
| null |
mucilage extrusion from seed coat [GO:0080001]; mucilage metabolic process involved in seed coat development [GO:0048359]; proteolysis [GO:0006508]; seed coat development [GO:0010214]
|
apoplast [GO:0048046]; extracellular region [GO:0005576]; secretory vesicle [GO:0099503]
|
serine-type endopeptidase activity [GO:0004252]
|
PF17766;PF05922;PF02225;PF00082;
|
2.60.40.2310;3.50.30.30;3.30.70.80;3.40.50.200;
|
Peptidase S8 family
| null |
SUBCELLULAR LOCATION: Secreted, cell wall {ECO:0000269|PubMed:12413398, ECO:0000269|PubMed:9188482}. Note=Intracellular spaces and cell wall.
| null | null | null |
BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 5.0. {ECO:0000269|PubMed:12413398};
|
BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 80 degrees Celsius. Thermostable. {ECO:0000269|PubMed:12413398};
|
FUNCTION: Serine protease. Has a substrate preference for the hydrophobic residues Phe and Ala and the basic residue Asp in the P1 position, and for Asp, Leu or Ala in the P1' position (PubMed:12413398). Essential for mucilage release from seed coats. Triggers the accumulation and/or activation of cell wall modifying enzymes necessary either for the loosening of the outer primary cell wall, or to facilitate swelling of the mucilage (PubMed:18266922). {ECO:0000269|PubMed:12413398, ECO:0000269|PubMed:18266922}.
|
Arabidopsis thaliana (Mouse-ear cress)
|
O65355
|
GGH2_ARATH
|
MWSYVWLPLVALSLFKDSIIMAKAATILLPSQTGFDISRSPVCSAPDPNLNYRPVIGILSHPGDGASGRLSNATDASSIAASYVKLAESGGARVIPLIFNEPEEILFQKLELVNGVILTGGWAKEGLYFEIVKKIFNKVLERNDAGEHFPIYAICLGFELLTMIISQNRDIFEKMDARNSASSLQFVENVNIQGTIFQRFPPELLKKLGTDCLVMQNHRFGISPQSFEGNIALSNFFKIVTTCVDDNGKVYVSTVQSTKYPVTGFQWHPEKNAFEWGSSKIPHSEDAIQVTQHAANHLVSEARKSLNRPESKKVLSNLIYNYKPTYCGYAGIGYDEVYIFTQQRSLL
|
3.4.19.9
| null |
tetrahydrofolylpolyglutamate metabolic process [GO:0046900]
|
extracellular space [GO:0005615]; plant-type cell wall [GO:0009505]; plant-type vacuole [GO:0000325]; vacuole [GO:0005773]
|
gamma-glutamyl-peptidase activity [GO:0034722]; omega peptidase activity [GO:0008242]
|
PF07722;
|
3.40.50.880;
|
Peptidase C26 family
| null |
SUBCELLULAR LOCATION: Vacuole {ECO:0000305|PubMed:21070406}. Secreted, extracellular space {ECO:0000250}. Secreted, cell wall {ECO:0000250}. Note=Extracellular or cell-wall bound.
|
CATALYTIC ACTIVITY: Reaction=(6S)-5,6,7,8-tetrahydrofolyl-(gamma-L-Glu)(n) + (n-1) H2O = (6S)-5,6,7,8-tetrahydrofolate + (n-1) L-glutamate; Xref=Rhea:RHEA:56784, Rhea:RHEA-COMP:14738, ChEBI:CHEBI:15377, ChEBI:CHEBI:29985, ChEBI:CHEBI:57453, ChEBI:CHEBI:141005; EC=3.4.19.9;
| null | null | null | null |
FUNCTION: Cleaves the polyglutamate sidechains of folate polyglutamates in the vacuole. Is important for polyglutamyl tail length determination before vacuolar exit. Plays a role on folate stability and intracellular folate content. Has endopeptidase activity against 4-amino-10-methylpteroyl penta-, tetra-, tri- and di-gamma-L-glutamate substrates and is responsible for the production of folic acid, also called pteroylglutamic acid (PteGlu) from teroylpolyglutamates. {ECO:0000269|PubMed:21070406}.
|
Arabidopsis thaliana (Mouse-ear cress)
|
O65359
|
SYP41_ARATH
|
MATRNRTLLFRKYRNSLRSVRAPLSSSSLTGTRSGGVGPVIEMASTSLLNPNRSYAPISTEDPGTSSKGAITVGLPPAWVDVSEEISVNIQRARTKMAELGKAHAKALMPSFGDGKEDQHNIESLTQEITFLLKKSEKQLQRLSASGPSEDSNVRKNVQRSLATDLQLLSMELRKKQSTYLKRLRQQKEDGMDLEMNLSRNRYRPEEDDFGDMLNEHQMSKIKKSEEVSVEREKEIQQVVESVNDLAQIMKDLSALVIDQGTIVDRIDYNIENVATTVEDGLKQLQKAERTQRHGGMVKCASVLVILCFIMLLLLILKEIFL
| null | null |
chloroplast organization [GO:0009658]; defense response to fungus [GO:0050832]; Golgi organization [GO:0007030]; Golgi to plasma membrane protein transport [GO:0043001]; Golgi to vacuole transport [GO:0006896]; intracellular protein transport [GO:0006886]; salicylic acid mediated signaling pathway [GO:0009863]; trans-Golgi network membrane organization [GO:0098629]; vesicle docking [GO:0048278]; vesicle fusion [GO:0006906]
|
SNARE complex [GO:0031201]; trans-Golgi network [GO:0005802]
|
SNAP receptor activity [GO:0005484]; SNARE binding [GO:0000149]
|
PF05739;
|
1.20.58.70;
|
Syntaxin family
| null |
SUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network membrane {ECO:0000269|PubMed:10888666, ECO:0000269|PubMed:11739776, ECO:0000269|PubMed:15342965, ECO:0000269|PubMed:15743878, ECO:0000269|PubMed:22307646}; Single-pass type IV membrane protein {ECO:0000255}. Note=SYP41 is found in a different region of the TGN than SYP42. {ECO:0000269|PubMed:11739776}.
| null | null | null | null | null |
FUNCTION: Contributes to the regulation of secretory and vacuolar transport pathways in the post-Golgi network, and to the maintenance of the Golgi apparatus and trans-Golgi network (TGN) morphologies (PubMed:22307646). Together with VTI12, required for membrane fusion (PubMed:15919093). Vesicle trafficking protein that functions in the secretory pathway and mediates liposome fusion; the fusion of phospholipid vesicles containing SYP41 and VTI12 is triggered by YKT61 and YKT62 (PubMed:15919093, PubMed:24021022). Required for extracellular resistance responses to a fungal pathogen (PubMed:22307646). Also involved in the protection of chloroplasts from salicylic acid-dependent biotic stress (PubMed:22307646). {ECO:0000269|PubMed:15919093, ECO:0000269|PubMed:22307646, ECO:0000269|PubMed:24021022}.
|
Arabidopsis thaliana (Mouse-ear cress)
|
O65375
|
LRX1_ARATH
|
MLFPPLRSLFLFTLLLSSVCFLQIKADHDDESDLGSDIKVDKRLKFENPKLRQAYIALQSWKKAIFSDPFNFTANWNGSDVCSYNGIYCAPSPSYPKTRVVAGIDLNHADMAGYLASELGLLSDLALFHINSNRFCGEVPLTFNRMKLLYELDLSNNRFVGKFPKVVLSLPSLKFLDLRYNEFEGKIPSKLFDRELDAIFLNHNRFRFGIPKNMGNSPVSALVLADNNLGGCIPGSIGQMGKTLNELILSNDNLTGCLPPQIGNLKKVTVFDITSNRLQGPLPSSVGNMKSLEELHVANNAFTGVIPPSICQLSNLENFTYSSNYFSGRPPICAASLLADIVVNGTMNCITGLARQRSDKQCSSLLARPVDCSKFGCYNIFSPPPPTFKMSPEVRTLPPPIYVYSSPPPPPSSKMSPTVRAYSPPPPPSSKMSPSVRAYSPPPPPYSKMSPSVRAYPPPPPPSPSPPPPYVYSSPPPPYVYSSPPPPPYVYSSPPPPPYVYSSPPPPYVYSSPPPPYVYSSPPPPPPSPPPPCPESSPPPPVVYYAPVTQSPPPPSPVYYPPVTQSPPPPSPVYYPPVTNSPPPPSPVYYPPVTYSPPPPSPVYYPQVTPSPPPPSPLYYPPVTPSPPPPSPVYYPPVTPSPPPPSPVYYPPVTPSPPPPSPVYYPSETQSPPPPTEYYYSPSQSPPPTKACKEGHPPQATPSYEPPPEYSYSSSPPPPSPTSYFPPMPSVSYDASPPPPPSYY
| null | null |
cell wall organization [GO:0071555]; trichoblast differentiation [GO:0010054]; unidimensional cell growth [GO:0009826]
|
extracellular region [GO:0005576]; plant-type cell wall [GO:0009505]; plasmodesma [GO:0009506]
|
structural constituent of cell wall [GO:0005199]
|
PF00560;PF08263;
|
3.80.10.10;
| null |
PTM: Hydroxylated on proline residues in the S-P-P-P-P repeat. {ECO:0000250}.; PTM: O-glycosylated on hydroxyprolines. {ECO:0000250}.
|
SUBCELLULAR LOCATION: Secreted, cell wall {ECO:0000269|PubMed:11331608}. Note=Specifically localized in the wall of the root hair proper.
| null | null | null | null | null |
FUNCTION: Modulates cell morphogenesis by regulating cell wall formation and assembly, and/or growth polarization. Together with LRX2, component of the extracellular mechanism regulating root hair morphogenesis and elongation. {ECO:0000269|PubMed:11331608, ECO:0000269|PubMed:12834403}.
|
Arabidopsis thaliana (Mouse-ear cress)
|
O65390
|
APA1_ARATH
|
MKIYSRTVAVSLIVSFLLCFSAFAERNDGTFRVGLKKLKLDSKNRLAARVESKQEKPLRAYRLGDSGDADVVVLKNYLDAQYYGEIAIGTPPQKFTVVFDTGSSNLWVPSSKCYFSLACLLHPKYKSSRSSTYEKNGKAAAIHYGTGAIAGFFSNDAVTVGDLVVKDQEFIEATKEPGITFVVAKFDGILGLGFQEISVGKAAPVWYNMLKQGLIKEPVFSFWLNRNADEEEGGELVFGGVDPNHFKGKHTYVPVTQKGYWQFDMGDVLIGGAPTGFCESGCSAIADSGTSLLAGPTTIITMINHAIGAAGVVSQQCKTVVDQYGQTILDLLLSETQPKKICSQIGLCTFDGTRGVSMGIESVVDKENAKLSNGVGDAACSACEMAVVWIQSQLRQNMTQERILNYVNELCERLPSPMGESAVDCAQLSTMPTVSLTIGGKVFDLAPEEYVLKVGEGPVAQCISGFIALDVAPPRGPLWILGDVFMGKYHTVFDFGNEQVGFAEAA
|
3.4.23.-
| null |
lipid metabolic process [GO:0006629]; proteolysis [GO:0006508]
|
extracellular region [GO:0005576]; plant-type vacuole [GO:0000325]; plasmodesma [GO:0009506]; secretory vesicle [GO:0099503]; vacuole [GO:0005773]
|
aspartic-type endopeptidase activity [GO:0004190]; endopeptidase activity [GO:0004175]
|
PF00026;PF05184;PF03489;
|
2.40.70.10;1.10.225.10;
|
Peptidase A1 family
| null |
SUBCELLULAR LOCATION: Vacuole {ECO:0000269|PubMed:17012602}. Note=Located in protein storage vacuoles (PSV) of the embryo.
| null | null | null |
BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 5.0-6.0 with insulin B chain as substrate and at 37 degrees Celsius. {ECO:0000269|PubMed:20079503};
| null |
FUNCTION: Involved in the breakdown of propeptides of storage proteins in protein-storage vacuoles (By similarity). Possesses aspartic protease activity in vitro. {ECO:0000250, ECO:0000269|PubMed:20079503}.
|
Arabidopsis thaliana (Mouse-ear cress)
|
O65396
|
GCST_ARATH
|
MRGGSLWQLGQSITRRLAQSDKKVVSRRYFASEADLKKTALYDFHVAHGGKMVPFAGWSMPIQYKDSIMDSTVNCRENGSLFDVAHMCGLSLKGKDCVPFLETLVVADVAGLAPGTGSLTVFTNEKGGAIDDSVITKVTDEHIYLVVNAGCRDKDLAHIEEHMKAFKSKGGDVSWHIHDERSLLALQGPLAAPVLQHLTKEDLSKLYFGNFQILDINGSTCFLTRTGYTGEDGFEISVPDEHAVDLAKAILEKSEGKVRLTGLGARDSLRLEAGLCLYGNDMEQHISPVEAGLTWAIGKRRRAEGGFLGADVILQQLKDGPTIRRVGFFSSGPPARSHSEVHDESGNKIGEITSGGFSPNLKKNIAMGYVKSGQHKTGTKVKILVRGKPYEGSITKMPFVATKYYKPT
|
2.1.2.10
| null |
glycine catabolic process [GO:0006546]
|
apoplast [GO:0048046]; chloroplast [GO:0009507]; chloroplast envelope [GO:0009941]; chloroplast stroma [GO:0009570]; chloroplast thylakoid [GO:0009534]; cytosolic ribosome [GO:0022626]; extracellular region [GO:0005576]; mitochondrion [GO:0005739]
|
aminomethyltransferase activity [GO:0004047]; mRNA binding [GO:0003729]; transaminase activity [GO:0008483]
|
PF01571;PF08669;
|
2.40.30.110;3.30.70.1400;4.10.1250.10;
|
GcvT family
| null |
SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250}.
|
CATALYTIC ACTIVITY: Reaction=(6S)-5,6,7,8-tetrahydrofolate + N(6)-[(R)-S(8)-aminomethyldihydrolipoyl]-L-lysyl-[protein] = (6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + N(6)-[(R)-dihydrolipoyl]-L-lysyl-[protein] + NH4(+); Xref=Rhea:RHEA:16945, Rhea:RHEA-COMP:10475, Rhea:RHEA-COMP:10492, ChEBI:CHEBI:15636, ChEBI:CHEBI:28938, ChEBI:CHEBI:57453, ChEBI:CHEBI:83100, ChEBI:CHEBI:83143; EC=2.1.2.10;
| null | null | null | null |
FUNCTION: The glycine decarboxylase (GDC) or glycine cleavage system catalyzes the degradation of glycine. {ECO:0000250}.
|
Arabidopsis thaliana (Mouse-ear cress)
|
O65398
|
GLX1_ARATH
|
MAEASDLLEWPKKDNRRFLHVVYRVGDLDRTIEFYTEVFGMKLLRKRDIPEEKYSNAFLGFGPETSNFVVELTYNYGVSSYDIGTGFGHFAISTQDVSKLVENVRAKGGNVTREPGPVKGGGSVIAFVKDPDGYTFELIQRGPTPEPFCQVMLRVGDLDRAIKFYEKALGMRLLRKIERPEYKYTIGMMGYAEEYESIVLELTYNYDVTEYTKGNAYAQIAIGTDDVYKSGEVIKIVNQELGGKITREAGPLPGLGTKIVSFLDPDGWKTVLVDNKDFLKELE
|
4.4.1.5
|
COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250|UniProtKB:Q9CPU0}; Note=Binds 1 zinc ion per subunit. In the homodimer, two zinc ions are bound between subunits. {ECO:0000250|UniProtKB:Q9CPU0};
|
methylglyoxal catabolic process to D-lactate via S-lactoyl-glutathione [GO:0019243]
|
chloroplast envelope [GO:0009941]; cytosol [GO:0005829]; extracellular region [GO:0005576]; peroxisome [GO:0005777]; plant-type vacuole [GO:0000325]; secretory vesicle [GO:0099503]
|
dioxygenase activity [GO:0051213]; lactoylglutathione lyase activity [GO:0004462]; metal ion binding [GO:0046872]
|
PF00903;
|
3.10.180.10;
|
Glyoxalase I family
|
PTM: Phosphorylated by SnRK2.8. {ECO:0000269|PubMed:17404219}.
| null |
CATALYTIC ACTIVITY: Reaction=(R)-S-lactoylglutathione = glutathione + methylglyoxal; Xref=Rhea:RHEA:19069, ChEBI:CHEBI:17158, ChEBI:CHEBI:57474, ChEBI:CHEBI:57925; EC=4.4.1.5; Evidence={ECO:0000250|UniProtKB:Q04760};
| null |
PATHWAY: Secondary metabolite metabolism; methylglyoxal degradation; (R)-lactate from methylglyoxal: step 1/2. {ECO:0000250|UniProtKB:Q04760}.
| null | null |
FUNCTION: Catalyzes the conversion of hemimercaptal, formed from methylglyoxal and glutathione, to S-lactoylglutathione. {ECO:0000250|UniProtKB:Q04760}.
|
Arabidopsis thaliana (Mouse-ear cress)
|
O65440
|
BAME3_ARATH
|
MADKIFTFFLILSSISPLLCSSLISPLNLSLIRQANVLISLKQSFDSYDPSLDSWNIPNFNSLCSWTGVSCDNLNQSITRLDLSNLNISGTISPEISRLSPSLVFLDISSNSFSGELPKEIYELSGLEVLNISSNVFEGELETRGFSQMTQLVTLDAYDNSFNGSLPLSLTTLTRLEHLDLGGNYFDGEIPRSYGSFLSLKFLSLSGNDLRGRIPNELANITTLVQLYLGYYNDYRGGIPADFGRLINLVHLDLANCSLKGSIPAELGNLKNLEVLFLQTNELTGSVPRELGNMTSLKTLDLSNNFLEGEIPLELSGLQKLQLFNLFFNRLHGEIPEFVSELPDLQILKLWHNNFTGKIPSKLGSNGNLIEIDLSTNKLTGLIPESLCFGRRLKILILFNNFLFGPLPEDLGQCEPLWRFRLGQNFLTSKLPKGLIYLPNLSLLELQNNFLTGEIPEEEAGNAQFSSLTQINLSNNRLSGPIPGSIRNLRSLQILLLGANRLSGQIPGEIGSLKSLLKIDMSRNNFSGKFPPEFGDCMSLTYLDLSHNQISGQIPVQISQIRILNYLNVSWNSFNQSLPNELGYMKSLTSADFSHNNFSGSVPTSGQFSYFNNTSFLGNPFLCGFSSNPCNGSQNQSQSQLLNQNNARSRGEISAKFKLFFGLGLLGFFLVFVVLAVVKNRRMRKNNPNLWKLIGFQKLGFRSEHILECVKENHVIGKGGRGIVYKGVMPNGEEVAVKKLLTITKGSSHDNGLAAEIQTLGRIRHRNIVRLLAFCSNKDVNLLVYEYMPNGSLGEVLHGKAGVFLKWETRLQIALEAAKGLCYLHHDCSPLIIHRDVKSNNILLGPEFEAHVADFGLAKFMMQDNGASECMSSIAGSYGYIAPEYAYTLRIDEKSDVYSFGVVLLELITGRKPVDNFGEEGIDIVQWSKIQTNCNRQGVVKIIDQRLSNIPLAEAMELFFVAMLCVQEHSVERPTMREVVQMISQAKQPNTF
|
2.7.11.1
| null |
cell differentiation [GO:0030154]; floral organ development [GO:0048437]; maintenance of root meristem identity [GO:0010078]; phloem development [GO:0010088]; phosphorylation [GO:0016310]; regulation of cell differentiation [GO:0045595]; regulation of meristem growth [GO:0010075]
|
endoplasmic reticulum membrane [GO:0005789]; plasma membrane [GO:0005886]
|
ATP binding [GO:0005524]; identical protein binding [GO:0042802]; peptide binding [GO:0042277]; peptide receptor activity [GO:0001653]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674]
|
PF00560;PF08263;PF00069;
|
3.80.10.10;1.10.510.10;
|
Protein kinase superfamily, Ser/Thr protein kinase family
| null |
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:28607033}; Single-pass type I membrane protein {ECO:0000255}. Endoplasmic reticulum membrane {ECO:0000269|PubMed:28607033}; Single-pass type I membrane protein {ECO:0000255}.
|
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:0000255|PROSITE-ProRule:PRU00159}; 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:0000255|PROSITE-ProRule:PRU00159};
| null | null | null | null |
FUNCTION: Necessary for male gametophyte development, as well as ovule specification and function (PubMed:16367950). Required for the development of high-ordered vascular strands within the leaf and a correlated control of leaf shape, size and symmetry (PubMed:16367950). LRR-rich receptor-like kinase (LRR-RLK) involved in the perception of CLE45 peptide ligand which mediates root growth inhibition by repressing protophloem differentiation; this mechanism requires CRN (PubMed:23569225, PubMed:25049386, PubMed:28607033). BRX, BAM3, and CLE45 act together to regulate the transition of protophloem cells from proliferation to differentiation, thus impinging on postembryonic growth capacity of the root meristem (PubMed:23569225, PubMed:25049386). Necessary for CLE45 peptide-triggered accumulation of MAKR5 in developing sieve elements (PubMed:27354416). {ECO:0000269|PubMed:16367950, ECO:0000269|PubMed:23569225, ECO:0000269|PubMed:25049386, ECO:0000269|PubMed:27354416, ECO:0000269|PubMed:28607033}.
|
Arabidopsis thaliana (Mouse-ear cress)
|
O65493
|
XCP1_ARATH
|
MAFSAPSLSKFSLLVAISASALLCCAFARDFSIVGYTPEHLTNTDKLLELFESWMSEHSKAYKSVEEKVHRFEVFRENLMHIDQRNNEINSYWLGLNEFADLTHEEFKGRYLGLAKPQFSRKRQPSANFRYRDITDLPKSVDWRKKGAVAPVKDQGQCGSCWAFSTVAAVEGINQITTGNLSSLSEQELIDCDTTFNSGCNGGLMDYAFQYIISTGGLHKEDDYPYLMEEGICQEQKEDVERVTISGYEDVPENDDESLVKALAHQPVSVAIEASGRDFQFYKGGVFNGKCGTDLDHGVAAVGYGSSKGSDYVIVKNSWGPRWGEKGFIRMKRNTGKPEGLCGINKMASYPTKTK
|
3.4.22.-
| null |
programmed cell death involved in cell development [GO:0010623]; proteolysis involved in protein catabolic process [GO:0051603]
|
extracellular space [GO:0005615]; lysosome [GO:0005764]; nucleus [GO:0005634]; plant-type vacuole [GO:0000325]; plasma membrane [GO:0005886]
|
cysteine-type endopeptidase activity [GO:0004197]
|
PF08246;PF00112;
|
3.90.70.10;
|
Peptidase C1 family
|
PTM: Autocleaves.
|
SUBCELLULAR LOCATION: Vacuole {ECO:0000269|PubMed:11788755}. Cell membrane {ECO:0000269|PubMed:11788755}. Note=Predominantly vacuolar. May be associated to plasma membrane.
| null | null | null | null | null |
FUNCTION: Cysteine protease involved in xylem tracheary element (TE) autolysis during xylogenesis in roots. Participates in micro autolysis within the intact central vacuole before mega autolysis is initiated by tonoplast implosion. {ECO:0000269|PubMed:18573193}.
|
Arabidopsis thaliana (Mouse-ear cress)
|
O65502
|
HC244_ARATH
|
MASLRLPAQLVTRGNLIHHNSSSSSSGRLSWRRSLTPENTIPLFPSSSSSSLNRERSIVVPVTCSAAAVNLAPGTPVRPTSILVVGATGTLGRQIVRRALDEGYDVRCLVRPRPAPADFLRDWGATVVNADLSKPETIPATLVGIHTVIDCATGRPEEPIKTVDWEGKVALIQCAKAMGIQKYVFYSIHNCDKHPEVPLMEIKYCTEKFLQESGLNHITIRLCGFMQGLIGQYAVPILEEKSVWGTDAPTRVAYMDTQDIARLTLIALRNEKINGKLLTFAGPRAWTTQEVITLCERLAGQDANVTTVPVSVLRVTRQLTRFFQWTNDVADRLAFSEVLSSDTVFSAPMTETNSLLGVDQKDMVTLEKYLQDYFSNILKKLKDLKAQSKQSDIYF
| null | null |
photosystem II assembly [GO:0010207]
|
chloroplast [GO:0009507]; chloroplast stroma [GO:0009570]; chloroplast thylakoid [GO:0009534]; chloroplast thylakoid membrane [GO:0009535]; photosystem II [GO:0009523]; plasma membrane [GO:0005886]; thylakoid membrane [GO:0042651]
|
translation initiation factor activity [GO:0003743]
|
PF05368;
|
3.40.50.720;
|
NmrA-type oxidoreductase family
| null |
SUBCELLULAR LOCATION: Plastid, chloroplast stroma {ECO:0000269|PubMed:23027666}. Plastid, chloroplast thylakoid membrane {ECO:0000269|PubMed:23027666}; Peripheral membrane protein {ECO:0000269|PubMed:23027666}; Stromal side {ECO:0000269|PubMed:23027666}. Note=Predominantly present at thylakoid membranes. {ECO:0000269|PubMed:23027666}.
| null | null | null | null | null |
FUNCTION: Auxiliary factor required, together with HCF173, for the biogenesis of photosystem II (PSII), especially for the synthesis of the reaction center proteins (e.g. D1), via the regulation of the corresponding mRNA (e.g. psbA) translation initiation (ribosomal loading) and stabilization (PubMed:29930106). Forms a trimeric complex with OHP1 and OHP2 that is required to promote PSII core subunit assembly (PubMed:29930106, PubMed:30397023). The trimeric complex forms a transient PSII reaction center-like complex with PsbA, PsbD, PsbE, PsbF and PsbI subunits in thylakoids for early assembly of PSII as well as PSII repair (PubMed:30397023). The trimeric complex is required for the recruitment of ribosomes to the psbA mRNA during PSII biogenesis and repair (PubMed:31991763). {ECO:0000269|PubMed:29930106, ECO:0000269|PubMed:30397023, ECO:0000269|PubMed:31991763}.
|
Arabidopsis thaliana (Mouse-ear cress)
|
O65508
|
NAC76_ARATH
|
MESVDQSCSVPPGFRFHPTDEELVGYYLRKKVASQKIDLDVIRDIDLYRIEPWDLQESCRIGYEERNEWYFFSHKDKKYPTGTRTNRATMAGFWKATGRDKAVYDKSKLIGMRKTLVFYKGRAPNGQKTDWIMHEYRLESDENAPPQEEGWVVCRAFKKKPMTGQAKNTETWSSSYFYDELPSGVRSVTEPLNYVSKQKQNVFAQDLMFKQELEGSDIGLNFIHCDQFIQLPQLESPSLPLTKRPVSLTSITSLEKNKNIYKRHLIEEDVSFNALISSGNKDKKKKKTSVMTTDWRALDKFVASQLMSQEDGVSGFGGHHEEDNNKIGHYNNEESNNKGSVETASSTLLSDREEENRFISGLLCSNLDYDLYRDLHV
| null | null |
cell wall organization [GO:0071555]; positive regulation of secondary cell wall biogenesis [GO:1901348]; regulation of DNA-templated transcription [GO:0006355]; xylem vessel member cell differentiation [GO:0048759]
|
nucleus [GO:0005634]
|
DNA-binding transcription factor activity [GO:0003700]; sequence-specific DNA binding [GO:0043565]; transcription cis-regulatory region binding [GO:0000976]
|
PF02365;
|
2.170.150.80;
|
Plant vascular related NAC-domain protein family
| null |
SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9C8W9, ECO:0000255|PROSITE-ProRule:PRU00353}.
| null | null | null | null | null |
FUNCTION: Transcription activator that binds to the secondary wall NAC binding element (SNBE), 5'-(T/A)NN(C/T)(T/C/G)TNNNNNNNA(A/C)GN(A/C/T)(A/T)-3', in the promoter of target genes (By similarity). Involved in xylem formation by promoting the expression of secondary wall-associated transcription factors and of genes involved in secondary wall biosynthesis and programmed cell death, genes driven by the secondary wall NAC binding element (SNBE). Triggers thickening of secondary walls (PubMed:25148240). {ECO:0000250|UniProtKB:Q9LVA1, ECO:0000269|PubMed:25148240}.
|
Arabidopsis thaliana (Mouse-ear cress)
|
O65517
|
SRS2_ARATH
|
MAGIFSLGGNNNNNGDEEEENQQQQKTNWVWYRSNANTNNINPSSSQQVWQIPPEQMLMHHHSHPQQQSLDLYPGHQIDVSDLATSSRSITISCRDCGNQAKKDCTHMRCRTCCKSRGFDCSTHVRSTWIPVARRRERQQQLHMSTSGGGGGSGSGGAGGGGSSIPKRHRDPTLPGTSSSSRLPSHSAGLEMGEASFPGEVSSDALFRCVKMSGVDDGGDGQYAYQTTVNIGGHLFKGILYDQGPESSYMSGGSGGSDHQSSSAGGGGGGHPFNPPVVTDGGGGVSSAMFVDPNSGGYYSSNMTTSVFMPPGTQFYQNPPRS
| null | null |
anther development [GO:0048653]; auxin biosynthetic process [GO:0009851]; auxin-activated signaling pathway [GO:0009734]; pollen development [GO:0009555]; positive regulation of DNA-templated transcription [GO:0045893]
|
nucleus [GO:0005634]
|
DNA binding [GO:0003677]; DNA-binding transcription factor activity [GO:0003700]; metal ion binding [GO:0046872]
|
PF05142;
| null |
SHI protein family
| null |
SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
| null | null | null | null | null |
FUNCTION: Transcription activator that binds DNA on 5'-ACTCTAC-3' and promotes auxin homeostasis-regulating gene expression (e.g. YUC genes), as well as genes affecting stamen development, cell expansion and timing of flowering. Synergistically with other SHI-related proteins, regulates gynoecium, stamen and leaf development in a dose-dependent manner, controlling apical-basal patterning. Promotes style and stigma formation, and influence vascular development during gynoecium development. May also have a role in the formation and/or maintenance of the shoot apical meristem (SAM). {ECO:0000269|PubMed:12361963, ECO:0000269|PubMed:16740145, ECO:0000269|PubMed:16740146, ECO:0000269|PubMed:18811619}.
|
Arabidopsis thaliana (Mouse-ear cress)
|
O65554
|
CIPK6_ARATH
|
MVGAKPVENGSDGGSSTGLLHGRYELGRLLGHGTFAKVYHARNIQTGKSVAMKVVGKEKVVKVGMVDQIKREISVMRMVKHPNIVELHEVMASKSKIYFAMELVRGGELFAKVAKGRLREDVARVYFQQLISAVDFCHSRGVYHRDLKPENLLLDEEGNLKVTDFGLSAFTEHLKQDGLLHTTCGTPAYVAPEVILKKGYDGAKADLWSCGVILFVLLAGYLPFQDDNLVNMYRKIYRGDFKCPGWLSSDARRLVTKLLDPNPNTRITIEKVMDSPWFKKQATRSRNEPVAATITTTEEDVDFLVHKSKEETETLNAFHIIALSEGFDLSPLFEEKKKEEKREMRFATSRPASSVISSLEEAARVGNKFDVRKSESRVRIEGKQNGRKGKLAVEAEIFAVAPSFVVVEVKKDHGDTLEYNNFCSTALRPALKDIFWTSTPA
|
2.7.11.1
|
COFACTOR: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
|
basipetal auxin transport [GO:0010540]; hyperosmotic salinity response [GO:0042538]; phosphorylation [GO:0016310]; response to calcium ion [GO:0051592]; response to salt stress [GO:0009651]; response to water deprivation [GO:0009414]; signal transduction [GO:0007165]
|
endoplasmic reticulum [GO:0005783]
|
ATP binding [GO:0005524]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674]
|
PF03822;PF00069;
|
3.30.310.80;1.10.510.10;
|
Protein kinase superfamily, CAMK Ser/Thr protein kinase family, SNF1 subfamily
|
PTM: Autophosphorylated.
|
SUBCELLULAR LOCATION: Endoplasmic reticulum {ECO:0000269|PubMed:21445098}. Note=Targeted to the cell membrane when interacting with CBL4 and ATK2.
|
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: CIPK serine-threonine protein kinases interact with CBL proteins. Binding of a CBL protein to the regulatory NAF domain of CIPK protein lead to the activation of the kinase in a calcium-dependent manner. Downstream of CBL1, CBL2, CBL3 and CBL9, regulates by phosphorylation the K(+) conductance and uptake of AKT1. Binds to CBL4 to modulate AKT2 activity by promoting a kinase interaction-dependent but phosphorylation-independent translocation of the channel to the plasma membrane. {ECO:0000269|PubMed:17898163, ECO:0000269|PubMed:21445098}.
|
Arabidopsis thaliana (Mouse-ear cress)
|
O65570
|
VILI4_ARATH
|
MSVSMRDLDPAFQGAGQKAGIEIWRIENFIPTPIPKSSIGKFFTGDSYIVLKTTALKTGALRHDIHYWLGKDTSQDEAGTAAVKTVELDAALGGRAVQYREVQGHETEKFLSYFKPCIIPQEGGVASGFKHVVAEEHITRLFVCRGKHVVHVKEVPFARSSLNHDDIYILDTKSKIFQFNGSNSSIQERAKALEVVQYIKDTYHDGTCEVATVEDGKLMADADSGEFWGFFGGFAPLPRKTANDEDKTYNSDITRLFCVEKGQANPVEGDTLKREMLDTNKCYILDCGIEVFVWMGRTTSLDDRKIASKAAEEMIRSSERPKSQMIRIIEGFETVPFRSKFESWTQETNTTVSEDGRGRVAALLQRQGVNVRGLMKAAPPKEEPQVFIDCTGNLQVWRVNGQAKTLLQAADHSKFYSGDCYVFQYSYPGEEKEEVLIGTWFGKQSVEEERGSAVSMASKMVESMKFVPAQARIYEGKEPIQFFVIMQSFIVFKGGISSGYKKYIAEKEVDDDTYNENGVALFRIQGSGPENMQAIQVDPVAASLNSSYYYILHNDSSVFTWAGNLSTATDQELAERQLDLIKPNQQSRAQKEGSESEQFWELLGGKAEYSSQKLTKEPERDPHLFSCTFTKEVLKVTEIYNFTQDDLMTEDIFIIDCHSEIFVWVGQEVVPKNKLLALTIGEKFIEKDSLLEKLSPEAPIYVIMEGGEPSFFTRFFTSWDSSKSAMHGNSFQRKLKIVKNGGTPVADKPKRRTPASYGGRASVPDKSQQRSRSMSFSPDRVRVRGRSPAFNALAATFESQNARNLSTPPPVVRKLYPRSVTPDSSKFAPAPKSSAIASRSALFEKIPPQEPSIPKPVKASPKTPESPAPESNSKEQEEKKENDKEEGSMSSRIESLTIQEDAKEGVEDEEDLPAHPYDRLKTTSTDPVSDIDVTRREAYLSSEEFKEKFGMTKEAFYKLPKWKQNKFKMAVQLF
| null | null |
actin crosslink formation [GO:0051764]; actin filament capping [GO:0051693]; actin filament depolymerization [GO:0030042]; actin filament organization [GO:0007015]; actin filament severing [GO:0051014]; cytoplasmic streaming [GO:0099636]; root hair elongation [GO:0048767]
|
cytoplasm [GO:0005737]; cytoskeleton [GO:0005856]; plasma membrane [GO:0005886]
|
actin filament binding [GO:0051015]; mRNA binding [GO:0003729]
|
PF00626;PF02209;
|
3.40.20.10;1.10.950.10;
|
Villin/gelsolin family
| null |
SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:21275995}.
| null | null | null | null | null |
FUNCTION: Binds actin and actin filament bundles in a Ca(2+)-insensitive manner, but caps the barbed end of actin filaments and is able to sever them in a calcium-dependent manner. Involved in root hair growth through regulating actin organization in a Ca(2+)-dependent manner. {ECO:0000269|PubMed:21275995, ECO:0000269|PubMed:22019634}.
|
Arabidopsis thaliana (Mouse-ear cress)
|
O65572
|
CCD1_ARATH
|
MAEKLSDGSSIISVHPRPSKGFSSKLLDLLERLVVKLMHDASLPLHYLSGNFAPIRDETPPVKDLPVHGFLPECLNGEFVRVGPNPKFDAVAGYHWFDGDGMIHGVRIKDGKATYVSRYVKTSRLKQEEFFGAAKFMKIGDLKGFFGLLMVNVQQLRTKLKILDNTYGNGTANTALVYHHGKLLALQEADKPYVIKVLEDGDLQTLGIIDYDKRLTHSFTAHPKVDPVTGEMFTFGYSHTPPYLTYRVISKDGIMHDPVPITISEPIMMHDFAITETYAIFMDLPMHFRPKEMVKEKKMIYSFDPTKKARFGVLPRYAKDELMIRWFELPNCFIFHNANAWEEEDEVVLITCRLENPDLDMVSGKVKEKLENFGNELYEMRFNMKTGSASQKKLSASAVDFPRINECYTGKKQRYVYGTILDSIAKVTGIIKFDLHAEAETGKRMLEVGGNIKGIYDLGEGRYGSEAIYVPRETAEEDDGYLIFFVHDENTGKSCVTVIDAKTMSAEPVAVVELPHRVPYGFHALFVTEEQLQEQTLI
|
1.14.99.n4
|
COFACTOR: Name=Fe(2+); Xref=ChEBI:CHEBI:29033; Evidence={ECO:0000250}; Note=Binds 1 Fe(2+) ion per subunit. {ECO:0000250};
|
carotene catabolic process [GO:0016121]; carotenoid catabolic process [GO:0016118]; xanthophyll catabolic process [GO:0016124]
|
chloroplast stroma [GO:0009570]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; Golgi apparatus [GO:0005794]; plant-type vacuole [GO:0000325]; plasma membrane [GO:0005886]; plasmodesma [GO:0009506]
|
9-cis-epoxycarotenoid dioxygenase activity [GO:0045549]; metal ion binding [GO:0046872]
|
PF03055;
| null |
Carotenoid oxygenase family
| null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12834401, ECO:0000269|PubMed:16507088}. Note=On the exterior surface of the plastids.
|
CATALYTIC ACTIVITY: Reaction=all-trans-zeaxanthin + 2 O2 = 2 (3R)-hydroxy-beta-ionone + 4,9-dimethyldodeca-2,4,6,8,10-pentaenedial; Xref=Rhea:RHEA:26393, ChEBI:CHEBI:15379, ChEBI:CHEBI:27547, ChEBI:CHEBI:53171, ChEBI:CHEBI:53173; EC=1.14.99.n4; Evidence={ECO:0000269|PubMed:11316814};
| null | null | null | null |
FUNCTION: Cleaves a variety of carotenoids symmetrically at both the 9-10 and 9'-10' double bonds. Active on beta,beta-carotene, lutein, zeaxanthin, all-trans-violaxanthin, 9-cis-violaxanthin and 9'-cis-neoxanthin. With most substrates, the carotenoid is symmetrically cleaved. Probably not involved in abscisic acid biosynthesis. {ECO:0000269|PubMed:11316814, ECO:0000269|PubMed:16507088}.
|
Arabidopsis thaliana (Mouse-ear cress)
|
O65583
|
UKL4_ARATH
|
MGSKSVVDMIEAASRAHFSGLHVNGHMNGLEPSALKETTSASEDIQRQPFVIGVAGGAASGKTTVCDMIIQQLHDQRVVLINLDSFYHNLTEEELARVHEYNFDHPDAFDTEHLLSCMEKLRQGQAVDIPKYDFKTYRSSVFRRVNPTDVIILEGILLFHDPRVRKLMNMKIFVCTDADVRLARRIKRDTVENGRDIGTVLDQYSKFVKPAFDDFILPTKKYADIIIPRGGDNHVAIDLIVQHICTKLGQHDLCKIYPNLYVIHSTFQIRGMHTLIRDSQTTKHDFVFYSDRLIRLVVEHGLGHLPFTEKQVITPTGCVYSGVDFCKRLCGVSVIRSGESMENALRACCKGIKIGKILIHREGDNGQQLVYEKLPNDISERHVLLLDPILGTGNSAVEAINLLISKGVPEGNIIFLNLISAPQGVHVVCKKFPRIKIVTSEIDNGLNEEFRVIPGMGEFGDRYFGTDDD
|
2.4.2.9; 2.7.1.48
|
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; Note=Binds 1 Mg(2+) ion per subunit. The magnesium is bound as Mg-PRPP. {ECO:0000250};
|
CTP salvage [GO:0044211]; phosphorylation [GO:0016310]; UMP salvage [GO:0044206]
|
cytoplasm [GO:0005737]
|
ATP binding [GO:0005524]; cytidine kinase activity [GO:0043771]; GTP binding [GO:0005525]; uracil phosphoribosyltransferase activity [GO:0004845]; uridine kinase activity [GO:0004849]
|
PF00485;PF14681;
|
3.40.50.2020;3.40.50.300;
|
Uridine kinase family; UPRTase family
| null | null |
CATALYTIC ACTIVITY: Reaction=diphosphate + UMP = 5-phospho-alpha-D-ribose 1-diphosphate + uracil; Xref=Rhea:RHEA:13017, ChEBI:CHEBI:17568, ChEBI:CHEBI:33019, ChEBI:CHEBI:57865, ChEBI:CHEBI:58017; EC=2.4.2.9; CATALYTIC ACTIVITY: Reaction=ATP + cytidine = ADP + CMP + H(+); Xref=Rhea:RHEA:24674, ChEBI:CHEBI:15378, ChEBI:CHEBI:17562, ChEBI:CHEBI:30616, ChEBI:CHEBI:60377, ChEBI:CHEBI:456216; EC=2.7.1.48; CATALYTIC ACTIVITY: Reaction=ATP + uridine = ADP + H(+) + UMP; Xref=Rhea:RHEA:16825, ChEBI:CHEBI:15378, ChEBI:CHEBI:16704, ChEBI:CHEBI:30616, ChEBI:CHEBI:57865, ChEBI:CHEBI:456216; EC=2.7.1.48;
| null |
PATHWAY: Pyrimidine metabolism; UMP biosynthesis via salvage pathway; UMP from uracil: step 1/1.; PATHWAY: Pyrimidine metabolism; CTP biosynthesis via salvage pathway; CTP from cytidine: step 1/3.; PATHWAY: Pyrimidine metabolism; UMP biosynthesis via salvage pathway; UMP from uridine: step 1/1.
| null | null |
FUNCTION: Involved in the pyrimidine salvage pathway. The uracil phosphoribosyltransferase (UPRT) activity, that catalyzes the conversion of uracil and 5-phospho-alpha-D-ribose 1-diphosphate (PRPP) to UMP and diphosphate, is unsure. {ECO:0000269|PubMed:19563437}.
|
Arabidopsis thaliana (Mouse-ear cress)
|
O65639
|
CSP1_ARATH
|
MASEDQSAARSTGKVNWFNASKGYGFITPDDGSVELFVHQSSIVSEGYRSLTVGDAVEFAITQGSDGKTKAVNVTAPGGGSLKKENNSRGNGARRGGGGSGCYNCGELGHISKDCGIGGGGGGGERRSRGGEGCYNCGDTGHFARDCTSAGNGDQRGATKGGNDGCYTCGDVGHVARDCTQKSVGNGDQRGAVKGGNDGCYTCGDVGHFARDCTQKVAAGNVRSGGGGSGTCYSCGGVGHIARDCATKRQPSRGCYQCGGSGHLARDCDQRGSGGGGNDNACYKCGKEGHFARECSSVA
| null | null |
cold acclimation [GO:0009631]; DNA duplex unwinding [GO:0032508]; response to cold [GO:0009409]; response to salt stress [GO:0009651]; response to water deprivation [GO:0009414]; RNA secondary structure unwinding [GO:0010501]
|
cytoplasm [GO:0005737]; nucleus [GO:0005634]; plasma membrane [GO:0005886]
|
double-stranded DNA binding [GO:0003690]; mRNA binding [GO:0003729]; RNA binding [GO:0003723]; single-stranded DNA binding [GO:0003697]; zinc ion binding [GO:0008270]
|
PF00313;PF00098;
|
2.40.50.140;4.10.60.10;
|
Cold shock protein (CSP) family
| null |
SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm {ECO:0000250}.
| null | null | null | null | null |
FUNCTION: Chaperone that binds to RNA, single- (ssDNA) and double-stranded (dsDNA) DNA, and unwinds nucleic acid duplex. Exhibits a DNA melting activity. May be involved in cold resistance. Prevents seed germination under dehydration or salt stress conditions. {ECO:0000269|PubMed:17169986, ECO:0000269|PubMed:19258348, ECO:0000269|PubMed:19269998}.
|
Arabidopsis thaliana (Mouse-ear cress)
|
O65660
|
PLAT1_ARATH
|
MARRDVLLPFLLLLATVSAVAFAEDDPDCVYTFYLRTGSIWKAGTDSIISARIYDKDGDYIGIKNLQAWAGLMGPDYNYFERGNLDIFSGRAPCLPSPICALNLTSDGSGDHHGWYVNYVEITTAGVHAQCSTQDFEIEQWLATDTSPYELTAVRNNCPVKLRDSVSRVGSEIRKKLSWVV
| null | null |
response to cold [GO:0009409]; response to salt stress [GO:0009651]; response to water deprivation [GO:0009414]
|
chloroplast thylakoid membrane [GO:0009535]; endoplasmic reticulum [GO:0005783]; plant-type vacuole [GO:0000325]; plasma membrane [GO:0005886]; plastoglobule [GO:0010287]; secretory vesicle [GO:0099503]; thylakoid [GO:0009579]
| null |
PF01477;
|
2.60.60.20;
| null | null |
SUBCELLULAR LOCATION: Endoplasmic reticulum {ECO:0000269|PubMed:25396746}. Plastid, chloroplast, plastoglobule {ECO:0000269|PubMed:22274653}. Note=Localizes to rod shaped ER structures that resemble ER bodies. {ECO:0000269|PubMed:25396746}.
| null | null | null | null | null |
FUNCTION: Positive regulator of abiotic stress tolerance involved in the regulation of plant growth. May be a downstream target of the abscisic acid (ABA) signaling pathway. {ECO:0000269|PubMed:25396746}.
|
Arabidopsis thaliana (Mouse-ear cress)
|
O65683
|
BZP11_ARATH
|
MESSSSGTTSSTIQTSSGSEESLMEQRKRKRMLSNRESARRSRMKKQKLLDDLTAQVNHLKKENTEIVTSVSITTQHYLTVEAENSVLRAQLDELNHRLQSLNDIIEFLDSSNNNNNNNMGMCSNPLVGLECDDFFVNQMNMSYIMNQPLMASSDALMY
| null | null |
negative regulation of translation [GO:0017148]; positive regulation of DNA-templated transcription [GO:0045893]; response to sucrose [GO:0009744]; sucrose induced translational repression [GO:0080149]
|
nucleus [GO:0005634]
|
DNA-binding transcription factor activity [GO:0003700]; protein heterodimerization activity [GO:0046982]; sequence-specific DNA binding [GO:0043565]; transcription cis-regulatory region binding [GO:0000976]
|
PF00170;
|
1.20.5.170;
| null | null |
SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00978, ECO:0000269|PubMed:15047879}.
| null | null | null | null | null |
FUNCTION: Transcription factor that binds to the DNA sequence 5'-ACTCAT-3' in target gene promoters. Promotes POX1/PRODH1 expression in response to hypoosmolarity stress (PubMed:15047879). Positively regulates the expression of ASN1 and POX2/PRODH2 genes, which are involved in amino acid metabolism (PubMed:18088315). Regulates several metabolic pathways such as myo-inositol, raffinose and trehalose. Regulates several trehalose metabolism genes, including TRE1, TPP5 and TPP6 (PubMed:21534971). Mediates recruitment of the histone acetylation machinery to activate auxin-induced transcription. Interacts with ADA2B adapter protein to promote ADA2B-mediated recruitment of SAGA-like histone acetyltransferase complexes to specific auxin-responsive genes (PubMed:24861440). {ECO:0000269|PubMed:15047879, ECO:0000269|PubMed:18088315, ECO:0000269|PubMed:21534971, ECO:0000269|PubMed:24861440}.
|
Arabidopsis thaliana (Mouse-ear cress)
|
O65686
|
RS16A_ARATH
|
MTVKIRLARLGCKHRPFYRVVVADEKSRRDGKQIEVLGFYDPLQGKEDADRVSLKFDRIKYWLSVGAQPTDTVESMLFRAGLIPPKPMVVVGSKNGQKSTSQHVSPITGEILN
| null | null |
embryo development ending in seed dormancy [GO:0009793]; mitochondrial translation [GO:0032543]
|
chloroplast [GO:0009507]; chloroplast envelope [GO:0009941]; plasma membrane [GO:0005886]; plastid [GO:0009536]; ribosome [GO:0005840]; small ribosomal subunit [GO:0015935]
|
mRNA binding [GO:0003729]; protein domain specific binding [GO:0019904]; structural constituent of ribosome [GO:0003735]
|
PF00886;
|
3.30.1320.10;
|
Bacterial ribosomal protein bS16 family
| null |
SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000269|PubMed:18453549}. Note=Not seen to be targeted to mitochondria. {ECO:0000269|PubMed:18453549}.
| null | null | null | null | null | null |
Arabidopsis thaliana (Mouse-ear cress)
|
O65717
|
CNGC1_ARATH
|
MNFRQEKFVRFQDWKSDKTSSDVEYSGKNEIQTGIFQRTISSISDKFYRSFESSSARIKLFKRSYKSYSFKEAVSKGIGSTHKILDPQGPFLQRWNKIFVLACIIAVSLDPLFFYVPIIDDAKKCLGIDKKMEITASVLRSFTDVFYVLHIIFQFRTGFIAPSSRVFGRGVLVEDKREIAKRYLSSHFIIDILAVLPLPQMVILIIIPHMRGSSSLNTKNMLKFIVFFQYIPRFIRIYPLYKEVTRTSGILTETAWAGAAFNLFLYMLASHVFGAFWYLFSIERETVCWKQACERNNPPCISKLLYCDPETAGGNAFLNESCPIQTPNTTLFDFGIFLDALQSGVVESQDFPQKFFYCFWWGLQNLSSLGQNLKTSTYIWEICFAVFISIAGLVLFSFLIGNMQTYLQSTTTRLEEMRVKRRDAEQWMSHRLLPENLRKRIRRYEQYKWQETRGVDEENLLSNLPKDLRRDIKRHLCLALLMRVPMFEKMDEQLLDALCDRLQPVLYTEESYIVREGDPVDEMLFIMRGKLLTITTNGGRTGFLNSEYLGAGDFCGEELLTWALDPHSSSNLPISTRTVRALMEVEAFALKADDLKFVASQFRRLHSKQLRHTFRYYSQQWKTWAACFIQAAWRRYIKKKLEESLKEEENRLQDALAKEACGSSPSLGATIYASRFAANILRTIRRSGSVRKPRMPERMPPMLLQKPAEPDFNSDD
| null | null | null |
plasma membrane [GO:0005886]
|
calmodulin binding [GO:0005516]; cAMP binding [GO:0030552]; cGMP binding [GO:0030553]; monoatomic ion channel activity [GO:0005216]
|
PF00027;PF00520;
|
1.10.287.70;1.10.287.630;2.60.120.10;
|
Cyclic nucleotide-gated cation channel (TC 1.A.1.5) family
| null |
SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
| null | null | null | null | null |
FUNCTION: Acts as a cyclic nucleotide-gated ion channel. Can be activated by cyclic AMP which leads to an opening of the cation channel. May be responsible for cAMP-induced calcium entry in cells and thus should be involved in the calcium signal transduction. Could transport K(+), Na(+) and Pb(2+). {ECO:0000269|PubMed:11115134, ECO:0000269|PubMed:11842144}.
|
Arabidopsis thaliana (Mouse-ear cress)
|
O65718
|
CNGC2_ARATH
|
MPSHPNFIFRWIGLFSDKFRRQTTGIDENSNLQINGGDSSSSGSDETPVLSSVECYACTQVGVPAFHSTSCDQAHAPEWRASAGSSLVPIQEGSVPNPARTRFRRLKGPFGEVLDPRSKRVQRWNRALLLARGMALAVDPLFFYALSIGRTTGPACLYMDGAFAAVVTVLRTCLDAVHLWHVWLQFRLAYVSRESLVVGCGKLVWDPRAIASHYARSLTGFWFDVIVILPVPQAVFWLVVPKLIREEKVKLIMTILLLIFLFQFLPKIYHCICLMRRMQKVTGYIFGTIWWGFALNLIAYFIASHVAGGCWYVLAIQRVASCIRQQCMRTGNCNLSLACKEEVCYQFVSPTSTVGYPCLSGNLTSVVNKPMCLDSNGPFRYGIYRWALPVISSNSLAVKILYPIFWGLMTLSTFANDLEPTSNWLEVIFSIVMVLSGLLLFTLLIGNIQVFLHAVMAKKRKMQIRCRDMEWWMKRRQLPSRLRQRVRRFERQRWNALGGEDELELIHDLPPGLRRDIKRYLCFDLINKVPLFRGMDDLILDNICDRAKPRVFSKDEKIIREGDPVQRMIFIMRGRVKRIQSLSKGVLATSTLEPGGYLGDELLSWCLRRPFLDRLPPSSATFVCLENIEAFSLGSEDLRYITDHFRYKFANERLKRTARYYSSNWRTWAAVNIQMAWRRRRKRTRGENIGGSMSPVSENSIEGNSERRLLQYAAMFMSIRPHDHLE
| null | null |
calcium ion import [GO:0070509]; defense response [GO:0006952]; nitric oxide mediated signal transduction [GO:0007263]; plant-type hypersensitive response [GO:0009626]
|
plasma membrane [GO:0005886]
|
calcium channel activity [GO:0005262]; calmodulin binding [GO:0005516]; cAMP binding [GO:0030552]; cGMP binding [GO:0030553]; intracellularly cAMP-activated cation channel activity [GO:0005222]; intracellularly cyclic nucleotide-activated monoatomic cation channel activity [GO:0005221]; inward rectifier potassium channel activity [GO:0005242]
|
PF00027;
|
1.10.287.70;1.10.287.630;2.60.120.10;
|
Cyclic nucleotide-gated cation channel (TC 1.A.1.5) family
| null |
SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
| null | null | null | null | null |
FUNCTION: Acts as a cyclic nucleotide-gated ion channel. Permeable to potassium and calcium in a cyclic nucleotide-dependent fashion (cAMP or cGMP). Could also transport lithium, cesium and rubium and displays a strong selectivity against sodium. Seems to directly participate in pathogen-induced calcium influx. May function in homeostasis, re-establishing ionic balance after defense action and/or other stimuli. Could mediate the initiation of the developmentally regulated cell death programs. {ECO:0000269|PubMed:10900264, ECO:0000269|PubMed:11506354}.
|
Arabidopsis thaliana (Mouse-ear cress)
|
O65719
|
HSP7C_ARATH
|
MAGKGEGPAIGIDLGTTYSCVGVWQHDRVEIIANDQGNRTTPSYVAFTDSERLIGDAAKNQVAMNPINTVFDAKRLIGRRFTDSSVQSDIKLWPFTLKSGPAEKPMIVVNYKGEDKEFSAEEISSMILIKMREIAEAYLGTTIKNAVVTVPAYFNDSQRQATKDAGVIAGLNVMRIINEPTAAAIAYGLDKKATSVGEKNVLIFDLGGGTFDVSLLTIEEGIFEVKATAGDTHLGGEDFDNRMVNHFVQEFKRKNKKDISGNPRALRRLRTACERAKRTLSSTAQTTIEIDSLFDGIDFYAPITRARFEELNIDLFRKCMEPVEKCLRDAKMDKNSIDDVVLVGGSTRIPKVQQLLVDFFNGKELCKSINPDEAVAYGAAVQAAILSGEGNEKVQDLLLLDVTPLSLGLETAGGVMTVLIQRNTTIPTKKEQVFSTYSDNQPGVLIQVYEGERARTKDNNLLGKFELSGIPPAPRGVPQITVCFDIDANGILNVSAEDKTTGQKNKITITNDKGRLSKDEIEKMVQEAEKYKSEDEEHKKKVDAKNALENYAYNMRNTIRDEKIGEKLAGDDKKKIEDSIEAAIEWLEANQLAECDEFEDKMKELESICNPIIAKMYQGGEAGGPAAGGMDEDVPPSAGGAGPKIEEVD
| null | null |
response to heat [GO:0009408]; response to virus [GO:0009615]
|
apoplast [GO:0048046]; chloroplast [GO:0009507]; cytosol [GO:0005829]; cytosolic ribosome [GO:0022626]; Golgi apparatus [GO:0005794]; nuclear matrix [GO:0016363]; plant-type cell wall [GO:0009505]; plant-type vacuole [GO:0000325]; plasma membrane [GO:0005886]; plasmodesma [GO:0009506]; vacuole [GO:0005773]
|
ATP binding [GO:0005524]; ATP-dependent protein folding chaperone [GO:0140662]; mRNA binding [GO:0003729]; protease binding [GO:0002020]
|
PF00012;
|
1.20.1270.10;3.30.30.30;3.30.420.40;
|
Heat shock protein 70 (TC 1.A.33) family, DnaK subfamily
| null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305|PubMed:14505352}. Nucleus matrix {ECO:0000269|PubMed:14505352}.
| null | null | null | null | null |
FUNCTION: In cooperation with other chaperones, Hsp70s are key components that facilitate folding of de novo synthesized proteins, assist translocation of precursor proteins into organelles, and are responsible for degradation of damaged protein under stress conditions. {ECO:0000305}.
|
Arabidopsis thaliana (Mouse-ear cress)
|
O65782
|
C83B1_ARATH
|
MDLLLIIAGLVAAAAFFFLRSTTKKSLRLPPGPKGLPIIGNLHQMEKFNPQHFLFRLSKLYGPIFTMKIGGRRLAVISSAELAKELLKTQDLNFTARPLLKGQQTMSYQGRELGFGQYTAYYREMRKMCMVNLFSPNRVASFRPVREEECQRMMDKIYKAADQSGTVDLSELLLSFTNCVVCRQAFGKRYNEYGTEMKRFIDILYETQALLGTLFFSDLFPYFGFLDNLTGLSARLKKAFKELDTYLQELLDETLDPNRPKQETESFIDLLMQIYKDQPFSIKFTHENVKAMILDIVVPGTDTAAAVVVWAMTYLIKYPEAMKKAQDEVRSVIGDKGYVSEEDIPNLPYLKAVIKESLRLEPVIPILLHRETIADAKIGGYDIPAKTIIQVNAWAVSRDTAAWGDNPNEFIPERFMNEHKGVDFKGQDFELLPFGSGRRMCPAMHLGIAMVEIPFANLLYKFDWSLPKGIKPEDIKMDVMTGLAMHKKEHLVLAPTKHI
|
1.14.14.45
|
COFACTOR: Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250|UniProtKB:Q96242};
|
adventitious root development [GO:0048830]; defense response by callose deposition in cell wall [GO:0052544]; defense response to bacterium [GO:0042742]; defense response to fungus [GO:0050832]; indole glucosinolate biosynthetic process [GO:0009759]; indoleacetic acid biosynthetic process [GO:0009684]; induced systemic resistance [GO:0009682]; response to insect [GO:0009625]; response to red light [GO:0010114]; shade avoidance [GO:0009641]; tryptophan biosynthetic process [GO:0000162]
|
endoplasmic reticulum [GO:0005783]; mitochondrion [GO:0005739]; plasma membrane [GO:0005886]
|
heme binding [GO:0020037]; iron ion binding [GO:0005506]; oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, NAD(P)H as one donor, and incorporation of one atom of oxygen [GO:0016709]
|
PF00067;
|
1.10.630.10;
|
Cytochrome P450 family
| null |
SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}.
|
CATALYTIC ACTIVITY: Reaction=(E)-(indol-3-yl)acetaldehyde oxime + glutathione + O2 + reduced [NADPH--hemoprotein reductase] = (E)-1-(glutathione-S-yl)-2-(1H-indol-3-yl)acetohydroximate + H(+) + 2 H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:52180, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:17545, ChEBI:CHEBI:57618, ChEBI:CHEBI:57925, ChEBI:CHEBI:58210, ChEBI:CHEBI:136444; EC=1.14.14.45; Evidence={ECO:0000269|PubMed:12970475}; CATALYTIC ACTIVITY: Reaction=(E)-phenylacetaldehyde oxime + glutathione + O2 + reduced [NADPH--hemoprotein reductase] = (Z)-1-(glutathione-S-yl)-2-phenylacetohydroximate + H(+) + 2 H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:52192, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:47793, ChEBI:CHEBI:57618, ChEBI:CHEBI:57925, ChEBI:CHEBI:58210, ChEBI:CHEBI:136447; EC=1.14.14.45; Evidence={ECO:0000269|PubMed:12970475};
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=3.1 uM for indole-3-acetaldoxime {ECO:0000269|PubMed:11158532, ECO:0000269|PubMed:11553739, ECO:0000269|PubMed:12970475}; KM=65 uM for p-hydroxyphenylacetaldoxime {ECO:0000269|PubMed:12970475}; KM=188 uM for phenylacetaldoxime {ECO:0000269|PubMed:12970475}; Note=kcat is 52 min(-1) with indole-3-acetaldoxime as substrate. kcat is 14 min(-1) with p-hydroxyphenylacetaldoxime as substrate. kcat is 47 min(-1) with phenylacetaldoxime as substrate. {ECO:0000269|PubMed:12970475};
| null | null | null |
FUNCTION: Involved in the metabolism of aromatic oximes. Catalyzes the oxime metabolizing step in indole glucosinolate biosynthesis by converting indole-3-acetaldoxime into indole-3-S-alkyl-thiohydroximate. Probably required for glucosinolate activation in response to pathogens. Functions in auxin homeostasis because indole-3-acetaldoxime also serves as a precursor for auxin biosynthesis. Specifically metabolizes (E)-p-hydroxyphenylacetaldoxime into an S-alkyl-thiohydroximate (PubMed:26361733). {ECO:0000269|PubMed:11114200, ECO:0000269|PubMed:11158532, ECO:0000269|PubMed:11333274, ECO:0000269|PubMed:11553739, ECO:0000269|PubMed:11805067, ECO:0000269|PubMed:12970475, ECO:0000269|PubMed:26361733}.
|
Arabidopsis thaliana (Mouse-ear cress)
|
O65797
|
ADS1_ARATH
|
MSLSASEKEENNKKMAADKAEMGRKKRAMWERKWKRLDIVKAFASLFVHFLCLLAPFNFTWPALRVALIVYTVGGLGITVSYHRNLAHRSFKVPKWLEYFFAYCGLLAIQGDPIDWVSTHRYHHQFTDSDRDPHSPNEGFWFSHLLWLFDTGYLVEKCGRRTNVEDLKRQWYYKFLQRTVLYHILTFGFLLYYFGGLSFLTWGMGIGVAMEHHVTCLINSLCHVWGSRTWKTNDTSRNVWWLSVFSFGESWHNNHHAFESSARQGLEWWQIDISWYIVRFLEIIGLATDVKLPSESQRRRMAMVR
|
1.14.19.-
|
COFACTOR: Name=Fe cation; Xref=ChEBI:CHEBI:24875; Evidence={ECO:0000250|UniProtKB:O00767};
|
unsaturated fatty acid biosynthetic process [GO:0006636]; very long-chain fatty acid biosynthetic process [GO:0042761]
|
chloroplast membrane [GO:0031969]; endoplasmic reticulum membrane [GO:0005789]
|
16:0 monogalactosyldiacylglycerol desaturase activity [GO:0009979]; metal ion binding [GO:0046872]; oxidoreductase activity, acting on paired donors, with oxidation of a pair of donors resulting in the reduction of molecular oxygen to two molecules of water [GO:0016717]
|
PF00487;
| null |
Fatty acid desaturase type 1 family
| null |
SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:23175755}; Multi-pass membrane protein {ECO:0000255}. Plastid, chloroplast membrane {ECO:0000305|PubMed:27062193}; Multi-pass membrane protein {ECO:0000255}.
| null | null |
PATHWAY: Lipid metabolism; polyunsaturated fatty acid biosynthesis. {ECO:0000305}.
| null | null |
FUNCTION: Involved in delta-9 desaturation of fatty acids (Probable) (PubMed:15240892, PubMed:17156034). Involved in the production of very-long-chain fatty acids (VLCFAs) (PubMed:23175755). May desaturate chloroplastic monogalactosyl diacylglycerol (MGDG) and alter chloroplast membrane fluidity, which is required to prime a cold acclimation response (PubMed:27062193). {ECO:0000269|PubMed:15240892, ECO:0000269|PubMed:17156034, ECO:0000269|PubMed:23175755, ECO:0000269|PubMed:27062193, ECO:0000305|PubMed:9559566}.
|
Arabidopsis thaliana (Mouse-ear cress)
|
O65896
|
CDA1_ARATH
|
MDKPSFVIQSKEAESAAKQLGVSVIQLLPSLVKPAQSYARTPISKFNVAVVGLGSSGRIFLGVNVEFPNLPLHHSIHAEQFLVTNLTLNGERHLNFFAVSAAPCGHCRQFLQEIRDAPEIKILITDPNNSADSDSAADSDGFLRLGSFLPHRFGPDDLLGKDHPLLLESHDNHLKISDLDSICNGNTDSSADLKQTALAAANRSYAPYSLCPSGVSLVDCDGKVYRGWYMESAAYNPSMGPVQAALVDYVANGGGGGYERIVGAVLVEKEDAVVRQEHTARLLLETISPKCEFKVFHCYEA
|
3.5.4.5
|
COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000305|PubMed:10024464}; Note=Binds 1 zinc ion per subunit. {ECO:0000305|PubMed:10024464};
|
cytidine catabolic process [GO:0006216]; cytidine deamination [GO:0009972]
|
cytosol [GO:0005829]; mitochondrion [GO:0005739]
|
cytidine deaminase activity [GO:0004126]; deoxycytidine deaminase activity [GO:0047844]; protein homodimerization activity [GO:0042803]; zinc ion binding [GO:0008270]
|
PF00383;PF08211;
|
3.40.140.10;
|
Cytidine and deoxycytidylate deaminase family
| null | null |
CATALYTIC ACTIVITY: Reaction=cytidine + H(+) + H2O = NH4(+) + uridine; Xref=Rhea:RHEA:16069, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16704, ChEBI:CHEBI:17562, ChEBI:CHEBI:28938; EC=3.5.4.5; Evidence={ECO:0000269|PubMed:10024464, ECO:0000269|PubMed:10469156, ECO:0000269|Ref.3}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16070; Evidence={ECO:0000269|PubMed:10024464, ECO:0000269|PubMed:10469156, ECO:0000269|Ref.3}; CATALYTIC ACTIVITY: Reaction=2'-deoxycytidine + H(+) + H2O = 2'-deoxyuridine + NH4(+); Xref=Rhea:RHEA:13433, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15698, ChEBI:CHEBI:16450, ChEBI:CHEBI:28938; EC=3.5.4.5; Evidence={ECO:0000269|PubMed:10024464, ECO:0000269|PubMed:10469156, ECO:0000269|Ref.3}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13434; Evidence={ECO:0000269|PubMed:10024464, ECO:0000269|PubMed:10469156, ECO:0000269|Ref.3};
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=150 uM for cytidine (at pH 7.5 and 37 degrees Celsius) {ECO:0000269|PubMed:10024464}; KM=250 uM for cytidine (at pH 7.5 and 25 degrees Celsius) {ECO:0000269|PubMed:10469156}; KM=226.1 uM for cytidine (at pH 8.0 and 25 degrees Celsius) {ECO:0000269|Ref.3}; KM=75 uM for 2'-deoxycytidine (at pH 7.5 and 37 degrees Celsius) {ECO:0000269|PubMed:10024464}; KM=120 uM for 2'-deoxycytidine (at pH 7.5 and 25 degrees Celsius) {ECO:0000269|PubMed:10469156}; KM=49.3 uM for 2'-deoxycytidine (at pH 8.0 and 25 degrees Celsius) {ECO:0000269|Ref.3}; Vmax=59.5 umol/min/mg enzyme toward cytidine (at pH 7.5 and 37 degrees Celsius) {ECO:0000269|PubMed:10024464}; Vmax=58 umol/min/mg enzyme toward cytidine (at pH 7.5 and 25 degrees Celsius) {ECO:0000269|PubMed:10469156}; Vmax=39.7 umol/min/mg enzyme toward cytidine (at pH 8.0 and 25 degrees Celsius) {ECO:0000269|Ref.3}; Vmax=49 umol/min/mg enzyme toward 2'-deoxycytidine (at pH 7.5 and 37 degrees Celsius) {ECO:0000269|PubMed:10024464}; Vmax=38 umol/min/mg enzyme toward 2'-deoxycytidine (at pH 7.5 and 25 degrees Celsius) {ECO:0000269|PubMed:10469156}; Vmax=24.4 umol/min/mg enzyme toward 2'-deoxycytidine (at pH 8.0 and 25 degrees Celsius, Ref.3) {ECO:0000269|PubMed:10024464, ECO:0000269|PubMed:10469156, ECO:0000269|Ref.3};
| null |
BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.5-8.0. {ECO:0000269|PubMed:10024464, ECO:0000269|PubMed:10469156, ECO:0000269|Ref.3};
| null |
FUNCTION: This enzyme scavenges exogenous and endogenous cytidine and 2'-deoxycytidine for UMP synthesis. Functions as a conventional cytidine deaminase. Has no affinity for RNA and is not involved in RNA-editing by C-to-U deamination. {ECO:0000269|PubMed:10024464, ECO:0000269|PubMed:10469156, ECO:0000269|Ref.3}.
|
Arabidopsis thaliana (Mouse-ear cress)
|
O65934
|
ABC1_MYCTU
|
MPMSQPAAPPVLTVRYEGSERTFAAGHDVVVGRDLRADVRVAHPLISRAHLLLRFDQGRWVAIDNGSLNGLYLNNRRVPVVDIYDAQRVHIGNPDGPALDFEVGRHRGSAGRPPQTTSIRLPNLSAGAWPTDGPPQTGTLGSGQLQQLPPATTRIPAAPPSGPQPRYPTGGQQLWPPSGPQRAPQIYRPPTAAPPPAGARGGTEAGNLATSMMKILRPGRLTGELPPGAVRIGRANDNDIVIPEVLASRHHATLVPTPGGTEIRDNRSINGTFVNGARVDAALLHDGDVVTIGNIDLVFADGTLARREENLLETRVGGLDVRGVTWTIDGDKTLLDGISLTARPGMLTAVIGPSGAGKSTLARLVAGYTHPTDGTVTFEGHNVHAEYASLRSRIGMVPQDDVVHGQLTVKHALMYAAELRLPPDTTKDDRTQVVARVLEELEMSKHIDTRVDKLSGGQRKRASVALELLTGPSLLILDEPTSGLDPALDRQVMTMLRQLADAGRVVLVVTHSLTYLDVCDQVLLLAPGGKTAFCGPPTQIGPVMGTTNWADIFSTVADDPDAAKARYLARTGPTPPPPPVEQPAELGDPAHTSLFRQFSTIARRQLRLIVSDRGYFVFLALLPFIMGALSMSVPGDVGFGFPNPMGDAPNEPGQILVLLNVGAVFMGTALTIRDLIGERAIFRREQAVGLSTTAYLIAKVCVYTVLAVVQSAIVTVIVLVGKGGPTQGAVALSKPDLELFVDVAVTCVASAMLGLALSAIAKSNEQIMPLLVVAVMSQLVFSGGMIPVTGRVPLDQMSWVTPARWGFAASAATVDLIKLVPGPLTPKDSHWHHTASAWWFDMAMLVALSVIYVGFVRWKIRLKAC
|
7.-.-.-
| null |
transmembrane transport [GO:0055085]
|
cytosol [GO:0005829]; membrane [GO:0016020]; peptidoglycan-based cell wall [GO:0009274]; plasma membrane [GO:0005886]
|
ABC-type transporter activity [GO:0140359]; ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; ATPase-coupled transmembrane transporter activity [GO:0042626]
|
PF01061;PF00005;PF00498;
|
2.60.200.20;3.40.50.300;
|
ABC transporter superfamily; ABC-2 integral membrane protein family
|
PTM: Phosphorylated by PknF. Can probably be phosphorylated in vivo by other kinases when PknF is missing. {ECO:0000269|PubMed:15135525, ECO:0000269|PubMed:15987910, ECO:0000269|PubMed:21622570}.
|
SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
| null | null | null | null | null |
FUNCTION: Involved in the translocation of an unknown substrate across the membrane. Transmembrane domains (TMD) form a pore in the membrane and the ATP-binding domain (NBD) is responsible for energy generation. Required for virulence. {ECO:0000269|PubMed:15135525, ECO:0000269|PubMed:16040957}.
|
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
|
O66200
|
CH60_ENTAG
|
MAAKDVKFGNDARVKMLRGVNVLADAVKVTLGPKGRNVVLDKSFGAPTITKDGVSVAREIELEDKFENMGAQMVKEVASKANDAAGDGTTTATVLAQAIITEGLKAVAAGMNPMDLKRGIDKAVASAVEELKALSVPCSDSKAIAQVGTISANSDETVGKLIAEAMDKVGKEGVITVEDGTGLEDELDVVEGMQFDRGYLSPYFINKPETGAVELESPFILLADKKISNIREMLPVLEAVAKAGKPLVIIAEDVEGEALATLVVNTMRGIVKVAAVKAPGFGDRRKAMLQDIATLTGGTVISEEIGMELEKATLEDLGQAKRVVINKDTTTIIDGVGEEAAIQGRVGQIRKQIEEATSDYDREKLQERVAKLAGGVAVIKVGAATEVEMKEKKARVDDALHATRAAVEEGVVAGGGVALVRVAAKLAGLTAQNEDQNVGIKVALRAMEAPLRQIVSNAGEEPSVVANNVKAGEGNYGYNAATEEYGNMIDFGILDPTKVTRSALQYAASVAGLMITTECMVTDMPKGDAPDLXAAGMGG
|
5.6.1.7
| null |
chaperone cofactor-dependent protein refolding [GO:0051085]; mitochondrial unfolded protein response [GO:0034514]; positive regulation of interferon-alpha production [GO:0032727]; positive regulation of interleukin-6 production [GO:0032755]; positive regulation of T cell activation [GO:0050870]; positive regulation of type II interferon production [GO:0032729]; protein import into mitochondrial intermembrane space [GO:0045041]; protein refolding [GO:0042026]; response to heat [GO:0009408]
|
GroEL-GroES complex [GO:1990220]
|
ATP binding [GO:0005524]; ATP-dependent protein folding chaperone [GO:0140662]; isomerase activity [GO:0016853]; protein-folding chaperone binding [GO:0051087]; unfolded protein binding [GO:0051082]
|
PF00118;
|
3.50.7.10;1.10.560.10;3.30.260.10;
|
Chaperonin (HSP60) family
| null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00600}.
|
CATALYTIC ACTIVITY: Reaction=ATP + H2O + a folded polypeptide = ADP + phosphate + an unfolded polypeptide.; EC=5.6.1.7; Evidence={ECO:0000255|HAMAP-Rule:MF_00600};
| null | null | null | null |
FUNCTION: Together with its co-chaperonin GroES, plays an essential role in assisting protein folding. The GroEL-GroES system forms a nano-cage that allows encapsulation of the non-native substrate proteins and provides a physical environment optimized to promote and accelerate protein folding. {ECO:0000255|HAMAP-Rule:MF_00600}.
|
Enterobacter agglomerans (Erwinia herbicola) (Pantoea agglomerans)
|
O66465
|
MRAY_AQUAE
|
MLYQLALLLKDYWFAFNVLKYITFRSFTAVLIAFFLTLVLSPSFINRLRKIQRLFGGYVREYTPESHEVKKYTPTMGGIVILIVVTLSTLLLMRWDIKYTWVVLLSFLSFGTIGFWDDYVKLKNKKGISIKTKFLLQVLSASLISVLIYYWADIDTILYFPFFKELYVDLGVLYLPFAVFVIVGSANAVNLTDGLDGLAIGPAMTTATALGVVAYAVGHSKIAQYLNIPYVPYAGELTVFCFALVGAGLGFLWFNSFPAQMFMGDVGSLSIGASLATVALLTKSEFIFAVAAGVFVFETISVILQIIYFRWTGGKRLFKRAPFHHHLELNGLPEPKIVVRMWIISILLAIIAISMLKLR
|
2.7.8.13
|
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255|HAMAP-Rule:MF_00038, ECO:0000269|PubMed:23990562, ECO:0000269|PubMed:27088606, ECO:0000269|PubMed:29459785}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000269|PubMed:23990562};
|
cell cycle [GO:0007049]; cell division [GO:0051301]; cell wall macromolecule biosynthetic process [GO:0044038]; cell wall organization [GO:0071555]; peptidoglycan biosynthetic process [GO:0009252]; regulation of cell shape [GO:0008360]
|
plasma membrane [GO:0005886]
|
identical protein binding [GO:0042802]; metal ion binding [GO:0046872]; phospho-N-acetylmuramoyl-pentapeptide-transferase activity [GO:0008963]; phosphotransferase activity, for other substituted phosphate groups [GO:0016780]; UDP-N-acetylmuramoyl-L-alanyl-D-glutamyl-meso-2,6-diaminopimelyl-D-alanyl-D-alanine:undecaprenyl-phosphate transferase activity [GO:0051992]
|
PF00953;PF10555;
| null |
Glycosyltransferase 4 family, MraY subfamily
| null |
SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-Rule:MF_00038}; Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_00038}.
|
CATALYTIC ACTIVITY: Reaction=di-trans,octa-cis-undecaprenyl phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-gamma-D-glutamyl-meso-2,6-diaminopimeloyl-D-alanyl-D-alanine = di-trans-octa-cis-undecaprenyl diphospho-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamyl-meso-2,6-diaminopimeloyl-D-alanyl-D-alanine + UMP; Xref=Rhea:RHEA:28386, ChEBI:CHEBI:57865, ChEBI:CHEBI:60392, ChEBI:CHEBI:61386, ChEBI:CHEBI:61387; EC=2.7.8.13; Evidence={ECO:0000255|HAMAP-Rule:MF_00038, ECO:0000269|PubMed:23990562, ECO:0000269|PubMed:27088606, ECO:0000269|PubMed:29459785};
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=190 uM for UDP-MurNAc-pentapeptide {ECO:0000269|PubMed:27088606};
|
PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis. {ECO:0000255|HAMAP-Rule:MF_00038}.
| null | null |
FUNCTION: Catalyzes the initial step of the lipid cycle reactions in the biosynthesis of the cell wall peptidoglycan: transfers peptidoglycan precursor phospho-MurNAc-pentapeptide from UDP-MurNAc-pentapeptide onto the lipid carrier undecaprenyl phosphate, yielding undecaprenyl-pyrophosphoryl-MurNAc-pentapeptide, known as lipid I. {ECO:0000255|HAMAP-Rule:MF_00038, ECO:0000269|PubMed:23990562, ECO:0000269|PubMed:27088606, ECO:0000269|PubMed:29459785}.
|
Aquifex aeolicus (strain VF5)
|
O66490
|
KAD_AQUAE
|
MILVFLGPPGAGKGTQAKRLAKEKGFVHISTGDILREAVQKGTPLGKKAKEYMERGELVPDDLIIALIEEVFPKHGNVIFDGFPRTVKQAEALDEMLEKKGLKVDHVLLFEVPDEVVIERLSGRRINPETGEVYHVKYNPPPPGVKVIQREDDKPEVIKKRLEVYREQTAPLIEYYKKKGILRIIDASKPVEEVYRQVLEVIGDGN
|
2.7.4.3
| null |
AMP salvage [GO:0044209]; CDP biosynthetic process [GO:0046705]; nucleoside diphosphate metabolic process [GO:0009132]; nucleoside monophosphate metabolic process [GO:0009123]; phosphorylation [GO:0016310]; UDP biosynthetic process [GO:0006225]
|
cytoplasm [GO:0005737]; cytosol [GO:0005829]; intracellular membrane-bounded organelle [GO:0043231]
|
adenylate kinase activity [GO:0004017]; ATP binding [GO:0005524]; cytidylate kinase activity [GO:0004127]; nucleoside diphosphate kinase activity [GO:0004550]; UMP kinase activity [GO:0033862]
|
PF00406;
|
3.40.50.300;
|
Adenylate kinase family
| null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00235}.
|
CATALYTIC ACTIVITY: Reaction=AMP + ATP = 2 ADP; Xref=Rhea:RHEA:12973, ChEBI:CHEBI:30616, ChEBI:CHEBI:456215, ChEBI:CHEBI:456216; EC=2.7.4.3; Evidence={ECO:0000255|HAMAP-Rule:MF_00235};
| null |
PATHWAY: Purine metabolism; AMP biosynthesis via salvage pathway; AMP from ADP: step 1/1. {ECO:0000255|HAMAP-Rule:MF_00235}.
| null | null |
FUNCTION: Catalyzes the reversible transfer of the terminal phosphate group between ATP and AMP. Plays an important role in cellular energy homeostasis and in adenine nucleotide metabolism. {ECO:0000255|HAMAP-Rule:MF_00235}.
|
Aquifex aeolicus (strain VF5)
|
O66663
|
KDTA_AQUAE
|
MQFEVLKRFFPKESLKNCKGALWVHTASIGEFNTFLPILKELKREHRILLTYFSPRAREYLKTKSDFYDCLHPLPLDNPFSVKRFEELSKPKALIVVEREFWPSLIIFTKVPKILVNAYAKGSLIEKILSKKFDLIIMRTQEDVEKFKTFGAKRVFSCGNLKFICQKGKGIKLKGEFIVAGSIHTGEVEIILKAFKEIKKTYSSLKLILVPRHIENAKIFEKKARDFGFKTSFFENLEGDVILVDRFGILKELYPVGKIAIVGGTFVNIGGHNLLEPTCWGIPVIYGPYTHKVNDLKEFLEKEGAGFEVKNETELVTKLTELLSVKKEIKVEEKSREIKGCYLEKLREFLRGL
|
2.4.99.12
| null |
lipid A biosynthetic process [GO:0009245]; lipopolysaccharide core region biosynthetic process [GO:0009244]
|
plasma membrane [GO:0005886]
|
Kdo transferase activity [GO:0043842]; transferase activity [GO:0016740]
|
PF04413;
|
3.40.50.11720;3.40.50.2000;
|
Glycosyltransferase group 1 family, Glycosyltransferase 30 subfamily
| null |
SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000305|PubMed:22474366}; Peripheral membrane protein {ECO:0000305|PubMed:22474366}; Cytoplasmic side {ECO:0000305|PubMed:22474366}.
|
CATALYTIC ACTIVITY: Reaction=CMP-3-deoxy-beta-D-manno-octulosonate + lipid IVA (E. coli) = alpha-Kdo-(2->6)-lipid IVA (E. coli) + CMP + H(+); Xref=Rhea:RHEA:28066, ChEBI:CHEBI:15378, ChEBI:CHEBI:58603, ChEBI:CHEBI:60364, ChEBI:CHEBI:60377, ChEBI:CHEBI:85987; EC=2.4.99.12; Evidence={ECO:0000269|PubMed:19546212, ECO:0000269|PubMed:22474366};
| null |
PATHWAY: Bacterial outer membrane biogenesis; LPS core biosynthesis.
| null |
BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Highly thermostable. Does not lose activity after 16 hours at 70 or 80 degrees Celsius, but incubation of the enzyme at 90 and 99 degrees Celsius for 1 hour results in gradual loss of activity. {ECO:0000269|PubMed:19546212};
|
FUNCTION: Involved in lipopolysaccharide (LPS) biosynthesis. Catalyzes the transfer of a single 3-deoxy-D-manno-octulosonate (Kdo) residue from CMP-Kdo to lipid IV(A), the tetraacyldisaccharide-1,4'-bisphosphate precursor of lipid A. Is strictly monofunctional, i.e. is capable of adding only a single Kdo residue to the acceptor lipid. {ECO:0000269|PubMed:19546212}.
|
Aquifex aeolicus (strain VF5)
|
O66990
|
PYRC_AQUAE
|
MLKLIVKNGYVIDPSQNLEGEFDILVENGKIKKIDKNILVPEAEIIDAKGLIVCPGFIDIHVHLRDPGQTYKEDIESGSRCAVAGGFTTIVCMPNTNPPIDNTTVVNYILQKSKSVGLCRVLPTGTITKGRKGKEIADFYSLKEAGCVAFTDDGSPVMDSSVMRKALELASQLGVPIMDHCEDDKLAYGVINEGEVSALLGLSSRAPEAEEIQIARDGILAQRTGGHVHIQHVSTKLSLEIIEFFKEKGVKITCEVNPNHLLFTEREVLNSGANARVNPPLRKKEDRLALIEGVKRGIIDCFATDHAPHQTFEKELVEFAMPGIIGLQTALPSALELYRKGIISLKKLIEMFTINPARIIGVDLGTLKLGSPADITIFDPNKEWILNEETNLSKSRNTPLWGKVLKGKVIYTIKDGKMVYKD
|
3.5.2.3
|
COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000255|HAMAP-Rule:MF_00220, ECO:0000269|PubMed:15381710, ECO:0000269|PubMed:15826652, ECO:0000269|PubMed:19128030, ECO:0000269|PubMed:24314009}; Note=Binds 1 Zn(2+) ion per subunit (PubMed:15381710, PubMed:15826652, PubMed:19128030, PubMed:24314009). Fully functional with a mononuclear metal center. Does not require a second metal for activity, although the conservation of the second metal-binding site during evolution leaves open the possibility that a second ion might bind in vivo (PubMed:24314009). {ECO:0000269|PubMed:15381710, ECO:0000269|PubMed:15826652, ECO:0000269|PubMed:19128030, ECO:0000269|PubMed:24314009};
|
'de novo' UMP biosynthetic process [GO:0044205]; purine nucleobase catabolic process [GO:0006145]
|
cytoplasm [GO:0005737]
|
allantoinase activity [GO:0004038]; dihydroorotase activity [GO:0004151]; zinc ion binding [GO:0008270]
|
PF01979;
|
3.20.20.140;2.30.40.10;
|
Metallo-dependent hydrolases superfamily, DHOase family, Class I DHOase subfamily
| null | null |
CATALYTIC ACTIVITY: Reaction=(S)-dihydroorotate + H2O = H(+) + N-carbamoyl-L-aspartate; Xref=Rhea:RHEA:24296, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30864, ChEBI:CHEBI:32814; EC=3.5.2.3; Evidence={ECO:0000255|HAMAP-Rule:MF_00220, ECO:0000269|PubMed:15381710, ECO:0000269|PubMed:24314009};
| null |
PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo pathway; (S)-dihydroorotate from bicarbonate: step 3/3. {ECO:0000255|HAMAP-Rule:MF_00220, ECO:0000305}.
| null | null |
FUNCTION: Catalyzes the reversible cyclization of carbamoyl aspartate to dihydroorotate. {ECO:0000255|HAMAP-Rule:MF_00220, ECO:0000269|PubMed:15381710, ECO:0000269|PubMed:24314009}.
|
Aquifex aeolicus (strain VF5)
|
O67049
|
AROE_AQUAE
|
MINAQTQLYGVIGFPVKHSLSPVFQNALIRYAGLNAVYLAFEINPEELKKAFEGFKALKVKGINVTVPFKEEIIPLLDYVEDTAKEIGAVNTVKFENGKAYGYNTDWIGFLKSLKSLIPEVKEKSILVLGAGGASRAVIYALVKEGAKVFLWNRTKEKAIKLAQKFPLEVVNSPEEVIDKVQVIVNTTSVGLKDKDPEIFNYDLIKKDHVVVDIIYKETKLLKKAKEKGAKLFDGLPMLLWQGIEAFKIWNGCEVPYSVAERSVRDLRG
|
1.1.1.25
| null |
amino acid biosynthetic process [GO:0008652]; aromatic amino acid family biosynthetic process [GO:0009073]; chorismate biosynthetic process [GO:0009423]; shikimate metabolic process [GO:0019632]
|
cytosol [GO:0005829]
|
NADP binding [GO:0050661]; shikimate 3-dehydrogenase (NADP+) activity [GO:0004764]
|
PF18317;PF01488;PF08501;
|
3.40.50.10860;3.40.50.720;
|
Shikimate dehydrogenase family
| null | null |
CATALYTIC ACTIVITY: Reaction=NADP(+) + shikimate = 3-dehydroshikimate + H(+) + NADPH; Xref=Rhea:RHEA:17737, ChEBI:CHEBI:15378, ChEBI:CHEBI:16630, ChEBI:CHEBI:36208, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.1.1.25; Evidence={ECO:0000255|HAMAP-Rule:MF_00222, ECO:0000269|PubMed:17649975};
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=42.4 uM for shikimate (at pH 9 and 25 degrees Celsius) {ECO:0000269|PubMed:17649975}; KM=42.4 uM for NADP (at pH 9 and 25 degrees Celsius) {ECO:0000269|PubMed:17649975}; Note=kcat is 55.5 sec(-1) for dehydrogenase activity (at pH 9 and 25 degrees Celsius). {ECO:0000269|PubMed:17649975};
|
PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 4/7. {ECO:0000255|HAMAP-Rule:MF_00222}.
| null | null |
FUNCTION: Involved in the biosynthesis of the chorismate, which leads to the biosynthesis of aromatic amino acids. Catalyzes the reversible NADPH linked reduction of 3-dehydroshikimate (DHSA) to yield shikimate (SA). {ECO:0000255|HAMAP-Rule:MF_00222, ECO:0000269|PubMed:17649975}.
|
Aquifex aeolicus (strain VF5)
|
O67082
|
RNC_AQUAE
|
MKMLEQLEKKLGYTFKDKSLLEKALTHVSYSKKEHYETLEFLGDALVNFFIVDLLVQYSPNKREGFLSPLKAYLISEEFFNLLAQKLELHKFIRIKRGKINETIIGDVFEALWAAVYIDSGRDANFTRELFYKLFKEDILSAIKEGRVKKDYKTILQEITQKRWKERPEYRLISVEGPHHKKKFIVEAKIKEYRTLGEGKSKKEAEQRAAEELIKLLEESE
|
3.1.26.3
|
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:11738048, ECO:0000269|PubMed:15016361, ECO:0000269|PubMed:16439209, ECO:0000269|PubMed:18047582, ECO:0000269|PubMed:21138964}; Note=Binds 2 Mg(2+) per subunit. Mn(2+) also supports catalytic activity. {ECO:0000269|PubMed:11738048, ECO:0000269|PubMed:15016361, ECO:0000269|PubMed:16439209, ECO:0000269|PubMed:18047582, ECO:0000269|PubMed:21138964};
|
mRNA processing [GO:0006397]; pre-miRNA processing [GO:0031054]; regulation of gene expression [GO:0010468]; RNA processing [GO:0006396]; rRNA processing [GO:0006364]; siRNA processing [GO:0030422]; tRNA processing [GO:0008033]
|
cytoplasm [GO:0005737]; RISC complex [GO:0016442]
|
deoxyribonuclease I activity [GO:0004530]; double-stranded RNA binding [GO:0003725]; identical protein binding [GO:0042802]; metal ion binding [GO:0046872]; ribonuclease III activity [GO:0004525]
|
PF00035;PF14622;
|
3.30.160.20;1.10.1520.10;
|
Ribonuclease III family
| null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
|
CATALYTIC ACTIVITY: Reaction=Endonucleolytic cleavage to 5'-phosphomonoester.; EC=3.1.26.3;
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=98 nM for 16S-u-hp RNA {ECO:0000269|PubMed:21138964};
| null |
BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8-9. {ECO:0000269|PubMed:21138964};
|
BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 70-85 degrees Celsius. {ECO:0000269|PubMed:21138964};
|
FUNCTION: Digests double-stranded RNA. Involved in the processing of primary rRNA transcript to yield the immediate precursors to the large and small rRNAs (23S and 16S). Also processes some mRNAs, and tRNAs when they are encoded in the rRNA operon. Probably processes pre-crRNA and tracrRNA of type II CRISPR loci if present in the organism. {ECO:0000269|PubMed:16439209, ECO:0000269|PubMed:21138964}.
|
Aquifex aeolicus (strain VF5)
|
O67233
|
CARB2_AQUAE
|
MSKKVVILGSGPNRIGQGIEFDYACVHAVFSLQEEGYYAVMVNCNPETVSTDYDTADKLYFEPIVFEHVMDIIEREKPEGVILQFGGQTPLKLALPLQKNGVKILGTKPESIDKAEDRELFRELIIELGLKQPPSGTARTKEEALKIAKEIGFPVLVRPSYVLGGRAMRIVYDEEELKEYLEEAVSVSHERPVLIDKFLDNSIELDVDAVSDGKDVLIGAVMEHIEEAGVHSGDSATSIPPYSLSKEIVEEVKEQTRKLAVALEVKGLINVQYAVQNNEVYVLEVNPRASRTVPFVSKSIGYPLAKIATKVAIGKSLREILPEVFERLEKGEAHFASDFLPKEKKIFSVKEVVFPWKRFPEVDPILGPEMKSTGEVMGIDKEFGLAYYKAQLSAGYRLPEKGNLFISVADRDKPKILELAKEFEKLGFGIYATSGTYKFLKEHGVNAKRVLKVSEGRPNVVDMIINGEIHLVINTPSGKREKSDAYYIRRACVQFNVPYYTTMRAGYAVLEAIKSIKKLKEEGKGLSVHSLQEIYNI
|
6.3.4.16; 6.3.5.5
|
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:P00968}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250|UniProtKB:P00968}; Note=Binds 2 Mg(2+) or Mn(2+) ions per subunit. {ECO:0000305};
|
'de novo' pyrimidine nucleobase biosynthetic process [GO:0006207]; 'de novo' UMP biosynthetic process [GO:0044205]; arginine biosynthetic process [GO:0006526]; citrulline biosynthetic process [GO:0019240]; glutamine metabolic process [GO:0006541]; UTP biosynthetic process [GO:0006228]
|
cytosol [GO:0005829]
|
aspartate carbamoyltransferase activity [GO:0004070]; ATP binding [GO:0005524]; carbamoyl-phosphate synthase (ammonia) activity [GO:0004087]; carbamoyl-phosphate synthase (glutamine-hydrolyzing) activity [GO:0004088]; dihydroorotase activity [GO:0004151]; metal ion binding [GO:0046872]
|
PF02786;PF02142;
|
3.40.50.20;3.30.470.20;3.40.50.1380;
|
CarB family
| null | null |
CATALYTIC ACTIVITY: Reaction=2 ATP + H2O + hydrogencarbonate + L-glutamine = 2 ADP + carbamoyl phosphate + 2 H(+) + L-glutamate + phosphate; Xref=Rhea:RHEA:18633, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:29985, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:58228, ChEBI:CHEBI:58359, ChEBI:CHEBI:456216; EC=6.3.5.5; Evidence={ECO:0000250|UniProtKB:P00968}; CATALYTIC ACTIVITY: Reaction=2 ATP + hydrogencarbonate + NH4(+) = 2 ADP + carbamoyl phosphate + 2 H(+) + phosphate; Xref=Rhea:RHEA:18029, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:28938, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:58228, ChEBI:CHEBI:456216; EC=6.3.4.16; Evidence={ECO:0000250|UniProtKB:P00968};
| null |
PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; carbamoyl phosphate from bicarbonate: step 1/1. {ECO:0000250|UniProtKB:P00968}.; PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo pathway; (S)-dihydroorotate from bicarbonate: step 1/3. {ECO:0000250|UniProtKB:P00968}.
| null | null |
FUNCTION: Large subunit of the glutamine-dependent carbamoyl phosphate synthetase (CPSase). CPSase catalyzes the formation of carbamoyl phosphate from the ammonia moiety of glutamine, carbonate, and phosphate donated by ATP, constituting the first step of 2 biosynthetic pathways, one leading to arginine and/or urea and the other to pyrimidine nucleotides. The large subunit (synthetase) binds the substrates ammonia (free or transferred from glutamine from the small subunit), hydrogencarbonate and ATP and carries out an ATP-coupled ligase reaction, activating hydrogencarbonate by forming carboxy phosphate which reacts with ammonia to form carbamoyl phosphate. {ECO:0000250|UniProtKB:P00968}.
|
Aquifex aeolicus (strain VF5)
|
O67496
|
ISPG_AQUAE
|
MIQKRKTRQIRVGNVKIGGDAPIVVQSMTSTKTHDVEATLNQIKRLYEAGCEIVRVAVPHKEDVEALEEIVKKSPMPVIADIHFAPSYAFLSMEKGVHGIRINPGNIGKEEIVREIVEEAKRRGVAVRIGVNSGSLEKDLLEKYGYPSAEALAESALRWSEKFEKWGFTNYKVSIKGSDVLQNVRANLIFAERTDVPLHIGITEAGMGTKGIIKSSVGIGILLYMGIGDTVRVSLTDDPVVEVETAYEILKSLGLRRRGVEIVACPTCGRIEVDLPKVVKEVQEKLSGVKTPLKVAVMGCVVNAIGEAREADIGLACGRGFAWLFKHGKPIKKVDESEMVDELLKEIQNMEKDGGTN
|
1.17.7.3
|
COFACTOR: Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; Evidence={ECO:0000255|HAMAP-Rule:MF_00159, ECO:0000269|PubMed:20932974}; Note=Binds 1 [4Fe-4S] cluster per subunit. {ECO:0000255|HAMAP-Rule:MF_00159, ECO:0000269|PubMed:20932974};
|
isopentenyl diphosphate biosynthetic process, methylerythritol 4-phosphate pathway [GO:0019288]; terpenoid biosynthetic process [GO:0016114]
| null |
4 iron, 4 sulfur cluster binding [GO:0051539]; 4-hydroxy-3-methylbut-2-en-1-yl diphosphate synthase activity [GO:0046429]; iron ion binding [GO:0005506]
|
PF04551;
|
3.20.20.20;3.30.413.10;
|
IspG family
| null | null |
CATALYTIC ACTIVITY: Reaction=(2E)-4-hydroxy-3-methylbut-2-enyl diphosphate + 2 H(+) + H2O + oxidized [flavodoxin] = 2-C-methyl-D-erythritol 2,4-cyclic diphosphate + reduced [flavodoxin]; Xref=Rhea:RHEA:43604, Rhea:RHEA-COMP:10622, Rhea:RHEA-COMP:10623, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:58483, ChEBI:CHEBI:128753; EC=1.17.7.3; Evidence={ECO:0000255|HAMAP-Rule:MF_00159};
| null |
PATHWAY: Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis via DXP pathway; isopentenyl diphosphate from 1-deoxy-D-xylulose 5-phosphate: step 5/6. {ECO:0000255|HAMAP-Rule:MF_00159}.
| null | null |
FUNCTION: Converts 2C-methyl-D-erythritol 2,4-cyclodiphosphate (ME-2,4cPP) into 1-hydroxy-2-methyl-2-(E)-butenyl 4-diphosphate. {ECO:0000255|HAMAP-Rule:MF_00159, ECO:0000269|PubMed:20932974}.
|
Aquifex aeolicus (strain VF5)
|
O67648
|
LPXC_AQUAE
|
MGLEKTVKEKLSFEGVGIHTGEYSKLIIHPEKEGTGIRFFKNGVYIPARHEFVVHTNHSTDLGFKGQRIKTVEHILSVLHLLEITNVTIEVIGNEIPILDGSGWEFYEAIRKNILNQNREIDYFVVEEPIIVEDEGRLIKAEPSDTLEVTYEGEFKNFLGRQKFTFVEGNEEEIVLARTFCFDWEIEHIKKVGLGKGGSLKNTLVLGKDKVYNPEGLRYENEPVRHKVFDLIGDLYLLGSPVKGKFYSFRGGHSLNVKLVKELAKKQKLTRDLPHLPSVQAL
|
3.5.1.108
|
COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000255|HAMAP-Rule:MF_00388, ECO:0000269|PubMed:11148046};
|
lipid A biosynthetic process [GO:0009245]
| null |
metal ion binding [GO:0046872]; UDP-3-O-[3-hydroxymyristoyl] N-acetylglucosamine deacetylase activity [GO:0008759]; UDP-3-O-acyl-N-acetylglucosamine deacetylase activity [GO:0103117]
|
PF03331;
|
3.30.230.20;3.30.1700.10;
|
LpxC family
| null | null |
CATALYTIC ACTIVITY: Reaction=a UDP-3-O-[(3R)-3-hydroxyacyl]-N-acetyl-alpha-D-glucosamine + H2O = a UDP-3-O-[(3R)-3-hydroxyacyl]-alpha-D-glucosamine + acetate; Xref=Rhea:RHEA:67816, ChEBI:CHEBI:15377, ChEBI:CHEBI:30089, ChEBI:CHEBI:137740, ChEBI:CHEBI:173225; EC=3.5.1.108; Evidence={ECO:0000255|HAMAP-Rule:MF_00388, ECO:0000269|PubMed:11148046, ECO:0000269|PubMed:15705580};
| null |
PATHWAY: Glycolipid biosynthesis; lipid IV(A) biosynthesis; lipid IV(A) from (3R)-3-hydroxytetradecanoyl-[acyl-carrier-protein] and UDP-N-acetyl-alpha-D-glucosamine: step 2/6. {ECO:0000255|HAMAP-Rule:MF_00388}.
| null | null |
FUNCTION: Catalyzes the hydrolysis of UDP-3-O-myristoyl-N-acetylglucosamine to form UDP-3-O-myristoylglucosamine and acetate, the committed step in lipid A biosynthesis. {ECO:0000255|HAMAP-Rule:MF_00388, ECO:0000269|PubMed:11148046}.
|
Aquifex aeolicus (strain VF5)
|
O67869
|
CARB1_AQUAE
|
MPKRTDIKKILIIGSGPIVIGQAAEFDYSGTQACKALKQEGYEVILVNSNPATIMTDPEMADKTYIEPLTADILEEIIKKERPDALLPTLGGQTGLNLAVELYENGVLERYGVELIGANYEAIKKGEDRELFKETMESIGLKVPESAVVRSVEEGLKAVEKIGFPVILRPAFTLGGTGSSVAYNVEEFKEKLKVALETSPIHEVLLDKSLIGWKEIEFEVVRDKADNVIIVCAIENFDPMGVHTGDSITVAPTQTLTDKEYQMLRDAAIAVIRAIGVDTGGSNIQFALSPESGDFYVIEMNPRVSRSSALASKATGFPIAKVAAKLAVGYTLDELKNDITKFTPASFEPSIDYVVVKIPRFDFAKFPEADRTLTTMMKSVGEVMAIGRTFKEALLKAVRSLELDRYGLAFPKLTNVDKVELERNLINPNDQRLWYIAEAFRRGYSVDEVYELTKIDRWFLYNIEEIVKFEEVLRKEELTPEILRQAKEMGYSDWEIAKIKGITEEEVRKLRKEEGIVPTFKGVDTCAGEFVAYTPYYYSSYERPYYTVDGQEILDED
|
6.3.4.16; 6.3.5.5
|
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:P00968}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250|UniProtKB:P00968}; Note=Binds 2 Mg(2+) or Mn(2+) ions per subunit. {ECO:0000305};
|
'de novo' pyrimidine nucleobase biosynthetic process [GO:0006207]; 'de novo' UMP biosynthetic process [GO:0044205]; arginine biosynthetic process [GO:0006526]; citrulline biosynthetic process [GO:0019240]; glutamine metabolic process [GO:0006541]; UTP biosynthetic process [GO:0006228]
|
cytosol [GO:0005829]
|
aspartate carbamoyltransferase activity [GO:0004070]; ATP binding [GO:0005524]; carbamoyl-phosphate synthase (ammonia) activity [GO:0004087]; carbamoyl-phosphate synthase (glutamine-hydrolyzing) activity [GO:0004088]; dihydroorotase activity [GO:0004151]; metal ion binding [GO:0046872]
|
PF02786;PF02787;
|
3.40.50.20;3.30.470.20;1.10.1030.10;
|
CarB family
| null | null |
CATALYTIC ACTIVITY: Reaction=2 ATP + H2O + hydrogencarbonate + L-glutamine = 2 ADP + carbamoyl phosphate + 2 H(+) + L-glutamate + phosphate; Xref=Rhea:RHEA:18633, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:29985, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:58228, ChEBI:CHEBI:58359, ChEBI:CHEBI:456216; EC=6.3.5.5; Evidence={ECO:0000250|UniProtKB:P00968}; CATALYTIC ACTIVITY: Reaction=2 ATP + hydrogencarbonate + NH4(+) = 2 ADP + carbamoyl phosphate + 2 H(+) + phosphate; Xref=Rhea:RHEA:18029, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:28938, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:58228, ChEBI:CHEBI:456216; EC=6.3.4.16; Evidence={ECO:0000250|UniProtKB:P00968};
| null |
PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; carbamoyl phosphate from bicarbonate: step 1/1. {ECO:0000250|UniProtKB:P00968}.; PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo pathway; (S)-dihydroorotate from bicarbonate: step 1/3. {ECO:0000250|UniProtKB:P00968}.
| null | null |
FUNCTION: Large subunit of the glutamine-dependent carbamoyl phosphate synthetase (CPSase). CPSase catalyzes the formation of carbamoyl phosphate from the ammonia moiety of glutamine, carbonate, and phosphate donated by ATP, constituting the first step of 2 biosynthetic pathways, one leading to arginine and/or urea and the other to pyrimidine nucleotides. The large subunit (synthetase) binds the substrates ammonia (free or transferred from glutamine from the small subunit), hydrogencarbonate and ATP and carries out an ATP-coupled ligase reaction, activating hydrogencarbonate by forming carboxy phosphate which reacts with ammonia to form carbamoyl phosphate. {ECO:0000250|UniProtKB:P00968}.
|
Aquifex aeolicus (strain VF5)
|
O67911
|
CATNT_AQUAE
|
MENIEIVSSGKHTLHGLNFYLSYFDDVAKVLPREHYCFIVGGWVRDRILGEPVGYNIDVDFLTTADPVELAKNFAKRIGGHFFVFEKRGFLIKRPTIASVVLHLPPYRYRFDFSPLKGKDLEKALIEDLKERDFTANAIAVNLDDVLSIGAKQTIVYDPTGGIKDLEQGLLRPVSIENLKRDPVRVLRGFRIAIEKNLQLTEDFYEFVKEDPRIVLKSAVERITHELFKIMKEKTAHKVIRELYEYGVLEAIIPEIGRLREVKDQGEHHIYPLDEHTLKTLEYLEQVIEDRAKYLSAELLENFGKKRVLGEFTDVELLKWGALFHDIGKPQTFAVREGKVTFYEHDKVGAQIVREIGERLRWGDEATEFVAKLVRHHLRPFFLREAFKKGELKRRGMANFWRECGDIAPHLFLLSIADAMASGDEEEDIKALMETIAELESFNRNEMKEEIQKPLLNGDEIMEILGIKPGKIVGILKKALLEAQIDGKVETKEEAIEFIKRSTKNLKPLDEG
|
2.7.7.-
|
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:24389024};
|
RNA 3'-end processing [GO:0031123]; tRNA processing [GO:0008033]
| null |
CTP:tRNA cytidylyltransferase activity [GO:0052927]; metal ion binding [GO:0046872]; nucleotide binding [GO:0000166]; tRNA binding [GO:0000049]
|
PF01966;PF01743;PF12627;
|
1.10.246.80;3.30.460.10;1.10.3090.10;
|
TRNA nucleotidyltransferase/poly(A) polymerase family
| null | null |
CATALYTIC ACTIVITY: Reaction=a tRNA precursor + 2 CTP = a tRNA with a 3' CC end + 2 diphosphate; Xref=Rhea:RHEA:60008, Rhea:RHEA-COMP:10465, Rhea:RHEA-COMP:15488, ChEBI:CHEBI:33019, ChEBI:CHEBI:37563, ChEBI:CHEBI:74896, ChEBI:CHEBI:83069; Evidence={ECO:0000269|PubMed:11701927, ECO:0000269|PubMed:24389024}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60009; Evidence={ECO:0000269|PubMed:11701927, ECO:0000269|PubMed:24389024};
| null | null | null | null |
FUNCTION: tRNA nucleotidyltransferase involved in the synthesis of the tRNA CCA terminus. Adds the two cytidine residues to tRNA. {ECO:0000269|PubMed:11701927, ECO:0000269|PubMed:24389024}.
|
Aquifex aeolicus (strain VF5)
|
O67931
|
SQRD_AQUAE
|
MAKHVVVIGGGVGGIATAYNLRNLMPDLKITLISDRPYFGFTPAFPHLAMGWRKFEDISVPLAPLLPKFNIEFINEKAESIDPDANTVTTQSGKKIEYDYLVIATGPKLVFGAEGQEENSTSICTAEHALETQKKLQELYANPGPVVIGAIPGVSCFGPAYEFALMLHYELKKRGIRYKVPMTFITSEPYLGHFGVGGIGASKRLVEDLFAERNIDWIANVAVKAIEPDKVIYEDLNGNTHEVPAKFTMFMPSFQGPEVVASAGDKVANPANKMVIVNRCFQNPTYKNIFGVGVVTAIPPIEKTPIPTGVPKTGMMIEQMAMAVAHNIVNDIRNNPDKYAPRLSAICIADFGEDAGFFFADPVIPPRERVITKMGKWAHYFKTAFEKYFLWKVRNGNIAPSFEEKVLEIFLKVHPIELCKDCEGAPGSRC
|
1.8.5.4
|
COFACTOR: Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000269|PubMed:19487671}; Note=Binds 1 FAD per subunit. {ECO:0000269|PubMed:19487671};
|
aerobic electron transport chain [GO:0019646]
|
membrane [GO:0016020]
|
identical protein binding [GO:0042802]; NAD(P)H dehydrogenase (quinone) activity [GO:0003955]; nucleotide binding [GO:0000166]; quinone binding [GO:0048038]; sulfide:quinone oxidoreductase activity [GO:0070224]
|
PF07992;
|
3.50.50.100;
|
SQRD family
| null |
SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:10816041, ECO:0000269|PubMed:19487671}; Peripheral membrane protein {ECO:0000269|PubMed:10816041, ECO:0000269|PubMed:19487671}.
|
CATALYTIC ACTIVITY: Reaction=n a quinone + n H(+) + n hydrogen sulfide = n a quinol + n sulfur; Xref=Rhea:RHEA:30239, ChEBI:CHEBI:15378, ChEBI:CHEBI:24646, ChEBI:CHEBI:26833, ChEBI:CHEBI:29919, ChEBI:CHEBI:132124; EC=1.8.5.4; Evidence={ECO:0000303|PubMed:10816041, ECO:0000303|PubMed:19487671};
| null | null | null | null |
FUNCTION: Catalyzes the oxidation of hydrogen sulfide, with the help of a quinone. Consecutive reaction cycles lead to the accumulation of a polysulfide product on the active site Cys residues; these products are released when they exceed a critical length, typically as cyclooctasulfur. {ECO:0000303|PubMed:10816041, ECO:0000303|PubMed:19487671}.
|
Aquifex aeolicus (strain VF5)
|
O68008
|
BACC_BACLI
|
MKTKVEKIYPLSNMQKGMLFHAMKDEASHAYFEQFIIELKGDVDERMFEESLNEVMKRHEILRASFHHRLDEPLHVIIKDRHMKFDYLDIRGRHDQDGVLERYLAEDRQKGFDLAKDTLMRACLIRMSDDSYQFVWTYHHILLDGWCLGIILDELLTIYEMKRKGQNHQLEDPRPYSDYIKWLEDQDKEEAQSYWESYLSGYDQKNSLPKLRTPSETGFKRREKTIECSKELTNRLIKLANRNHVTINTVLQSIWGVILAKYNNSEDVVFGTVVSGRDAEVEGIETMVGVFINTIPTRIRLDKDKLFKDVLRQTQADALESSRYNYMNLAEVQALSELKNDLIDHVMVFENYAVDQKAFEEKNDVGFEMVNVSGEEQTNYHFSISAALDDQLKLLFIYDENVYDTTIIETLEKHIITVAEQVAEDETQTLRDINLVSKEEQHRILDTFNDTKTGYPKDKPLHELFEEQAMKTPDHTALVFGAQRMTYRELNEKANQTARLLREKGIGRGSIAAIIADRSFEMIIGIIGILKAGGAYLPIDPETPKHRIAFMLSDTKAGVLLAQGKAADGIDCEADIIHLDKGVADGFSKKRLSSVNDSGDTAYIIYTSGSTGMPKGVVTPHYSAARVVKNTNYIDITEDDAILQLSNYSFDGSVFDIFGALLNGASLVLIEKETVLNTHELAEVIKKEQVSVMFITTALFNTLADINIGCLAKLRKIFLGGERASIPHVRKVLNHVGRDKLIHVYGPTESTVYATYYFINEIDDEAETIPIGSPLANTSVLIMDEAGKLLPIGVPGELCIAGDGLSKGYLNREELTAEKFIPHPFIPGERLYKTGDLAKWLPDGNIEFIGRIDHQVKIRGFRIELGEIESRLEMHEDINETIVTVREDEESRPYICAYITANREISLDELKGFLGEKLPEYMIPAYFVKMDKLPLTKNGKVDRKALPEPDRTAGAENEYEAPRNETEEKLAAIWRDILKVEKSGINDHFFEMGGHSLKAAAMAARIRKELKAEIPLGQIFKTPTIKGLGEYIRSTKDSVYSSIQKVEEKEYYRLSSAQKRLYILDQIEGSGLSYNIPFTMKVKGRFDIRRFENALKTIIQRHEALRTSFLMADGEPVQKIEKEVDFSIKCSKIQSLSIQEIIKQFVRPFDLKKAPLFRTEVVKVDDEEHIILFDMHHIISDGASMGVLTKEICDLYGGKELKPLSLQYKDYSEWQRDFYQKDEMKRQKEYWLNIFKGEIPVLNMPTDYPRPQMHSVEGDRIGFAIDGELTKKLKRIAKDNGATMYMLLLAAYTVLLRTYSGQEDVIIGTPIQGRKHHELKHVIGMFVNTLAMRNHPKGDKTFAEYLQDVKETALKAYENQDYQFDDLVEQLDLERDMSRNPLFDTMFVLQNLEKADAEIEGLTFEPFESDIHISKFDLTLSAIEKDSKIEFDLEYCTKLFKRETVERMAAHFVRVLEDISKRTDKRLDQIEAMSEDEKNTLLYRFNDTKTDAPTDKTICQLFAERAETSPDKTAVVFEDQTLTYRQLHERSNQLARFLREKGVQPDTAVGIMVDRSPEMIIGLLGILKAGGAYLPLDPAYPEDRIKYILGDSQTKFLLSEEALIKKRAFIKEADMINIDIHDKQIAAQDAAQLEPVSRSGDLAYIIYTSGSTGKPKGVLIEQKGLSNLVSAVVKLMHLNTGSRVIQFASLSFDASAFEIFPALAAGSALVLGRQEEMMPGQPLTSFLRQYNITHATLPPTVLDVLNESGLENLKVIVSAGSACSEELAKRWSGNRLFINAYGPTETTVCATAGIYEGSGRPHIGSPIANTNVYVLDQNQKPVPTGVVGELCVGGMSLARGYLNRPELTAEKFISHPFASGERLYRTGDLARWLPDGHLEFLGRIDHQVKIRGYRIELGEIENQLLKLDKIDEAAVIARKDDDHSDYLCAYIVSKEDWTSTEISEWLEKELPHYMIPAYFVRLDKLPLTSNDKVDRKALPAPDRHVATGAVYEAPRNDTEAKLVDIWRDVLGAGDIGISHHFFAAGGDSIKALQIVSRLSRLGLKLEMKDLFANPRIKDLAKYVKKQSQRKNANTIVTGHAELTPIQKWYFANNKEELDHFNQSFVLFRKGGFDESCVKKAFNKIMEQHDALRMIYEEKGGDFIQYNRSFREDLFDLDVYDVRGLDRQAEKVYELATSIQKLSSIRKGKLVHLGIFRADEGDHLLIVIHHLVVDGVSWRILFEDFETLYSQALKGQTLEIGYKTDSYQEFARRLKAYAHSRTLSKEAEYWRNIAKARVRFIPPKNVLKEDVYENSTTLSIKLGKEATADLLRNTNRAYNTEINDILLTALLTGARDITGENKLKVMMEGHGREDILEGVDITRTIGWFTTMYPVLLDAGEEKALSQQIKMVKETLRKIPNKGIGYGLLKYMAEDPDFTNEEKARISFNYLGDIDADMNRGEFSGSSFSEGESIGGKIARSHSIEINAIVMNHELVIHTTFNQMEYEKDTISRLNHQLKERLEQIIKHCTQQTESERTPSDYGDTNISLAELEEIKGKYRSAIEKIYPLANMQKGMLFHAIEDHTSDAYFQQTVMDIEGYVDPAILEASFNDIMKRHEILRASYEYEIVEEPRQIIIENRSIDFTYFNIAKSSAQQQEMFIERLLNEDRKKGFDLSKDVLMRAYLLKTAERSYRLVWSHHHILLDGWCLGIIMRELFVIYENRMNGKASPLKETKPYSDYIKWLERQDQEEARQYWREYLKGYEEQAQLPTLTKRKKSSRYDRREKVIHLSKQLTKQLKELAAKNSVTLHTVIQTIWGLMLTRYTKIDDVVFGTVVSGREANVDGIEDMIGLFINTIPTRIRFNEQARFNDCLQKVQEDAIQSNRYNYMNLAEVQALSSLKKDLIDHILVFENYEADEQDFEESQMKTGFKVNEISAAEQSITAFSMSVTPGEELTLVLTYDGNVYDRDIINNIEGHIKRVAEQVTANENRKIAEIDMLAEEERKTLLYEFNRTNADYPRNKTIHQLFEEQAERTPGHTAVVFEKEELSYKALNERSNQLAGLLREKGVKPDMIVGVMAERSVEMIVGMLAVLKAGGAYLPIDPEYPEDRIRYMIEDSGISILLKKADKQIDVDFTCIDMNEKGLAKDMAAENLGHTSGSSDMAYVIYTSGSTGKPKGVMVNHQSIVNTLYWRKQSYGYSTADATLQVPSFSFDSSVEDIFTTLISGAKLVLIRDLRMNPREIIGVLRTHKATNLLAVPSFYLNLLDTIEQPLDDLRFVTVAGEGFNESLIRQHFEKLPNVKLFNEYGPTENSVCSTRGELRKDDEKVVIGRPISNHKVYILNHNQQLLPLGTPGELCLSGEGLARGYLNRPDLTLEKFVPNPFAPGESMYRTGDLARFLPDGQIEYLGRIDHQVKIRGFRIELGEIENQLLKIEGIDAAAVMAREDQAGGKYLCAYIVADKAAGVADVRKCLLKELPDYMVPSYFVKLDQLPLTANGKIDRKALPEPSSTISEATYEAPRNRTEEKLVSIWEDVLGIENIGISHNFFELGGHSLKAAALTAKLHKEMKIEVPLRQLFETPTIKDIGDFIESMKESPYASITQAEEKEYYALSSAQRRLYILNQIEPGGLSYNMPFAMKIAGDFDVDRFEDAFRQLIERHEALRTAFVMVDGEPVQKIEKEVDFKVKYGRLGQDPLEEKIKAFIKPFALEKAPLLRAEVLKASGDEHVLMLDMHHIISDGVSMAIFTRELAELYEGKTLPPLTIQYKDFSEWQKLFYQKDEVKRQEDYWLNVFQGEVPVLNLPADEKRPQKRSIEGDIVQFEIDGETSAMLNKLAKENGATMYMLLLAGYTTLLAKYTGQEDIVVGSPIAGRHHSDLKHVIGLFINTLAMRNHPKGDMPFADYLKEVKETALKAYENQDYPFDELVEKLDVKRDMSRHPLFDTMLVLQNFDGDEADIDGLTFQPLQTEVNISKFDLTLTAAETNEGIQCVFNYSTKLFKRSTIERMAGHLINILKEAANDPHMPLSDVNMLSDEEMNALLDQNQGKQADYPQDQTVHQLFEQQADKTPEQTAVVYADEKLTYRELNERANQLARLLRDKGADADQPVAIMIEPSLEMIISMLAVLKAGAAYVPIEPEQLAKRTNEILSDSRAAILLVKGSVKENVAFAGEIVNVADGLIDAKVASNLSASGSADQNAYIIYTSGSTGKPKGVFVRHGNVVNYTTWFMKEAGLTENDKAMLVSSYAFDLGYTSIFSALLSGSELHIARKECYTNAHRALKYIKENGITYIKLTPSLFNIFVNDPGFSAEKPCATLRLVVLGGEMINTRDVETFYNQYPDHVVMNHYGPTETTIGSVFKVIDPEHLDSFKECPVIGTPIHNTNAYVLDENMKLLPEGVYGELCIAGAGVTGGYVNRPDETKEKFIENPFAPHTKMYRTGDLARRLSDGNIELAGRIDTQVKVRGYRIEPEEIKNRLLAHDDIKEAFIAAREDHKGAKQLCAYFTADAELPFEDIRTYLMHELPEYMIPSSFVQIEKMPLSANGKIDTAALPEPQPGKETEYEPPRNETEEKLVQIWEEVLGIDKIGITHHFFAAGGDSIKALQMISRLSREGLSLEMKDLFANPQIKSLSRYVKAESDKSASYETVEGEVLLTPIQQEYFSLNKTDRNHYNHAVMLYRKNGFDESIVKRVFKEIIKHHDALRTVFTEEDGKIIQYNRGPDKQLFDLFVYDVSSENDQPQKVYQLATELQQSIDIETGPLVKLAVFKTNNGDHLLIIIHHLVVDGISWRILFEDLAIGYSQLANGEKVEFYPKTASYQAYARHIAEYAKSVKLLSEKQYWLKAIAEGVEFLDMNENAGAFKVEDSRTFSTELEKEETKRLLRETNRAYHTEINDILITALLVAARDMNGQNQLRITLEGHGREQVADGIDISRTVGWFTSKYPVFIDLGQETDMSRTIKMVKEHLRNVPNKGIGYGILKYLTRDSEIAKGAASPILFNYLGQLDEDINSGEFSSSHLSPGEAAGKGITREHPLEINAVVFRGKLAIQTTYNTRAYSEDVVRAFAQNYKEALKAVIRHCAEREETEKTPSDYGDKGISLDQLEEIKLKYKGMEIEKIYPLANMQRGMLFHALEDKESQAYFEQMAINMKGLIDERLFAETFNDIMERHEILRASIEYEITDEPRNVIIKDRKINLDYHDLRKQSPAEREQVIQAYRKADREKGFRLNSEPLIRAALMRTEDDSYTFIWTNHHILLDGWSRGIIMGELFHMYHMKEARQKHRLEEARPYSDYIGWLQQQDKEAAKAYWRNYLSGFTEKSPISVLAGSSGHAKYKRKEAVIEFPEQLTGRITELASRNNVTFHTVLQCIWGMLLARYNQTDDVVFGTVISGRDAQVTGIEKMVGLFINTVPTRIRLDKSQSFKELIKSVQEQALEGRTYHDMNLSEVQSLSELKRELLDHILIFENYAVDQSAFETSGKRGAGFVFEEIHAEEQTNYGFNIVAVPGERLVIKLTYDGNIYHDHIIAGIKGHLQQVMEQVVQHEDQSLNDITVLSEAERNRLLYEWNDTKAEYPNQTIHRLFEEQAEKTPELAAVVSGNDKLTYRELNEKSNQLARYLRDKGVKADTIVAIMAERSPEMVVGIMGILKAGGAYLPIDPDYPEERIKYMLEDSGAAIILADHKQDLGTLHQEAVELTGDFSSYPADNLEPAGNADSLAYIIYTSGSTGKPKGVMIRQRGLVNYITWADRVYVQGEQLDFALYSSIAFDLTVTSIFTPLISGNRVIVYRHSEDGEPLIRKVFRDQKAGIVKLTPSHLSLVKDMDASGSSIKRLIVGGEDLKTELAKEITERFHHNIEIYNEYGPTETVVGCMIYQYDAGWDRQVSVPIGKPASNVQLYILDERQEVQPVGIAGELYISGDGVAKGYLNKPELTSEKFLPNPFLPGERMYRTGDLAKMRPDGHIEYLGRIDHQVKIRGYRIELGEIEHQLLRHSDIKEAAVAAKTDQNNDQVLCAYVVSERDITQKDIKTFLAKELPEYMVPSYLLKLDELPLTPNGKVDLKALPEPDRSAGALLEYEPPRHELEEKMAAIWEDILNIEQIGINANIFDIGANSLNVMSFVSRLYAELGFRVPFKDIFSKPTIKELSDFLKHAQDLLKDYTDDCMQLTRAEEGGKNLFCFPPAASMGIAYMGLAKHLKQHSVYSFNFIPSANRIRKYADIIKNIQGEGPYTLIGYSSGGILAFDVAKELNRQGYEVEDLIIIDSKYRTKAEKHQFTEEEYREEISKTFELEKYRDVEKLLSDYLVDLVMKSYVYIQNTVTTGAIDGHISYIKSSDNQRGENMMMWEKATSKTFTVVQGAGTHMQMISKSHPDILERNARLIHDIINKTVKI
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5.1.1.11; 5.1.1.13
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COFACTOR: Name=pantetheine 4'-phosphate; Xref=ChEBI:CHEBI:47942; Evidence={ECO:0000305}; Note=Binds 5 phosphopantetheines covalently. {ECO:0000305};
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amino acid activation for nonribosomal peptide biosynthetic process [GO:0043041]; antibiotic biosynthetic process [GO:0017000]; carboxylic acid metabolic process [GO:0019752]; secondary metabolite biosynthetic process [GO:0044550]
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cytosol [GO:0005829]
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aspartate racemase activity [GO:0047689]; ATP binding [GO:0005524]; hydrolase activity [GO:0016787]; ligase activity [GO:0016874]; phenylalanine racemase (ATP-hydrolyzing) activity [GO:0047462]; phosphopantetheine binding [GO:0031177]
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PF00501;PF13193;PF00668;PF00550;PF00975;
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3.30.300.30;3.40.50.980;1.10.1200.10;3.40.50.1820;3.30.559.10;1.10.287.490;3.30.559.30;
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ATP-dependent AMP-binding enzyme family
| null | null |
CATALYTIC ACTIVITY: Reaction=L-aspartate = D-aspartate; Xref=Rhea:RHEA:14973, ChEBI:CHEBI:29990, ChEBI:CHEBI:29991; EC=5.1.1.13; CATALYTIC ACTIVITY: Reaction=ATP + H2O + L-phenylalanine = AMP + D-phenylalanine + diphosphate + H(+); Xref=Rhea:RHEA:20201, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57981, ChEBI:CHEBI:58095, ChEBI:CHEBI:456215; EC=5.1.1.11;
| null |
PATHWAY: Antibiotic biosynthesis; bacitracin biosynthesis.
| null | null |
FUNCTION: Induces peptide synthesis, activates and incorporates five amino acids, forms a thiazoline ring between the first two amino acids and incorporates a D-glutamine in the fourth position.
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Bacillus licheniformis
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O68252
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PCEA_SULMU
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MEKKKKPELSRRDFGKLIIGGGAAATIAPFGVPGANAAEKEKNAAEIRQQFAMTAGSPIIVNDKLERYAEVRTAFTHPTSFFKPNYKGEVKPWFLSAYDEKVRQIENGENGPKMKAKNVGEARAGRALEAAGWTLDINYGNIYPNRFFMLWSGETMTNTQLWAPVGLDRRPPDTTDPVELTNYVKFAARMAGADLVGVARLNRNWVYSEAVTIPADVPYEQSLHKEIEKPIVFKDVPLPIETDDELIIPNTCENVIVAGIAMNREMMQTAPNSMACATTAFCYSRMCMFDMWLCQFIRYMGYYAIPSCNGVGQSVAFAVEAGLGQASRMGACITPEFGPNVRLTKVFTNMPLVPDKPIDFGVTEFCETCKKCARECPSKAITEGPRTFEGRSIHNQSGKLQWQNDYNKCLGYWPESGGYCGVCVAVCPFTKGNIWIHDGVEWLIDNTRFLDPLMLGMDDALGYGAKRNITEVWDGKINTYGLDADHFRDTVSFRKDRVKKS
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1.21.99.5
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COFACTOR: Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; Evidence={ECO:0000269|PubMed:28671181, ECO:0000269|PubMed:29378885, ECO:0000269|PubMed:8663199}; Note=Binds 2 [4Fe-4S] clusters. {ECO:0000269|PubMed:28671181, ECO:0000269|PubMed:29378885, ECO:0000269|PubMed:8663199}; COFACTOR: Name=corrinoid; Xref=ChEBI:CHEBI:33913; Evidence={ECO:0000269|PubMed:11976751, ECO:0000269|PubMed:12420164, ECO:0000269|PubMed:24433392, ECO:0000269|PubMed:28671181, ECO:0000269|PubMed:8663199, ECO:0000269|Ref.6}; Note=The corrinoid cofactor is norpseudovitamin B12 (norpseudo-B12), a natural B12 cofactor that lacks a characteristic methyl group of the cobamide structure (PubMed:24433392, PubMed:28671181, Ref.6). In vitro, can function with singly substituted benzimidazolyl-norcobamides cofactors (PubMed:29378885). {ECO:0000269|PubMed:24433392, ECO:0000269|PubMed:28671181, ECO:0000269|PubMed:29378885, ECO:0000269|Ref.6};
| null |
cytoplasm [GO:0005737]; plasma membrane [GO:0005886]
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4 iron, 4 sulfur cluster binding [GO:0051539]; metal ion binding [GO:0046872]; oxidoreductase activity [GO:0016491]
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PF13486;PF13484;
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3.30.70.20;
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PceA family
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PTM: Predicted to be exported by the Tat system. The position of the signal peptide cleavage has not been experimentally proven. {ECO:0000255|PROSITE-ProRule:PRU00648}.
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SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16802174, ECO:0000269|PubMed:8663199, ECO:0000269|PubMed:9696761}. Cell inner membrane {ECO:0000269|PubMed:16802174}; Peripheral membrane protein {ECO:0000269|PubMed:16802174}; Cytoplasmic side {ECO:0000269|PubMed:16802174}. Cell inner membrane {ECO:0000269|PubMed:16802174}; Peripheral membrane protein {ECO:0000269|PubMed:16802174}; Periplasmic side {ECO:0000269|PubMed:16802174}. Note=The localization of the enzyme is dependent on the electron acceptor utilized. When the cells are grown with pyruvate plus fumarate, a major part of the enzyme is either localized in the cytoplasm or membrane associated facing the cytoplasm. In cells grown on pyruvate or formate as electron donors and PCE as electron acceptor, most of the enzyme is detected at the periplasmic side of the cytoplasmic membrane. {ECO:0000269|PubMed:16802174}.
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CATALYTIC ACTIVITY: Reaction=A + chloride + H(+) + trichloroethene = AH2 + tetrachloroethene; Xref=Rhea:RHEA:20353, ChEBI:CHEBI:13193, ChEBI:CHEBI:15378, ChEBI:CHEBI:16602, ChEBI:CHEBI:17300, ChEBI:CHEBI:17499, ChEBI:CHEBI:17996; EC=1.21.99.5; Evidence={ECO:0000269|PubMed:11976751, ECO:0000269|PubMed:12420164, ECO:0000269|PubMed:24433392, ECO:0000269|PubMed:28671181, ECO:0000269|PubMed:8663199}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:20355; Evidence={ECO:0000269|PubMed:11976751, ECO:0000269|PubMed:12420164, ECO:0000269|PubMed:24433392, ECO:0000269|PubMed:28671181, ECO:0000269|PubMed:8663199}; CATALYTIC ACTIVITY: Reaction=AH2 + trichloroethene = (Z)-1,2-dichloroethene + A + chloride + H(+); Xref=Rhea:RHEA:67992, ChEBI:CHEBI:13193, ChEBI:CHEBI:15378, ChEBI:CHEBI:16602, ChEBI:CHEBI:17499, ChEBI:CHEBI:17996, ChEBI:CHEBI:28805; Evidence={ECO:0000269|PubMed:11976751, ECO:0000269|PubMed:12420164, ECO:0000269|PubMed:24433392, ECO:0000269|PubMed:28671181, ECO:0000269|PubMed:8663199}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67993; Evidence={ECO:0000269|PubMed:11976751, ECO:0000269|PubMed:12420164, ECO:0000269|PubMed:24433392, ECO:0000269|PubMed:28671181, ECO:0000269|PubMed:8663199};
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BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.2 mM for tetrachloroethene (with reduced methyl viologen as electron donor) {ECO:0000269|PubMed:8663199}; KM=200 uM for tetrachloroethene (with reduced methyl viologen as electron donor) {ECO:0000269|PubMed:11976751}; KM=0.24 mM for trichloroethene (with reduced methyl viologen as electron donor) {ECO:0000269|PubMed:8663199}; KM=240 uM for trichloroethene (with reduced methyl viologen as electron donor) {ECO:0000269|PubMed:11976751}; KM=250 uM for trans-1,3-dichloropropene (with reduced methyl viologen as electron donor) {ECO:0000269|PubMed:11976751}; KM=250 uM for 1,1,3-trichloropropene (with reduced methyl viologen as electron donor) {ECO:0000269|PubMed:11976751}; KM=600 uM for 2,3-dichloropropene (with reduced methyl viologen as electron donor) {ECO:0000269|PubMed:11976751}; KM=99 uM for 4-BP {ECO:0000269|PubMed:28671181}; KM=95 uM for 2,4-DBP {ECO:0000269|PubMed:28671181}; KM=158 uM for 2,4,6-TBP {ECO:0000269|PubMed:28671181};
| null |
BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is about 8.0. {ECO:0000269|PubMed:8663199};
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BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 42 degrees Celsius. {ECO:0000269|PubMed:8663199};
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FUNCTION: Catalyzes the reductive dechlorination of tetrachloroethene (PCE) to trichloroethene (TCE) and of trichloroethene to cis-1,2-dichloroethene (DCE) (PubMed:11976751, PubMed:12420164, PubMed:24433392, PubMed:28671181, PubMed:8663199). In addition, trans-1,3-dichloropropene, 1,1,3-trichloropropene and 2,3-dichloropropene are reduced to a mixture of mono-chloropropenes, 1,1-dichloropropene, and 2-chloropropene, respectively (PubMed:11976751). Is also able to convert brominated phenols such as 4-bromophenol (4-BP), 2,4-dibromophenol (2,4-DBP) and 2,4,6-tribromophenol (2,4,6-TBP) (PubMed:28671181). Utilizes formate or pyruvate as electron donors (PubMed:16802174, PubMed:24433392). Titanium(III) citrate could also serve as electron donor (PubMed:11976751). Reduced methyl viologen can act as the artificial electron donor (PubMed:11976751, PubMed:12420164, PubMed:8663199). {ECO:0000269|PubMed:11976751, ECO:0000269|PubMed:12420164, ECO:0000269|PubMed:16802174, ECO:0000269|PubMed:24433392, ECO:0000269|PubMed:28671181, ECO:0000269|PubMed:8663199}.
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Sulfurospirillum multivorans (Dehalospirillum multivorans)
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O68691
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SCTF_YERPE
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MSNFSGFTKGTDIADLDAVAQTLKKPADDANKAVNDSIAALKDKPDNPALLADLQHSINKWSVIYNINSTIVRSMKDLMQGILQKFP
| null | null |
protein secretion by the type III secretion system [GO:0030254]
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cell surface [GO:0009986]; extracellular region [GO:0005576]; type III protein secretion system complex [GO:0030257]
| null |
PF09392;
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1.20.58.90;
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SctF family
| null |
SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:16135236, ECO:0000269|PubMed:28196868, ECO:0000269|PubMed:29458689}. Cell surface {ECO:0000269|PubMed:16135236, ECO:0000269|PubMed:29458689}. Note=Targeted to the T3SS apparatus via the combined action of an N-terminal secretion signal and the YscE-YscG chaperone. {ECO:0000269|PubMed:29458689}.
| null | null | null | null | null |
FUNCTION: Component of the type III secretion system (T3SS), also called injectisome, which is used to inject bacterial effector proteins into eukaryotic host cells (PubMed:16135236). YscF/SctF forms the external needle filament that protrudes from the bacterial surface (PubMed:16135236, PubMed:19968786, PubMed:28196868). Essential for the calcium-dependent regulation of T3SS and Yop secretion (PubMed:16135236). Required to block Yop secretion in the presence of extracellular calcium (PubMed:16135236). May be the extracellular T3SS component that senses extracellular calcium and/or participates in transmitting the calcium signal to the cytoplasmic compartment where the block in secretion is initiated (PubMed:16135236). {ECO:0000269|PubMed:16135236, ECO:0000269|PubMed:19968786, ECO:0000269|PubMed:28196868}.; FUNCTION: During infection, can induce innate immune responses (PubMed:24643544, PubMed:25644012). The needle proteins interact with host TLR2 or TLR4, and induce signaling by NF-kappa-B and/or AP-1 (PubMed:24643544, PubMed:25644012). This activation is MyD88 dependent and results in increased expression of cytokines, including TNF-alpha, IL-6 and IL-8 (PubMed:24643544, PubMed:25644012). Innate immune responses are modulated by the N-terminal region of YscF/SctF (PubMed:25644012). {ECO:0000269|PubMed:24643544, ECO:0000269|PubMed:25644012}.
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Yersinia pestis
|
O68900
|
PET_ECO44
|
MNKIYSIKYSAATGGLIAVSELAKKVICKTNRKISAALLSLAVISYTNIIYAANMDISKAWARDYLDLAQNKGVFQPGSTHVKIKLKDGTDFSFPALPVPDFSSATANGAATSIGGAYAVTVAHNAKNKSSANYQTYGSTQYTQINRMTTGNDFSIQRLNKYVVETRGADTSFNYNENNQNIIDRYGVDVGNGKKEIIGFRVGSGNTTFSGIKTSQTYQADLLSASLFHITNLRANTVGGNKVEYENDSYFTNLTTNGDSGSGVYVFDNKEDKWVLLGTTHGIIGNGKTQKTYVTPFDSKTTNELKQLFIQNVNIDNNTATIGGGKITIGNTTQDIEKNKNNQNKDLVFSGGGKISLKENLDLGYGGFIFDENKKYTVSAEGNNNVTFKGAGIDIGKGSTVDWNIKYASNDALHKIGEGSLNVIQAQNTNLKTGNGTVILGAQKTFNNIYVAGGPGTVQLNAENALGEGDYAGIFFTENGGKLDLNGHNQTFKKIAATDSGTTITNSNTTKESVLSVNNQNNYIYHGNVDGNVRLEHHLDTKQDNARLILDGDIQANSISIKNAPLVMQGHATDHAIFRTTKTNNCPEFLCGVDWVTRIKNAENSVNQKNKTTYKSNNQVSDLSQPDWETRKFRFDNLNIEDSSLSIARNADVEGNIQAKNSVINIGDKTAYIDLYSGKNITGAGFTFRQDIKSGDSIGESKFTGGIMATDGSISIGDKAIVTLNTVSSLDRTALTIHKGANVTASSSLFTTSNIKSGGDLTLTGATESTGEITPSMFYAAGGYELTEDGANFTAKNQASVTGDIKSEKAAKLSFGSADKDNSATRYSQFALAMLDGFDTSYQGSIKAAQSSLAMNNALWKVTGNSELKKLNSTGSMVLFNGGKNIFNTLTVDELTTSNSAFVMRTNTQQADQLIVKNKLEGANNLLLVDFIEKKGNDKNGLNIDLVKAPENTSKDVFKTETQTIGFSDVTPEIKQQEKDGKSVWTLTGYKTVANADAAKKATSLMSGGYKAFLAEVNNLNKRMGDLRDINGEAGAWARIMSGTGSAGGGFSDNYTHVQVGADNKHELDGLDLFTGVTMTYTDSHAGSDAFSGETKSVGAGLYASAMFESGAYIDLIGKYVHHDNEYTATFAGLGTRDYSSHSWYAGAEVGYRYHVTDSAWIEPQAELVYGAVSGKQFSWKDQGMNLTMKDKDFNPLIGRTGVDVGKSFSGKDWKVTARAGLGYQFDLFANGETVLRDASGEKRIKGEKDGRMLMNVGLNAEIRDNVRFGLEFEKSAFGKYNVDNAINANFRYSF
|
3.4.21.-
| null |
proteolysis [GO:0006508]
|
cell outer membrane [GO:0009279]; cell surface [GO:0009986]; extracellular region [GO:0005576]; periplasmic space [GO:0042597]
|
serine-type endopeptidase activity [GO:0004252]
|
PF03797;PF13018;PF02395;
|
2.160.20.20;2.40.10.120;2.40.128.130;
| null |
PTM: Cleaved to release the mature protein from the outer membrane.
|
SUBCELLULAR LOCATION: [Serine protease pet autotransporter]: Periplasm {ECO:0000250}.; SUBCELLULAR LOCATION: [Serine protease pet]: Secreted. Cell surface.; SUBCELLULAR LOCATION: [Serine protease pet translocator]: Cell outer membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Note=The cleaved C-terminal fragment (autotransporter domain) is localized in the outer membrane. {ECO:0000250}.
| null | null | null | null | null |
FUNCTION: Serine protease with enterotoxic and cytotoxic activity. Internalization into the host cell is required for the induction of cytopathic effects. However, the serine activity is not necessary for secretion and internalization into the host cell. {ECO:0000269|PubMed:10225873, ECO:0000269|PubMed:10496914, ECO:0000269|PubMed:11160002, ECO:0000269|PubMed:9632580}.
|
Escherichia coli O44:H18 (strain 042 / EAEC)
|
O69054
|
PTXD_STUST
|
MLPKLVITHRVHDEILQLLAPHCELMTNQTDSTLTREEILRRCRDAQAMMAFMPDRVDADFLQACPELRVVGCALKGFDNFDVDACTARGVWLTFVPDLLTVPTAELAIGLAVGLGRHLRAADAFVRSGEFQGWQPQFYGTGLDNATVGILGMGAIGLAMADRLQGWGATLQYHEAKALDTQTEQRLGLRQVACSELFASSDFILLALPLNADTQHLVNAELLALVRPGALLVNPCRGSVVDEAAVLAALERGQLGGYAADVFEMEDWARADRPRLIDPALLAHPNTLFTPHIGSAVRAVRLEIERCAAQNIIQVLAGARPINAANRLPKAEPAAC
|
1.20.1.1
| null | null |
cytosol [GO:0005829]
|
glycerate dehydrogenase activity [GO:0008465]; glyoxylate reductase (NADP+) activity [GO:0030267]; hydroxypyruvate reductase activity [GO:0016618]; NAD binding [GO:0051287]; phosphonate dehydrogenase activity [GO:0050609]
|
PF00389;PF02826;
|
3.40.50.720;
|
D-isomer specific 2-hydroxyacid dehydrogenase family
| null | null |
CATALYTIC ACTIVITY: Reaction=H2O + NAD(+) + phosphonate = H(+) + NADH + phosphate; Xref=Rhea:RHEA:13173, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16215, ChEBI:CHEBI:43474, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.20.1.1; Evidence={ECO:0000269|PubMed:11278981};
| null | null |
BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.25-7.75.;
|
BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 35 degrees Celsius.;
|
FUNCTION: Catalyzes phosphite (phosphonate) oxidation. {ECO:0000269|PubMed:11278981}.
|
Stutzerimonas stutzeri (Pseudomonas stutzeri)
|
O69078
|
CSRA_PSEAE
|
MLILTRRVGETLMVGDDVTVTVLGVKGNQVRIGVNAPKEVAVHREEIYQRIQKEKDQEPNH
| null | null |
mRNA catabolic process [GO:0006402]; negative regulation of translational initiation [GO:0045947]; positive regulation of translational initiation [GO:0045948]; protein secretion by the type III secretion system [GO:0030254]; protein secretion by the type VI secretion system [GO:0033103]; quorum sensing [GO:0009372]; regulation of carbohydrate metabolic process [GO:0006109]; regulation of secondary metabolic process [GO:0043455]; regulation of single-species biofilm formation [GO:1900190]
|
cytosol [GO:0005829]
|
mRNA 5'-UTR binding [GO:0048027]
|
PF02599;
|
2.60.40.4380;
|
CsrA/RsmA family
| null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00167}.
| null | null | null | null | null |
FUNCTION: A key translational regulator that binds mRNA to regulate translation initiation and/or mRNA stability. Mediates global changes in gene expression, shifting from rapid growth to stress survival by linking envelope stress, the stringent response and the catabolite repression systems. Usually binds in the 5'-UTR; binding at or near the Shine-Dalgarno sequence prevents ribosome-binding, repressing translation, binding elsewhere in the 5'-UTR can activate translation and/or stabilize the mRNA. Its function is antagonized by small RNA(s). {ECO:0000255|HAMAP-Rule:MF_00167}.; FUNCTION: Binds to mRNA to regulate gene activity at a post-transcriptional level (Probable). Represses expression of many toxic extracellular enzymes and compounds; decreases translation of lasI and rhlI (PubMed:11673439). Positively controls swarming motility and rhanolipid and lipase, possibly via expression of rhlA; activates transcription of the CsrA/RsmA antagonistic sRNA RsmZ (PubMed:15126453). Overexpression dramatically reduces extracellular protease, elastase (lasB) and staphyolytic (lasA) activities, decreases HCN production, decreases levels of autoinducers 3-oxo-C12-HSL (3-oxo-N-(tetrahydro-2-oxo-3-furanyl)-dodecanamide) and C4-HSL (N-butanoylhomoserine lactone), and abolishes production of cytotoxic internal lectin PA-IL (lecA) (PubMed:11673439). Control of hcn expression is post-transcriptional (PubMed:11673439). Replaces endogenous gene(s) in E.coli and P.fluorescens (PubMed:16359708). {ECO:0000269|PubMed:11673439, ECO:0000269|PubMed:15126453, ECO:0000269|PubMed:16359708}.; FUNCTION: Probably binds to and is sequestered by non-coding small RNA (sRNA) RsmZ; overexpression of rsmZ produces very similar phenotypes to deletion of rsmA, while rsmZ deletion has no phenotype (PubMed:15126453). {ECO:0000269|PubMed:15126453}.
|
Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
|
O69174
|
ENO_STAAU
|
MPIITDVYAREVLDSRGNPTVEVEVLTESGAFGRALVPSGASTGEHEAVELRDGDKSRYLGKGVTKAVENVNEIIAPEIIEGEFSVLDQVSIDKMMIALDGTPNKGKLGANAILGVSIAVARAAADLLGQPLYKYLGGFNGKQLPVPMMNIVNGGSHSDAPIAFQEFMILPVGATTFKESLRWGTEIFHNLKSILSQRGLETAVGDEGGFAPKFEGTEDAVETIIQAIEAAGYKPGEEVFLGFDCASSEFYENGVYDYSKFEGEHGAKRTAAEQVDYLEQLVDKYPIITIEDGMDENDWDGWKQLTERIGDRVQLVGDDLFVTNTEILAKGIENGIGNSILIKVNQIGTLTETFDAIEMAQKAGYTAVVSHRSGETEDTTIADIAVATNAGQIKTGSLSRTDRIAKYNQLLRIEDELFETAKYDGIKSFYNLDK
|
4.2.1.11
|
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255|HAMAP-Rule:MF_00318, ECO:0000269|PubMed:26627653}; Note=Binds a second Mg(2+) ion via substrate during catalysis. {ECO:0000255|HAMAP-Rule:MF_00318};
|
glycolytic process [GO:0006096]
|
cell surface [GO:0009986]; extracellular region [GO:0005576]; phosphopyruvate hydratase complex [GO:0000015]
|
magnesium ion binding [GO:0000287]; phosphopyruvate hydratase activity [GO:0004634]
|
PF00113;PF03952;
|
3.20.20.120;3.30.390.10;
|
Enolase family
| null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00318, ECO:0000269|PubMed:15158195}. Secreted {ECO:0000255|HAMAP-Rule:MF_00318, ECO:0000269|PubMed:15158195}. Cell surface {ECO:0000255|HAMAP-Rule:MF_00318, ECO:0000269|PubMed:15158195}. Note=Fractions of enolase are present in both the cytoplasm and on the cell surface (PubMed:15158195). Once secreted, it remains attached to the cell surface (PubMed:15158195). {ECO:0000255|HAMAP-Rule:MF_00318, ECO:0000269|PubMed:15158195}.
|
CATALYTIC ACTIVITY: Reaction=(2R)-2-phosphoglycerate = H2O + phosphoenolpyruvate; Xref=Rhea:RHEA:10164, ChEBI:CHEBI:15377, ChEBI:CHEBI:58289, ChEBI:CHEBI:58702; EC=4.2.1.11; Evidence={ECO:0000255|HAMAP-Rule:MF_00318, ECO:0000269|PubMed:26627653}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:10165; Evidence={ECO:0000269|PubMed:26627653};
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.37 mM for 2-phosphoglycerate by octamer {ECO:0000269|PubMed:26627653}; Note=kcat is 83 sec(-1) for octamer. {ECO:0000269|PubMed:26627653};
|
PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 4/5. {ECO:0000255|HAMAP-Rule:MF_00318}.
| null | null |
FUNCTION: Catalyzes the reversible conversion of 2-phosphoglycerate (2-PG) into phosphoenolpyruvate (PEP) (PubMed:26627653). It is essential for the degradation of carbohydrates via glycolysis. {ECO:0000255|HAMAP-Rule:MF_00318, ECO:0000269|PubMed:26627653}.; FUNCTION: 'Moonlights' as a laminin receptor. Binds laminin when expressed on the bacterial cell surface; this probably induces destruction of the extracellular matrix, favoring invasion and dissemination. {ECO:0000269|PubMed:15158195}.
|
Staphylococcus aureus
|
O69199
|
CYAB_AERHY
|
MSSQHFQGRFEVEFKYRLSDVDAFTCALAALNPEVMLEDNQEQDSYFDTPEHSLAAEGKSLVIRTMQPSGIQLWIVKGPEADRCEAVNITDADKAASMLRTLGYRQVLAISKRRSIYFVGPFHVTRDHLEGIGDFAELAIMTDDEALLPDYRQQLQDLATRLGLSSAQLETRSYRTLCEQSLTLNSEKVPS
|
4.6.1.1
| null |
cAMP biosynthetic process [GO:0006171]
|
cytoplasm [GO:0005737]
|
adenylate cyclase activity [GO:0004016]; ATP binding [GO:0005524]
|
PF01928;
|
2.40.320.10;
|
Adenylyl cyclase CyaB family
| null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
|
CATALYTIC ACTIVITY: Reaction=ATP = 3',5'-cyclic AMP + diphosphate; Xref=Rhea:RHEA:15389, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:58165; EC=4.6.1.1; Evidence={ECO:0000269|PubMed:22984449};
| null | null |
BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 9.5. {ECO:0000269|PubMed:9642185};
|
BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 65 degrees Celsius. {ECO:0000269|PubMed:9642185};
|
FUNCTION: In vitro, CyaB catalyzes the biosynthesis of cyclic AMP (cAMP) from ATP. It seems that under the physiological conditions CyaB has no function in cAMP processes. In vitro, it is also able to hydrolyze substrates such as thiamine triphosphate (ThTP) and inorganic triphosphate (PPPi) at a low rate. It has a slight preference for ThTP over ATP and PPPi in the presence of manganese ions. This PPPase activity is probably not of physiological importance. {ECO:0000269|PubMed:22984449, ECO:0000269|PubMed:9642185}.
|
Aeromonas hydrophila
|
O69652
|
CDS1_MYCTU
|
MSGGACIAVRSLSRSWTDNAIRLIEADARRSADTHLLRYPLPAAWCTDVDVELYLKDETTHITGSLKHRLARSLFLYALCNGWINENTTVVEASSGSTAVSEAYFAALLGLPFIAVMPAATSASKIALIESQGGRCHFVQNSSQVYAEAERVAKETGGHYLDQFTNAERATDWRGNNNIAESIYVQMREEKHPTPEWIVVGAGTGGTSATIGRYIRYRRHATRLCVVDPENSAFFPAYSEGRYDIVMPTSSRIEGIGRPRVEPSFLPGVVDRMVAVPDAASIAAARHVSAVLGRRVGPSTGTNLWGAFGLLAEMVKQGRSGSVVTLLADSGDRYADTYFSDEWVSAQGLDPAGPAAALVEFERSCRWT
|
4.4.1.1
|
COFACTOR: Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; Evidence={ECO:0000255|HAMAP-Rule:MF_00868, ECO:0000269|PubMed:34439535};
|
cell redox homeostasis [GO:0045454]; cysteine biosynthetic process [GO:0019344]; hydrogen sulfide biosynthetic process [GO:0070814]; L-cysteine catabolic process to pyruvate [GO:0019450]; positive regulation of cellular respiration [GO:1901857]; regulation of sulfur metabolic process [GO:0042762]
|
cytoplasm [GO:0005737]; cytosol [GO:0005829]; plasma membrane [GO:0005886]
|
lyase activity [GO:0016829]; pyridoxal phosphate binding [GO:0030170]
|
PF00291;
|
3.40.50.1100;
|
Cysteine synthase/cystathionine beta-synthase family, Cds1 subfamily
| null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
|
CATALYTIC ACTIVITY: Reaction=H2O + L-cysteine = H(+) + hydrogen sulfide + NH4(+) + pyruvate; Xref=Rhea:RHEA:24931, ChEBI:CHEBI:15361, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28938, ChEBI:CHEBI:29919, ChEBI:CHEBI:35235; EC=4.4.1.1; Evidence={ECO:0000255|HAMAP-Rule:MF_00868, ECO:0000269|PubMed:34439535}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:24932; Evidence={ECO:0000255|HAMAP-Rule:MF_00868, ECO:0000269|PubMed:34439535};
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=11.26 mM for cysteine {ECO:0000269|PubMed:34439535}; Note=kcat is 78.71 sec(-1). {ECO:0000269|PubMed:34439535};
| null | null | null |
FUNCTION: A cysteine desulfhydrase that generates hydrogen sulfide, H(2)S. The H(2)S produced by this enzyme stimulates respiration in M.tuberculosis, mediated primarily via cytochrome bd with a lesser contribution from cytochrome bc1/aa3. H(2)S modulates the balance between respiration and glycolysis, and also contributes to redox homeostasis. Probably eliminates toxic levels of Cys (which can induce oxidative stress). {ECO:0000269|PubMed:34439535}.
|
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
|
O69711
|
NMTR_MYCTU
|
MGHGVEGRNRPSAPLDSQAAAQVASTLQALATPSRLMILTQLRNGPLPVTDLAEAIGMEQSAVSHQLRVLRNLGLVVGDRAGRSIVYSLYDTHVAQLLDEAIYHSEHLHLGLSDRHPSAG
| null | null | null | null |
DNA binding [GO:0003677]; DNA-binding transcription factor activity [GO:0003700]; metal ion binding [GO:0046872]
|
PF01022;
|
1.10.10.10;
| null | null | null | null | null | null | null | null |
FUNCTION: Represses transcription of ctpJ/nmtA, by binding to its promoter region. {ECO:0000269|PubMed:12163508}.
|
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
|
O69729
|
TCRY_MYCTU
|
MGITAATEMALRRHLVAQLDNQLGGTSYRSVLMYPEKMPRPPWRHETHNYIRSGPGPRFLDAPGQPAGMVAAVVSDGTTVAAGYLTGSGSRAALTSTGRSQLERIAGSRTPLTLDLDGLGRYRVLAAPSRNGHDVIVTGLSMGNVDATMLQMLIIFGIVTVIALVAATTAGIVIIKRALAPLRRVAQTASEVVDLPLDRGEVKLPVRVPEPDANPSTEVGQLGSALNRMLDHIAAALSARQASETCVRQFVADASHELRTPLAAIRGYTELTQRIGDDPEAVAHAMSRVASETERITRLVEDLLLLARLDSGRPLERGPVDMSRLAVDAVSDAHVAGPDHQWALDLPPEPVVIPGDAARLHQVVTNLLANARVHTGPGTIVTTRLSTGPTHVVLQVIDNGPGIPAALQSEVFERFARGDTSRSRQAGSTGLGLAIVSAVVKAHNGTITVSSSPGYTEFAVRLPLDGWQPLESSPR
|
2.7.13.3
|
COFACTOR: Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240; Evidence={ECO:0000269|PubMed:19962420};
|
phosphorelay signal transduction system [GO:0000160]; protein autophosphorylation [GO:0046777]
|
cytosol [GO:0005829]; plasma membrane [GO:0005886]
|
ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; calcium ion binding [GO:0005509]; magnesium ion binding [GO:0000287]; phosphorelay sensor kinase activity [GO:0000155]; protein homodimerization activity [GO:0042803]
|
PF00672;PF02518;PF00512;
|
1.10.287.130;6.10.340.10;3.30.565.10;
| null |
PTM: Autophosphorylated.
|
SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}.
|
CATALYTIC ACTIVITY: Reaction=ATP + protein L-histidine = ADP + protein N-phospho-L-histidine.; EC=2.7.13.3;
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=10 mM for ATP {ECO:0000269|PubMed:19962420};
| null | null | null |
FUNCTION: Member of the two-component regulatory system TcrY/TcrX. Activates TcrX by phosphorylation. {ECO:0000269|PubMed:12595424, ECO:0000269|PubMed:19962420}.
|
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
|
O69762
|
HCHL_PSEFL
|
MSTYEGRWKTVKVEIEDGIAFVILNRPEKRNAMSPTLNREMIDVLETLEQDPAAGVLVLTGAGEAWTAGMDLKEYFREVDAGPEILQEKIRREASQWQWKLLRMYAKPTIAMVNGWCFGGGFSPLVACDLAICADEATFGLSEINWGIPPGNLVSKAMADTVGHRQSLYYIMTGKTFGGQKAAEMGLVNESVPLAQLREVTIELARNLLEKNPVVLRAAKHGFKRCRELTWEQNEDYLYAKLDQSRLLDTEGGREQGMKQFLDDKSIKPGLQAYKR
|
4.1.2.61
| null |
isoprenoid catabolic process [GO:0008300]
| null |
trans-feruloyl-CoA hydratase activity [GO:0050548]; vanillin synthase activity [GO:0050547]
|
PF00378;
|
6.10.250.2850;
|
Enoyl-CoA hydratase/isomerase family
| null | null |
CATALYTIC ACTIVITY: Reaction=(E)-feruloyl-CoA + H2O = acetyl-CoA + vanillin; Xref=Rhea:RHEA:62412, ChEBI:CHEBI:15377, ChEBI:CHEBI:18346, ChEBI:CHEBI:57288, ChEBI:CHEBI:87305; EC=4.1.2.61; Evidence={ECO:0000269|PubMed:10222033, ECO:0000269|PubMed:9461612}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:62413; Evidence={ECO:0000269|PubMed:9461612}; CATALYTIC ACTIVITY: Reaction=(E)-caffeoyl-CoA + H2O = 3,4-dihydroxybenzaldehyde + acetyl-CoA; Xref=Rhea:RHEA:36307, ChEBI:CHEBI:15377, ChEBI:CHEBI:50205, ChEBI:CHEBI:57288, ChEBI:CHEBI:87136; EC=4.1.2.61; Evidence={ECO:0000269|PubMed:10222033}; CATALYTIC ACTIVITY: Reaction=(E)-4-coumaroyl-CoA + H2O = 4-hydroxybenzaldehyde + acetyl-CoA; Xref=Rhea:RHEA:62416, ChEBI:CHEBI:15377, ChEBI:CHEBI:17597, ChEBI:CHEBI:57288, ChEBI:CHEBI:85008; EC=4.1.2.61; Evidence={ECO:0000269|PubMed:10222033}; CATALYTIC ACTIVITY: Reaction=(E)-feruloyl-CoA + H2O = 3-hydroxy-3-(4-hydroxy-3-methoxyphenyl)propanoyl-CoA; Xref=Rhea:RHEA:14517, ChEBI:CHEBI:15377, ChEBI:CHEBI:58004, ChEBI:CHEBI:87305; EC=4.1.2.61; Evidence={ECO:0000269|PubMed:10222033, ECO:0000269|PubMed:9461612}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:14518; Evidence={ECO:0000269|PubMed:9461612}; CATALYTIC ACTIVITY: Reaction=3-hydroxy-3-(4-hydroxy-3-methoxyphenyl)propanoyl-CoA = acetyl-CoA + vanillin; Xref=Rhea:RHEA:18725, ChEBI:CHEBI:18346, ChEBI:CHEBI:57288, ChEBI:CHEBI:58004; Evidence={ECO:0000269|PubMed:10222033, ECO:0000269|PubMed:9461612}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:18726; Evidence={ECO:0000269|PubMed:9461612}; CATALYTIC ACTIVITY: Reaction=(E)-caffeoyl-CoA + H2O = 3-hydroxy-3-(3,4-dihydroxyphenyl)propanoyl-CoA; Xref=Rhea:RHEA:62424, ChEBI:CHEBI:15377, ChEBI:CHEBI:87136, ChEBI:CHEBI:145752; Evidence={ECO:0000269|PubMed:10222033}; CATALYTIC ACTIVITY: Reaction=3-hydroxy-3-(3,4-dihydroxyphenyl)propanoyl-CoA = 3,4-dihydroxybenzaldehyde + acetyl-CoA; Xref=Rhea:RHEA:62428, ChEBI:CHEBI:50205, ChEBI:CHEBI:57288, ChEBI:CHEBI:145752; Evidence={ECO:0000269|PubMed:10222033}; CATALYTIC ACTIVITY: Reaction=(E)-4-coumaroyl-CoA + H2O = 3-hydroxy-3-(4-hydroxyphenyl)propanoyl-CoA; Xref=Rhea:RHEA:40991, ChEBI:CHEBI:15377, ChEBI:CHEBI:73500, ChEBI:CHEBI:85008; Evidence={ECO:0000269|PubMed:10222033}; CATALYTIC ACTIVITY: Reaction=3-hydroxy-3-(4-hydroxyphenyl)propanoyl-CoA = 4-hydroxybenzaldehyde + acetyl-CoA; Xref=Rhea:RHEA:40995, ChEBI:CHEBI:17597, ChEBI:CHEBI:57288, ChEBI:CHEBI:73500; Evidence={ECO:0000269|PubMed:10222033};
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=11.8 uM for feruloyl-CoA {ECO:0000269|PubMed:18479250}; KM=2.4 uM for feruloyl-CoA {ECO:0000269|PubMed:10222033}; KM=5.3 uM for 4-coumaroyl-CoA {ECO:0000269|PubMed:10222033}; KM=1.6 uM for caffeoyl-CoA {ECO:0000269|PubMed:10222033}; Vmax=36.5 nmol/sec/mg enzyme with feruloyl-CoA as substrate {ECO:0000269|PubMed:10222033}; Vmax=73.3 nmol/sec/mg enzyme with 4-coumaroyl-CoA as substrate {ECO:0000269|PubMed:10222033}; Vmax=15.2 nmol/sec/mg enzyme with caffeoyl-CoA as substrate {ECO:0000269|PubMed:10222033}; Note=kcat is 3.72 sec(-1) with feruloyl-CoA as substrate. {ECO:0000269|PubMed:18479250};
| null |
BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8.5-9.5. {ECO:0000269|PubMed:10222033};
| null |
FUNCTION: Catalyzes the hydration of the acyl-CoA thioester of ferulic acid and the subsequent retro-aldol cleavage of the hydrated intermediate to yield vanillin (4-hydroxy-3-methoxy-benzaldehyde) (PubMed:10222033, PubMed:9461612). The enzyme is also active with caffeoyl-CoA and 4-coumaroyl-CoA producing 3,4-dihydroxybenzaldehyde and 4-hydroxybenzaldehyde, respectively (PubMed:10222033). {ECO:0000269|PubMed:10222033, ECO:0000269|PubMed:9461612}.
|
Pseudomonas fluorescens
|
O70126
|
AURKB_MOUSE
|
MAQKENAYPWPYGSKTSQSGLNTLSQRVLRKEPATTSALALVNRFNSQSTAAPGQKLAENKSQGSTASQGSQNKQPFTIDNFEIGRPLGKGKFGNVYLAREKKSRFIVALKILFKSQIEKEGVEHQLRREIEIQAHLKHPNILQLYNYFYDQQRIYLILEYAPRGELYKELQKSRTFDEQRTATIMEELSDALTYCHKKKVIHRDIKPENLLLGLQGELKIADFGWSVHAPSLRRKTMCGTLDYLPPEMIEGRMHNEMVDLWCIGVLCYELMVGNPPFESPSHSETYRRIVKVDLKFPSSVPSGAQDLISKLLKHNPWQRLPLAEVAAHPWVRANSRRVLPPSAL
|
2.7.11.1
| null |
abscission [GO:0009838]; cell cycle G2/M phase transition [GO:0044839]; cellular response to UV [GO:0034644]; cleavage furrow formation [GO:0036089]; mitotic cell cycle [GO:0000278]; mitotic cytokinesis [GO:0000281]; mitotic cytokinesis checkpoint signaling [GO:0044878]; mitotic spindle midzone assembly [GO:0051256]; mitotic spindle organization [GO:0007052]; negative regulation of B cell apoptotic process [GO:0002903]; negative regulation of cGAS/STING signaling pathway [GO:0160049]; negative regulation of cytokinesis [GO:0032466]; negative regulation of innate immune response [GO:0045824]; negative regulation of transcription by RNA polymerase II [GO:0000122]; positive regulation of attachment of mitotic spindle microtubules to kinetochore [GO:1902425]; positive regulation of cytokinesis [GO:0032467]; positive regulation of lateral attachment of mitotic spindle microtubules to kinetochore [GO:1905116]; positive regulation of mitotic cell cycle spindle assembly checkpoint [GO:0090267]; positive regulation of mitotic cytokinesis [GO:1903490]; positive regulation of mitotic sister chromatid segregation [GO:0062033]; positive regulation of mitotic sister chromatid separation [GO:1901970]; positive regulation of protein phosphorylation [GO:0001934]; positive regulation of telomere capping [GO:1904355]; positive regulation of telomere maintenance via telomerase [GO:0032212]; post-translational protein modification [GO:0043687]; protein localization to kinetochore [GO:0034501]; protein phosphorylation [GO:0006468]; regulation of cytokinesis [GO:0032465]
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chromocenter [GO:0010369]; chromosome [GO:0005694]; chromosome passenger complex [GO:0032133]; chromosome, centromeric region [GO:0000775]; condensed chromosome, centromeric region [GO:0000779]; cytoplasm [GO:0005737]; kinetochore [GO:0000776]; microtubule cytoskeleton [GO:0015630]; midbody [GO:0030496]; mitotic spindle midzone [GO:1990023]; mitotic spindle pole [GO:0097431]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; spindle microtubule [GO:0005876]; spindle midzone [GO:0051233]; spindle pole centrosome [GO:0031616]
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ATP binding [GO:0005524]; histone H3S28 kinase activity [GO:0044022]; kinase binding [GO:0019900]; protein kinase activity [GO:0004672]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674]
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PF00069;
|
1.10.510.10;
|
Protein kinase superfamily, Ser/Thr protein kinase family, Aurora subfamily
|
PTM: The phosphorylation of Thr-237 requires the binding to INCENP and occurs by means of an autophosphorylation mechanism. Thr-237 phosphorylation is indispensable for the AURKB kinase activity. {ECO:0000250|UniProtKB:Q96GD4}.; PTM: Acetylated at Lys-220 by KAT5 at kinetochores, increasing AURKB activity and promoting accurate chromosome segregation in mitosis. {ECO:0000250|UniProtKB:Q96GD4}.; PTM: Ubiquitinated by different BCR (BTB-CUL3-RBX1) E3 ubiquitin ligase complexes. Ubiquitinated by the BCR(KLHL9-KLHL13) E3 ubiquitin ligase complex, ubiquitination leads to removal from mitotic chromosomes and is required for cytokinesis. During anaphase, the BCR(KLHL21) E3 ubiquitin ligase complex recruits the CPC complex from chromosomes to the spindle midzone and mediates the ubiquitination of AURKB. Ubiquitination of AURKB by BCR(KLHL21) E3 ubiquitin ligase complex may not lead to its degradation by the proteasome. Deubiquitinated by USP35; inhibiting CDH1-mediated degradation of AURKB. {ECO:0000250|UniProtKB:Q96GD4}.
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SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q96GD4}. Chromosome {ECO:0000250|UniProtKB:Q96GD4}. Chromosome, centromere {ECO:0000250|UniProtKB:Q96GD4}. Chromosome, centromere, kinetochore {ECO:0000250|UniProtKB:Q96GD4}. Cytoplasm, cytoskeleton, spindle {ECO:0000250|UniProtKB:Q96GD4}. Midbody {ECO:0000250|UniProtKB:Q96GD4}. Note=Localizes on chromosome arms and inner centromeres from prophase through metaphase and then transferring to the spindle midzone and midbody from anaphase through cytokinesis. Colocalized with gamma tubulin in the midbody. Proper localization of the active, Thr-237-phosphorylated form during metaphase may be dependent upon interaction with SPDYC. Colocalized with SIRT2 during cytokinesis with the midbody. Localization (and probably targeting of the CPC) to the inner centromere occurs predominantly in regions with overlapping mitosis-specific histone phosphorylations H3pT3 and H2ApT12. {ECO:0000250|UniProtKB:Q96GD4}.
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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:0000269|PubMed:24034696}; 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:0000269|PubMed:24034696};
| null | null | null | null |
FUNCTION: Serine/threonine-protein kinase component of the chromosomal passenger complex (CPC), a complex that acts as a key regulator of mitosis (By similarity). The CPC complex has essential functions at the centromere in ensuring correct chromosome alignment and segregation and is required for chromatin-induced microtubule stabilization and spindle assembly (By similarity). Involved in the bipolar attachment of spindle microtubules to kinetochores and is a key regulator for the onset of cytokinesis during mitosis (By similarity). Required for central/midzone spindle assembly and cleavage furrow formation (By similarity). Key component of the cytokinesis checkpoint, a process required to delay abscission to prevent both premature resolution of intercellular chromosome bridges and accumulation of DNA damage: phosphorylates CHMP4C, leading to retain abscission-competent VPS4 (VPS4A and/or VPS4B) at the midbody ring until abscission checkpoint signaling is terminated at late cytokinesis (By similarity). AURKB phosphorylates the CPC complex subunits BIRC5/survivin, CDCA8/borealin and INCENP (By similarity). Phosphorylation of INCENP leads to increased AURKB activity (By similarity). Other known AURKB substrates involved in centromeric functions and mitosis are CENPA, DES/desmin, GPAF, KIF2C, NSUN2, RACGAP1, SEPTIN1, VIM/vimentin, HASPIN, and histone H3 (By similarity). A positive feedback loop involving HASPIN and AURKB contributes to localization of CPC to centromeres (By similarity). Phosphorylation of VIM controls vimentin filament segregation in cytokinetic process, whereas histone H3 is phosphorylated at 'Ser-10' and 'Ser-28' during mitosis (H3S10ph and H3S28ph, respectively) (PubMed:11784863). AURKB is also required for kinetochore localization of BUB1 and SGO1 (By similarity). Phosphorylation of p53/TP53 negatively regulates its transcriptional activity (By similarity). Key regulator of active promoters in resting B- and T-lymphocytes: acts by mediating phosphorylation of H3S28ph at active promoters in resting B-cells, inhibiting RNF2/RING1B-mediated ubiquitination of histone H2A and enhancing binding and activity of the USP16 deubiquitinase at transcribed genes (PubMed:24034696). Acts as an inhibitor of CGAS during mitosis: catalyzes phosphorylation of the N-terminus of CGAS during the G2-M transition, blocking CGAS liquid phase separation and activation, and thereby preventing CGAS-induced autoimmunity (By similarity). Phosphorylates KRT5 during anaphase and telophase (PubMed:29518391). Phosphorylates ATXN10 which promotes phosphorylation of ATXN10 by PLK1 and may play a role in the regulation of cytokinesis and stimulating the proteasomal degradation of ATXN10 (By similarity). {ECO:0000250|UniProtKB:Q96GD4, ECO:0000269|PubMed:11784863, ECO:0000269|PubMed:24034696, ECO:0000269|PubMed:29518391}.
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Mus musculus (Mouse)
|
O70127
|
ABCBB_RAT
|
MSDSVILRSVKKFGEENHAFESDGSHNNDKKSRLQDKMKEGDIRVGFFELFRFSSSKDIWLMLMGGVCALLHGMAQPGILIIFGIMTDIFIKYDIERQELEIPGKACVNNTIVWINSSFHQNMTNGTVCGLVDIESEMIKFSGIYAGVGMTVLILGYFQIRLWVITGARQIRRMRKIYFRRIMRMEIGWFDCTSVGELNSRFADDIEKINDAIADQLAHFLQRMSTAMCGLLLGFYRGWKLTLVILAVSPLIGIGAAVIGLSIAKFTELELKAYAKAGSIADEVLSSIRTVAAFGGENKEVERYEKNLVFAQRWGIWKGMVMGFFTGYMWCLIFFCYALAFWYGSTLVLDEEEYTPGTLVQIFLCVILAAMNIGHASSCLEIFSTGCSAATNIFQTIDRQPVIDCMSGDGYKLDRIKGEIEFHNVTFHYPSRPDVKILDNLSMVIKPGETTALVGSSGAGKSTALQLIQRFYDPCEGMVTLDGHDIRSLNIRWLRDQIGIVEQEPVLFSTTIAENIRFGREDATMEDIVQAAKDANAYNFIMALPQQFDTLVGEGGGQMSGGQKQRVAIARALIRNPKILLLDMATSALDNESEARVQEALNKIQHGHTIISVAHRLSTVRAADVIIGFEHGVAVERGTHEELLERKGVYFMLVTLQSQGDNAHKETSIMGKDATEGGTLERTFSRGSYRDSLRASIRQRSKSQLSLLTHDPPLAVADHKSSYKDSKDNDVLVEEVEPAPVRRILKYNIPEWHYILVGSLSAAINGAVTPIYSLLFSQLLGTFSLLDKEQQRSEIHSMCLFFVILGCVSIFTQFLQGYTFAKSGELLTKRLRKFGFKAMLGQDIGWFDDLRNNPGVLTTRLATDASQVQGATGSQVGMMVNSFTNIIAALLIAFFFSWKLSLIITIFFPFLALSGAVQTKMLTGFASQDKQALEKAGQITSEALSNIRTVAGIGVEGRFIKAFEVELQTSYKTAVRKANIYGLCFAFSQGIAFLANSAAYRYGGYLIAYEGLGFSHVFRVVSSVALSATAVGRTFSYTPSYAKAKISAARFFQLLDRKPPINVYSEAGEKWDNFQGKIDFIDCKFTYPSRPDIQVLNGLSVSVNPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGTVMIDGHDSKKVNIQFLRSNIGIVSQEPVLFDCSIMDNIKYGDNTKEISVERAIAAAKQAQLHDFVMSLPEKYETNVGIQGSQLSRGEKQRIAIARAIVRDPKILLLDEATSALDTESEKTVQTALDKAREGRTCIVIAHRLSTIQNSDIIAVVSQGVVIEKGTHEKLMAQKGAYYKLVITGAPIS
|
7.6.2.-
| null |
bile acid and bile salt transport [GO:0015721]; bile acid metabolic process [GO:0008206]; bile acid signaling pathway [GO:0038183]; canalicular bile acid transport [GO:0015722]; cellular response to xenobiotic stimulus [GO:0071466]; cholesterol homeostasis [GO:0042632]; fatty acid metabolic process [GO:0006631]; lipid homeostasis [GO:0055088]; phospholipid homeostasis [GO:0055091]; positive regulation of bile acid secretion [GO:0120189]; protein ubiquitination [GO:0016567]; regulation of bile acid metabolic process [GO:1904251]; regulation of bile acid secretion [GO:0120188]; regulation of fatty acid beta-oxidation [GO:0031998]; response to estrogen [GO:0043627]; response to ethanol [GO:0045471]; response to organic cyclic compound [GO:0014070]; response to oxidative stress [GO:0006979]; response to xenobiotic stimulus [GO:0009410]; transmembrane transport [GO:0055085]; xenobiotic export from cell [GO:0046618]; xenobiotic metabolic process [GO:0006805]; xenobiotic transmembrane transport [GO:0006855]
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apical part of cell [GO:0045177]; apical plasma membrane [GO:0016324]; cell surface [GO:0009986]; endosome [GO:0005768]; Golgi membrane [GO:0000139]; intercellular canaliculus [GO:0046581]; intracellular canaliculus [GO:0046691]; membrane [GO:0016020]; plasma membrane [GO:0005886]; recycling endosome [GO:0055037]; recycling endosome membrane [GO:0055038]
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ABC-type bile acid transporter activity [GO:0015432]; ABC-type oligopeptide transporter activity [GO:0015421]; ABC-type xenobiotic transporter activity [GO:0008559]; ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; bile acid transmembrane transporter activity [GO:0015125]; canalicular bile acid transmembrane transporter activity [GO:0015126]; carbohydrate transmembrane transporter activity [GO:0015144]
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PF00664;PF00005;
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1.20.1560.10;3.40.50.300;
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ABC transporter superfamily, ABCB family, Multidrug resistance exporter (TC 3.A.1.201) subfamily
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PTM: Ubiquitinated; short-chain ubiquitination regulates cell-Surface expression of ABCB11. {ECO:0000269|PubMed:18829893}.; PTM: N-glycosylated. {ECO:0000250|UniProtKB:O95342}.
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SUBCELLULAR LOCATION: Apical cell membrane {ECO:0000269|PubMed:11113123, ECO:0000269|PubMed:17082223, ECO:0000269|PubMed:9545351}; Multi-pass membrane protein {ECO:0000255}. Recycling endosome membrane {ECO:0000269|PubMed:11113123, ECO:0000269|PubMed:15121884}; Multi-pass membrane protein {ECO:0000255}. Endosome {ECO:0000269|PubMed:11113123}. Cell membrane {ECO:0000269|PubMed:15121884, ECO:0000269|PubMed:22262466, ECO:0000269|PubMed:24643070}; Multi-pass membrane protein {ECO:0000255}. Note=Internalized at the canalicular membrane through interaction with the adapter protein complex 2 (AP-2) (PubMed:22262466). At steady state, localizes in the canalicular membrane but is also present in recycling endosomes. ABCB11 constantly and rapidly exchanges between the two sites through tubulo-vesicles carriers that move along microtubules (PubMed:11113123, PubMed:15121884). Microtubule-dependent trafficking of ABCB11 is enhanced by taurocholate and cAMP and regulated by STK11 through a PKA-mediated pathway (PubMed:11113123, PubMed:24643070). Trafficking of newly synthesized ABCB11 through endosomal compartment to the bile canalicular membrane is accelerated by cAMP but not by taurocholate (PubMed:11113123). Cell membrane expression is up-regulated by short- and medium-chain fatty acids (By similarity). {ECO:0000250|UniProtKB:O95342, ECO:0000269|PubMed:11113123, ECO:0000269|PubMed:15121884, ECO:0000269|PubMed:22262466, ECO:0000269|PubMed:24643070}.
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CATALYTIC ACTIVITY: Reaction=ATP + cholate(in) + H2O = ADP + cholate(out) + H(+) + phosphate; Xref=Rhea:RHEA:50048, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29747, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; Evidence={ECO:0000269|PubMed:16332456, ECO:0000269|PubMed:9545351}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50049; Evidence={ECO:0000269|PubMed:16332456}; CATALYTIC ACTIVITY: Reaction=ATP + H2O + taurocholate(in) = ADP + H(+) + phosphate + taurocholate(out); Xref=Rhea:RHEA:50052, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:36257, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; Evidence={ECO:0000269|PubMed:15901796, ECO:0000269|PubMed:16332456, ECO:0000269|PubMed:17082223, ECO:0000269|PubMed:18985798, ECO:0000269|PubMed:9545351}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50053; Evidence={ECO:0000269|PubMed:15901796, ECO:0000269|PubMed:16332456, ECO:0000269|PubMed:17082223, ECO:0000269|PubMed:18985798}; CATALYTIC ACTIVITY: Reaction=ATP + glycocholate(in) + H2O = ADP + glycocholate(out) + H(+) + phosphate; Xref=Rhea:RHEA:50056, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29746, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; Evidence={ECO:0000269|PubMed:16332456, ECO:0000269|PubMed:9545351}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50057; Evidence={ECO:0000269|PubMed:16332456}; CATALYTIC ACTIVITY: Reaction=ATP + glycochenodeoxycholate(in) + H2O = ADP + glycochenodeoxycholate(out) + H(+) + phosphate; Xref=Rhea:RHEA:50060, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:36252, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; Evidence={ECO:0000269|PubMed:16332456}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50061; Evidence={ECO:0000269|PubMed:16332456}; CATALYTIC ACTIVITY: Reaction=ATP + H2O + taurochenodeoxycholate(in) = ADP + H(+) + phosphate + taurochenodeoxycholate(out); Xref=Rhea:RHEA:50064, ChEBI:CHEBI:9407, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; Evidence={ECO:0000269|PubMed:16332456, ECO:0000269|PubMed:9545351}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50065; Evidence={ECO:0000269|PubMed:16332456}; CATALYTIC ACTIVITY: Reaction=ATP + glycoursodeoxycholate(in) + H2O = ADP + glycoursodeoxycholate(out) + H(+) + phosphate; Xref=Rhea:RHEA:50068, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:132030, ChEBI:CHEBI:456216; Evidence={ECO:0000269|PubMed:16332456}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50069; Evidence={ECO:0000269|PubMed:16332456}; CATALYTIC ACTIVITY: Reaction=ATP + H2O + tauroursodeoxycholate(in) = ADP + H(+) + phosphate + tauroursodeoxycholate(out); Xref=Rhea:RHEA:50072, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:132028, ChEBI:CHEBI:456216; Evidence={ECO:0000269|PubMed:16332456, ECO:0000269|PubMed:9545351}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50073; Evidence={ECO:0000269|PubMed:16332456}; CATALYTIC ACTIVITY: Reaction=ATP + H2O + taurodeoxycholate(in) = ADP + H(+) + phosphate + taurodeoxycholate(out); Xref=Rhea:RHEA:50080, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:36261, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; Evidence={ECO:0000269|PubMed:16332456}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50081; Evidence={ECO:0000269|PubMed:16332456}; CATALYTIC ACTIVITY: Reaction=ATP + H2O + pravastatin(in) = ADP + H(+) + phosphate + pravastatin(out); Xref=Rhea:RHEA:63908, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:63660, ChEBI:CHEBI:456216; Evidence={ECO:0000269|PubMed:15901796}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:63909; Evidence={ECO:0000305|PubMed:15901796};
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BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=9.7 uM for taurocholate {ECO:0000269|PubMed:16332456}; KM=25.7 uM for glycocholate {ECO:0000269|PubMed:16332456}; KM=10.2 uM for taurochenodeoxycholate {ECO:0000269|PubMed:16332456}; KM=5.6 uM for glycochenodeoxycholate {ECO:0000269|PubMed:16332456}; KM=22.2 uM for taurocholate {ECO:0000269|PubMed:18985798}; Vmax=2200 pmol/min/mg enzyme for taurocholate transport {ECO:0000269|PubMed:16332456}; Vmax=237 pmol/min/mg enzyme for taurocholate transport {ECO:0000269|PubMed:18985798};
| null | null | null |
FUNCTION: Catalyzes the transport of the major hydrophobic bile salts, such as taurine and glycine-conjugated cholic acid across the canalicular membrane of hepatocytes in an ATP-dependent manner, therefore participates in hepatic bile acid homeostasis and consequently to lipid homeostasis through regulation of biliary lipid secretion in a bile salts dependent manner (PubMed:15901796, PubMed:16332456, PubMed:17082223, PubMed:18985798, PubMed:9545351). Transports taurine-conjugated bile salts more rapidly than glycine-conjugated bile salts (PubMed:16332456). Also transports non-bile acid compounds, such as pravastatin and fexofenadine in an ATP-dependent manner and may be involved in their biliary excretion (PubMed:15901796, PubMed:18245269). {ECO:0000269|PubMed:15901796, ECO:0000269|PubMed:16332456, ECO:0000269|PubMed:17082223, ECO:0000269|PubMed:18245269, ECO:0000269|PubMed:18985798, ECO:0000269|PubMed:9545351}.
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Rattus norvegicus (Rat)
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O70129
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C5AR1_CAVPO
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MMVTVSYDYDYNSTFLPDGFVDNYVERLSFGDLVAVVIMVVVFLVGVPGNALVVWVTACEARRHINAIWFLNLAAADLLSCLALPILLVSTVHLNHWYFGDTACKVLPSLILLNMYTSILLLATISADRLLLVLSPIWCQRFRGGCLAWTACGLAWVLALLLSSPSFLYRRTHNEHFSFKVYCVTDYGRDISKERAVALVRLLVGFIVPLITLTACYTFLLLRTWSRKATRSAKTVKVVVAVVSSFFVFWLPYQVTGILLAWHSPNSATYRNTKALDAVCVAFAYINCCINPIIYVVAGHGFQGRLLKSLPSVLRNVLTEESLDKRHQSFARSTVDTMPQKSESV
| null | null |
chemotaxis [GO:0006935]; inflammatory response [GO:0006954]; mRNA transcription by RNA polymerase II [GO:0042789]; phospholipase C-activating G protein-coupled receptor signaling pathway [GO:0007200]; positive regulation of cytosolic calcium ion concentration [GO:0007204]; positive regulation of epithelial cell proliferation [GO:0050679]; positive regulation of ERK1 and ERK2 cascade [GO:0070374]
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apical part of cell [GO:0045177]; basolateral plasma membrane [GO:0016323]; cytoplasmic vesicle [GO:0031410]
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complement component C5a receptor activity [GO:0004878]; G protein-coupled receptor activity [GO:0004930]
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PF00001;
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1.20.1070.10;
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G-protein coupled receptor 1 family
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PTM: Sulfation plays a critical role in the association of C5aR with C5a, but no significant role in the ability of the receptor to transduce a signal and mobilize calcium in response to a small peptide agonist. {ECO:0000250|UniProtKB:P21730}.; PTM: Phosphorylated on serine residues in response to C5a binding, resulting in internalization of the receptor and short-term desensitization to C5a. {ECO:0000250|UniProtKB:P21730}.
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SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:9576615}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P21730}. Cytoplasmic vesicle {ECO:0000250|UniProtKB:P21730}. Note=Phosphorylated C5aR colocalizes with ARRB1 and ARRB2 in cytoplasmic vesicles. {ECO:0000250|UniProtKB:P21730}.
| null | null | null | null | null |
FUNCTION: Receptor for the chemotactic and inflammatory peptide anaphylatoxin C5a (PubMed:9576615). The ligand interacts with at least two sites on the receptor: a high-affinity site on the extracellular N-terminus, and a second site in the transmembrane region which activates downstream signaling events. Receptor activation stimulates chemotaxis, granule enzyme release, intracellular calcium release and superoxide anion production (By similarity). {ECO:0000250|UniProtKB:P21730, ECO:0000269|PubMed:9576615}.
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Cavia porcellus (Guinea pig)
|
O70131
|
NINJ1_MOUSE
|
MESGTEEYELNGDLRPGSPGSPDALPPRWGLRNRPINVNHYANKKSAAESMLDIALLMANASQLKAVVEQGNDFAFFVPLVVLISISLVLQIGVGVLLIFLVKYDLNNPAKHAKLDFLNNLATGLVFIIVVVNIFITAFGVQKPVMDVAPRQ
| null | null |
angiogenesis [GO:0001525]; behavior [GO:0007610]; cell adhesion [GO:0007155]; heterotypic cell-cell adhesion [GO:0034113]; hyaloid vascular plexus regression [GO:1990384]; inflammatory response [GO:0006954]; killing of cells of another organism [GO:0031640]; leukocyte chemotaxis involved in inflammatory response [GO:0002232]; macrophage chemotaxis [GO:0048246]; muscle cell differentiation [GO:0042692]; pericyte cell migration [GO:1905351]; positive regulation of angiogenesis [GO:0045766]; positive regulation of cell-matrix adhesion [GO:0001954]; positive regulation of inflammatory response [GO:0050729]; positive regulation of osteoclast development [GO:2001206]; positive regulation of toll-like receptor 4 signaling pathway [GO:0034145]; programmed cell death [GO:0012501]; protein homooligomerization [GO:0051260]; pyroptosis [GO:0070269]; regulation of angiogenesis [GO:0045765]; tissue regeneration [GO:0042246]
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extracellular region [GO:0005576]; filopodium membrane [GO:0031527]; plasma membrane [GO:0005886]; synaptic membrane [GO:0097060]
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cell adhesion mediator activity [GO:0098631]; cell-cell adhesion mediator activity [GO:0098632]; lipopolysaccharide binding [GO:0001530]; membrane destabilizing activity [GO:0140912]
|
PF04923;
| null |
Ninjurin family
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PTM: [Ninjurin-1]: Cleaved by MMP9 protease to generate the Secreted ninjurin-1 form. {ECO:0000269|PubMed:23142597, ECO:0000269|PubMed:32883094}.; PTM: [Ninjurin-1]: N-linked glycosylation is required for homooligomerization. {ECO:0000269|PubMed:28067406}.
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SUBCELLULAR LOCATION: [Ninjurin-1]: Cell membrane {ECO:0000269|PubMed:24917672, ECO:0000269|PubMed:27815839, ECO:0000269|PubMed:31091274, ECO:0000269|PubMed:33472215}; Multi-pass membrane protein {ECO:0000255}. Synaptic cell membrane {ECO:0000269|PubMed:27815839}; Multi-pass membrane protein {ECO:0000255}.; SUBCELLULAR LOCATION: [Secreted ninjurin-1]: Secreted {ECO:0000269|PubMed:23142597, ECO:0000269|PubMed:32883094}.
| null | null | null | null | null |
FUNCTION: [Ninjurin-1]: Effector of necroptotic and pyroptotic programmed cell death that mediates plasma membrane rupture (cytolysis) (PubMed:19557008, PubMed:33472215, PubMed:36468682, PubMed:37196676, PubMed:37198476). Acts downstream of Gasdermin (GSDMA, GSDMB, GSDMC, GSDMD, or GSDME) or MLKL during pyroptosis or necroptosis, respectively: oligomerizes in response to death stimuli and promotes plasma membrane rupture by introducing hydrophilic faces of 2 alpha helices into the hydrophobic membrane, leading to release intracellular molecules named damage-associated molecular patterns (DAMPs) that propagate the inflammatory response (PubMed:33472215, PubMed:37196676, PubMed:37198476). Acts as a regulator of Toll-like receptor 4 (TLR4) signaling triggered by lipopolysaccharide (LPS) during systemic inflammation; directly binds LPS (PubMed:25860173). Involved in leukocyte migration during inflammation by promoting transendothelial migration of macrophages via homotypic binding (PubMed:24917672). Promotes the migration of monocytes across the brain endothelium to central nervous system inflammatory lesions (By similarity). Also acts as a homophilic transmembrane adhesion molecule involved in various processes such as axonal growth, cell chemotaxis and angiogenesis (PubMed:24347169, PubMed:24917672, PubMed:31526566). Promotes cell adhesion by mediating homophilic interactions via its extracellular N-terminal adhesion motif (N-NAM) (PubMed:24917672, PubMed:30510259). Involved in the progression of the inflammatory stress by promoting cell-to-cell interactions between immune cells and endothelial cells (PubMed:24917672, PubMed:30510259). Plays a role in nerve regeneration by promoting maturation of Schwann cells (PubMed:31526566). Acts as a regulator of angiogenesis (PubMed:25766274, PubMed:30354207). Promotes the formation of new vessels by mediating the interaction between capillary pericyte cells and endothelial cells (PubMed:25766274, PubMed:30354207). Also mediates vascular functions in penile tissue as well as vascular formation (PubMed:24979788). Promotes osteoclasts development by enhancing the survival of prefusion osteoclasts (PubMed:30700695). Also involved in striated muscle growth and differentiation (PubMed:31091274). Also involved in cell senescence in a p53/TP53 manner, possibly by acting as an indirect regulator of p53/TP53 mRNA translation (PubMed:23690620, PubMed:29073078). {ECO:0000250|UniProtKB:Q92982, ECO:0000269|PubMed:19557008, ECO:0000269|PubMed:23690620, ECO:0000269|PubMed:24347169, ECO:0000269|PubMed:24917672, ECO:0000269|PubMed:24979788, ECO:0000269|PubMed:25766274, ECO:0000269|PubMed:25860173, ECO:0000269|PubMed:29073078, ECO:0000269|PubMed:30354207, ECO:0000269|PubMed:30510259, ECO:0000269|PubMed:30700695, ECO:0000269|PubMed:31091274, ECO:0000269|PubMed:31526566, ECO:0000269|PubMed:33472215, ECO:0000269|PubMed:36468682, ECO:0000269|PubMed:37196676, ECO:0000269|PubMed:37198476}.; FUNCTION: [Secreted ninjurin-1]: Secreted form generated by cleavage, which has chemotactic activity (PubMed:23142597). Acts as an anti-inflammatory mediator by promoting monocyte recruitment, thereby ameliorating atherosclerosis (PubMed:32883094). {ECO:0000269|PubMed:23142597, ECO:0000269|PubMed:32883094}.
|
Mus musculus (Mouse)
|
O70132
|
FEV_RAT
|
MRQSGTSQPLLINMYLPDPVGDGLFKEGKSPSWGPLSPAVQKGSGQIQLWQFLLELLADRANAGCIAWEGGHGEFKLTDPDEVARRWGERKSKPNMNYDKLSRALRYYYDKNIMSKVHGKRYAYRFDFQGLAQACQPPPAHAHAAAAAAAAAAAAQDGALYKLPAGLAPLPFPGLSKLNLMAASAGVAPAGFSYWPGPNATAAAAATAALYPTPGLQPPPGPFGAVAAASHLGGHYH
| null | null |
maternal behavior [GO:0042711]; neuron fate specification [GO:0048665]; neuron maturation [GO:0042551]; positive regulation of DNA-templated transcription [GO:0045893]; positive regulation of gene expression [GO:0010628]; positive regulation of transcription by RNA polymerase II [GO:0045944]; regulation of transcription by RNA polymerase II [GO:0006357]
|
nuclear speck [GO:0016607]; nucleus [GO:0005634]
|
DNA-binding transcription activator activity, RNA polymerase II-specific [GO:0001228]; DNA-binding transcription factor activity [GO:0003700]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; double-stranded DNA binding [GO:0003690]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]; sequence-specific double-stranded DNA binding [GO:1990837]
|
PF00178;
|
1.10.10.10;
|
ETS family
| null |
SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00237}.
| null | null | null | null | null |
FUNCTION: Functions as a transcriptional regulator. May function as a transcriptional repressor. Functions in the differentiation and the maintenance of the central serotonergic neurons. May play a role in cell growth. {ECO:0000269|PubMed:10575032, ECO:0000269|PubMed:9468386}.
|
Rattus norvegicus (Rat)
|
O70133
|
DHX9_MOUSE
|
MGDIKNFLYAWCGKRKMTPAYEIRAVGNKNRQKFMCEVRVEGFNYAGMGNSTNKKDAQSNAARDFVNYLVRINEVKSEEVPAVGIVPPPPILSDTSDSTASAAEGLPAPMGGPLPPHLALKAEENNSGVESSGYGSPGPTWDRGANLKDYYSRKEEQEVQATLESEEVDLNAGLHGNWTLENAKARLNQYFQKEKIQGEYKYTQVGPDHNRSFIAEMTIYIKQLGRRIFAREHGSNKKLAAQSCALSLVRQLYHLGVIEAYSGLTKKKEGERVEPYKVFLSPDLELQLQNVVQELDLEIVPPPVDPSMPVILNIGKLAHFEPSQRQNAVGVVPWSPPQSNWNPWTSSNIDEGPLAYASTEQISMDLKNELTYQMEQDHNLQSVLQERELLPVKKFEAEILEAISSNSVVIIRGATGCGKTTQVPQYILDDFIQNDRAAECNIVVTQPRRISAVAVAERVAYERGEEPGKSCGYSVRFESILPRPHASIMFCTVGVLLRKLEAGIRGISHVIVDEIHERDINTDFLLVVLRDVVLAYPEVRIVLMSATIDTTMFCEYFFNCPIIEVYGRTFPVQEYFLEDCIQMTQFIPPPKDKKKKDKEDDGGEDDDANCNLICGDEYGPETKLSMSQLNEKETPFELIEALLKYIETLNVPGAVLVFLPGWNLIYTMQKHLENNSHFGSHRYQILPLHSQIPREEQRKVFDPVPDGVTKVILSTNIAETSITINDVVYVIDSCKQKVKLFTAHNNMTNYATVWASKTNLEQRKGRAGRVRPGFCFHLCSRARFDRLETHMTPEMFRTPLHEIALSIKLLRLGGIGQFLAKAIEPPPLDAIIEAEHTLRELDALDANDELTPLGRILAKLPIEPRFGKMMIMGCIFYVGDAVCTISAATCFPEPFISEGKRLGYIHRNFAGNRFSDHVALLSVFQAWDDARMSGEEAEIRFCEQKRLNMATLRMTWEAKVQLKEILINSGFPEDCLLTQVFTNTGPDNNLDVVISLLAFGVYPNVCYHKEKRKILTTEGRNALIHKSSVNCPFSSQDMKYPSPFFVFGEKIRTRAISAKGMTLVTPLQLLLFASKKVQSDGQIVFIDDWIRLQISHEAAACITIRAAMEALVVEVSKQPNIISQLDPVNEHMLNTIRQISRPSAAGINLMIGSVRYGDGPRPPKMARYDNGSGYRRGYGGGGYGGGGYGGGYGSGGFGGGFGSGGGFGGGFNSGGGGFGSGGGGFGSGGGGFGGGGGGFSGGGGGGFGGGRGGGGGGFGGSGGFGNGGGGYGVGGGGYGGGGGGGYGGGSGGYGGGGYGGGEGYSISPNSYRGNYGGGGGGYRGGSQGGYRNNFGGDYRGSSGDYRGSGGGYRGSGGFQRRGYGGGYFGQGRGGGGGGGY
|
3.6.4.13
| null |
alternative mRNA splicing, via spliceosome [GO:0000380]; cellular response to exogenous dsRNA [GO:0071360]; cellular response to heat [GO:0034605]; cellular response to tumor necrosis factor [GO:0071356]; circadian rhythm [GO:0007623]; CRD-mediated mRNA stabilization [GO:0070934]; DNA duplex unwinding [GO:0032508]; DNA-templated transcription termination [GO:0006353]; G-quadruplex DNA unwinding [GO:0044806]; inflammatory response [GO:0006954]; innate immune response [GO:0045087]; miRNA-mediated post-transcriptional gene silencing [GO:0035195]; mRNA transport [GO:0051028]; negative regulation of nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay [GO:1900152]; positive regulation of cytoplasmic translation [GO:2000767]; positive regulation of DNA repair [GO:0045739]; positive regulation of DNA replication [GO:0045740]; positive regulation of DNA topoisomerase (ATP-hydrolyzing) activity [GO:2000373]; positive regulation of fibroblast proliferation [GO:0048146]; positive regulation of inflammatory response [GO:0050729]; positive regulation of innate immune response [GO:0045089]; positive regulation of interferon-alpha production [GO:0032727]; positive regulation of interferon-beta production [GO:0032728]; positive regulation of interleukin-18 production [GO:0032741]; positive regulation of interleukin-6 production [GO:0032755]; positive regulation of NF-kappaB transcription factor activity [GO:0051092]; positive regulation of response to cytokine stimulus [GO:0060760]; positive regulation of RNA export from nucleus [GO:0046833]; positive regulation of transcription by RNA polymerase II [GO:0045944]; positive regulation of tumor necrosis factor production [GO:0032760]; pyroptosis [GO:0070269]; regulation of cytoplasmic translation [GO:2000765]; regulation of defense response to virus by host [GO:0050691]; regulation of mRNA processing [GO:0050684]; RISC complex assembly [GO:0070922]; RNA secondary structure unwinding [GO:0010501]
|
actin cytoskeleton [GO:0015629]; centrosome [GO:0005813]; CRD-mediated mRNA stability complex [GO:0070937]; cytoplasm [GO:0005737]; cytoplasmic ribonucleoprotein granule [GO:0036464]; cytosol [GO:0005829]; nuclear body [GO:0016604]; nuclear stress granule [GO:0097165]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]; perichromatin fibrils [GO:0005726]; ribonucleoprotein complex [GO:1990904]; RISC complex [GO:0016442]; RISC-loading complex [GO:0070578]
|
3'-5' DNA helicase activity [GO:0043138]; 3'-5' DNA/RNA helicase activity [GO:0033679]; 3'-5' RNA helicase activity [GO:0034458]; ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; chromatin DNA binding [GO:0031490]; DNA binding [GO:0003677]; DNA helicase activity [GO:0003678]; DNA replication origin binding [GO:0003688]; double-stranded DNA binding [GO:0003690]; double-stranded RNA binding [GO:0003725]; importin-alpha family protein binding [GO:0061676]; metal ion binding [GO:0046872]; mRNA binding [GO:0003729]; nucleoside triphosphate diphosphatase activity [GO:0047429]; promoter-specific chromatin binding [GO:1990841]; regulatory region RNA binding [GO:0001069]; ribonucleoside triphosphate phosphatase activity [GO:0017111]; RISC complex binding [GO:1905172]; RNA binding [GO:0003723]; RNA helicase activity [GO:0003724]; RNA polymerase binding [GO:0070063]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]; RNA stem-loop binding [GO:0035613]; sequence-specific mRNA binding [GO:1990825]; single-stranded 3'-5' DNA helicase activity [GO:1990518]; single-stranded DNA binding [GO:0003697]; single-stranded RNA binding [GO:0003727]; transcription coactivator activity [GO:0003713]; triplex DNA binding [GO:0045142]
|
PF00270;PF00035;PF21010;PF04408;PF00271;PF07717;
|
1.20.120.1080;3.30.160.20;3.40.50.300;
|
DEAD box helicase family, DEAH subfamily
|
PTM: Methylated. PRMT1-mediated methylation of undefined Arg residues in the nuclear transport domain (NTD) is required for nuclear import of DHX9. {ECO:0000250|UniProtKB:Q08211}.; PTM: Phosphorylated by PRKDC; phosphorylation occurs in a RNA-dependent manner. Phosphorylated by EIF2AK2/PKR; this phosphorylation reduces its association with double-stranded RNA. {ECO:0000250|UniProtKB:Q08211}.
|
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:17303075}. Nucleus, nucleoplasm {ECO:0000250|UniProtKB:Q08211}. Nucleus, nucleolus {ECO:0000269|PubMed:10413677}. Cytoplasm {ECO:0000250|UniProtKB:Q08211}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:Q08211}. Note=Nucleoplasmic shuttling protein. Its nuclear import involves the nucleocytoplasmic transport receptor Importin alpha/Importin beta receptor pathway in a Ran-dependent manner. In interphase, localizes in nuclear stress granules and at perichromatin fibrils and in cytoplasmic ribonucleoprotein granules. Colocalizes with WRN and H2AX at centrosomes in a microtubule-dependent manner following DNA damaging agent treatment. Excluded from the mitotic nucleus as early as prophase and re-entered the nucleus at telophase. Recruited in diffuse and discrete intranuclear foci (GLFG-body) in a NUP98-dependent manner (By similarity). Colocalizes with SP7 in the nucleus (PubMed:17303075). Colocalizes with ACTB at nuclear actin filaments inside the nucleus or at the nuclear pore. Colocalizes with HNRNPC at nuclear ribonucleoprotein complex proteins in the nucleus. Localized in cytoplasmic mRNP granules containing untranslated mRNAs (By similarity). {ECO:0000250|UniProtKB:Q08211, ECO:0000269|PubMed:17303075}.
|
CATALYTIC ACTIVITY: Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.13; Evidence={ECO:0000250|UniProtKB:Q08211};
| null | null | null | null |
FUNCTION: Multifunctional ATP-dependent nucleic acid helicase that unwinds DNA and RNA in a 3' to 5' direction and that plays important roles in many processes, such as DNA replication, transcriptional activation, post-transcriptional RNA regulation, mRNA translation and RNA-mediated gene silencing. Requires a 3'-single-stranded tail as entry site for acid nuclei unwinding activities as well as the binding and hydrolyzing of any of the four ribo- or deoxyribo-nucleotide triphosphates (NTPs). Unwinds numerous nucleic acid substrates such as double-stranded (ds) DNA and RNA, DNA:RNA hybrids, DNA and RNA forks composed of either partially complementary DNA duplexes or DNA:RNA hybrids, respectively, and also DNA and RNA displacement loops (D- and R-loops), triplex-helical DNA (H-DNA) structure and DNA- and RNA-based G-quadruplexes. Binds dsDNA, single-stranded DNA (ssDNA), dsRNA, ssRNA and poly(A)-containing RNA. Binds also to circular dsDNA or dsRNA of either linear and/or circular forms and stimulates the relaxation of supercoiled DNAs catalyzed by topoisomerase TOP2A. Plays a role in DNA replication at origins of replication and cell cycle progression. Plays a role as a transcriptional coactivator acting as a bridging factor between polymerase II holoenzyme and transcription factors or cofactors, such as BRCA1, CREBBP, RELA and SMN1. Binds to the CDKN2A promoter. Plays several roles in post-transcriptional regulation of gene expression. In cooperation with NUP98, promotes pre-mRNA alternative splicing activities of a subset of genes (By similarity). As component of a large PER complex, is involved in the negative regulation of 3' transcriptional termination of circadian target genes such as PER1 and NR1D1 and the control of the circadian rhythms (PubMed:22767893). Acts also as a nuclear resolvase that is able to bind and neutralize harmful massive secondary double-stranded RNA structures formed by inverted-repeat Alu retrotransposon elements that are inserted and transcribed as parts of genes during the process of gene transposition (PubMed:28355180). Involved in the positive regulation of nuclear export of constitutive transport element (CTE)-containing unspliced mRNA. Component of the coding region determinant (CRD)-mediated complex that promotes cytoplasmic MYC mRNA stability. Plays a role in mRNA translation. Positively regulates translation of selected mRNAs through its binding to post-transcriptional control element (PCE) in the 5'-untranslated region (UTR). Involved with LARP6 in the translation stimulation of type I collagen mRNAs for CO1A1 and CO1A2 through binding of a specific stem-loop structure in their 5'-UTRs. Stimulates LIN28A-dependent mRNA translation probably by facilitating ribonucleoprotein remodeling during the process of translation. Also plays a role as a small interfering (siRNA)-loading factor involved in the RNA-induced silencing complex (RISC) loading complex (RLC) assembly, and hence functions in the RISC-mediated gene silencing process. Binds preferentially to short double-stranded RNA, such as those produced during rotavirus intestinal infection (PubMed:28636595). This interaction may mediate NLRP9 inflammasome activation and trigger inflammatory response, including IL18 release and pyroptosis (PubMed:28636595). Finally, mediates the attachment of heterogeneous nuclear ribonucleoproteins (hnRNPs) to actin filaments in the nucleus (By similarity). {ECO:0000250|UniProtKB:Q08211, ECO:0000269|PubMed:22767893, ECO:0000269|PubMed:28355180, ECO:0000269|PubMed:28636595}.
|
Mus musculus (Mouse)
|
O70137
|
ALX3_MOUSE
|
MDPERCAPFSVGPAAGPYAAAGDEAPGPQGTPDAAPHLHPAPPRGPRLSRFPACGPLEPYLPEPAKPPAKYLQDLGPGPVLNGGHFYEGSAEAEEKASKAASFPQLPVDCRGGPRDGPSNVQASPGPCLASLSVPLSPGLPDSMELAKTKSKKRRNRTTFSTFQLEELEKVFQKTHYPDVYAREQLALRTDLTEARVQVWFQNRRAKWRKRERYGKMQEGRNPFTTAYDISVLPRTDSHPQLQNSLWPSPGSGSPGGPCLMSPEGIPSPCMSPYSHSHGNVAGFMGVPASPAAHPGIYSIHGFPPALGGHSFEPSPDGDYKSPSLVSLRMKPKEPPGLLNWTT
| null | null |
embryonic forelimb morphogenesis [GO:0035115]; embryonic hindlimb morphogenesis [GO:0035116]; embryonic skeletal system morphogenesis [GO:0048704]; pattern specification process [GO:0007389]; regulation of apoptotic process [GO:0042981]; regulation of DNA-templated transcription [GO:0006355]; regulation of transcription by RNA polymerase II [GO:0006357]
|
nucleus [GO:0005634]
|
DNA binding [GO:0003677]; DNA-binding transcription factor activity [GO:0003700]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; RNA polymerase II transcription regulatory region sequence-specific DNA binding [GO:0000977]
|
PF00046;
|
1.10.10.60;
|
Paired homeobox family
| null |
SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00108}.
| null | null | null | null | null |
FUNCTION: Transcriptional regulator with a possible role in patterning of mesoderm during development.
|
Mus musculus (Mouse)
|
O70138
|
MMP8_MOUSE
|
MFRLKTLPLLIFLHTQLANAFPVPEHLEEKNIKTAENYLRKFYNLPSNQFRSSRNATMVAEKLKEMQRFFSLAETGKLDAATMGIMEMPRCGVPDSGDFLLTPGSPKWTHTNLTYRIINHTPQLSRAEVKTAIEKAFHVWSVASPLTFTEILQGEADINIAFVSRDHGDNSPFDGPNGILAHAFQPGQGIGGDAHFDSEETWTQDSKNYNLFLVAAHEFGHSLGLSHSTDPGALMYPNYAYREPSTYSLPQDDINGIQTIYGPSDNPIQPTGPSTPKACDPHLRFDATTTLRGEIYFFKDKYFWRRHPQLRTVDLNFISLFWPFLPNGLQAAYEDFDRDLVFLFKGRQYWALSGYDLQQGYPRDISNYGFPRSVQAIDAAVSYNGKTYFFINNQCWRYDNQRRSMDPGYPKSIPSMFPGVNCRVDAVFLQDSFFLFFSGPQYFAFNFVSHRVTRVARSNLWLNCS
|
3.4.24.34
|
COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250}; Note=Binds 3 Ca(2+) ions per subunit. {ECO:0000250}; COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250}; Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000250};
|
cellular response to lipopolysaccharide [GO:0071222]; collagen catabolic process [GO:0030574]; endodermal cell differentiation [GO:0035987]; extracellular matrix organization [GO:0030198]; positive regulation of microglial cell activation [GO:1903980]; positive regulation of neuroinflammatory response [GO:0150078]; positive regulation of tumor necrosis factor production [GO:0032760]; positive regulation of tumor necrosis factor-mediated signaling pathway [GO:1903265]; protein catabolic process [GO:0030163]; proteolysis [GO:0006508]
|
extracellular matrix [GO:0031012]; extracellular space [GO:0005615]
|
calcium ion binding [GO:0005509]; endopeptidase activity [GO:0004175]; metalloendopeptidase activity [GO:0004222]; metallopeptidase activity [GO:0008237]; peptidase activity [GO:0008233]; serine-type endopeptidase activity [GO:0004252]; tumor necrosis factor binding [GO:0043120]; zinc ion binding [GO:0008270]
|
PF00045;PF00413;PF01471;
|
3.40.390.10;2.110.10.10;
|
Peptidase M10A family
| null |
SUBCELLULAR LOCATION: Cytoplasmic granule. Secreted, extracellular space, extracellular matrix. Note=Stored in intracellular granules and released during inflammatory conditions.
|
CATALYTIC ACTIVITY: Reaction=Cleavage of interstitial collagens in the triple helical domain. Unlike EC 3.4.24.7, this enzyme cleaves type III collagen more slowly than type I.; EC=3.4.24.34;
| null | null | null | null |
FUNCTION: Can degrade fibrillar type I, II, and III collagens. May play a role in the degradation of collagen fibers during uterine involution.
|
Mus musculus (Mouse)
|
O70143
|
SHC3_RAT
|
MLPRTKYNRFRNDSVTSVDDLLHSLSVSGSGGKVSAEPAASPYLVSGEALRKAPDDGPGSLGHLLHKVSHLKLSSSGLRGLSSAARERAGARLSGSCSAPSLAAPDGGSATPGSRAPAASMSATRKSRASDEPLPRPPRGAPHASDQVLGSGVTYVVKYLGCIEVLRSMRSLDFSTRTQVTREAISRVCEAVPGAKGAFKKRKPPSKMLSSILGKSNLQFAGMSISLTISTASLNLRTPDSKQIISNHHMRSISFASGGDPDTTDYVAYVAKDPVNRRACHILECCDGLAQDVIGSIGQAFELRFKQYLQCPSKIPALQDRMQSLDEPWTEEEGDGPDHPYYNSVPNKMPPPGGFLDARLKARPHAPDAAQFSGKEQTYYQGRHLGDAFGEDWQRAPTRQGSLDIYSTPEGKAHMVPVGETPTYVNTQPVPPQVWPAATSSTESSPRKDLFDMKPFEDALRNQPLGPVLSKAASVECISPVTPRAPDAKMLEELNAEPWYQGEMSRKEAEALLQEDGDFLVRKSTTNPGSFVLTGMHNGQAKHLLLVDPEGTVRTKDRVFDSISHLITYHLESSLPIVSAGSELCLRQPVERKP
| null | null |
intracellular signal transduction [GO:0035556]; learning or memory [GO:0007611]; synaptic transmission, glutamatergic [GO:0035249]; transmembrane receptor protein tyrosine kinase signaling pathway [GO:0007169]
|
cytosol [GO:0005829]; plasma membrane [GO:0005886]; synapse [GO:0045202]
|
phosphotyrosine residue binding [GO:0001784]; protein tyrosine kinase activity [GO:0004713]; receptor tyrosine kinase binding [GO:0030971]; signaling receptor binding [GO:0005102]
|
PF00640;PF00017;
|
2.30.29.30;3.30.505.10;
| null |
PTM: Tyrosine phosphorylated. {ECO:0000250}.
| null | null | null | null | null | null |
FUNCTION: Signaling adapter that couples activated growth factor receptors to signaling pathway in neurons. Involved in the signal transduction pathways of neurotrophin-activated Trk receptors in cortical neurons (By similarity). {ECO:0000250}.
|
Rattus norvegicus (Rat)
|
O70145
|
NCF2_MOUSE
|
MSLAEAIRLWNEGVLAADKKDWKGALEAFSEVQDPHSRICFNIGCVNTILENLQAAEQAFTKSINRDKHSAVAYFQRGMLYYRMEKYDLAIKDLKEALTQLRGNQLIDYKILGLQFKLFACEVLYNIALMHAKKEEWKKAEEQLALATNMKSEPRHSKIDKAMESIWKQKLFEPVVIPVGRLFRPNERQVAQLAKKDYLGKATVVASVVHQDNFSGFAPLQPQSAEPPPRPKTPEIFRALEGEAHRVLFGFVPETPEELQVMPGNIVFVLKKGSDNWATVMFNGQKGLVPCNYLEPVELRIHPQSQPQEDTSPESDIPPPPNSSPPGRLQLSPGHKQKEPKELKLSVPMPYMLKVHYKYTVVMETRLGLPYSQLRNMVSKKLALSPEHTKLSYRRRDSHELLLLSEESMKDAWGQVKNYCLTLWCEHTVGDQGLIDEPIQRENSDASKQTTEPQPKEGTQVVAIFSYEAAQPEDLEFVEGDVILVLSHVNEEWLEGECKGKVGIFPKAFVEGCAAKNLEGIPREV
| null | null |
cellular response to hormone stimulus [GO:0032870]; NADP catabolic process [GO:0006742]; phagocytosis [GO:0006909]; positive regulation of blood pressure [GO:0045777]; positive regulation of neuron apoptotic process [GO:0043525]; regulation of reactive oxygen species biosynthetic process [GO:1903426]; respiratory burst [GO:0045730]; response to glucose [GO:0009749]; response to lipopolysaccharide [GO:0032496]; response to organic cyclic compound [GO:0014070]; superoxide anion generation [GO:0042554]; superoxide metabolic process [GO:0006801]
|
acrosomal vesicle [GO:0001669]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; NADPH oxidase complex [GO:0043020]
|
small GTPase binding [GO:0031267]; superoxide-generating NADPH oxidase activator activity [GO:0016176]
|
PF00564;PF00018;PF00515;PF13181;
|
2.30.30.40;1.25.40.10;
|
NCF2/NOXA1 family
| null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P19878}.
| null | null | null | null | null |
FUNCTION: NCF2, NCF1, and a membrane bound cytochrome b558 are required for activation of the latent NADPH oxidase (necessary for superoxide production). {ECO:0000250|UniProtKB:P19878}.
|
Mus musculus (Mouse)
|
O70146
|
TESK1_MOUSE
|
MAGERPPLRGPGPGEAPGEGPGGAGGGPGRGRPSSYRALRSAVSSLARVDDFDCAEKIGAGFFSEVYKVRHRQSGQVMVLKMNKLPSNRSNTLREVQLMNRLRHPNILRFMGVCVHQGQLHALTEYMNGGTLEQLLSSPEPLSWPVRLHLALDIAQGLRYLHAKGVFHRDLTSKNCLVRREDRGFTAVVGDFGLAEKIPVYREGTRKEPLAVVGSPYWMAPEVLRGELYDEKADVFAFGIVLCELIARVPADPDYLPRTEDFGLDVPAFRTLVGNDCPLPFLLLAIHCCSMEPSTRAPFTEITQHLEQILEQQPEATPLAKPPLTKAPLTYNQGSVPRGGPSATLPRPDPRLSRSRSDLFLPPSPESPPSWGDNLTRVNPFSLREDLRGGKIKLLDTPCKPATPLPLVPPSPLTSTQLPLVTTPDILVQPETPVRRCRSLPSSPELPRRMETALPGPGPSPMGPTEERMDCEGSSPEPEPPGLAPQLPLAVATDNFISTCSSASQPWSPRSGPPLNNNPPAVVVNSPQGWAREPWNRAQHSLPRAAALERTEPSPPPSAPREPEEGLPCPGCCLGPFSFGFLSMCPRPTPAVARYRNLNCEAGSLLCHRGHHAKPPTPSLQLPGARS
|
2.7.12.1
|
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; COFACTOR: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
|
actin cytoskeleton organization [GO:0030036]; establishment of vesicle localization [GO:0051650]; negative regulation of cilium assembly [GO:1902018]; negative regulation of phosphorylation [GO:0042326]; negative regulation of protein autophosphorylation [GO:0031953]; phosphorylation [GO:0016310]; podocyte cell migration [GO:0090521]; positive regulation of protein localization to nucleus [GO:1900182]; positive regulation of protein phosphorylation [GO:0001934]; positive regulation of stress fiber assembly [GO:0051496]; positive regulation of substrate adhesion-dependent cell spreading [GO:1900026]; regulation of actin cytoskeleton organization [GO:0032956]; regulation of protein localization [GO:0032880]; spermatogenesis [GO:0007283]
|
centrosome [GO:0005813]; cytoplasm [GO:0005737]; cytoplasmic vesicle [GO:0031410]; lamellipodium [GO:0030027]; nucleus [GO:0005634]; perinuclear region of cytoplasm [GO:0048471]
|
ATP binding [GO:0005524]; metal ion binding [GO:0046872]; protein kinase activity [GO:0004672]; protein kinase binding [GO:0019901]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674]; protein serine/threonine/tyrosine kinase activity [GO:0004712]; protein tyrosine kinase activity [GO:0004713]
|
PF07714;
|
1.10.510.10;
|
Protein kinase superfamily, TKL Ser/Thr protein kinase family
|
PTM: Autophosphorylated on serine and tyrosine residues. {ECO:0000250|UniProtKB:Q63572}.
|
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q15569}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q63572}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:Q15569}. Cell projection, lamellipodium {ECO:0000250|UniProtKB:Q63572}. Note=Colocalizes with SPRY4 in vesicular spots in the cytoplasm (By similarity). Localized to F-actin-rich lamellipodia at the cell periphery following fibronectin-mediated cell adhesion of Schwann cells (By similarity). {ECO:0000250|UniProtKB:Q15569, ECO:0000250|UniProtKB:Q63572}.
|
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=2.7.12.1; 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=2.7.12.1; 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=2.7.12.1;
| null | null | null | null |
FUNCTION: Dual specificity protein kinase activity catalyzing autophosphorylation and phosphorylation of exogenous substrates on both serine/threonine and tyrosine residues (By similarity). Regulates the cellular cytoskeleton by enhancing actin stress fiber formation via phosphorylation of cofilin and by preventing microtubule breakdown via inhibition of TAOK1/MARKK kinase activity (By similarity). Inhibits podocyte motility via regulation of actin cytoskeletal dynamics and phosphorylation of CFL1 (PubMed:30115939). Positively regulates integrin-mediated cell spreading, via phosphorylation of cofilin (By similarity). Suppresses ciliogenesis via multiple pathways; phosphorylation of CFL1, suppression of ciliary vesicle directional trafficking to the ciliary base, and by facilitating YAP1 nuclear localization where it acts as a transcriptional corepressor of the TEAD4 target genes AURKA and PLK1 (By similarity). Probably plays a central role at and after the meiotic phase of spermatogenesis (By similarity). {ECO:0000250|UniProtKB:Q15569, ECO:0000250|UniProtKB:Q63572, ECO:0000269|PubMed:30115939}.
|
Mus musculus (Mouse)
|
O70150
|
KCC1B_RAT
|
MLLLKKQTEDISSVYEIREKLGSGAFSEVMLAQERGSAHLVALKCIPKKALRGKEALVENEIAVLRRISHPNIVALEDVHESPSHLYLAMELVTGGELFDRIMERGSYTEKDASHLVGQVLGAVSYLHSLGIVHRDLKPENLLYATPFEDSKIMVSDFGLSKIQAGNMLGTACGTPGYVAPELLEQKPYGKAVDVWALGVISYILLCGYPPFYDESDPELFSQILRASYEFDSPFWDDISESAKDFIRHLLERDPQKRFTCQQALQHLWISGDAALDRDILGSVSEQIQKNFARTHWKRAFNATSFLRHIRKLGQSPEGEEASRQGMTRHSHPGLGTSQSPKW
|
2.7.11.17
| null |
phosphorylation [GO:0016310]
|
cytoplasm [GO:0005737]; nucleus [GO:0005634]
|
ATP binding [GO:0005524]; calmodulin binding [GO:0005516]; calmodulin-dependent protein kinase activity [GO:0004683]; protein serine kinase activity [GO:0106310]
|
PF00069;
|
1.10.510.10;
|
Protein kinase superfamily, CAMK Ser/Thr protein kinase family, CaMK subfamily
|
PTM: Isoform 1 and isoform 2 are phosphorylated by CAMKK1. {ECO:0000305}.
|
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {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=2.7.11.17; 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=2.7.11.17;
| null | null | null | null |
FUNCTION: Calcium/calmodulin-dependent protein kinase belonging to a proposed calcium-triggered signaling cascade. In vitro, isoform 1 and isoform 2 phosphorylate CREB1, SYN1/synapsin I. Phosphorylates and activates CAMK1. {ECO:0000269|PubMed:9405489}.
|
Rattus norvegicus (Rat)
|
O70152
|
DPM1_MOUSE
|
MASTGASRSLAASPRPPQGRSSRQDKYSVLLPTYNERENLPLIVWLLVKSFSESAINYEIIIIDDGSPDGTREVAEQLAEIYGPDRILLRPREKKLGLGTAYIHGIKHATGNYVIIMDADLSHHPKFIPEFIRKQKEGNFDIVSGTRYKGNGGVYGWDLKRKIISRGANFITQILLRPGASDLTGSFRLYRKEVLQKLIEKCVSKGYVFQMEMIVRARQMNYTIGEVPISFVDRVYGESKLGGNEIVSFLKGLLTLFATT
|
2.4.1.83
|
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:Q8U4M3}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250|UniProtKB:Q8U4M3}; Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250|UniProtKB:Q8U4M3}; Note=Binds 1 divalent metal cation. {ECO:0000250|UniProtKB:Q8U4M3};
|
dolichol metabolic process [GO:0019348]; dolichol-linked oligosaccharide biosynthetic process [GO:0006488]; GDP-mannose metabolic process [GO:0019673]; GPI anchor biosynthetic process [GO:0006506]; protein mannosylation [GO:0035268]; protein O-linked mannosylation [GO:0035269]
|
dolichol-phosphate-mannose synthase complex [GO:0033185]; endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]; membrane [GO:0016020]
|
alcohol binding [GO:0043178]; dolichyl-phosphate beta-D-mannosyltransferase activity [GO:0004582]; dolichyl-phosphate-mannose-protein mannosyltransferase activity [GO:0004169]; mannose binding [GO:0005537]; metal ion binding [GO:0046872]
|
PF00535;
| null |
Glycosyltransferase 2 family
| null |
SUBCELLULAR LOCATION: Endoplasmic reticulum.
|
CATALYTIC ACTIVITY: Reaction=a dolichyl phosphate + GDP-alpha-D-mannose = a dolichyl beta-D-mannosyl phosphate + GDP; Xref=Rhea:RHEA:21184, Rhea:RHEA-COMP:9517, Rhea:RHEA-COMP:9527, ChEBI:CHEBI:57527, ChEBI:CHEBI:57683, ChEBI:CHEBI:58189, ChEBI:CHEBI:58211; EC=2.4.1.83; Evidence={ECO:0000305|PubMed:9535917};
| null |
PATHWAY: Protein modification; protein glycosylation. {ECO:0000269|PubMed:9535917}.
| null | null |
FUNCTION: Transfers mannose from GDP-mannose to dolichol monophosphate to form dolichol phosphate mannose (Dol-P-Man) which is the mannosyl donor in pathways leading to N-glycosylation, glycosyl phosphatidylinositol membrane anchoring, and O-mannosylation of proteins; catalytic subunit of the dolichol-phosphate mannose (DPM) synthase complex. {ECO:0000305|PubMed:9535917}.
|
Mus musculus (Mouse)
|
O70156
|
OLR1_RAT
|
MAFDDKMKPVNGQPDQKSCGKKPKGLHLLSSTWWCPAAVTLAILCLVLSVTLIVQQTQLLQVSDLLKQYQANLTQQDHILEGQMSAQKKAENASQESKRELKEQIDTLTWKLNEKSKEQEKLLQQNQNLQEALQRAVNASEESKWELKEQIDILNWKLNGISKEQKELLQQNQNLQEALQKAEKYSEESQRELKEQIDTLSWKLNEKSKEQEELLQQNQNLQEALQRAANSSGPCPQDWIWHKENCYLFHGPFNWEKSRENCLSLDAQLLQISTTDDLNFVLQATSHSTSPFWMGLHRKNPNHPWLWENGSPLSFQFFRTRGVSLQMYSSGTCAYIQGGVVFAENCILTAFSICQKKANLLLTQ
| null | null |
immune system process [GO:0002376]; inflammatory response [GO:0006954]; leukocyte cell-cell adhesion [GO:0007159]; lipoprotein metabolic process [GO:0042157]; negative regulation of gene expression [GO:0010629]; response to hydrogen peroxide [GO:0042542]
|
extracellular region [GO:0005576]; membrane raft [GO:0045121]; plasma membrane [GO:0005886]; receptor complex [GO:0043235]
|
carbohydrate binding [GO:0030246]; identical protein binding [GO:0042802]; low-density lipoprotein particle receptor activity [GO:0005041]
|
PF00059;
|
3.10.100.10;
| null |
PTM: N-glycosylated. {ECO:0000250}.
|
SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Lipid-anchor {ECO:0000250}. Cell membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}. Membrane raft {ECO:0000250}. Secreted {ECO:0000250}. Note=A secreted form also exists. Localization to membrane rafts requires palmitoylation (By similarity). {ECO:0000250}.
| null | null | null | null | null |
FUNCTION: Receptor that mediates the recognition, internalization and degradation of oxidatively modified low density lipoprotein (oxLDL) by vascular endothelial cells. OxLDL is a marker of atherosclerosis that induces vascular endothelial cell activation and dysfunction, resulting in pro-inflammatory responses, pro-oxidative conditions and apoptosis. Its association with oxLDL induces the activation of NF-kappa-B through an increased production of intracellular reactive oxygen and a variety of pro-atherogenic cellular responses including a reduction of nitric oxide (NO) release, monocyte adhesion and apoptosis. In addition to binding oxLDL, it acts as a receptor for the HSP70 protein involved in antigen cross-presentation to naive T-cells in dendritic cells, thereby participating in cell-mediated antigen cross-presentation. Also involved in inflammatory process, by acting as a leukocyte-adhesion molecule at the vascular interface in endotoxin-induced inflammation. Also acts as a receptor for advanced glycation end (AGE) products, activated platelets, monocytes, apoptotic cells and both Gram-negative and Gram-positive bacteria. {ECO:0000269|PubMed:12538855, ECO:0000269|PubMed:9837956}.
|
Rattus norvegicus (Rat)
|
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