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
O22131
LBD18_ARATH
MSGGGNTITAVGGGGGGCGGGGSSGGGGSSGGGGGGPCGACKFLRRKCVPGCIFAPYFDSEQGSAYFAAVHKVFGASNVSKLLLHIPVHRRSDAVVTICYEAQARIRDPIYGCVAHIFALQQQVVNLQAEVSYLQAHLASLELPQPQTRPQPMPQPQPLFFTPPPPLAITDLPASVSPLPSTYDLASIFDQTTSSSAWATQQRRFIDPRHQYGVSSSSSSVAVGLGGENSHDLQALAHELLHRQGSPPPAATDHSPSRTMSR
null
null
callus formation [GO:1990110]; hormone-mediated signaling pathway [GO:0009755]; lateral root formation [GO:0010311]; positive regulation of DNA-templated transcription [GO:0045893]; xylem development [GO:0010089]
nucleus [GO:0005634]
null
PF03195;
null
LOB domain-containing protein family
null
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:19088331}.
null
null
null
null
null
FUNCTION: Involved in the positive regulation of tracheary element (TE) differentiation. Involved in a positive feedback loop that maintains or promotes NAC030/VND7 expression that regulates TE differentiation-related genes (PubMed:19088331). Functions in the initiation and emergence of lateral roots, in conjunction with LBD16, downstream of ARF7 and ARF19 (PubMed:19717544, PubMed:23749813). Transcriptional activator that directly regulates EXPA14, a gene encoding a cell wall-loosening factor that promotes lateral root emergence. Activates EXPA14 by directly binding to a specific region of its promoter (PubMed:22974309). Transcriptional activator that directly regulates EXPA17, a gene encoding a cell wall-loosening factor that promotes lateral root emergence (PubMed:23872272). Acts downstream of the auxin influx carriers AUX1 and LAX1 in the regulation of lateral root initiation and development (PubMed:26059335). {ECO:0000269|PubMed:19088331, ECO:0000269|PubMed:19717544, ECO:0000269|PubMed:22974309, ECO:0000269|PubMed:23749813, ECO:0000269|PubMed:23872272, ECO:0000269|PubMed:26059335}.
Arabidopsis thaliana (Mouse-ear cress)
O22133
BEN1_ARATH
MVREEQEEDDNNNNNNGGGERKLLVADETVPSLLDETGLVCVTGGSGFVASWLIMRLLQRGYSVRATVRTNSEGNKKDISYLTELPFASERLQIFTADLNEPESFKPAIEGCKAVFHVAHPMDPNSNETEETVTKRTVQGLMGILKSCLDAKTVKRFFYTSSAVTVFYSGGNGGGGGEVDESVWSDVEVFRNQKEKRVSSSYVVSKMAAETAALEFGGKNGLEVVTLVIPLVVGPFISSSLPSSVFISLAMLFGNYKEKYLFDTYNMVHIDDVARAMIFLLEKPVAKGRYICSSVEMKIDEVFEFLSTKFPQFQLPSIDLNKYKVEKRMGLSSKKLKSAGFEFKYGAEEIFSGAIRSCQARGFL
1.1.1.-
null
brassinosteroid biosynthetic process [GO:0016132]; brassinosteroid metabolic process [GO:0016131]; regulation of brassinosteroid biosynthetic process [GO:0010422]; response to absence of light [GO:0009646]
cytoplasm [GO:0005737]
oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor [GO:0016616]
PF01370;
3.40.50.720;
NAD(P)-dependent epimerase/dehydratase family
null
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17521414}.
null
null
PATHWAY: Plant hormone biosynthesis; brassinosteroid biosynthesis. {ECO:0000269|PubMed:17521414}.
null
null
FUNCTION: Element of the brassinosteroid metabolic pathway that regulates typhasterol (TY), castasterone (CS) and brassinolide (BL) levels (PubMed:17521414). Involved in the control of organ elongation (PubMed:17521414, PubMed:23893742). {ECO:0000269|PubMed:17521414, ECO:0000269|PubMed:23893742}.
Arabidopsis thaliana (Mouse-ear cress)
O22145
OSGP2_ARATH
MVRLFLTLSPAISRFNLYPGISILARNNNSLRLQKHHKLKTKTPTFSLISPSSSPNFQRTRFYSTETRISSLPYSENPNFDDNLVVLGIETSCDDTAAAVVRGNGEILSQVISSQAELLVQYGGVAPKQAEEAHSRVIDKVVQDALDKANLTEKDLSAVAVTIGPGLSLCLRVGVRKARRVAGNFSLPIVGVHHMEAHALVARLVEQELSFPFMALLISGGHNLLVLAHKLGQYTQLGTTVDDAIGEAFDKTAKWLGLDMHRSGGPAVEELALEGDAKSVKFNVPMKYHKDCNFSYAGLKTQVRLAIEAKEIDAKCPVSSATNEDRRNRADIAASFQRVAVLHLEEKCERAIDWALELEPSIKHMVISGGVASNKYVRLRLNNIVENKNLKLVCPPPSLCTDNGVMVAWTGLEHFRVGRYDPPPPATEPEDYVYDLRPRWPLGEEYAKGRSEARSMRTARIHPSLTSIIRADSLQQQTQT
2.3.1.234
COFACTOR: Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240; Evidence={ECO:0000255|HAMAP-Rule:MF_03179}; Note=Binds 1 divalent metal cation per subunit. {ECO:0000255|HAMAP-Rule:MF_03179};
embryo development ending in seed dormancy [GO:0009793]; mitochondrial tRNA threonylcarbamoyladenosine modification [GO:0072670]
mitochondrial inner membrane [GO:0005743]
metal ion binding [GO:0046872]; N(6)-L-threonylcarbamoyladenine synthase activity [GO:0061711]
PF00814;
3.30.420.40;
KAE1 / TsaD family
null
SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000255|HAMAP-Rule:MF_03179, ECO:0000269|PubMed:19694617}; Peripheral membrane protein {ECO:0000269|PubMed:19694617}.
CATALYTIC ACTIVITY: Reaction=adenosine(37) in tRNA + L-threonylcarbamoyladenylate = AMP + H(+) + N(6)-L-threonylcarbamoyladenosine(37) in tRNA; Xref=Rhea:RHEA:37059, Rhea:RHEA-COMP:10162, Rhea:RHEA-COMP:10163, ChEBI:CHEBI:15378, ChEBI:CHEBI:73682, ChEBI:CHEBI:74411, ChEBI:CHEBI:74418, ChEBI:CHEBI:456215; EC=2.3.1.234; Evidence={ECO:0000255|HAMAP-Rule:MF_03179};
null
null
null
null
FUNCTION: Required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in mitochondrial tRNAs that read codons beginning with adenine. Probably involved in the transfer of the threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the N6 group of A37. Involved in mitochondrial genome maintenance (By similarity). May have a role in embryonic development in plants. {ECO:0000255|HAMAP-Rule:MF_03179}.
Arabidopsis thaliana (Mouse-ear cress)
O22149
PME17_ARATH
MMAFRAYIINFVILCILVASTVSGYNQKDVKAWCSQTPNPKPCEYFLTHNSNNEPIKSESEFLKISMKLVLDRAILAKTHAFTLGPKCRDTREKAAWEDCIKLYDLTVSKINETMDPNVKCSKLDAQTWLSTALTNLDTCRAGFLELGVTDIVLPLMSNNVSNLLCNTLAINKVPFNYTPPEKDGFPSWVKPGDRKLLQSSTPKDNAVVAKDGSGNFKTIKEAIDAASGSGRFVIYVKQGVYSENLEIRKKNVMLRGDGIGKTIITGSKSVGGGTTTFNSATVAAVGDGFIARGITFRNTAGASNEQAVALRSGSDLSVFYQCSFEAYQDTLYVHSNRQFYRDCDVYGTVDFIFGNAAAVLQNCNIFARRPRSKTNTITAQGRSDPNQNTGIIIHNSRVTAASDLRPVLGSTKTYLGRPWRQYSRTVFMKTSLDSLIDPRGWLEWDGNFALKTLFYAEFQNTGPGASTSGRVTWPGFRVLGSASEASKFTVGTFLAGGSWIPSSVPFTSGL
3.1.1.11
null
cell wall modification [GO:0042545]; defense response to Gram-negative bacterium [GO:0050829]; pectin catabolic process [GO:0045490]; response to bacterium [GO:0009617]; response to fungus [GO:0009620]
extracellular region [GO:0005576]
aspartyl esterase activity [GO:0045330]; pectinesterase activity [GO:0030599]; pectinesterase inhibitor activity [GO:0046910]
PF01095;PF04043;
1.20.140.40;2.160.20.10;
PMEI family; Pectinesterase family
null
SUBCELLULAR LOCATION: Secreted, cell wall {ECO:0000250}.
CATALYTIC ACTIVITY: Reaction=[(1->4)-alpha-D-galacturonosyl methyl ester](n) + n H2O = [(1->4)-alpha-D-galacturonosyl](n) + n H(+) + n methanol; Xref=Rhea:RHEA:22380, Rhea:RHEA-COMP:14570, Rhea:RHEA-COMP:14573, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17790, ChEBI:CHEBI:140522, ChEBI:CHEBI:140523; EC=3.1.1.11;
null
PATHWAY: Glycan metabolism; pectin degradation; 2-dehydro-3-deoxy-D-gluconate from pectin: step 1/5.
null
null
FUNCTION: Acts in the modification of cell walls via demethylesterification of cell wall pectin. {ECO:0000250}.
Arabidopsis thaliana (Mouse-ear cress)
O22152
YAB1_ARATH
MSMSSMSSPSSAVCSPDHFSPSDHLCYVQCNFCQTILAVNVPYTSLFKTVTVRCGCCTNLLSVNMRSYVLPASNQLQLQLGPHSYFNPQDILEELRDAPSNMNMMMMNQHPTMNDIPSFMDLHQQHEIPKAPPVNRPPEKRQRVPSAYNRFIKEEIQRIKAGNPDISHREAFSAAAKNWAHFPHIHFGLVPDNQPVKKTNMPQQEGEDNMVMKEGFYAPAAANVGVTPY
null
COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000269|PubMed:10323860, ECO:0000269|PubMed:11092895}; Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000269|PubMed:10323860, ECO:0000269|PubMed:11092895};
abaxial cell fate specification [GO:0010158]; cell fate commitment [GO:0045165]; fruit development [GO:0010154]; inflorescence meristem growth [GO:0010450]; meristem structural organization [GO:0009933]; polarity specification of adaxial/abaxial axis [GO:0009944]; regulation of flower development [GO:0009909]; regulation of leaf development [GO:2000024]; regulation of shoot apical meristem development [GO:1902183]; specification of floral organ identity [GO:0010093]; specification of plant organ position [GO:0090706]
nucleus [GO:0005634]
DNA-binding transcription factor activity [GO:0003700]; metal ion binding [GO:0046872]; transcription cis-regulatory region binding [GO:0000976]
PF04690;
1.10.30.10;
YABBY family
null
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10323860}.
null
null
null
null
null
FUNCTION: Involved in the abaxial cell fate determination during embryogenesis and organogenesis. Regulates the initiation of embryonic shoot apical meristem (SAM) development (PubMed:10323860, PubMed:10331982, PubMed:10457020, PubMed:11812777, PubMed:12417699, PubMed:19837869, PubMed:9878633, Ref.3, Ref.6). Required during flower formation and development, particularly for the patterning of floral organs. Positive regulator of class B (AP3 and PI) activity in whorls 2 and 3. Negative regulator of class B activity in whorl 1 and of SUP activity in whorl 3. Interacts with class A proteins (AP1, AP2 and LUG) to repress class C (AG) activity in whorls 1 and 2. Contributes to the repression of KNOX genes (STM, KNAT1/BP and KNAT2) to avoid ectopic meristems. Binds DNA without sequence specificity. In vitro, can compete and displace the AP1 protein binding to DNA containing CArG box (PubMed:10323860, PubMed:10331982, PubMed:10457020, PubMed:11812777, PubMed:12417699, PubMed:9878633, Ref.3, Ref.6). {ECO:0000269|PubMed:10323860, ECO:0000269|PubMed:10331982, ECO:0000269|PubMed:10457020, ECO:0000269|PubMed:11812777, ECO:0000269|PubMed:12417699, ECO:0000269|PubMed:19837869, ECO:0000269|PubMed:9878633, ECO:0000269|Ref.3, ECO:0000269|Ref.6}.
Arabidopsis thaliana (Mouse-ear cress)
O22197
RHC1A_ARATH
MSSSRNTHWCHRCQRAVRLHGQEPVCFYCGGGFVEELDMAQASPFDMFRSHRGVVERDQTFDLMDAFSVFMRNRLAERSHDREIRGRTISSGPENFPGLAPLLIFGGQVPYRLTGDNAVEALFNGGSPGIGITRGNTGDYFFGPGLEELFEQLSAGTTRRGPPPAPRSAIDALPTIKIAQRHLRSSDSNCPVCKDEFELGSEAKQMPCNHIYHSDCIVPWLVQHNSCPVCRQELPSASGPSSSQNRTTPTRNYRSSSSSSSSNSRENGNERRNPFSSFWPFRSSGSSSSSTQNRGGTRNSDTSDENHNYHQQQHQQSYMGYSGWPFDY
2.3.2.27
null
negative regulation of gibberellic acid mediated signaling pathway [GO:0009938]; protein ubiquitination [GO:0016567]; response to salt stress [GO:0009651]; ubiquitin-dependent protein catabolic process [GO:0006511]
cytoplasm [GO:0005737]; nucleus [GO:0005634]; plant-type cell wall [GO:0009505]
metal ion binding [GO:0046872]; ubiquitin protein ligase activity [GO:0061630]
PF13639;PF14369;
3.30.40.10;
null
null
null
CATALYTIC ACTIVITY: Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.; EC=2.3.2.27;
null
PATHWAY: Protein modification; protein ubiquitination. {ECO:0000305}.
null
null
FUNCTION: Probable E3 ubiquitin-protein ligase that may possess E3 ubiquitin ligase activity in vitro. {ECO:0000250|UniProtKB:Q9ZT50}.
Arabidopsis thaliana (Mouse-ear cress)
O22203
C98A3_ARATH
MSWFLIAVATIAAVVSYKLIQRLRYKFPPGPSPKPIVGNLYDIKPVRFRCYYEWAQSYGPIISVWIGSILNVVVSSAELAKEVLKEHDQKLADRHRNRSTEAFSRNGQDLIWADYGPHYVKVRKVCTLELFTPKRLESLRPIREDEVTAMVESVFRDCNLPENRAKGLQLRKYLGAVAFNNITRLAFGKRFMNAEGVVDEQGLEFKAIVSNGLKLGASLSIAEHIPWLRWMFPADEKAFAEHGARRDRLTRAIMEEHTLARQKSSGAKQHFVDALLTLKDQYDLSEDTIIGLLWDMITAGMDTTAITAEWAMAEMIKNPRVQQKVQEEFDRVVGLDRILTEADFSRLPYLQCVVKESFRLHPPTPLMLPHRSNADVKIGGYDIPKGSNVHVNVWAVARDPAVWKNPFEFRPERFLEEDVDMKGHDFRLLPFGAGRRVCPGAQLGINLVTSMMSHLLHHFVWTPPQGTKPEEIDMSENPGLVTYMRTPVQAVATPRLPSDLYKRVPYDM
1.14.-.-
COFACTOR: Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250};
coumarin biosynthetic process [GO:0009805]; flavonoid biosynthetic process [GO:0009813]; lignin biosynthetic process [GO:0009809]; phenylpropanoid biosynthetic process [GO:0009699]
cytosol [GO:0005829]; endoplasmic reticulum [GO:0005783]; intracellular membrane-bounded organelle [GO:0043231]; membrane [GO:0016020]; mitochondrion [GO:0005739]
heme binding [GO:0020037]; identical protein binding [GO:0042802]; iron ion binding [GO:0005506]; monooxygenase activity [GO:0004497]; oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen [GO:0016705]; p-coumarate 3-hydroxylase activity [GO:0046409]
PF00067;
1.10.630.10;
Cytochrome P450 family
null
SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}.
null
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=7 uM for 5-O-(4-coumaroyl) shikimate {ECO:0000269|PubMed:11429408}; KM=18 uM for 5-O-(4-coumaroyl) quinate {ECO:0000269|PubMed:11429408}; Note=kcat is 612 min(-1) with 5-O-(4-coumaroyl) shikimate as substrate. kcat is 399 min(-1) with 5-O-(4-coumaroyl) quinate as substrate. {ECO:0000269|PubMed:11429408};
null
null
null
FUNCTION: Cytochrome P450 which catalyzes 3'-hydroxylation of p-coumaric esters of shikimic/quinic acids to form lignin monomers. Can use p-coumarate, p-coumaraldehyde, p-coumaroyl methyl ester, 5-O-(4-coumaroyl) D-quinate and 5-O-(4-coumaroyl) shikimate as substrates, but not p-coumaryl alcohol, p-coumaroyl CoA, 1-O-p-coumaroyl-beta-D-glucose, p-hydroxy-cinnamyl alcohol, cinnamate, caffeate or ferulate. Has a weak activity on tri(p-coumaroyl)spermidine, but none on triferuloylspermidine. Hydroxylates preferentially the 5-O-isomer, but can also convert the 4-O- and 3-O-isomers with a lower efficiency. Involved in the biosynthesis of the coumarins scopoletin and scopolin. Essential for the biosynthesis of lignin. {ECO:0000269|PubMed:11429408, ECO:0000269|PubMed:11967091, ECO:0000269|PubMed:11967092, ECO:0000269|PubMed:16377748, ECO:0000269|PubMed:16405932}.
Arabidopsis thaliana (Mouse-ear cress)
O22208
BZP17_ARATH
MAEPITKEQPPPPAPDPNSTYPPPSDFDSISIPPLDDHFSDQTPIGELMSDLGFPDGEFELTFDGMDDLYFPAENESFLIPINTSNQEQFGDFTPESESSGISGDCIVPKDADKTITTSGCINRESPRDSDDRCSGADHNLDLPTPLSSQGSGNCGSDVSEATNESSPKSRNVAVDQKVKVEEAATTTTSITKRKKEIDEDLTDESRNSKYRRSGEDADASAVTGEEDEKKRARLMRNRESAQLSRQRKKHYVEELEEKVRNMHSTITDLNGKISYFMAENATLRQQLGGNGMCPPHLPPPPMGMYPPMAPMPYPWMPCPPYMVKQQGSQVPLIPIPRLKPQNTLGTSKAKKSESKKSEAKTKKVASISFLGLLFCLFLFGALAPIVNVNYGGISGAFYGNYRSNYITDQIYSQHRDRVLDTSRSGAGTGVSNSNGMHRGRDSDRGARKNISATESSVTPGNGSEPLVASLFVPRNDKLVKIDGNLIINSILASEKAVASRKASESKERKADLMISKDYTPALPLPDVGRTEELAKHLYRSKAEKQKALSSGSADTLKDQVKTKAANGEMQQWFREGVAGPMFSSGMCTEVFQFDVSSTSGAIIPAATNVSAEHGKNTTDTHKQQNRRILRGLPIPLPGSDFNLTKEHQRNSSSKEIKPASSMVVSVLVDPREGGDGDIDGMIGGPKSLSRVFVVVLLDSAKYVTYSCVLPRSGAPHLVTT
null
null
hyperosmotic salinity response [GO:0042538]; positive regulation of DNA-templated transcription [GO:0045893]; regulation of DNA-templated transcription [GO:0006355]
endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]; Golgi membrane [GO:0000139]; nucleus [GO:0005634]
DNA-binding transcription factor activity [GO:0003700]; sequence-specific DNA binding [GO:0043565]; transcription cis-regulatory region binding [GO:0000976]
PF00170;
1.20.5.170;
BZIP family
null
SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:20876872, ECO:0000305|PubMed:17662035}; Single-pass membrane protein {ECO:0000255}. Golgi apparatus membrane {ECO:0000305|PubMed:20876872}; Single-pass membrane protein {ECO:0000255}. Nucleus {ECO:0000269|PubMed:17662035, ECO:0000269|PubMed:20876872}. Note=Translocates to the nucleus following salt treatment, heat shock or tunicamycin treatment (ER stress) (PubMed:17662035, PubMed:20876872). Relocation of BZIP17 from ER to the nucleus occurs through the Golgi and is S2P-dependent (PubMed:20876872). {ECO:0000269|PubMed:17662035, ECO:0000269|PubMed:20876872}.
null
null
null
null
null
FUNCTION: Transcriptional activator involved in salt and osmotic stress responses. Functions as a stress sensor and transducer in a signaling pathway that resembles an ER stress response. Following salt stress, BZIP17 is cleaved by SBT6.1 (S1P) and S2P at the C-terminus and the N-terminal bZIP component is translocated to the nucleus, where it activates the expression of salt stress response genes (PubMed:17662035). Functions as a stress sensor and transducer in ER stress signaling pathway. ER stress induces proteolysis of BZIP17 by SBT6.1 (S1P) and S2P, and the N-terminal bZIP component is translocated to the nucleus, where it activates the expression and production of ER chaperones, as well as protein involved in brassinosteroid (BR) signaling, which is required for stress acclimation and growth (PubMed:20876872). {ECO:0000269|PubMed:17662035, ECO:0000269|PubMed:20876872}.
Arabidopsis thaliana (Mouse-ear cress)
O22212
PRP4L_ARATH
MEPNKDDNVSLAATAQISAPPVLQDASSLPGFSAIPPVVPPSFPPPMAPIPMMPHPPVARPPTFRPPVSQNGGVKTSDSDSESDDEHIEISEESKQVRERQEKALQDLLVKRRAAAMAVPTNDKAVRDRLRRLGEPITLFGEQEMERRARLTQLLTRYDINGQLDKLVKDHEEDVTPKEEVDDEVLEYPFFTEGPKELREARIEIAKFSVKRAAVRIQRAKRRRDDPDEDMDAETKWALKHAKHMALDCSNFGDDRPLTGCSFSRDGKILATCSLSGVTKLWEMPQVTNTIAVLKDHKERATDVVFSPVDDCLATASADRTAKLWKTDGTLLQTFEGHLDRLARVAFHPSGKYLGTTSYDKTWRLWDINTGAELLLQEGHSRSVYGIAFQQDGALAASCGLDSLARVWDLRTGRSILVFQGHIKPVFSVNFSPNGYHLASGGEDNQCRIWDLRMRKSLYIIPAHANLVSQVKYEPQEGYFLATASYDMKVNIWSGRDFSLVKSLAGHESKVASLDITADSSCIATVSHDRTIKLWTSSGNDDEDEEKETMDIDL
null
null
cell fate determination [GO:0001709]; cell-cell signaling [GO:0007267]; embryo sac development [GO:0009553]; embryo sac egg cell differentiation [GO:0009560]; mRNA splicing, via spliceosome [GO:0000398]
nuclear speck [GO:0016607]; spliceosomal complex [GO:0005681]; U4/U6 x U5 tri-snRNP complex [GO:0046540]
U4 snRNA binding [GO:0030621]; U6 snRNA binding [GO:0017070]
PF08799;PF00400;
4.10.280.110;2.130.10.10;
null
null
SUBCELLULAR LOCATION: Nucleus speckle {ECO:0000269|PubMed:18702672}. Note=Colocalizes with CLO. {ECO:0000269|PubMed:18702672}.
null
null
null
null
null
FUNCTION: Participates in pre-mRNA splicing. Part of the U4/U5/U6 tri-snRNP complex, one of the building blocks of the spliceosome (By similarity). Essential for reproduction. In female gametophyte, is necessary for the egg cell and central cell fate determination and hence reproductive success. Involved in a mechanism that prevents accessory cells from adopting gametic cell fate (PubMed:17326723). Modulates egg cell signaling center that regulates the development of all female gametophytic cells (PubMed:22190635). {ECO:0000250|UniProtKB:O43172, ECO:0000269|PubMed:17326723, ECO:0000269|PubMed:22190635}.
Arabidopsis thaliana (Mouse-ear cress)
O22213
CKX1_ARATH
MGLTSSLRFHRQNNKTFLGIFMILVLSCIPGRTNLCSNHSVSTPKELPSSNPSDIRSSLVSLDLEGYISFDDVHNVAKDFGNRYQLPPLAILHPRSVFDISSMMKHIVHLGSTSNLTVAARGHGHSLQGQALAHQGVVIKMESLRSPDIRIYKGKQPYVDVSGGEIWINILRETLKYGLSPKSWTDYLHLTVGGTLSNAGISGQAFKHGPQINNVYQLEIVTGKGEVVTCSEKRNSELFFSVLGGLGQFGIITRARISLEPAPHMVKWIRVLYSDFSAFSRDQEYLISKEKTFDYVEGFVIINRTDLLNNWRSSFSPNDSTQASRFKSDGKTLYCLEVVKYFNPEEASSMDQETGKLLSELNYIPSTLFSSEVPYIEFLDRVHIAERKLRAKGLWEVPHPWLNLLIPKSSIYQFATEVFNNILTSNNNGPILIYPVNQSKWKKHTSLITPNEDIFYLVAFLPSAVPNSSGKNDLEYLLKQNQRVMNFCAAANLNVKQYLPHYETQKEWKSHFGKRWETFAQRKQAYDPLAILAPGQRIFQKTTGKLSPIQLAKSKATGSPQRYHYASILPKPRTV
1.5.99.12
COFACTOR: Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250|UniProtKB:Q9FUJ1};
cytokinin catabolic process [GO:0009823]; meristem development [GO:0048507]
vacuole [GO:0005773]
cytokinin dehydrogenase activity [GO:0019139]; FAD binding [GO:0071949]
PF09265;PF01565;
3.30.465.10;3.40.462.10;3.30.43.10;
Oxygen-dependent FAD-linked oxidoreductase family
null
SUBCELLULAR LOCATION: Vacuole {ECO:0000269|PubMed:14555694}.
CATALYTIC ACTIVITY: Reaction=A + H2O + N(6)-dimethylallyladenine = 3-methyl-2-butenal + adenine + AH2; Xref=Rhea:RHEA:13625, ChEBI:CHEBI:13193, ChEBI:CHEBI:15377, ChEBI:CHEBI:15825, ChEBI:CHEBI:16708, ChEBI:CHEBI:17499, ChEBI:CHEBI:17660; EC=1.5.99.12; Evidence={ECO:0000269|PubMed:20825956};
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.5 uM for isopentenyladenine {ECO:0000269|PubMed:14555694}; Vmax=0.1 nmol/h/mg enzyme {ECO:0000269|PubMed:14555694};
null
null
null
FUNCTION: Catalyzes the oxidation of cytokinins, a family of N(6)-substituted adenine derivatives that are plant hormones, where the substituent is an isopentenyl group (PubMed:11504909, PubMed:14555694). Catalyzes in vitro the oxidation of various types of cytokinin nucleotides that are known as direct products of cytokinin biosynthesis (PubMed:20825956). Promotes adventitious root initiation downstream of MYC2-dependent jasmonate signaling (PubMed:34329421). Cytokinin degraded by CKX1 is required for cell division in the female gametophyte by modulating the expression of cell cycle genes (PubMed:35995110). {ECO:0000269|PubMed:11504909, ECO:0000269|PubMed:14555694, ECO:0000269|PubMed:20825956, ECO:0000269|PubMed:34329421, ECO:0000269|PubMed:35995110}.
Arabidopsis thaliana (Mouse-ear cress)
O22218
ACA4_ARATH
MSNLLRDFEVEAKNPSLEARQRWRSSVSIVKNRTRRFRNIRDLDKLADYENKKHQIQEKIRVAFFVQKAALHFIDAAARPEYKLTDEVKKAGFSIEADELASMVRKNDTKSLAQKGGVEELAKKVSVSLSEGIRSSEVPIREKIFGENRYTEKPARSFLMFVWEALHDITLIILMVCAVVSIGVGVATEGFPRGMYDGTGILLSILLVVMVTAISDYKQSLQFRDLDREKKKIIVQVTRDGSRQEISIHDLVVGDVVHLSIGDQVPADGIFISGYNLEIDESSLSGESEPSHVNKEKPFLLSGTKVQNGSAKMLVTTVGMRTEWGKLMETLVDGGEDETPLQVKLNGVATIIGKIGLSFAVLTFVVLCIRFVLDKATSGSFTNWSSEDALTLLDYFAISVTIIVVAVPEGLPLAVTLSLAFAMKKLMSDRALVRHLAACETMGSSTCICTDKTGTLTTNHMVVNKVWICDKVQERQEGSKESFELELSEEVQSTLLQGIFQNTGSEVVKDKDGNTQILGSPTERAILEFGLLLGGDFNTQRKEHKILKIEPFNSDKKKMSVLIALPGGGARAFCKGASEIVLKMCENVVDSNGESVPLTEERITSISDIIEGFASEALRTLCLVYKDLDEAPSGELPDGGYTMVAVVGIKDPVRPGVREAVQTCQAAGITVRMVTGDNISTAKAIAKECGIYTEGGLAIEGSEFRDLSPHEMRAIIPKIQVMARSLPLDKHTLVSNLRKIGEVVAVTGDGTNDAPALHEADIGLAMGIAGTEVAKENADVIIMDDNFKTIVNVARWGRAVYINIQKFVQFQLTVNVVALIINFVSACITGSAPLTAVQLLWVNMIMDTLGALALATEPPNEGLMKRAPIARTASFITKTMWRNIAGQSVYQLIVLGILNFAGKSLLKLDGPDSTAVLNTVIFNSFVFCQVFNEINSREIEKINVFKGMFNSWVFTWVMTVTVVFQVIIVEFLGAFASTVPLSWQHWLLSILIGSLNMIVAVILKCVPVESRHHHDGYDLLPSGPSSSNSA
7.2.2.10
null
defense response to bacterium [GO:0042742]; monoatomic anion homeostasis [GO:0055081]; negative regulation of programmed cell death [GO:0043069]; response to nematode [GO:0009624]
chloroplast [GO:0009507]; cytosol [GO:0005829]; plant-type vacuole [GO:0000325]; plant-type vacuole membrane [GO:0009705]; vacuolar membrane [GO:0005774]; vacuole [GO:0005773]
ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; calmodulin binding [GO:0005516]; metal ion binding [GO:0046872]; P-type calcium transporter activity [GO:0005388]
PF12515;PF13246;PF00689;PF00690;PF00122;PF00702;
1.20.5.170;3.40.1110.10;2.70.150.10;1.20.1110.10;3.40.50.1000;
Cation transport ATPase (P-type) (TC 3.A.3) family, Type IIB subfamily
null
SUBCELLULAR LOCATION: Vacuole membrane {ECO:0000269|PubMed:11115896, ECO:0000269|PubMed:17151019}; Multi-pass membrane protein {ECO:0000255}. Note=Tonoplast. Small vacuoles. {ECO:0000269|PubMed:11115896}.
CATALYTIC ACTIVITY: Reaction=ATP + Ca(2+)(in) + H2O = ADP + Ca(2+)(out) + H(+) + phosphate; Xref=Rhea:RHEA:18105, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29108, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=7.2.2.10;
null
null
null
null
FUNCTION: This magnesium-dependent enzyme catalyzes the hydrolysis of ATP coupled with the translocation of calcium from the cytosol into small vacuoles.
Arabidopsis thaliana (Mouse-ear cress)
O22229
TRXB3_ARATH
MAASPKIGIGIASVSSPHRVSAASSALSPPPHLFFLTTTTTTRHGGSYLLRQPTRTRSSDSLRLRVSATANSPSSSSSGGEIIENVVIIGSGPAGYTAAIYAARANLKPVVFEGYQMGGVPGGQLMTTTEVENFPGFPDGITGPDLMEKMRKQAERWGAELYPEDVESLSVTTAPFTVQTSERKVKCHSIIYATGATARRLRLPREEEFWSRGISACAICDGASPLFKGQVLAVVGGGDTATEEALYLTKYARHVHLLVRRDQLRASKAMQDRVINNPNITVHYNTETVDVLSNTKGQMSGILLRRLDTGEETELEAKGLFYGIGHSPNSQLLEGQVELDSSGYVLVREGTSNTSVEGVFAAGDVQDHEWRQAVTAAGSGCIAALSAERYLTSNNLLVEFHQPQTEEAKKEFTQRDVQEKFDITLTKHKGQYALRKLYHESPRVILVLYTSPTCGPCRTLKPILNKVVDEYNHDVHFVEIDIEEDQEIAEAAGIMGTPCVQFFKNKEMLRTISGVKMKKEYREFIEANK
1.8.1.9
COFACTOR: Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250|UniProtKB:P9WHH1}; Note=Binds 1 FAD per subunit. {ECO:0000250|UniProtKB:P9WHH1};
cell redox homeostasis [GO:0045454]; hydrogen peroxide catabolic process [GO:0042744]; positive regulation of catalytic activity [GO:0043085]; regulation of chlorophyll biosynthetic process [GO:0010380]; regulation of starch biosynthetic process [GO:0010581]; removal of superoxide radicals [GO:0019430]
chloroplast [GO:0009507]; chloroplast stroma [GO:0009570]; cytosol [GO:0005829]
enzyme activator activity [GO:0008047]; oxidoreductase activity, acting on a sulfur group of donors, disulfide as acceptor [GO:0016671]; thioredoxin-disulfide reductase (NADP) activity [GO:0004791]
PF07992;PF00085;
3.50.50.60;3.40.30.10;
Class-II pyridine nucleotide-disulfide oxidoreductase family
null
SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000269|PubMed:16884685}.
CATALYTIC ACTIVITY: Reaction=[thioredoxin]-dithiol + NADP(+) = [thioredoxin]-disulfide + H(+) + NADPH; Xref=Rhea:RHEA:20345, Rhea:RHEA-COMP:10698, Rhea:RHEA-COMP:10700, ChEBI:CHEBI:15378, ChEBI:CHEBI:29950, ChEBI:CHEBI:50058, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.8.1.9; Evidence={ECO:0000269|PubMed:16884685};
null
null
null
null
FUNCTION: Thioredoxin reductase (TR) that exhibits both TR and thioredoxin (Trx) activities. Contains a C-terminal functional Trx domain. Functions as an electron donor for plastidial 2-Cys peroxiredoxins and participates in a NADPH-dependent hydrogen peroxide scavenging system in chloroplasts in the dark. Required for chlorophyll biosynthesis and biogenesis of the photosynthetic apparatus. Activates aerobic cyclase which converts Mg-protoporhyrin monomethyl ester into protochlorophyllide. Involved in a light-dependent regulation of starch biosynthesis by redox activation of the ADP-glucose pyrophosphorylase (AGPase), a central enzyme of starch synthesis. {ECO:0000269|PubMed:16884685, ECO:0000269|PubMed:18625226, ECO:0000269|PubMed:19470473}.
Arabidopsis thaliana (Mouse-ear cress)
O22259
ERF71_ARATH
MCGGAIISDFIWSKSESEPSQLGSVSSRKKRKPVSVSEERDGKRERKNLYRGIRQRPWGKWAAEIRDPSKGVRVWLGTFKTADEAARAYDVAAIKIRGRKAKLNFPNTQVEEEADTKPGGNQNELISENQVESLSEDLMALEDYMRFYQIPVADDQSATDIGNLWSYQDSN
null
null
cellular response to hypoxia [GO:0071456]; defense response [GO:0006952]; ethylene-activated signaling pathway [GO:0009873]; positive regulation of DNA-templated transcription [GO:0045893]; regulation of root development [GO:2000280]; response to anoxia [GO:0034059]; response to water deprivation [GO:0009414]
nucleus [GO:0005634]
DNA-binding transcription factor activity [GO:0003700]; sequence-specific double-stranded DNA binding [GO:1990837]
PF00847;
3.30.730.10;
AP2/ERF transcription factor family, ERF subfamily
PTM: In presence of oxygen, the N-terminal cysteine residue (Cys-2) of ERF71 can be oxidized by cysteine oxidases, thus preparing the protein for N-end rule pathway-mediated proteasomal degradation (Probable). Under low oxygen levels, Cys oxidation is prevented, ERF71 is stabilized and confers tolerance to hypoxia (Probable). {ECO:0000305|PubMed:22020279}.
SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00366, ECO:0000269|PubMed:20113439, ECO:0000269|PubMed:21946064}.
null
null
null
null
null
FUNCTION: Transcriptional activator that binds specifically to the cis-acting element GCC box 5'-AGCCGCC-3', or to the CRT/DRE element 5'-[AG]CCGAC-3' (PubMed:25344007). Plays an important role in root development via root cell expansion regulation (PubMed:25344007). Transcriptional activator involved in the hypoxic stress response (PubMed:20113439, PubMed:21615413, PubMed:21946064). Plays a role in low oxygen signaling and contributes to tolerance to anoxia stress by enhancing anaerobic gene expression and ethanolic fermentation (PubMed:20113439, PubMed:22020279). Plays a role in the regulation of hypoxia-induced root slanting (PubMed:28698356). Contributes to the promotion of adventitious root elongation under hypoxia, an adaptation response that strengthens the root system in upper soil layers where oxygen shortage may last for shorter time periods (PubMed:29996004). Transcriptional activator involved in the osmotic stress response (PubMed:21946064). May play a role in defense response against the fungal pathogen Fusarium graminearum downstream of ethylene signaling (PubMed:31819723). {ECO:0000269|PubMed:20113439, ECO:0000269|PubMed:21615413, ECO:0000269|PubMed:21946064, ECO:0000269|PubMed:22020279, ECO:0000269|PubMed:25344007, ECO:0000269|PubMed:28698356, ECO:0000269|PubMed:29996004, ECO:0000269|PubMed:31819723}.
Arabidopsis thaliana (Mouse-ear cress)
O22263
PDI21_ARATH
MAKSQIWFGFALLALLLVSAVADDVVVLTDDSFEKEVGKDKGALVEFYAPWCGHCKKLAPEYEKLGASFKKAKSVLIAKVDCDEQKSVCTKYGVSGYPTIQWFPKGSLEPQKYEGPRNAEALAEYVNKEGGTNVKLAAVPQNVVVLTPDNFDEIVLDQNKDVLVEFYAPWCGHCKSLAPTYEKVATVFKQEEGVVIANLDADAHKALGEKYGVSGFPTLKFFPKDNKAGHDYDGGRDLDDFVSFINEKSGTSRDSKGQLTSKAGIVESLDALVKELVAASEDEKKAVLSRIEEEASTLKGSTTRYGKLYLKLAKSYIEKGSDYASKETERLGRVLGKSISPVKADELTLKRNILTTFVASS
5.3.4.1
null
double fertilization forming a zygote and endosperm [GO:0009567]; embryo development ending in seed dormancy [GO:0009793]; embryo sac development [GO:0009553]; pollen tube development [GO:0048868]; protein folding [GO:0006457]; response to endoplasmic reticulum stress [GO:0034976]
cytosol [GO:0005829]; endoplasmic reticulum [GO:0005783]; plant-type cell wall [GO:0009505]; plant-type vacuole [GO:0000325]; secretory vesicle [GO:0099503]
protein disulfide isomerase activity [GO:0003756]
PF07749;PF00085;
1.20.1150.12;3.40.30.10;
Protein disulfide isomerase family
null
SUBCELLULAR LOCATION: Endoplasmic reticulum {ECO:0000269|PubMed:19050167}.
CATALYTIC ACTIVITY: Reaction=Catalyzes the rearrangement of -S-S- bonds in proteins.; EC=5.3.4.1;
null
null
null
null
FUNCTION: Protein disulfide isomerase that may be required for proper pollen development, ovule fertilization and embryo development. {ECO:0000269|PubMed:19050167}.
Arabidopsis thaliana (Mouse-ear cress)
O22264
MYB12_ARATH
MGRAPCCEKVGIKRGRWTAEEDQILSNYIQSNGEGSWRSLPKNAGLKRCGKSCRLRWINYLRSDLKRGNITPEEEELVVKLHSTLGNRWSLIAGHLPGRTDNEIKNYWNSHLSRKLHNFIRKPSISQDVSAVIMTNASSAPPPPQAKRRLGRTSRSAMKPKIHRTKTRKTKKTSAPPEPNADVAGADKEALMVESSGAEAELGRPCDYYGDDCNKNLMSINGDNGVLTFDDDIIDLLLDESDPGHLYTNTTCGGDGELHNIRDSEGARGFSDTWNQGNLDCLLQSCPSVESFLNYDHQVNDASTDEFIDWDCVWQEGSDNNLWHEKENPDSMVSWLLDGDDEATIGNSNCENFGEPLDHDDESALVAWLLS
null
null
flavonoid biosynthetic process [GO:0009813]; flavonol biosynthetic process [GO:0051555]; positive regulation of DNA-templated transcription [GO:0045893]; positive regulation of flavonol biosynthetic process [GO:1900386]; response to auxin [GO:0009733]; response to ethylene [GO:0009723]; response to light stimulus [GO:0009416]; response to salt stress [GO:0009651]; response to UV-B [GO:0010224]
nucleus [GO:0005634]
DNA-binding transcription factor activity [GO:0003700]; transcription cis-regulatory region binding [GO:0000976]
PF00249;
1.10.10.60;
null
null
SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00625}.
null
null
null
null
null
FUNCTION: Flavonol-specific transcription activator involved in the regulation of several genes of flavonoid biosynthesis. Activates the expression of CHS, CHI, F3H and FLS1. Controls flavonol biosynthesis mainly in the root (PubMed:17419845, PubMed:20731781). Confers tolerance to UV-B (PubMed:19895401). {ECO:0000269|PubMed:15923334, ECO:0000269|PubMed:17419845, ECO:0000269|PubMed:19895401, ECO:0000269|PubMed:20731781}.
Arabidopsis thaliana (Mouse-ear cress)
O22265
SR43C_ARATH
MQKVFLAMDTCALVIHQSLSRIKLSPPKSSSSSSSAFSPESLPIRRIELCFRGAICAAVQRNYEETTSSVEEAEEDDESSSSYGEVNKIIGSRTAGEGAMEYLIEWKDGHSPSWVPSSYIAADVVSEYETPWWTAARKADEQALSQLLEDRDVDAVDENGRTALLFVAGLGSDKCVRLLAEAGADLDHRDMRGGLTALHMAAGYVRPEVVEALVELGADIEVEDERGLTALELAREILKTTPKGNPMQFGRRIGLEKVINVLEGQVFEYAEVDEIVEKRGKGKDVEYLVRWKDGGDCEWVKGVHVAEDVAKDYEDGLEYAVAESVIGKRVGDDGKTIEYLVKWTDMSDATWEPQDNVDSTLVLLYQQQQPMNE
null
null
protein heterotrimerization [GO:0070208]; protein import into chloroplast thylakoid membrane [GO:0045038]; response to high light intensity [GO:0009644]
chloroplast [GO:0009507]; chloroplast envelope [GO:0009941]; chloroplast stroma [GO:0009570]; chloroplast thylakoid membrane [GO:0009535]; cytosol [GO:0005829]; protein-containing complex [GO:0032991]; signal recognition particle, endoplasmic reticulum targeting [GO:0005786]
disordered domain specific binding [GO:0097718]; identical protein binding [GO:0042802]; metal ion binding [GO:0046872]; protein domain specific binding [GO:0019904]; protein-macromolecule adaptor activity [GO:0030674]
PF12796;PF00385;
2.40.50.40;1.25.40.20;
null
null
SUBCELLULAR LOCATION: Plastid, chloroplast stroma {ECO:0000269|PubMed:9878634}.
null
null
null
null
null
FUNCTION: Component of the chloroplast signal recognition particle pathway. Required for post-translational targeting of proteins into the thylakoid membrane but seems to be dispensable for co-translational targeting with a translating ribosome present. May be able to function independently of cpFTSY and FFC/cpSRP54 in targeting LHCPs to the thylakoids. Acts as a highly specific chaperone for LHCPs, preventing aggregation and being able to dissolve aggregates. {ECO:0000269|PubMed:10480939, ECO:0000269|PubMed:15292240, ECO:0000269|PubMed:17513500, ECO:0000269|PubMed:20498370, ECO:0000269|PubMed:9878634}.
Arabidopsis thaliana (Mouse-ear cress)
O22267
CKI1_ARATH
MMVKVTKLVASRPIVVFCVLAFLVVVFECIWISNWRTTTENLVKEVASFTEDLRTSLVSEIENIGKFTYAKTNLSTIGLARVIDSYITNNDTGFTEIQTQIAPLLFVAYSTILQVSQVSYISRDGLMFSYIAESNTSVAVFANSSSNSSRGDYTWYTQTVDQLTGRLNGNSTKSQSLDVTHTDWFQAAQSNNYTTAFVGTSLGGEDNETLIQSVVSLYSKKGLVSLGFPVKTLTEVLNSLNLHGEELYMWTKDGTVLVREGSLNDSFFISNGSICFGRESNSLWSQCIPENCSSSGYEVEIKRLRYQAFCSVIEVSGVPLRYTLMFPNKGGATRIKHQAEKAKYQLIVVMIFLGFGWPVWFVWFMMQATRREMHMRATLINQMEATQQAERKSMNKSQAFANASHDIRGALAGMKGLIDICRDGVKPGSDVDTTLNQVNVCAKDLVALLNSVLDMSKIESGKMQLVEEDFNLSKLLEDVIDFYHPVAMKKGVDVVLDPHDGSVFKFSNVRGDSGRLKQILNNLVSNAVKFTVDGHIAVRAWAQRPGSNSSVVLASYPKGVSKFVKSMFCKNKEESSTYETEISNSIRNNANTMEFVFEVDDTGKGIPMEMRKSVFENYVQVRETAQGHQGTGLGLGIVQSLVRLMGGEIRITDKAMGEKGTCFQFNVLLTTLESPPVSDMKVRQEIEAGGDYVSTPNLGLTINTSLGGSMNIRNLSPRFNNCLSSSPKQEGSRVVLLLKNEERRRVTEKYIKNLGIKVTVVEKWEHLSYALERLFGFSPQSSMGRAECSLSCPSSRELPFIGMDGIDSRSQLPKRRSISFSAVVLLVIDAKTGPFFELCDIVKQFRRGLPHGISCKVVWLNESSTRVSERGDISCSRPLHGSRLMEVLKMLPEFGGTVLKEPPTELQRESLLRHSFVAERSPKHKVQEEGPSSMFNKKLGKRIMASTDSESETRVKSVRTGRKPIGNPEDEQETSKPSDDEFLRGKRVLVVDDNFISRKVATGKLKKMGVSEVEQCDSGKEALRLVTEGLTQREEQGSVDKLPFDYIFMDCQMPEMDGYEATREIRKVEKSYGVRTPIIAVSGHDPGSEEARETIQAGMDAFLDKSLNQLANVIREIESKRH
2.7.13.3
null
cytokinin-activated signaling pathway [GO:0009736]; embryo sac development [GO:0009553]; phloem or xylem histogenesis [GO:0010087]; secondary growth [GO:0080117]
nucleus [GO:0005634]; plasma membrane [GO:0005886]; plasmodesma [GO:0009506]
phosphorelay sensor kinase activity [GO:0000155]; protein histidine kinase activity [GO:0004673]; protein homodimerization activity [GO:0042803]
PF02518;PF00512;PF00072;
1.10.287.130;3.40.50.2300;3.30.565.10;
null
null
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:19622803}; Multi-pass membrane protein {ECO:0000269|PubMed:19622803}.
CATALYTIC ACTIVITY: Reaction=ATP + protein L-histidine = ADP + protein N-phospho-L-histidine.; EC=2.7.13.3;
null
null
null
null
FUNCTION: Essential protein. Functions as a histidine kinase and transmits the stress signal to a downstream MAPK cascade. This protein undergoes an ATP-dependent autophosphorylation at a conserved histidine residue in the kinase core, and a phosphoryl group is then transferred to a conserved aspartate residue in the receiver domain. Required for the development of megagametophyte in female gametophyte (embryo sac) independently of cytokinin. Contributes to vascular bundle formation and secondary growth in a cytokinin-independent manner, probably by promoting the maintenance of mitotic activity and/or identity of procambial cells. Seems to influence and promote the cytokinin signaling pathway. {ECO:0000269|PubMed:10610126, ECO:0000269|PubMed:12426401, ECO:0000269|PubMed:12774227, ECO:0000269|PubMed:18077346, ECO:0000269|PubMed:19622803, ECO:0000269|PubMed:20363773, ECO:0000269|PubMed:8875940}.
Arabidopsis thaliana (Mouse-ear cress)
O22268
DIM1A_ARATH
MAGGKIRKEKPKASNRAPSNHYQGGISFHKSKGQHILKNPLLVDSIVQKAGIKSTDVILEIGPGTGNLTKKLLEAGKEVIAVELDSRMVLELQRRFQGTPFSNRLKVIQGDVLKTELPRFDICVANIPYQISSPLTFKLLFHPTSFRCAVIMYQREFAMRLVAQPGDNLYCRLSVNTQLYARVSHLLKVGKNNFRPPPKVDSSVVRIEPRRPGPQVNKKEWDGFLRVCFIRKNKTLGSIFKQKSVLSMLEKNFKTLQAVLASLQNNGEPALNTTSMDLGDQSMGMEDDDNEMDDDDMEMDEGEGDGGETSEFKEKVMNVLKEGGFEEKRSSKLSQQEFLYLLSLFNKSGIHFT
2.1.1.-
null
cell division [GO:0051301]; cell fate specification [GO:0001708]
cytosol [GO:0005829]; nucleolus [GO:0005730]; nucleus [GO:0005634]
RNA binding [GO:0003723]; rRNA (adenine-N6,N6-)-dimethyltransferase activity [GO:0000179]
PF00398;
1.10.8.480;3.40.50.150;
Class I-like SAM-binding methyltransferase superfamily, rRNA adenine N(6)-methyltransferase family
null
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:19929881, ECO:0000269|PubMed:22829145}. Nucleus, nucleolus {ECO:0000269|PubMed:19929881, ECO:0000269|PubMed:22829145}.
CATALYTIC ACTIVITY: Reaction=adenosine(1785)/adenosine(1786) in 18S rRNA + 4 S-adenosyl-L-methionine = 4 H(+) + N(6)-dimethyladenosine(1785)/N(6)-dimethyladenosine(1786) in 18S rRNA + 4 S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:47640, Rhea:RHEA-COMP:11866, Rhea:RHEA-COMP:11867, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:74411, ChEBI:CHEBI:74493; Evidence={ECO:0000269|PubMed:22829145};
null
null
null
null
FUNCTION: N6-adenine methyltransferase which modifies the AA dinucleotide at the plant nuclear 18S rRNA nucleotides A1785 and A1786 (PubMed:22829145). Required for generating appropriate patterns of gene expression during root development, including the cell-specific expression of transcriptional regulators involved in root hair and non-hair cells patterning (PubMed:22829145). {ECO:0000269|PubMed:22829145, ECO:0000305|PubMed:19929881}.
Arabidopsis thaliana (Mouse-ear cress)
O22286
BPM3_ARATH
MSTVGGIEQLIPDSVSTSFIETVNGSHQFTIQGYSLAKGMSPGKFIQSDIFSVGGYDWAIYFYPDGKNPEDQSSYISLFIALASDSNDIRALFELTLMDQSGKGKHKVHSHFDRALEGGPYTLKYKGSMWGYKRFFKRSALETSDYLKDDCLVINCTVGVVRARLEGPKQYGIVLPLSNMGQGLKDLLDSEVGCDIAFQVGDETYKAHKLILAARSPVFRAQFFGPIGNNNVDRIVIDDIEPSIFKAMLSFIYTDVLPNVHEITGSTSASSFTNMIQHLLAAADLYDLARLKILCEVLLCEKLDVDNVATTLALAEQHQFLQLKAFCLEFVASPANLGAVMKSEGFKHLKQSCPTLLSELLNTVAAADKSSTSGQSNKKRSASSVLGCDTTNVRQLRRRTRKEVRAVS
null
null
cellular response to salt stress [GO:0071472]; protein ubiquitination [GO:0016567]; regulation of protein ubiquitination [GO:0031396]; response to osmotic stress [GO:0006970]
cytosol [GO:0005829]; nucleus [GO:0005634]
identical protein binding [GO:0042802]
PF00651;PF21355;
1.25.40.420;
Tdpoz family
null
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:19843165}. Cytoplasm {ECO:0000269|PubMed:19843165}.
null
null
PATHWAY: Protein modification; protein ubiquitination. {ECO:0000269|PubMed:15618422}.
null
null
FUNCTION: May act as a substrate-specific adapter of an E3 ubiquitin-protein ligase complex (CUL3-RBX1-BTB) which mediates the ubiquitination and subsequent proteasomal degradation of target proteins. {ECO:0000269|PubMed:15618422}.
Arabidopsis thaliana (Mouse-ear cress)
O22287
GMPP1_ARATH
MKALILVGGFGTRLRPLTLSFPKPLVDFANKPMILHQIEALKAVGVDEVVLAINYQPEVMLNFLKDFETKLEIKITCSQETEPLGTAGPLALARDKLLDGSGEPFFVLNSDVISEYPLKEMLEFHKSHGGEASIMVTKVDEPSKYGVVVMEESTGRVEKFVEKPKLYVGNKINAGIYLLNPSVLDKIELRPTSIEKETFPKIAAAQGLYAMVLPGFWMDIGQPRDYITGLRLYLDSLRKKSPAKLTSGPHIVGNVLVDETATIGEGCLIGPDVAIGPGCIVESGVRLSRCTVMRGVRIKKHACISSSIIGWHSTVGQWARIENMTILGEDVHVSDEIYSNGGVVLPHKEIKSNILKPEIVM
2.7.7.13
null
cellulose biosynthetic process [GO:0030244]; defense response to bacterium [GO:0042742]; GDP-mannose biosynthetic process [GO:0009298]; L-ascorbic acid biosynthetic process [GO:0019853]; protein glycosylation [GO:0006486]; response to ammonium ion [GO:0060359]; response to heat [GO:0009408]; response to jasmonic acid [GO:0009753]; response to ozone [GO:0010193]; response to salt stress [GO:0009651]
cytosol [GO:0005829]; nucleus [GO:0005634]
GTP binding [GO:0005525]; mannose-1-phosphate guanylyltransferase (GTP) activity [GO:0004475]
PF00132;PF00483;
2.160.10.10;
Transferase hexapeptide repeat family
null
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:23424245}. Nucleus {ECO:0000269|PubMed:23424245}.
CATALYTIC ACTIVITY: Reaction=alpha-D-mannose 1-phosphate + GTP + H(+) = diphosphate + GDP-alpha-D-mannose; Xref=Rhea:RHEA:15229, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019, ChEBI:CHEBI:37565, ChEBI:CHEBI:57527, ChEBI:CHEBI:58409; EC=2.7.7.13; Evidence={ECO:0000269|PubMed:10097187, ECO:0000269|PubMed:35677252};
null
PATHWAY: Nucleotide-sugar biosynthesis; GDP-alpha-D-mannose biosynthesis; GDP-alpha-D-mannose from alpha-D-mannose 1-phosphate (GTP route): step 1/1. {ECO:0000269|PubMed:10097187}.
null
null
FUNCTION: Essential protein during embryogenesis (PubMed:15266054). Catalyzes a reaction of the Smirnoff-Wheeler pathway, the major route to ascorbate biosynthesis in plants. Plays an essential role in plant growth and development and cell-wall architecture. Provides GDP-mannose, used for cell wall carbohydrate biosynthesis, protein N-glycosylation, as well as for the biosynthesis of the antioxidant ascorbate. {ECO:0000269|PubMed:10097187, ECO:0000269|PubMed:10655235, ECO:0000269|PubMed:11226227, ECO:0000269|PubMed:12671089, ECO:0000269|PubMed:15064386, ECO:0000269|PubMed:15266054, ECO:0000269|PubMed:16244149, ECO:0000269|PubMed:16720601, ECO:0000269|PubMed:18849295, ECO:0000269|PubMed:19011088, ECO:0000269|PubMed:8790441, ECO:0000269|PubMed:9390448}.
Arabidopsis thaliana (Mouse-ear cress)
O22315
SR34_ARATH
MSSRSSRTVYVGNLPGDIREREVEDLFSKYGPVVQIDLKVPPRPPGYAFVEFDDARDAEDAIHGRDGYDFDGHRLRVELAHGGRRSSDDTRGSFNGGGRGGGRGRGDGGSRGPSRRSEFRVLVTGLPSSASWQDLKDHMRKGGDVCFSQVYRDARGTTGVVDYTCYEDMKYALKKLDDTEFRNAFSNGYVRVREYDSRKDSRSPSRGRSYSKSRSRSRGRSVSRSRSRSRSRSRSPKAKSSRRSPAKSTSRSPGPRSKSRSPSPRRSRSRSRSPLPSVQKEGSKSPSKPSPAKSPIHTRSPSR
null
null
mRNA processing [GO:0006397]; RNA splicing [GO:0008380]
cytoplasm [GO:0005737]; interchromatin granule [GO:0035061]; nuclear speck [GO:0016607]; nucleus [GO:0005634]; spliceosomal complex [GO:0005681]
mRNA binding [GO:0003729]
PF00076;
3.30.70.330;
Splicing factor SR family, SR subfamily
PTM: Extensively phosphorylated on serine residues in the RS domain. {ECO:0000269|PubMed:10215626, ECO:0000269|PubMed:10652154, ECO:0000269|PubMed:15166240}.
SUBCELLULAR LOCATION: Nucleus speckle {ECO:0000269|PubMed:15034145, ECO:0000269|PubMed:15686520, ECO:0000269|PubMed:16895966}. Nucleus, nucleoplasm {ECO:0000269|PubMed:15034145, ECO:0000269|PubMed:15686520, ECO:0000269|PubMed:16895966}.
null
null
null
null
null
FUNCTION: General splicing factor. Can promote splice site selection in vitro presumably by antagonizing the effects of the A1 heterogeneous nuclear ribonucleoprotein. May have an essential function during early plant development. {ECO:0000269|PubMed:10215626}.
Arabidopsis thaliana (Mouse-ear cress)
O22347
TBA1_ELEIN
MRECISIHIGQAGIQVGNACWELYCLEHGIQADGQMPGDKTIGGGDDAFNTFFSETGAGKHVPRAVFVDLEPTVIDEVRTGTYRQLFHPEQLISGKEDAANNFARGHYTIGKEIVDLCLDRIRKLADNCTGLQGFLVFNAVGGGTGSGLGSLLLERLSVDYGKKSKLGFTVYPSPQVSTSVVEPYNSVLSTHSLLEHTDVAVLLDNEAIYDICRRSLDIERPTYTNLNRLVSQVISSLTASLRFDGALNVDVNEFQTNLVPYPRIHFMLSSYAPVISAEKAYHEQLSVAEITNSAFEPSSMMAKCDPRHGKYMACCLMYRGDVVPKDVNAAVATIKTKRTIQFVDWCPTGFKCGINYQPPSVVPGGDLAKVQRAVCMISNSTSVVEVFSRIDHKFDLMYAKRAFVHWYVGEGMEEGEFSEAREDLAALEKDYEEVGAEFDEGEEGDEGDEY
3.6.5.-
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:P68363};
microtubule cytoskeleton organization [GO:0000226]; mitotic cell cycle [GO:0000278]
cytoplasm [GO:0005737]; microtubule [GO:0005874]
GTP binding [GO:0005525]; hydrolase activity [GO:0016787]; metal ion binding [GO:0046872]; structural constituent of cytoskeleton [GO:0005200]
PF00091;PF03953;
1.10.287.600;3.30.1330.20;3.40.50.1440;
Tubulin family
PTM: Undergoes a tyrosination/detyrosination cycle, the cyclic removal and re-addition of a C-terminal tyrosine residue by the enzymes tubulin tyrosine carboxypeptidase (TTCP) and tubulin tyrosine ligase (TTL), respectively. {ECO:0000250}.; PTM: Acetylation of alpha chains at Lys-40 stabilizes microtubules and affects affinity and processivity of microtubule motors. This modification has a role in multiple cellular functions, ranging from cell motility, cell cycle progression or cell differentiation to intracellular trafficking and signaling (By similarity). {ECO:0000250}.
SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton.
CATALYTIC ACTIVITY: Reaction=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:58189; Evidence={ECO:0000250|UniProtKB:P68363}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19670; Evidence={ECO:0000250|UniProtKB:P68363};
null
null
null
null
FUNCTION: Tubulin is the major constituent of microtubules, a cylinder consisting of laterally associated linear protofilaments composed of alpha- and beta-tubulin heterodimers. Microtubules grow by the addition of GTP-tubulin dimers to the microtubule end, where a stabilizing cap forms. Below the cap, tubulin dimers are in GDP-bound state, owing to GTPase activity of alpha-tubulin.
Eleusine indica (Goosegrass) (Cynosurus indicus)
O22415
SNAIF_SAMNI
MRVVTKLLYLVVLAICGLGIHGALTHTRVTPPVYPSVSFNLTGADTYGPFLRALQEKVILGNHTAFDLPVLNPESQVSDSNRFVLVPLTNPSGDTVTLAIDVVNLYVVAFSSNGRSYFFSGSTAVQRDNLFVDTTQEELNFTGNYISLERQVGFGRVYIPLGPKSLAQAISSLRTYTLSAGDTKPLARGLLVVIQMVSEAARFRYIELRIRTSITDASEFTPDLLMLSMENNWSSMSSEIQQAQPGGIFPGVVQLRDERNNPIEVTNFRRLFELTYIAVLLYGCAPVTSNSYTNNAIDAQIIKMPVFRGGGYEKVCSVVEVTRRISGWDGLCVDVRDGHYIDGNTVQLGPCGNECNQLWTFRTDGTIRWLGKCLTTSSSVMIYDCNTVPPEATKWVVSTDGTITNPRSGLVLTAPQAAEGTALSLENNIHAARQGWTVGDVEPLVTFIVGYKQMCLTENGENNFVWLEDCVLNRVEQEWALYGDGTIRVNSNRSLCVTSEDHEPSDLIVILKCEGSGNQRWVFNTNGTISNPNAKLVMDVAQSNVSLRKIILYPPTGNPNQQWITTTQPA
3.2.2.22
null
defense response [GO:0006952]; negative regulation of translation [GO:0017148]
null
carbohydrate binding [GO:0030246]; nucleotide binding [GO:0000166]; rRNA N-glycosylase activity [GO:0030598]; toxin activity [GO:0090729]
PF00652;PF00161;
2.80.10.50;3.40.420.10;4.10.470.10;
Ribosome-inactivating protein family, Type 2 RIP subfamily
PTM: The precursor is processed in two chains, A and B, that are linked by a disulfide bond (PubMed:9541002). A small truncated form corresponding roughly to the second ricin B-type lectin domain of the B chain, TrSNAIf, can also be produced (PubMed:9541002). {ECO:0000269|PubMed:9541002}.; PTM: N-glycosylated. {ECO:0000250|UniProtKB:Q41358}.
null
CATALYTIC ACTIVITY: Reaction=Endohydrolysis of the N-glycosidic bond at one specific adenosine on the 28S rRNA.; EC=3.2.2.22; Evidence={ECO:0000255|RuleBase:RU004915};
null
null
null
null
FUNCTION: Neu5Ac(alpha2-6)Gal/GalNAc specific agglutinin (PubMed:12023903). Behaves as a type-2 ribosome-inactivating protein (PubMed:12023903). Strongly inhibits mammalian but not plant ribosomes (PubMed:12023903). The A chain is responsible for inhibiting protein synthesis through the catalytic inactivation of 60S ribosomal subunits by removing adenine from position 4,324 of 28S rRNA (Probable). The B chain binds to cell receptors and probably facilitates the entry into the cell of the A chain; B chains are also responsible for cell agglutination (lectin activity) (Probable). Involved in plant defense against insects (PubMed:18951590). {ECO:0000269|PubMed:12023903, ECO:0000269|PubMed:18951590, ECO:0000305}.; FUNCTION: [TrSNAIf]: Binds Neu5Ac(alpha2-6)Gal/GalNAc but has no clear agglutination activity. {ECO:0000269|PubMed:9541002}.
Sambucus nigra (European elder)
O22446
HDA19_ARATH
MDTGGNSLASGPDGVKRKVCYFYDPEVGNYYYGQGHPMKPHRIRMTHALLAHYGLLQHMQVLKPFPARDRDLCRFHADDYVSFLRSITPETQQDQIRQLKRFNVGEDCPVFDGLYSFCQTYAGGSVGGSVKLNHGLCDIAINWAGGLHHAKKCEASGFCYVNDIVLAILELLKQHERVLYVDIDIHHGDGVEEAFYATDRVMTVSFHKFGDYFPGTGHIQDIGYGSGKYYSLNVPLDDGIDDESYHLLFKPIMGKVMEIFRPGAVVLQCGADSLSGDRLGCFNLSIKGHAECVKFMRSFNVPLLLLGGGGYTIRNVARCWCYETGVALGVEVEDKMPEHEYYEYFGPDYTLHVAPSNMENKNSRQMLEEIRNDLLHNLSKLQHAPSVPFQERPPDTETPEVDEDQEDGDKRWDPDSDMDVDDDRKPIPSRVKREAVEPDTKDKDGLKGIMERGKGCEVEVDESGSTKVTGVNPVGVEEASVKMEEEGTNKGGAEQAFPPKT
3.5.1.98
COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250|UniProtKB:Q8GXJ1}; Note=Binds 1 zinc ion per subunit. {ECO:0000250|UniProtKB:Q8GXJ1};
defense response to bacterium [GO:0042742]; DNA-mediated transformation [GO:0009294]; jasmonic acid and ethylene-dependent systemic resistance [GO:0009861]; negative regulation of DNA-templated transcription [GO:0045892]; negative regulation of response to salt stress [GO:1901001]; positive regulation of stem cell population maintenance [GO:1902459]; regulation of multicellular organismal development [GO:2000026]; regulation of transcription by RNA polymerase II [GO:0006357]
histone deacetylase complex [GO:0000118]; nucleus [GO:0005634]
histone deacetylase activity [GO:0004407]; zinc ion binding [GO:0008270]
PF00850;
3.40.800.20;
Histone deacetylase family, HD type 1 subfamily
null
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15749761, ECO:0000269|PubMed:16699543}. Note=excluded from the nucleolus, but associated with the condensing chromatids.
CATALYTIC ACTIVITY: Reaction=H2O + N(6)-acetyl-L-lysyl-[histone] = acetate + L-lysyl-[histone]; Xref=Rhea:RHEA:58196, Rhea:RHEA-COMP:9845, Rhea:RHEA-COMP:11338, ChEBI:CHEBI:15377, ChEBI:CHEBI:29969, ChEBI:CHEBI:30089, ChEBI:CHEBI:61930; EC=3.5.1.98; Evidence={ECO:0000269|PubMed:16699543};
null
null
null
null
FUNCTION: Responsible for the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4). Histone deacetylation gives a tag for epigenetic repression and plays an important role in transcriptional regulation, cell cycle progression and developmental events. Histone deacetylases act via the formation of large multiprotein complexes. HDA19 is involved in jasmonic acid and ethylene signaling of pathogen response. Part of a repressor complex including APETALA2 (AP2) and TOPLESS (TPL) that control the expression domains of numerous floral organ identity genes (PubMed:23034631). Involved in negative regulation of salinity stress response (PubMed:29018096). Represses the expression of stress tolerance-related genes, genes coding for late embryogenesis abundant (LEA) proteins that prevent protein aggregation, and positive regulators of abscisic acid (ABA) signaling, such as ABI5 and NAC019 (PubMed:29018096). {ECO:0000269|PubMed:11117260, ECO:0000269|PubMed:11134508, ECO:0000269|PubMed:15749761, ECO:0000269|PubMed:16699543, ECO:0000269|PubMed:23034631, ECO:0000269|PubMed:29018096}.
Arabidopsis thaliana (Mouse-ear cress)
O22448
GPX5_CHLRE
MANPEFYGLSTTTLSGQPFPFKDLEGKAVLIVNVASKCGFTPQYKGLEELYQQYKDRGLVILGFPCNQFGGQEPGDASAIGEFCQRNFGVTFPIMEKSDVNGNDANPVFKYLKSQKKQFMMEMIKWNFEKFLVDKSGQVVARFSSMATPASLAPEIEKVLNA
1.11.1.24; 1.11.1.9
null
cellular oxidant detoxification [GO:0098869]; cellular response to oxidative stress [GO:0034599]; response to photooxidative stress [GO:0080183]
cytosol [GO:0005829]; mitochondrion [GO:0005739]; nucleus [GO:0005634]
glutathione peroxidase activity [GO:0004602]; phospholipid-hydroperoxide glutathione peroxidase activity [GO:0047066]; selenium binding [GO:0008430]; thioredoxin peroxidase activity [GO:0008379]
PF00255;
3.40.30.10;
Glutathione peroxidase family
PTM: Cys-87 is S-selanylated when selenium levels are high. S-selanylation may increase or be important for glutathione peroxidase activity. {ECO:0000269|PubMed:29124185}.
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|Ref.10}. Note=Localizes to the cytoplasm in nitrogen-replete and nitrogen-deplete conditions. {ECO:0000269|Ref.10}.
CATALYTIC ACTIVITY: Reaction=2 glutathione + H2O2 = glutathione disulfide + 2 H2O; Xref=Rhea:RHEA:16833, ChEBI:CHEBI:15377, ChEBI:CHEBI:16240, ChEBI:CHEBI:57925, ChEBI:CHEBI:58297; EC=1.11.1.9; Evidence={ECO:0000269|PubMed:29124185}; CATALYTIC ACTIVITY: Reaction=[thioredoxin]-dithiol + a hydroperoxide = [thioredoxin]-disulfide + an alcohol + H2O; Xref=Rhea:RHEA:62620, Rhea:RHEA-COMP:10698, Rhea:RHEA-COMP:10700, ChEBI:CHEBI:15377, ChEBI:CHEBI:29950, ChEBI:CHEBI:30879, ChEBI:CHEBI:35924, ChEBI:CHEBI:50058; EC=1.11.1.24; Evidence={ECO:0000269|PubMed:19690965};
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=54 uM for hydrogen peroxide (with cytosolic thioredoxin) (at 30 degrees Celsius and pH 7.9) {ECO:0000269|PubMed:19690965}; KM=732 uM for tert-butyl hydroperoxide (with cytosolic thioredoxin) (at 30 degrees Celsius and pH 7.9) {ECO:0000269|PubMed:19690965}; KM=63 uM for cumene hydroperoxide (with cytosolic thioredoxin) (at 30 degrees Celsius and pH 7.9) {ECO:0000269|PubMed:19690965}; Note=kcat is 7.4 sec(-1) for the reduction of hydrogen peroxide (with cytosolic thioredoxin) (at 30 degrees Celsius and pH 7.9) (PubMed:19690965). kcat is 7.4 sec(-1) for the reduction of tert-butyl hydroperoxide (with cytosolic thioredoxin) (at 30 degrees Celsius and pH 7.9) (PubMed:19690965). kcat is 7.4 sec(-1) for the reduction of cumene hydroperoxide (with cytosolic thioredoxin) (at 30 degrees Celsius and pH 7.9) (PubMed:19690965). {ECO:0000269|PubMed:19690965};
null
null
null
FUNCTION: Has thioredoxin peroxidase activity (PubMed:19690965). May also have glutathione peroxidase activity, although this activity is controversial (PubMed:29124185). Protects cells against reactive oxygen species, which may include photooxidative stress, hydrogen peroxide and organic hydroperoxides (PubMed:19690965, PubMed:29124185, PubMed:32344528, PubMed:32599138, Ref.1). {ECO:0000269|PubMed:19690965, ECO:0000269|PubMed:29124185, ECO:0000269|PubMed:32344528, ECO:0000269|PubMed:32599138, ECO:0000269|Ref.1}.
Chlamydomonas reinhardtii (Chlamydomonas smithii)
O22456
SEP3_ARATH
MGRGRVELKRIENKINRQVTFAKRRNGLLKKAYELSVLCDAEVALIIFSNRGKLYEFCSSSSMLRTLERYQKCNYGAPEPNVPSREALAVELSSQQEYLKLKERYDALQRTQRNLLGEDLGPLSTKELESLERQLDSSLKQIRALRTQFMLDQLNDLQSKERMLTETNKTLRLRLADGYQMPLQLNPNQEEVDHYGRHHHQQQQHSQAFFQPLECEPILQIGYQGQQDGMGAGPSVNNYMLGWLPYDTNSI
null
null
cell fate specification [GO:0001708]; flower development [GO:0009908]; mucilage extrusion from seed coat [GO:0080001]; plant ovule development [GO:0048481]; positive regulation of transcription by RNA polymerase II [GO:0045944]; seed coat development [GO:0010214]; specification of floral organ identity [GO:0010093]; specification of floral organ number [GO:0048833]
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]; 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}.
null
null
null
null
null
FUNCTION: Probable transcription factor active in inflorescence development and floral organogenesis. Functions with SEPALLATA1/AGL2 and SEPALLATA2/AGL4 to ensure proper development of petals, stamens and carpels and to prevent the indeterminate growth of the flower meristem. Interacts with APETALA1, AGAMOUS or APETALA3/PISTILLATA to form complexes, that could be involved in genes regulation during floral meristem development (PubMed:10821278, PubMed:11206550). Binds specifically to the CArG box DNA sequence 5'-CC (A/T)6 GG-3' (PubMed:16080001). {ECO:0000269|PubMed:10821278, ECO:0000269|PubMed:11206550, ECO:0000269|PubMed:16080001}.
Arabidopsis thaliana (Mouse-ear cress)
O22467
MSI1_ARATH
MGKDEEEMRGEIEERLINEEYKIWKKNTPFLYDLVITHALEWPSLTVEWLPDREEPSGKDYSVQKMILGTHTSESEPNYLMLAQVQLPLDDTESEARQYDDDRSEFGGFGCATGKVQIIQQINHDGEVNRARYMPQNPFIIATKTVNAEVYVFDYSKHPSKPPLDGACNPDLKLRGHSSEGYGLSWSKFKQGHLLSGSDDAQICLWDINATPKNKSLDAQQIFKAHEGVVEDVAWHLRHEYLFGSVGDDQYLLIWDLRSPSASKPVQSVVAHSMEVNCLAFNPFNEWVVATGSTDKTVKLFDLRKLSTALHTFDSHKEEVFQVGWNPKNETILASCCLGRRLMVWDLSRIDEEQTVEDAEDGPPELLFIHGGHTSKISDFSWNPCEDWVISSVAEDNILQIWQMAENIYHDEDDAPGEEPSKAS
null
null
DNA replication [GO:0006260]; embryo development ending in seed dormancy [GO:0009793]; flower development [GO:0009908]; heterochromatin formation [GO:0031507]; heterochromatin organization [GO:0070828]; leaf development [GO:0048366]; pollen development [GO:0009555]; positive regulation of cell cycle [GO:0045787]; regulation of DNA-templated transcription [GO:0006355]; regulation of flower development [GO:0009909]; seed coat development [GO:0010214]; seed development [GO:0048316]; trichome differentiation [GO:0010026]
chromatin silencing complex [GO:0005677]; Cul4-RING E3 ubiquitin ligase complex [GO:0080008]; DRM complex [GO:0070176]; nucleus [GO:0005634]; protein-containing complex [GO:0032991]
histone binding [GO:0042393]; nucleosome binding [GO:0031491]
PF12265;PF00400;
2.130.10.10;
WD repeat RBAP46/RBAP48/MSI1 family
null
SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
null
null
null
null
null
FUNCTION: Core histone-binding subunit that may target chromatin assembly factors, chromatin remodeling factors and histone deacetylases to their histone substrates in a manner that is regulated by nucleosomal DNA. Component of several complexes which regulate chromatin metabolism. These include the chromatin assembly factor 1 (CAF-1) complex, which is required for chromatin assembly following DNA replication and DNA repair, and the fertilization independent seed (FIS) complex, a polycomb group protein complex which is required to maintain the transcriptionally repressive state of homeotic genes throughout development. Required for several aspects of plant development including normal leaf expansion, correct development of flowers, normal endosperm development, repression of parthenogenetic seed development and repression of floral homeotic genes in leaf tissue. Also required for the recruitment of chromosomal DNA into heterochromatic chromocenters. Also involved in regulation of imprinted genes. Acts together with RBR1 to repress the expression of MET1 during female gametogenesis. This in turn activates expression of the imprinted genes FIS2 and FWA. {ECO:0000269|PubMed:11163246, ECO:0000269|PubMed:12736201, ECO:0000269|PubMed:12970192, ECO:0000269|PubMed:15151989, ECO:0000269|PubMed:15854908, ECO:0000269|PubMed:16452472, ECO:0000269|PubMed:17021044, ECO:0000269|PubMed:18045841, ECO:0000269|PubMed:18700816}.
Arabidopsis thaliana (Mouse-ear cress)
O22476
BRI1_ARATH
MKTFSSFFLSVTTLFFFSFFSLSFQASPSQSLYREIHQLISFKDVLPDKNLLPDWSSNKNPCTFDGVTCRDDKVTSIDLSSKPLNVGFSAVSSSLLSLTGLESLFLSNSHINGSVSGFKCSASLTSLDLSRNSLSGPVTTLTSLGSCSGLKFLNVSSNTLDFPGKVSGGLKLNSLEVLDLSANSISGANVVGWVLSDGCGELKHLAISGNKISGDVDVSRCVNLEFLDVSSNNFSTGIPFLGDCSALQHLDISGNKLSGDFSRAISTCTELKLLNISSNQFVGPIPPLPLKSLQYLSLAENKFTGEIPDFLSGACDTLTGLDLSGNHFYGAVPPFFGSCSLLESLALSSNNFSGELPMDTLLKMRGLKVLDLSFNEFSGELPESLTNLSASLLTLDLSSNNFSGPILPNLCQNPKNTLQELYLQNNGFTGKIPPTLSNCSELVSLHLSFNYLSGTIPSSLGSLSKLRDLKLWLNMLEGEIPQELMYVKTLETLILDFNDLTGEIPSGLSNCTNLNWISLSNNRLTGEIPKWIGRLENLAILKLSNNSFSGNIPAELGDCRSLIWLDLNTNLFNGTIPAAMFKQSGKIAANFIAGKRYVYIKNDGMKKECHGAGNLLEFQGIRSEQLNRLSTRNPCNITSRVYGGHTSPTFDNNGSMMFLDMSYNMLSGYIPKEIGSMPYLFILNLGHNDISGSIPDEVGDLRGLNILDLSSNKLDGRIPQAMSALTMLTEIDLSNNNLSGPIPEMGQFETFPPAKFLNNPGLCGYPLPRCDPSNADGYAHHQRSHGRRPASLAGSVAMGLLFSFVCIFGLILVGREMRKRRRKKEAELEMYAEGHGNSGDRTANNTNWKLTGVKEALSINLAAFEKPLRKLTFADLLQATNGFHNDSLIGSGGFGDVYKAILKDGSAVAIKKLIHVSGQGDREFMAEMETIGKIKHRNLVPLLGYCKVGDERLLVYEFMKYGSLEDVLHDPKKAGVKLNWSTRRKIAIGSARGLAFLHHNCSPHIIHRDMKSSNVLLDENLEARVSDFGMARLMSAMDTHLSVSTLAGTPGYVPPEYYQSFRCSTKGDVYSYGVVLLELLTGKRPTDSPDFGDNNLVGWVKQHAKLRISDVFDPELMKEDPALEIELLQHLKVAVACLDDRAWRRPTMVQVMAMFKEIQAGSGIDSQSTIRSIEDGGFSTIEMVDMSIKEVPEGKL
2.7.10.1; 2.7.11.1
null
anther wall tapetum cell differentiation [GO:0048657]; brassinosteroid homeostasis [GO:0010268]; brassinosteroid mediated signaling pathway [GO:0009742]; detection of brassinosteroid stimulus [GO:0009729]; leaf development [GO:0048366]; microtubule bundle formation [GO:0001578]; phosphorylation [GO:0016310]; pollen exine formation [GO:0010584]; positive regulation of flower development [GO:0009911]; response to UV-B [GO:0010224]; seedling development [GO:0090351]; skotomorphogenesis [GO:0009647]
endosome [GO:0005768]; endosome membrane [GO:0010008]; plasma membrane [GO:0005886]; protein-containing complex [GO:0032991]
ATP binding [GO:0005524]; identical protein binding [GO:0042802]; protein heterodimerization activity [GO:0046982]; protein homodimerization activity [GO:0042803]; protein kinase activity [GO:0004672]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674]; steroid binding [GO:0005496]; transmembrane receptor protein tyrosine kinase activity [GO:0004714]
PF20141;PF00560;PF13855;PF08263;PF00069;
3.30.1490.310;3.80.10.10;1.10.510.10;
Protein kinase superfamily, Ser/Thr protein kinase family
PTM: Autophosphorylated on Tyr-831, Tyr-956 and maybe Tyr-1072. Phosphorylated on at least 12 sites, with a preference for Ser residues. Transphosphorylated on Ser-887 by SERK1 and on Ser-838, Thr-846, Ser-858 and Ser-1166 by BAK1. Phosphorylation on Ser-1166 enhances the kinase activity. {ECO:0000269|PubMed:11027724, ECO:0000269|PubMed:12150928, ECO:0000269|PubMed:12150929, ECO:0000269|PubMed:15894717, ECO:0000269|PubMed:18694562, ECO:0000269|PubMed:19105183, ECO:0000269|PubMed:19124768}.; PTM: Glycosylated. {ECO:0000269|PubMed:17588517}.
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:26071421}; Single-pass type I membrane protein {ECO:0000305}. Endosome membrane; Single-pass type I membrane protein.
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:0000305}; 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:0000305}; CATALYTIC ACTIVITY: Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-[protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858, ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=2.7.10.1; Evidence={ECO:0000255|PROSITE-ProRule:PRU10027};
null
null
null
null
FUNCTION: Receptor with a dual specificity kinase activity acting on both serine/threonine- and tyrosine-containing substrates. Regulates, in response to brassinosteroid binding, a signaling cascade involved in plant development, including expression of light- and stress-regulated genes, promotion of cell elongation, normal leaf and chloroplast senescence, and flowering. Binds brassinolide (BL), and less effectively castasterone (CS), but not 2,3,22,23-O-tetramethylbrassinolide or ecdysone. May be involved in a feedback regulation of brassinosteroid biosynthesis. Phosphorylates BRI1-associated receptor kinase 1 (BAK1), Transthyretin-Like protein (TTL) and SERK1 on 'Ser-299' and 'Thr-462' in vitro (PubMed:15319482). May have a guanylyl cyclase activity (PubMed:10557222, PubMed:10938344, PubMed:17138891, PubMed:17520012, PubMed:18694562, PubMed:19124768). Phosphorylates BSK1, BSK2 and BSK3 in vitro (PubMed:18653891). Phosphorylates BSK1, BSK3, BSK5, BSK6, BSK8 and BSK11 in vitro (PubMed:23496207). {ECO:0000269|PubMed:10557222, ECO:0000269|PubMed:10938344, ECO:0000269|PubMed:15319482, ECO:0000269|PubMed:17138891, ECO:0000269|PubMed:17520012, ECO:0000269|PubMed:18653891, ECO:0000269|PubMed:18694562, ECO:0000269|PubMed:19124768, ECO:0000269|PubMed:23496207}.
Arabidopsis thaliana (Mouse-ear cress)
O22527
CLH1_ARATH
MAAIEDSPTFSSVVTPAAFEIGSLPTTEIPVDPVENDSTAPPKPVRITCPTVAGTYPVVLFFHGFYLRNYFYSDVLNHIASHGYILVAPQLCKLLPPGGQVEVDDAGSVINWASENLKAHLPTSVNANGKYTSLVGHSRGGKTAFAVALGHAATLDPSITFSALIGIDPVAGTNKYIRTDPHILTYKPESFELDIPVAVVGTGLGPKWNNVMPPCAPTDLNHEEFYKECKATKAHFVAADYGHMDMLDDDLPGFVGFMAGCMCKNGQRKKSEMRSFVGGIVVAFLKYSLWGEKAEIRLIVKDPSVSPAKLDPSPELEEASGIFV
3.1.1.14
null
chlorophyll catabolic process [GO:0015996]; defense response to bacterium [GO:0042742]; defense response to fungus [GO:0050832]
cytosol [GO:0005829]; nucleus [GO:0005634]; plant-type vacuole [GO:0000325]
chlorophyllase activity [GO:0047746]; pheophytinase b activity [GO:0102293]
PF07224;
3.40.50.1820;
AB hydrolase superfamily, Lipase family
null
SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:17996203}.
CATALYTIC ACTIVITY: Reaction=a chlorophyll + H2O = a chlorophyllide + H(+) + phytol; Xref=Rhea:RHEA:19605, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17327, ChEBI:CHEBI:139291, ChEBI:CHEBI:139292; EC=3.1.1.14; Evidence={ECO:0000269|PubMed:10611389}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19606; Evidence={ECO:0000269|PubMed:10611389}; CATALYTIC ACTIVITY: Reaction=chlorophyll a + H2O = chlorophyllide a + H(+) + phytol; Xref=Rhea:RHEA:38011, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17327, ChEBI:CHEBI:58416, ChEBI:CHEBI:83348; EC=3.1.1.14; Evidence={ECO:0000269|PubMed:10611389}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38012; Evidence={ECO:0000269|PubMed:10611389};
null
PATHWAY: Porphyrin-containing compound metabolism; chlorophyll degradation. {ECO:0000305}.
null
null
FUNCTION: Catalyzes the hydrolysis of ester bond in chlorophyll to yield chlorophyllide and phytol (PubMed:10611389, PubMed:11950974). Shows a preferential activity toward chlorophyll a (PubMed:11950974). Does not seem to be required for chlorophyll degradation during senescence (PubMed:17996203, PubMed:18349515, PubMed:31779896). May modulate the balance between different plant defense pathways (PubMed:15598807). {ECO:0000269|PubMed:10611389, ECO:0000269|PubMed:11950974, ECO:0000269|PubMed:15598807, ECO:0000269|PubMed:17996203, ECO:0000269|PubMed:18349515, ECO:0000269|PubMed:31779896}.
Arabidopsis thaliana (Mouse-ear cress)
O22558
STY8_ARATH
MTIKDESESCGSRAVVASPSQENPRHYRMKLDVYSEVLQRLQESNYEEATLPDFEDQLWLHFNRLPARYALDVKVERAEDVLTHQRLLKLAADPATRPVFEVRSVQVSPRISADSDPAVEEDAQSSHQPSGPGVLAPPTFGSSPNFEAITQGSKIVEDVDSVVNATLSTRPMHEITFSTIDKPKLLSQLTSLLGELGLNIQEAHAFSTVDGFSLDVFVVDGWSQEETDGLRDALSKEILKLKDQPGSKQKSISFFEHDKSSNELIPACIEIPTDGTDEWEIDVTQLKIEKKVASGSYGDLHRGTYCSQEVAIKFLKPDRVNNEMLREFSQEVFIMRKVRHKNVVQFLGACTRSPTLCIVTEFMARGSIYDFLHKQKCAFKLQTLLKVALDVAKGMSYLHQNNIIHRDLKTANLLMDEHGLVKVADFGVARVQIESGVMTAETGTYRWMAPEVIEHKPYNHKADVFSYAIVLWELLTGDIPYAFLTPLQAAVGVVQKGLRPKIPKKTHPKVKGLLERCWHQDPEQRPLFEEIIEMLQQIMKEVNVVV
2.7.11.1
null
chloroplast organization [GO:0009658]; phosphorylation [GO:0016310]; signal transduction [GO:0007165]
cytosol [GO:0005829]
ATP binding [GO:0005524]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674]; protein serine/threonine/tyrosine kinase activity [GO:0004712]
PF07714;
1.10.510.10;
Protein kinase superfamily, Ser/Thr protein kinase family
PTM: Autophosphorylated on serine and threonine residues. Autophosphorylated at Thr-439. {ECO:0000269|PubMed:17090544, ECO:0000269|PubMed:21799034}.
SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:17090544, ECO:0000269|PubMed:21799034}.
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:17090544}; 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:17090544};
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=21.6 uM for ATP {ECO:0000269|PubMed:17090544};
null
null
null
FUNCTION: Serine/threonine protein kinase that specifically phosphorylates chloroplast precursor proteins in the cytosol within the cleavable presequences (transit peptides). May be part of a cytosolic regulatory network involved in chloroplast protein import. Does not phosphorylate mitochondrion precursor proteins. Specific for ATP and does not utilize other NTPs (PubMed:16429265, PubMed:17090544). Plays a role in chloroplast biogenesis and differentiation in cotyledons, possibly through phosphorylation of chloroplast preproteins (PubMed:21799034). {ECO:0000269|PubMed:17090544, ECO:0000269|PubMed:21799034}.
Arabidopsis thaliana (Mouse-ear cress)
O22607
MSI4_ARATH
MESDEAAAVSPQATTPSGGTGASGPKKRGRKPKTKEDSQTPSSQQQSDVKMKESGKKTQQSPSVDEKYSQWKGLVPILYDWLANHNLVWPSLSCRWGPQLEQATYKNRQRLYLSEQTDGSVPNTLVIANCEVVKPRVAAAEHISQFNEEARSPFVKKYKTIIHPGEVNRIRELPQNSKIVATHTDSPDVLIWDVETQPNRHAVLGAANSRPDLILTGHQDNAEFALAMCPTEPFVLSGGKDKSVVLWSIQDHITTIGTDSKSSGSIIKQTGEGTDKNESPTVGPRGVYHGHEDTVEDVAFSPTSAQEFCSVGDDSCLILWDARTGTNPVTKVEKAHDADLHCVDWNPHDDNLILTGSADNTVRLFDRRKLTANGVGSPIYKFEGHKAAVLCVQWSPDKSSVFGSSAEDGLLNIWDYDRVSKKSDRAAKSPAGLFFQHAGHRDKVVDFHWNASDPWTIVSVSDDCETTGGGGTLQIWRMSDLIYRPEEEVVAELEKFKSHVMTCASKP
null
null
cell differentiation [GO:0030154]; DNA repair [GO:0006281]; epigenetic regulation of gene expression [GO:0040029]; flower development [GO:0009908]; gene silencing by RNA-directed DNA methylation [GO:0080188]; regulation of DNA-templated transcription [GO:0006355]; regulation of photoperiodism, flowering [GO:2000028]; regulation of timing of transition from vegetative to reproductive phase [GO:0048510]; response to diterpene [GO:1904629]; response to UV-B [GO:0010224]; systemic acquired resistance [GO:0009627]
Cul4-RING E3 ubiquitin ligase complex [GO:0080008]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; ESC/E(Z) complex [GO:0035098]; histone deacetylase complex [GO:0000118]; mitochondrion [GO:0005739]; nucleolus [GO:0005730]; nucleus [GO:0005634]; NuRD complex [GO:0016581]; Rpd3L complex [GO:0033698]; Rpd3L-Expanded complex [GO:0070210]
histone binding [GO:0042393]; metal ion binding [GO:0046872]; nucleosome binding [GO:0031491]
PF12265;PF00400;
2.130.10.10;
WD repeat RBAP46/RBAP48/MSI1 family
null
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:14745447, ECO:0000269|PubMed:22960247}.
null
null
null
null
null
FUNCTION: Core histone-binding subunit that may target chromatin assembly factors, chromatin remodeling factors and histone deacetylases to their histone substrates in a manner that is regulated by nucleosomal DNA. Component of the flowering autonomous pathway which positively regulates flowering by promoting transcriptional repression of the flowering repressor FLC. May promote histone deacetylation at the FLC locus leading to the formation of repressive chromatin structures. Forms a histone deacetylase complex with HDA5, HDA6 and FLD that represses FLC gene expression to control flowering time (PubMed:25922987). Also negatively regulates cold-responsive genes. Acts together with PDP1 and MSI5 to regulate the function of the PRC2 complex on FLC (PubMed:29314758). Required for systemic acquired resistance (SAR) toward pathogenic bacteria (e.g. Pseudomonas syringae pv tomato DC3000 (avrPto)) (PubMed:32392578). Together with FLD and MSI4/FVE, contributes to dehydroabietinal-dependent (DA, a diterpenoid tricyclic diterpene) activation of flowering ans SAR (PubMed:32392578). {ECO:0000269|PubMed:12548286, ECO:0000269|PubMed:14593187, ECO:0000269|PubMed:14745447, ECO:0000269|PubMed:14745450, ECO:0000269|PubMed:25922987, ECO:0000269|PubMed:29314758, ECO:0000269|PubMed:32392578}.
Arabidopsis thaliana (Mouse-ear cress)
O22609
DEGP1_ARATH
MATTTSCSLLLSSTLFLHSPPSSHLSFFNLSSSRSSPISLYPIRSKRYFRILSKLSLNDNNRDDDDDTLHFTPFSAVKPFFLLCTSVALSFSLFAASPAVESASAFVVSTPKKLQTDELATVRLFQENTPSVVYITNLAVRQDAFTLDVLEVPQGSGSGFVWDKQGHIVTNYHVIRGASDLRVTLADQTTFDAKVVGFDQDKDVAVLRIDAPKNKLRPIPVGVSADLLVGQKVFAIGNPFGLDHTLTTGVISGLRREISSAATGRPIQDVIQTDAAINPGNSGGPLLDSSGTLIGINTAIYSPSGASSGVGFSIPVDTVGGIVDQLVRFGKVTRPILGIKFAPDQSVEQLGVSGVLVLDAPPSGPAGKAGLQSTKRDGYGRLVLGDIITSVNGTKVSNGSDLYRILDQCKVGDEVTVEVLRGDHKEKISVTLEPKPDES
3.4.21.-
null
photosystem II repair [GO:0010206]; protein catabolic process [GO:0030163]; proteolysis [GO:0006508]
chloroplast [GO:0009507]; chloroplast thylakoid [GO:0009534]; chloroplast thylakoid membrane [GO:0009535]; cytosol [GO:0005829]; nucleus [GO:0005634]; thylakoid [GO:0009579]; thylakoid lumen [GO:0031977]
identical protein binding [GO:0042802]; serine-type endopeptidase activity [GO:0004252]; serine-type peptidase activity [GO:0008236]
PF13180;PF13365;
2.30.42.10;2.40.10.10;
Peptidase S1C family
null
SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane {ECO:0000269|PubMed:11719511, ECO:0000269|PubMed:21877139, ECO:0000269|PubMed:9507020}; Peripheral membrane protein {ECO:0000269|PubMed:11719511, ECO:0000269|PubMed:9507020}; Lumenal side {ECO:0000269|PubMed:11719511, ECO:0000269|PubMed:9507020}.
null
null
null
null
null
FUNCTION: Serine protease that is required at high temperature. May be involved in the degradation of damaged proteins. In vivo, can degrade beta-casein. {ECO:0000269|PubMed:21877139, ECO:0000269|PubMed:9507020}.
Arabidopsis thaliana (Mouse-ear cress)
O22655
PROF4_MAIZE
MSWQAYVDEHLMCEIEGQHLSAAAIVGHDGSVWAQSESFPELKPEEVAGIIKDFDEPGTLAPTGLFVGGTKYMVIQGEPGVVIRGKKGTGGITIKKTGMSLIIGVYDEPMTPGQCNMVVERLGDYLIEQGF
null
null
nuclear migration [GO:0007097]; pollen development [GO:0009555]; pollen tube growth [GO:0009860]; regulation of actin cytoskeleton organization [GO:0032956]; sequestering of actin monomers [GO:0042989]
cell cortex [GO:0005938]; cytoskeleton [GO:0005856]
actin monomer binding [GO:0003785]; proline-rich region binding [GO:0070064]
PF00235;
3.30.450.30;
Profilin family
PTM: Phosphorylated by MAP kinases. {ECO:0000250}.
SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton.
null
null
null
null
null
FUNCTION: Binds to actin and affects the structure of the cytoskeleton. At high concentrations, profilin prevents the polymerization of actin, whereas it enhances it at low concentrations. By binding to PIP2, it inhibits the formation of IP3 and DG. Has a high affinity for poly-proline.
Zea mays (Maize)
O22666
RGP3_ARATH
MAQLYSSVKPTPMLKDELDIVIPTIRNLDFLEMWRPFFEQYHLIIVQDGDPSKVINIPVGFDYELYNRNDINRILGPKASCISFKDSACRCFGYMVSKKKYIYTIDDDCFVAKDPTGKEINALEQHIKNLLSPSTPHFFNTLYDPYRDGADFVRGYPFSMREGAITAVSHGLWLNIPDYDAPTQLVKPLEKNSRYVDAVMTIPKGTLFPMCGMNLAFDRELIGPAMYFGLMGDGQPIGRYDDMWAGWCVKVICDHMGWGVKTGLPYIWHSKASNPFVNLKKEYNGIFWQEEAIPFFQSVTLPKECTSVQQCYLELAKLVREKLGKVDPYFITLATGMVTWIEAWEELNSAEGTEAEAPKGKN
5.4.99.30
COFACTOR: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250|UniProtKB:Q8H8T0}; Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:Q8H8T0};
cell wall organization [GO:0071555]; plant-type cell wall biogenesis [GO:0009832]; UDP-L-arabinose metabolic process [GO:0033356]
cytosol [GO:0005829]; Golgi apparatus [GO:0005794]; membrane [GO:0016020]; plasmodesma [GO:0009506]
intramolecular transferase activity [GO:0016866]; UDP-arabinopyranose mutase activity [GO:0052691]
PF03214;
null
RGP family
PTM: Reversibly glycosylated in vitro by UDP-glucose, UDP-xylose and UDP-galactose, but not UDP-mannose. {ECO:0000250|UniProtKB:Q9SRT9}.
SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:21478444}. Golgi apparatus {ECO:0000269|PubMed:21478444}. Note=Soluble and membrane-associated.
CATALYTIC ACTIVITY: Reaction=UDP-beta-L-arabinofuranose = UDP-beta-L-arabinopyranose; Xref=Rhea:RHEA:28350, ChEBI:CHEBI:61457, ChEBI:CHEBI:61463; EC=5.4.99.30; Evidence={ECO:0000269|PubMed:21478444};
null
null
null
null
FUNCTION: UDP-L-arabinose mutase involved in the biosynthesis of cell wall non-cellulosic polysaccharides. Catalyzes the interconvertion of UDP-L-arabinopyranose (UDP-Arap) and UDP-L-arabinofuranose (UDP-Araf). Preferentially catalyzes the formation of UDP-Arap from UDP-Araf. At thermodynamic equilibrium in vitro the ratio of the pyranose form over the furanose form is 95:5. Is not active on other UDP-sugars (UDP-Gal, UDP-Xyl, UDP-Glc, GDP-Man and GDP-Fuc). Is probably active as heteromer in vivo. {ECO:0000269|PubMed:21478444}.
Arabidopsis thaliana (Mouse-ear cress)
O22682
CYSK4_ARATH
MAFASPSLRLLPQSPLGRITSKLHRFSTAKLSLFSFHHDSSSSLAVRTPVSSFVVGAISGKSSTGTKSKSKTKRKPPPPPPVTTVAEEQHIAESETVNIAEDVTQLIGSTPMVYLNRVTDGCLADIAAKLESMEPCRSVKDRIGLSMINEAENSGAITPRKTVLVEPTTGNTGLGIAFVAAAKGYKLIVTMPASINIERRMLLRALGAEIVLTNPEKGLKGAVDKAKEIVLKTKNAYMFQQFDNTANTKIHFETTGPEIWEDTMGNVDIFVAGIGTGGTVTGTGGFLKMMNKDIKVVGVEPSERSVISGDNPGYLPGILDVKLLDEVFKVSNGEAIEMARRLALEEGLLVGISSGAAAVAAVSLAKRAENAGKLITVLFPSHGERYITTALFSSINREVQEMRY
2.5.1.144
COFACTOR: Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; Evidence={ECO:0000250|UniProtKB:P0A1E3};
cysteine biosynthetic process from serine [GO:0006535]; photosynthesis [GO:0015979]; photosynthetic acclimation [GO:0009643]; regulation of hydrogen peroxide metabolic process [GO:0010310]; regulation of superoxide metabolic process [GO:0090322]
chloroplast [GO:0009507]; chloroplast thylakoid lumen [GO:0009543]; thylakoid lumen [GO:0031977]
cysteine synthase activity [GO:0004124]
PF00291;
3.40.50.1100;
Cysteine synthase/cystathionine beta-synthase family
null
SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid lumen {ECO:0000269|PubMed:18431481, ECO:0000269|PubMed:22829322}.
CATALYTIC ACTIVITY: Reaction=O-acetyl-L-serine + thiosulfate = acetate + H(+) + S-sulfo-L-cysteine; Xref=Rhea:RHEA:30891, ChEBI:CHEBI:15378, ChEBI:CHEBI:30089, ChEBI:CHEBI:33542, ChEBI:CHEBI:58340, ChEBI:CHEBI:62225; EC=2.5.1.144; Evidence={ECO:0000269|PubMed:20179139};
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.46 mM for O-acetyl-L-serine {ECO:0000269|PubMed:20179139}; KM=0.93 mM for thiosulfate {ECO:0000269|PubMed:20179139}; Vmax=20.7 mmol/min/mg enzyme toward thiosulfate {ECO:0000269|PubMed:20179139};
null
BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8-9. {ECO:0000269|PubMed:20179139};
BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 30 degrees Celsius. {ECO:0000269|PubMed:20179139};
FUNCTION: S-sulfocysteine synthase that plays an important role in chloroplast function and is essential for light-dependent redox regulation and photosynthetic performance within the chloroplast (PubMed:20179139, PubMed:22829322, PubMed:23333972). Probably unable to interact with SAT and to form the decameric Cys synthase complex (CSC) required for O-acetylserine (thiol)-lyase (OAS-TL) enzymatic activity (PubMed:18223034). Lacks OAS-TL activity (PubMed:20179139). {ECO:0000269|PubMed:18223034, ECO:0000269|PubMed:20179139, ECO:0000269|PubMed:22829322, ECO:0000269|PubMed:23333972}.
Arabidopsis thaliana (Mouse-ear cress)
O22703
RZ1B_ARATH
MKDRENDGNLESRIFVGGLSWDVTERQLESTFDRYGKITECQIMVGRDTGRPRGFGFITFTDRRGADDAIKHMHGRELGNKVISVNKAEPKVGGEDVDQLKKGGGYSSRGKGTEDECFKCRRPGHWARDCPSTGDDRERFRVPLAMRSRIGDIDGHRDRYGDRDLEREREREREFDRYMDGRRDRDGGRYSYRDRFDSGDKYEPRDHYPFERYAPPGDRFVSDRYGMPEHHLENEYRGRERSYDRDRYARDTSDRYGDMGPIRDEGRPYRSRPGPYDRPSRPGGRPSSYERW
null
null
negative regulation of DNA-templated transcription [GO:0045892]; positive regulation of mRNA splicing, via spliceosome [GO:0048026]; response to cold [GO:0009409]; response to water deprivation [GO:0009414]
nuclear speck [GO:0016607]; nucleus [GO:0005634]
DNA binding [GO:0003677]; mRNA binding [GO:0003729]; nucleic acid binding [GO:0003676]; zinc ion binding [GO:0008270]
PF00076;PF00098;
3.30.70.330;4.10.60.10;
null
null
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:20850334}.
null
null
null
null
null
FUNCTION: Binds RNA and DNA sequences non-specifically. May be involved in tolerance to cold stress. {ECO:0000269|PubMed:20850334}.
Arabidopsis thaliana (Mouse-ear cress)
O22715
AP1M2_ARATH
MAGAASALFLLDIKGRVLVWRDYRGDVSAAQAERFFTKLIEKEGDSQSNDPVAYDNGVTYMFVQHSNVYLMIASRQNCNAASLLFFLHRVVDVFKHYFEELEEESLRDNFVVVYELLDEMMDFGYPQYTEARILSEFIKTDAYRMEVTQRPPMAVTNAVSWRSEGIQYKKNEVFLDVIENVNILVNSNGQIVRSDVVGALKMRTYLTGMPECKLGLNDRVLLEAQGRATKGKAIDLEDIKFHQCVRLARFENDRTISFIPPDGAFDLMTYRLSTQVKPLIWVEAQIESHSRSRVEMLIKARSQFKERSTATNVEIELPVPTDASNPTVRTSLGSASYAPEKDALVWKIKSFPGNKEYMLRAEFHLPSITAEEATPERKAPIRVKFEIPYFTVSGIQVRYLKIIEKSGYQALPWVRYITMAGEYELRLV
null
null
clathrin-coated vesicle cargo loading, AP-1-mediated [GO:0035653]; intracellular protein transport [GO:0006886]; post-Golgi vesicle-mediated transport [GO:0006892]; vacuolar transport [GO:0007034]
AP-1 adaptor complex [GO:0030121]; early endosome membrane [GO:0031901]; nucleus [GO:0005634]; trans-Golgi network [GO:0005802]; trans-Golgi network transport vesicle membrane [GO:0012510]
clathrin adaptor activity [GO:0035615]
PF00928;PF01217;
3.30.450.60;2.60.40.1170;
Adaptor complexes medium subunit family
null
SUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network membrane {ECO:0000269|PubMed:23543752, ECO:0000269|PubMed:23733933, ECO:0000269|PubMed:23766365}; Peripheral membrane protein {ECO:0000305|PubMed:11598180}; Cytoplasmic side {ECO:0000305|PubMed:11598180}. Early endosome membrane {ECO:0000269|PubMed:23766365}; Peripheral membrane protein {ECO:0000305|PubMed:11598180}; Cytoplasmic side {ECO:0000305|PubMed:11598180}. Cytoplasmic vesicle, clathrin-coated vesicle membrane {ECO:0000305|PubMed:23733933}; Peripheral membrane protein {ECO:0000305|PubMed:11598180}; Cytoplasmic side {ECO:0000305|PubMed:11598180}.
null
null
null
null
null
FUNCTION: Subunit of clathrin-associated adaptor protein complex 1 that plays a role in protein sorting at the trans-Golgi network and early endosomes (TGN/EE). The AP complexes mediate the recruitment of clathrin to membranes and the recognition of sorting signals within the cytosolic tails of transmembrane cargo molecules. Required for KNOLLE localization at the cell plate to mediate cytokinesis. Functions redundantly with AP1M1 in multiple post-Golgi trafficking pathways leading from the TGN to the vacuole, the plasma membrane, and the cell-division plane. {ECO:0000269|PubMed:23543752, ECO:0000269|PubMed:23733933, ECO:0000269|PubMed:23766365}.
Arabidopsis thaliana (Mouse-ear cress)
O22752
MLO7_ARATH
MITRSRCRRSLLWFLVFHGGATATGAPSGGKELSQTPTWAVAVVCTFLILISHLLEKGLQRLANWLWKKHKNSLLEALEKIKAELMILGFISLLLTFGEPYILKICVPRKAALSMLPCLSEDTVLFQKLAPSSLSRHLLAAGDTSINCKQGSEPLITLKGLHQLHILLFFLAIFHIVYSLITMMLSRLKIRGWKKWEQETLSNDYEFSIDHSRLRLTHETSFVREHTSFWTTTPFFFYVGCFFRQFFVSVERTDYLTLRHGFISAHLAPGRKFNFQRYIKRSLEDDFKLVVGISPVLWASFVIFLLFNVNGWRTLFWASIPPLLIILAVGTKLQAIMATMALEIVETHAVVQGMPLVQGSDRYFWFDCPQLLLHLIHFALFQNAFQITHFFWIWYSFGLKSCFHKDFNLVVSKLFLCLGALILCSYITLPLYALVTQMGSHMKKAVFDEQMAKALKKWHKDIKLKKGKARKLPSKTLGVSESFSLSSSSSATTLHRSKTTGHSSNIIYYKQEDEEDEMSDLEAGAEDAIDRIQQQEMQFHNS
null
null
defense response [GO:0006952]; pollen tube reception [GO:0010483]; response to biotic stimulus [GO:0009607]
cytoplasm [GO:0005737]; endomembrane system [GO:0012505]; plasma membrane [GO:0005886]
calmodulin binding [GO:0005516]
PF03094;
null
MLO family
null
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:21071669}; Multi-pass membrane protein {ECO:0000269|PubMed:21071669}. Endomembrane system {ECO:0000269|PubMed:21071669}. Note=In synergids of unfertilized mature female gametophytes, present in a punctate pattern of endomembranes throughout the cytoplasm. Become polarly localized to the basal half of the synergids, to the filiform apparatus, upon pollen tube arrival at the micropyle. This relocalization upon fertilization requires FER.
null
null
null
null
null
FUNCTION: May be involved in modulation of pathogen defense and leaf cell death. Activity seems to be regulated by Ca(2+)-dependent calmodulin binding and seems not to require heterotrimeric G proteins (By similarity). Controls pollen tube reception in the female gametophyte synergids. {ECO:0000250, ECO:0000269|PubMed:21071669}.
Arabidopsis thaliana (Mouse-ear cress)
O22755
ATL44_ARATH
MTRPSRLLETAAPPPQPSEEMIAAESDMVVILSALLCALICVAGLAAVVRCAWLRRFTAGGDSPSPNKGLKKKALQSLPRSTFTAAESTSGAAAEEGDSTECAICLTDFADGEEIRVLPLCGHSFHVECIDKWLVSRSSCPSCRRILTPVRCDRCGHASTAEMKDQAHRHQHHQHSSTTIPTFLP
2.3.2.27
null
protein autoubiquitination [GO:0051865]; protein monoubiquitination [GO:0006513]; protein ubiquitination [GO:0016567]
membrane [GO:0016020]
metal ion binding [GO:0046872]; ubiquitin protein ligase activity [GO:0061630]
PF13639;
3.30.40.10;
RING-type zinc finger family, ATL subfamily
PTM: Auto-monoubiquitination. {ECO:0000269|Ref.7}.
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:0000305};
null
PATHWAY: Protein modification; protein ubiquitination. {ECO:0000305}.
null
null
FUNCTION: E3 ubiquitin-protein ligase that possess E3 ubiquitin ligase activity in vitro and mediates protein monoubiquitination (Ref.7). Triggers the monoubiquitination of phosphorylated BIK1 in response to pathogen-associated molecular pattern (PAMP) detection (Ref.7). {ECO:0000269|Ref.7}.
Arabidopsis thaliana (Mouse-ear cress)
O22763
BZP10_ARATH
MNSIFSIDDFSDPFWETPPIPLNPDSSKPVTADEVSQSQPEWTFEMFLEEISSSAVSSEPLGNNNNAIVGVSSAQSLPSVSGQNDFEDDSRFRDRDSGNLDCAAPMTTKTVIVDSDDYRRVLKNKLETECATVVSLRVGSVKPEDSTSSPETQLQPVQSSPLTQGELGVTSSLPAEVKKTGVSMKQVTSGSSREYSDDEDLDEENETTGSLKPEDVKKSRRMLSNRESARRSRRRKQEQTSDLETQVNDLKGEHSSLLKQLSNMNHKYDEAAVGNRILKADIETLRAKVKMAEETVKRVTGMNPMLLGRSSGHNNNNRMPITGNNRMDSSSIIPAYQPHSNLNHMSNQNIGIPTILPPRLGNNFAAPPSQTSSPLQRIRNGQNHHVTPSANPYGWNTEPQNDSAWPKKCVD
null
null
plant-type hypersensitive response [GO:0009626]; positive regulation of DNA-templated transcription [GO:0045893]; positive regulation of seed maturation [GO:2000693]; response to molecule of oomycetes origin [GO:0002240]
cytoplasm [GO:0005737]; nucleus [GO:0005634]
DNA-binding transcription factor activity [GO:0003700]; nutrient reservoir activity [GO:0045735]; protein heterodimerization activity [GO:0046982]; sequence-specific DNA binding [GO:0043565]; transcription cis-regulatory region binding [GO:0000976]
PF00170;PF12498;
1.20.5.170;
BZIP family
null
SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00978, ECO:0000269|PubMed:16957775}. Cytoplasm {ECO:0000269|PubMed:16957775}. Note=Shuttles between the nucleus and the cytoplasm. Retained outside the nucleus by LSD1 to prevent cell death.
null
null
null
null
null
FUNCTION: Transcription factor that binds to the C-box-like motif (5'-TGCTGACGTCA-3') and G-box-like motif (5'-CCACGTGGCC-3'), ABRE elements, of gene promoters. Binds to the 5'-ACGT-3' motif of seed storage protein (SSP) encoding gene promoters (e.g. At2S and CRU3) and promotes their expression in seeds when in complex with ABI3 and BZIP53. Involved in the defense responses to the biotrophic pathogen Hyaloperonospora parasitica and oxidative stress responses; mediates positively cell death (PubMed:12657652, PubMed:16957775, PubMed:19261733, PubMed:19531597). Promotes BZIP53-mediated response to hypoosmolarity stress that leads to POX1/PRODH1 accumulation (PubMed:16810321). {ECO:0000269|PubMed:12657652, ECO:0000269|PubMed:16810321, ECO:0000269|PubMed:16957775, ECO:0000269|PubMed:19261733, ECO:0000269|PubMed:19531597}.
Arabidopsis thaliana (Mouse-ear cress)
O22765
TRPA1_ARATH
MDLLKTPSSTVGLSETFARLKSQGKVALIPYITAGDPDLSTTAKALKVLDSCGSDIIELGVPYSDPLADGPAIQAAARRSLLKGTNFNSIISMLKEVIPQLSCPIALFTYYNPILRRGVENYMTVIKNAGVHGLLVPDVPLEETETLRNEARKHQIELVLLTTPTTPKERMNAIVEASEGFIYLVSSVGVTGTRESVNEKVQSLLQQIKEATSKPVAVGFGISKPEHVKQVAEWGADGVIVGSAMVKILGESESPEQGLKELEFFTKSLKSALVS
4.1.2.8; 4.2.1.20
null
auxin biosynthetic process [GO:0009851]
chloroplast [GO:0009507]; cytoplasm [GO:0005737]; cytosol [GO:0005829]
indole-3-glycerol-phosphate lyase activity [GO:0033984]; tryptophan synthase activity [GO:0004834]
PF00290;
3.20.20.70;
TrpA family
null
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:18844775}.
CATALYTIC ACTIVITY: Reaction=(1S,2R)-1-C-(indol-3-yl)glycerol 3-phosphate + L-serine = D-glyceraldehyde 3-phosphate + H2O + L-tryptophan; Xref=Rhea:RHEA:10532, ChEBI:CHEBI:15377, ChEBI:CHEBI:33384, ChEBI:CHEBI:57912, ChEBI:CHEBI:58866, ChEBI:CHEBI:59776; EC=4.2.1.20; Evidence={ECO:0000269|PubMed:18844775}; CATALYTIC ACTIVITY: Reaction=(1S,2R)-1-C-(indol-3-yl)glycerol 3-phosphate = D-glyceraldehyde 3-phosphate + indole; Xref=Rhea:RHEA:14081, ChEBI:CHEBI:16881, ChEBI:CHEBI:58866, ChEBI:CHEBI:59776; EC=4.1.2.8; Evidence={ECO:0000269|PubMed:18844775};
null
PATHWAY: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 5/5.
null
null
FUNCTION: The alpha subunit is responsible for the aldol cleavage of indoleglycerol phosphate to indole and glyceraldehyde 3-phosphate (By similarity). Contributes to the tryptophan-independent indole biosynthesis, and possibly to auxin production. {ECO:0000250, ECO:0000269|PubMed:18844775}.
Arabidopsis thaliana (Mouse-ear cress)
O22768
UNE12_ARATH
MASNNPHDNLSDQTPSDDFFEQILGLPNFSASSAAGLSGVDGGLGGGAPPMMLQLGSGEEGSHMGGLGGSGPTGFHNQMFPLGLSLDQGKGPGFLRPEGGHGSGKRFSDDVVDNRCSSMKPVFHGQPMQQPPPSAPHQPTSIRPRVRARRGQATDPHSIAERLRRERIAERIRALQELVPTVNKTDRAAMIDEIVDYVKFLRLQVKVLSMSRLGGAGAVAPLVTDMPLSSSVEDETGEGGRTPQPAWEKWSNDGTERQVAKLMEENVGAAMQLLQSKALCMMPISLAMAIYHSQPPDTSSVVKPENNPPQ
null
null
double fertilization forming a zygote and endosperm [GO:0009567]; regulation of defense response [GO:0031347]; regulation of DNA-templated transcription [GO:0006355]; regulation of gene expression [GO:0010468]; regulation of salicylic acid mediated signaling pathway [GO:2000031]; response to abscisic acid [GO:0009737]; response to osmotic stress [GO:0006970]; response to salt [GO:1902074]
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]
PF00010;
4.10.280.10;
null
null
SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00981}.
null
null
null
null
null
FUNCTION: Required for ovule fertilization. {ECO:0000269|PubMed:15634699}.
Arabidopsis thaliana (Mouse-ear cress)
O22775
XXT2_ARATH
MIERCLGAYRCRRIQRALRQLKVTILCLLLTVVVLRSTIGAGKFGTPEQDLDEIRQHFHARKRGEPHRVLEEIQTGGDSSSGDGGGNSGGSNNYETFDINKIFVDEGEEEKPDPNKPYTLGPKISDWDEQRSDWLAKNPSFPNFIGPNKPRVLLVTGSAPKPCENPVGDHYLLKSIKNKIDYCRLHGIEIFYNMALLDAEMAGFWAKLPLIRKLLLSHPEIEFLWWMDSDAMFTDMAFELPWERYKDYNLVMHGWNEMVYDQKNWIGLNTGSFLLRNNQWALDLLDTWAPMGPKGKIREEAGKVLTRELKDRPVFEADDQSAMVYLLATQRDAWGNKVYLESGYYLHGYWGILVDRYEEMIENYHPGLGDHRWPLVTHFVGCKPCGKFGDYPVERCLKQMDRAFNFGDNQILQIYGFTHKSLASRKVKRVRNETSNPLEMKDELGLLHPAFKAVKVQTNQV
2.4.-.-; 2.4.2.39
null
polysaccharide biosynthetic process [GO:0000271]; xyloglucan biosynthetic process [GO:0009969]; xyloglucan metabolic process [GO:0010411]
cytosol [GO:0005829]; endosome [GO:0005768]; Golgi apparatus [GO:0005794]; Golgi membrane [GO:0000139]; Golgi trans cisterna [GO:0000138]; trans-Golgi network [GO:0005802]
hexosyltransferase activity [GO:0016758]; protein homodimerization activity [GO:0042803]; UDP-xylosyltransferase activity [GO:0035252]; xyloglucan 6-xylosyltransferase activity [GO:0033843]
PF05637;
null
Glycosyltransferase 34 family
null
SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000269|PubMed:22665445, ECO:0000269|PubMed:25392066}; Single-pass type II membrane protein {ECO:0000305|PubMed:25392066}.
CATALYTIC ACTIVITY: Reaction=Transfers an alpha-D-xylosyl residue from UDP-D-xylose to a glucose residue in xyloglucan, forming an alpha-(1->6)-D-xylosyl-D-glucose linkage.; EC=2.4.2.39; Evidence={ECO:0000269|PubMed:16982611};
null
null
null
null
FUNCTION: Xylosyltransferase specific to UDP-D-xylose that accepts both cellopentaose and cellohexaose as substrates, with a better use of cellohexaose, to produce xyloglucan. Adds preferentially the first xylosyl residue to the fourth glucosyl residue from the reducing end of both acceptors. Transfer one xylose mainly to the second glucose residue from the non-reducing end. The acceptor should have a minimum of four glucose residues (PubMed:16982611, PubMed:18544630). Associates with other xyloglucan-synthesizing enzymes to form multiprotein complexes for xyloglucan synthesis in the Golgi (PubMed:25392066). {ECO:0000269|PubMed:16982611, ECO:0000269|PubMed:18544630, ECO:0000269|PubMed:25392066}.
Arabidopsis thaliana (Mouse-ear cress)
O22781
SUVH2_ARATH
MSTLLPFPDLNLMPDSQSSTAGTTAGDTVVTGKLEVKSEPIEEWQTPPSSTSDQSANTDLIAEFIRISELFRSAFKPLQVKGLDGVSVYGLDSGAIVAVPEKENRELIEPPPGFKDNRVSTVVVSPKFERPRELARIAILGHEQRKELRQVMKRTRMTYESLRIHLMAESMKNHVLGQGRRRRSDMAAAYIMRDRGLWLNYDKHIVGPVTGVEVGDIFFYRMELCVLGLHGQTQAGIDCLTAERSATGEPIATSIVVSGGYEDDEDTGDVLVYTGHGGQDHQHKQCDNQRLVGGNLGMERSMHYGIEVRVIRGIKYENSISSKVYVYDGLYKIVDWWFAVGKSGFGVFKFRLVRIEGQPMMGSAVMRFAQTLRNKPSMVRPTGYVSFDLSNKKENVPVFLYNDVDGDQEPRHYEYIAKAVFPPGIFGQGGISRTGCECKLSCTDDCLCARKNGGEFAYDDNGHLLKGKHVVFECGEFCTCGPSCKSRVTQKGLRNRLEVFRSKETGWGVRTLDLIEAGAFICEYAGVVVTRLQAEILSMNGDVMVYPGRFTDQWRNWGDLSQVYPDFVRPNYPSLPPLDFSMDVSRMRNVACYISHSKEPNVMVQFVLHDHNHLMFPRVMLFALENISPLAELSLDYGLADEVNGKLAICN
null
null
epigenetic regulation of gene expression [GO:0040029]; gene silencing by RNA-directed DNA methylation [GO:0080188]
chromosome, centromeric region [GO:0000775]; heterochromatin [GO:0000792]; nucleus [GO:0005634]
double-stranded DNA binding [GO:0003690]; histone methyltransferase activity [GO:0042054]; zinc ion binding [GO:0008270]
PF05033;PF02182;PF00856;
2.170.270.10;2.30.280.10;
Class V-like SAM-binding methyltransferase superfamily, Histone-lysine methyltransferase family, Suvar3-9 subfamily
null
SUBCELLULAR LOCATION: Nucleus. Chromosome, centromere. Note=Associates with centromeric constitutive heterochromatin.
null
null
null
null
null
FUNCTION: Histone methyltransferase family member that plays a central role in gene silencing (PubMed:15775980, PubMed:16384625, PubMed:19043555, PubMed:24463519, PubMed:27171427). Together with MORC6 and SUVH9, regulates the silencing of some transposable elements (TEs) (PubMed:27171427). According to PubMed:15775980, it is required for normal methylation of 'Lys-9' and 'Lys-27' of histone H3, 'Lys-20' of H4, and cytosine, but PubMed:19043555 see no significant effect on histone methylation when the gene is mutated. According to PubMed:19043555, the protein does not bind S-adenosyl-L-methionine and lacks methyltransferase activity. Instead, it may function downstream of DRM2 in RNA-directed DNA methylation, binding to methylated DNA and recruiting DNA-directed RNA polymerase V to chromatin (PubMed:24463519, PubMed:27171427). {ECO:0000269|PubMed:15775980, ECO:0000269|PubMed:16384625, ECO:0000269|PubMed:19043555, ECO:0000269|PubMed:24463519, ECO:0000269|PubMed:27171427}.
Arabidopsis thaliana (Mouse-ear cress)
O22784
PDLP3_ARATH
MGFYSLKQLLLLYIIIMALFSDLKLAKSSSPEYTNLIYKGCARQRLSDPSGLYSQALSAMYGLLVTQSTKTRFYKTTTGTTSQTSVTGLFQCRGDLSNNDCYNCVSRLPVLSGKLCGKTIAARVQLSGCYLLYEISGFAQISGMELLFKTCGKNNVAGTGFEQRRDTAFGVMQNGVVQGHGFYATTYESVYVLGQCEGDIGDSDCSGCIKNALQRAQVECGSSISGQIYLHKCFVGYSFYPNGVPKRSSPYPSSGSSGSSSSSSSSGTTGKTVAIIVGGTAGVGFLVICLLFVKNLMKKKYDDY
null
null
plasmodesmata-mediated intercellular transport [GO:0010497]; transport of virus in multicellular host [GO:0046739]
plasma membrane [GO:0005886]; plasmodesma [GO:0009506]
null
PF01657;
3.30.430.20;
Cysteine-rich repeat secretory protein family, Plasmodesmata-located proteins (PDLD) subfamily
null
SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q8GXV7}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:Q8GXV7}. Cell junction, plasmodesma {ECO:0000269|PubMed:18215111, ECO:0000269|PubMed:20886105, ECO:0000269|PubMed:25393742}. Note=Co-localizes with the Grapevine fanleaf virus (GFLV) 2B-MP at the base of tubules within modified plasmodesmata.
null
null
null
null
null
FUNCTION: Modulates cell-to-cell trafficking. {ECO:0000250|UniProtKB:Q8GXV7}.
Arabidopsis thaliana (Mouse-ear cress)
O22785
PR19B_ARATH
MNCAISGEVPVEPVVSTKSGLLFERRLIERHISDYGKCPVTGEPLTIDDIVPIKTGEIIKPKTLHTASIPGLLGTFQNEWDGLMLSNFALEQQLHTARQELSHALYQHDSACRVIARLKKERDEARQLLAEVERHIPAAPEAVTANAALSNGKRAAVDEELGPDAKKLCPGISAEIITELTDCNAALSQKRKKRQIPQTLASIDTLERFTQLSSHPLHKTNKPGICSMDILHSKDVIATGGVDATAVLFDRPSGQILSTLTGHSKKVTSVKFVGDSDLVLTASADKTVRIWRNPGDGNYACGYTLNDHSAEVRAVTVHPTNKYFVSASLDGTWCFYDLSSGSCLAQVSDDSKNVDYTAAAFHPDGLILGTGTSQSVVKIWDVKSQANVAKFDGHTGEVTAISFSENGYFLATAAEDGVRLWDLRKLRNFKSFLSADANSVEFDPSGSYLGIAASDIKVYQTASVKAEWNLIKTLPDLSGTGKATCVKFGSDAQYVAVGSMDRNLRIFGLPGDEKANVDDDSAQDS
2.3.2.27
null
defense response to bacterium [GO:0042742]; DNA repair [GO:0006281]; innate immune response [GO:0045087]; mRNA splicing, via spliceosome [GO:0000398]; protein K63-linked ubiquitination [GO:0070534]
Cul4-RING E3 ubiquitin ligase complex [GO:0080008]; endoplasmic reticulum [GO:0005783]; nucleus [GO:0005634]; plant-type cell wall [GO:0009505]; Prp19 complex [GO:0000974]; U2-type catalytic step 1 spliceosome [GO:0071006]
ubiquitin protein ligase activity [GO:0061630]
PF08606;PF00400;
2.130.10.10;3.30.40.10;
WD repeat PRP19 family
null
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:19629177}.
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:18393940};
null
PATHWAY: Protein modification; protein ubiquitination. {ECO:0000269|PubMed:18393940}.
null
null
FUNCTION: Probable ubiquitin-protein ligase which is mainly involved pre-mRNA splicing and DNA repair (By similarity). Component of the MAC complex that probably regulates defense responses through transcriptional control and thereby is essential for plant innate immunity. {ECO:0000250|UniProtKB:Q9UMS4, ECO:0000269|PubMed:18393940, ECO:0000269|PubMed:19629177}.
Arabidopsis thaliana (Mouse-ear cress)
O22788
PXG3_ARATH
MAGEAEALATTAPLAPVTSQRKVRNDLEETLPKPYMARALAAPDTEHPNGTEGHDSKGMSVMQQHVAFFDQNDDGIVYPWETYKGFRDLGFNPISSIFWTLLINLAFSYVTLPSWVPSPLLPVYIDNIHKAKHGSDSSTYDTEGRYVPVNLENIFSKYALTVKDKLSFKEVWNVTEGNRMAIDPFGWLSNKVEWILLYILAKDEDGFLSKEAVRGCFDGSLFEQIAKERANSRKQD
1.11.2.3
COFACTOR: Name=heme b; Xref=ChEBI:CHEBI:60344; Evidence={ECO:0000250}; Note=Binds 1 heme b (iron(II)-protoporphyrin IX) group. {ECO:0000250}; COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000269|PubMed:19467604};
(R)-2-hydroxy-alpha-linolenic acid biosynthetic process [GO:1902609]; defense response to fungus [GO:0050832]; oxylipin metabolic process [GO:0031407]; regulation of reactive oxygen species metabolic process [GO:2000377]; response to abscisic acid [GO:0009737]; response to cold [GO:0009409]; response to desiccation [GO:0009269]; response to fungus [GO:0009620]; response to salicylic acid [GO:0009751]; response to salt stress [GO:0009651]; stomatal movement [GO:0010118]
chloroplast membrane [GO:0031969]; endoplasmic reticulum [GO:0005783]; intracellular membrane-bounded organelle [GO:0043231]; monolayer-surrounded lipid storage body [GO:0012511]; plant-type vacuole [GO:0000325]
18-hydroxyoleate peroxygenase activity [GO:0102070]; calcium ion binding [GO:0005509]; monooxygenase activity [GO:0004497]; plant seed peroxidase activity [GO:1990137]
PF05042;
null
Caleosin family
PTM: Phosphorylated. Increased phosphorylation upon stress. {ECO:0000269|PubMed:19467604}.
SUBCELLULAR LOCATION: Microsome membrane. Plastid, chloroplast membrane. Lipid droplet.
CATALYTIC ACTIVITY: Reaction=RH + ROOH = ROH + ROH.; EC=1.11.2.3;
null
null
null
null
FUNCTION: Probable calcium-binding peroxygenase. May be involved in the degradation of storage lipid in oil bodies, in abiotic stress-related signaling pathway and in drought tolerance through stomatal control under water deficit conditions. {ECO:0000269|PubMed:19467604, ECO:0000269|PubMed:20952421}.
Arabidopsis thaliana (Mouse-ear cress)
O22793
MORF2_ARATH
MALPLSGTRHLTRALLSNVTLMAPPRIPSSVHYGGSRLGCSTRFFSIRCGANRSGSTYSPLNSGSNFSDRPPTEMAPLFPGCDYEHWLIVMDKPGGEGATKQQMIDCYIQTLAKVVGSEEEAKKRIYNVSCERYLGFGCEIDEETSTKLEGLPGVLFVLPDSYVDPENKDYGAELFVNGEIVQRSPERQRRVEPQPQRAQDRPRYNDRTRYSRRRENTR
null
null
cytidine to uridine editing [GO:0016554]; endonucleolytic cleavage of tetracistronic rRNA transcript (SSU-rRNA, LSU-rRNA, 4.5S-rRNA, 5S-rRNA) [GO:0002103]; mitochondrial mRNA modification [GO:0080156]; mRNA processing [GO:0006397]; plastid organization [GO:0009657]
chloroplast [GO:0009507]; endoplasmic reticulum [GO:0005783]; mitochondrion [GO:0005739]
protein dimerization activity [GO:0046983]; protein homodimerization activity [GO:0042803]
null
3.30.70.80;
MORF family
null
SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000269|PubMed:12678554, ECO:0000269|PubMed:25583991, ECO:0000269|PubMed:28213559}.
null
null
null
null
null
FUNCTION: Involved in plastid rRNA processing and consequently in translation and early chloroplast differentiation (PubMed:12678554). Involved in organellar RNA editing. Required for the processing of multiple editing sites in plastids (PubMed:22411807, PubMed:23818871). {ECO:0000269|PubMed:12678554, ECO:0000269|PubMed:22411807, ECO:0000269|PubMed:23818871}.
Arabidopsis thaliana (Mouse-ear cress)
O22806
BUBR1_ARATH
MAAETKVQVSDPEAEFLNSKQETGYEWELFKENVRPLKRGRNVGILNHALKSHSDHQLRKNLIEKRRNLIEAIDEYEGDDPLSPWIECIKWVQEAFPPGGECSGLLVIYEQCVRKFWHSERYKDDLRYLKVWLEYAEHCADAEVIYKFLEVNEIGKTHAVYYIAYALHIEFKNKVKTANEIFNLGISRDAKPVEKLNDAYKKFMVRTMRRSNTADEEPKENNDLPSRSFGTLLSRGDNNARRQALGSSNPQAKKLKPNQSSKTPFAIYADAVSDTTSGNQPESDKSRPEFGSWLMLGGRAERNKENNSLPRKWASFKVPQKPIVRTVAAASASTFEVFVDEEECTEEEEEKKKNDETISSSSNVLPLNGGREIKKETELLRQNPLRHFPPNSFLR
null
null
meiotic sister chromatid cohesion, centromeric [GO:0051754]; mitotic spindle assembly checkpoint signaling [GO:0007094]
chromocenter [GO:0010369]; cytoplasm [GO:0005737]; kinetochore [GO:0000776]; kinetochore microtubule [GO:0005828]; microtubule organizing center [GO:0005815]; nucleus [GO:0005634]; spindle microtubule [GO:0005876]
protein kinase activity [GO:0004672]
PF08311;
1.25.40.430;
null
null
SUBCELLULAR LOCATION: Chromosome {ECO:0000269|PubMed:19710914}. Cytoplasm {ECO:0000269|PubMed:19710914}. Nucleus {ECO:0000269|PubMed:19710914}. Chromosome, centromere, kinetochore {ECO:0000269|PubMed:19710914}. Cytoplasm, cytoskeleton, spindle {ECO:0000269|PubMed:19710914}. Cytoplasm, cytoskeleton, microtubule organizing center {ECO:0000250|UniProtKB:O60566}. Note=Cytoplasmic in interphase cells. Accumulates onto both kinetochores and the spindle microtubules in cell arrested in metaphase. Associates with unattached kinetochores in early prophase upon spindle assembly checkpoint (SAC) activation. Present in chromocenters.
null
null
null
null
null
FUNCTION: Essential component of the mitotic checkpoint. Required for normal mitosis progression. The mitotic checkpoint delays anaphase until all chromosomes are properly attached to the mitotic spindle. One of its checkpoint functions may be to inhibit the activity of the anaphase-promoting complex/cyclosome (APC/C) by blocking the binding of CDC20 to APC/C (By similarity). {ECO:0000250, ECO:0000269|PubMed:19710914}.
Arabidopsis thaliana (Mouse-ear cress)
O22822
U74F2_ARATH
MEHKRGHVLAVPYPTQGHITPFRQFCKRLHFKGLKTTLALTTFVFNSINPDLSGPISIATISDGYDHGGFETADSIDDYLKDFKTSGSKTIADIIQKHQTSDNPITCIVYDAFLPWALDVAREFGLVATPFFTQPCAVNYVYYLSYINNGSLQLPIEELPFLELQDLPSFFSVSGSYPAYFEMVLQQFINFEKADFVLVNSFQELELHENELWSKACPVLTIGPTIPSIYLDQRIKSDTGYDLNLFESKDDSFCINWLDTRPQGSVVYVAFGSMAQLTNVQMEELASAVSNFSFLWVVRSSEEEKLPSGFLETVNKEKSLVLKWSPQLQVLSNKAIGCFLTHCGWNSTMEALTFGVPMVAMPQWTDQPMNAKYIQDVWKAGVRVKTEKESGIAKREEIEFSIKEVMEGERSKEMKKNVKKWRDLAVKSLNEGGSTDTNIDTFVSRVQSK
2.4.1.-
null
benzoate metabolic process [GO:0018874]; para-aminobenzoic acid metabolic process [GO:0046482]; positive regulation of seed germination [GO:0010030]; salicylic acid metabolic process [GO:0009696]
cytosol [GO:0005829]
benzoic acid glucosyltransferase activity [GO:0052641]; nicotinate-O-glucosyltransferase activity [GO:0090704]; quercetin 3-O-glucosyltransferase activity [GO:0080043]; quercetin 7-O-glucosyltransferase activity [GO:0080044]; salicylic acid glucosyltransferase (ester-forming) activity [GO:0052639]; salicylic acid glucosyltransferase (glucoside-forming) activity [GO:0052640]; UDP-glucose:4-aminobenzoate acylglucosyltransferase activity [GO:0080002]; UDP-glucosyltransferase activity [GO:0035251]
PF00201;
3.40.50.2000;
UDP-glycosyltransferase family
null
null
null
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=80 uM for anthranilate {ECO:0000269|PubMed:12475971, ECO:0000269|PubMed:17085977, ECO:0000269|PubMed:18385129}; KM=190 uM for salicylate {ECO:0000269|PubMed:12475971, ECO:0000269|PubMed:17085977, ECO:0000269|PubMed:18385129}; KM=540 uM for benzoate {ECO:0000269|PubMed:12475971, ECO:0000269|PubMed:17085977, ECO:0000269|PubMed:18385129}; KM=920 uM for 4-aminobenzoate {ECO:0000269|PubMed:12475971, ECO:0000269|PubMed:17085977, ECO:0000269|PubMed:18385129};
null
null
null
FUNCTION: Glycosyltransferase that glucosylates benzoic acid and derivatives. Substrate preference is benzoic acid > salicylic acid (SA) > 3-hydroxybenzoic acid > 4-hydroxybenzoic acid. Catalyzes the formation of both SA 2-O-beta-D-glucoside (SAG) and SA glucose ester (SGE). Has high affinity for the tryptophan precursor anthranilate. Catalyzes the formation of anthranilate glucose ester. Is the major source of this activity in the plant. {ECO:0000269|PubMed:11641410, ECO:0000269|PubMed:12475971, ECO:0000269|PubMed:17085977, ECO:0000269|PubMed:18226820, ECO:0000269|PubMed:18385129}.
Arabidopsis thaliana (Mouse-ear cress)
O22823
LSM6B_ARATH
MSGVGEKASGTTKTPADFLKSIRGKPVVVKLNSGVDYRGILTCLDGYMNIAMEQTEEYVNGQLKNTYGDAFVRGNNVLYISTTKGTLSDGA
null
null
deadenylation-dependent decapping of nuclear-transcribed mRNA [GO:0000290]; maturation of SSU-rRNA [GO:0030490]; mRNA splicing, via spliceosome [GO:0000398]
Lsm1-7-Pat1 complex [GO:1990726]; Lsm2-8 complex [GO:0120115]; nucleolus [GO:0005730]; nucleus [GO:0005634]; P-body [GO:0000932]; sno(s)RNA-containing ribonucleoprotein complex [GO:0005732]; spliceosomal complex [GO:0005681]; U4/U6 x U5 tri-snRNP complex [GO:0046540]; U6 snRNP [GO:0005688]
mRNA binding [GO:0003729]
PF01423;
2.30.30.100;
SnRNP Sm proteins family
null
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:23221597}. Nucleus {ECO:0000269|PubMed:23221597}.
null
null
null
null
null
FUNCTION: Component of LSM protein complexes, which are involved in RNA processing. Component of the cytoplasmic LSM1-LSM7 complex which is involved in mRNA degradation by promoting decapping and leading to accurate 5'-3' mRNA decay. The cytoplasmic LSM1-LSM7 complex regulates developmental gene expression by the decapping of specific development-related transcripts. Component of the nuclear LSM2-LSM8 complex which is involved splicing nuclear mRNAs. LSM2-LSM8 binds directly to the U6 small nuclear RNAs (snRNAs) and is essential for accurate splicing of selected development-related mRNAs through the stabilization of the spliceosomal U6 snRNA. Plays a critical role in the regulation of development-related gene expression. {ECO:0000269|PubMed:23221597, ECO:0000269|PubMed:23620288}.
Arabidopsis thaliana (Mouse-ear cress)
O22832
STAD7_ARATH
MALKFNPLVASQPYKFPSSTRPPTPSFRSPKFLCLASSSPALSSGPKEVESLKKPFTPPREVHVQVLHSMPPQKIEIFKSMENWAEENLLIHLKDVEKSWQPQDFLPDPASDGFEDQVRELRERARELPDDYFVVLVGDMITEEALPTYQTMLNTLDGVRDETGASPTSWAIWTRAWTAEENRHGDLLNKYLYLSGRVDMRQIEKTIQYLIGSGMDPRTENNPYLGFIYTSFQERATFISHGNTARQAKEHGDIKLAQICGTIAADEKRHETAYTKIVEKLFEIDPDGTVMAFADMMRKKISMPAHLMYDGRNDNLFDNFSSVAQRLGVYTAKDYADILEFLVGRWKIQDLTGLSGEGNKAQDYLCGLAPRIKRLDERAQARAKKGPKIPFSWIHDREVQL
1.14.19.2
COFACTOR: Name=Fe(2+); Xref=ChEBI:CHEBI:29033; Evidence={ECO:0000250|UniProtKB:P22337}; Note=Binds 2 Fe(2+) ions per subunit. {ECO:0000250|UniProtKB:P22337};
defense response [GO:0006952]; fatty acid biosynthetic process [GO:0006633]; fatty acid metabolic process [GO:0006631]
chloroplast stroma [GO:0009570]; cytosol [GO:0005829]
acyl-[acyl-carrier-protein] desaturase activity [GO:0045300]; metal ion binding [GO:0046872]; stearoyl-[acp] desaturase activity [GO:0102786]; stearoyl-CoA 9-desaturase activity [GO:0004768]
PF03405;
1.10.620.20;
Fatty acid desaturase type 2 family
null
SUBCELLULAR LOCATION: Plastid, chloroplast stroma {ECO:0000269|PubMed:18431481}.
CATALYTIC ACTIVITY: Reaction=2 H(+) + O2 + octadecanoyl-[ACP] + 2 reduced [2Fe-2S]-[ferredoxin] = (9Z)-octadecenoyl-[ACP] + 2 H2O + 2 oxidized [2Fe-2S]-[ferredoxin]; Xref=Rhea:RHEA:11776, Rhea:RHEA-COMP:9656, Rhea:RHEA-COMP:9924, Rhea:RHEA-COMP:10000, Rhea:RHEA-COMP:10001, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:33737, ChEBI:CHEBI:33738, ChEBI:CHEBI:78495, ChEBI:CHEBI:78783; EC=1.14.19.2; Evidence={ECO:0000250|UniProtKB:P22337};
null
PATHWAY: Lipid metabolism; fatty acid metabolism.
null
null
FUNCTION: Converts stearoyl-ACP to oleoyl-ACP by introduction of a cis double bond between carbons 9 and 10 of the acyl chain. Required for the activation of certain jasmonic acid (JA)-mediated responses and the repression of the salicylic acid (SA) signaling pathway. {ECO:0000269|PubMed:11309146, ECO:0000269|PubMed:11481500, ECO:0000269|PubMed:14601670, ECO:0000269|PubMed:14615603, ECO:0000269|PubMed:15195945, ECO:0000269|PubMed:15828688}.
Arabidopsis thaliana (Mouse-ear cress)
O22833
LRK54_ARATH
MSRTIGSRVIFLILALFCCTENSRGKLVMQGSAGFFKGYRTLTSTKKHAYGQAFEDEIVPFKNSANDTVTSFSVTFFFAIAPEDKHKGAHGMAFVISPTRGITGASADQYLGIFNKANNGDSSNHVIAVELDINKDEEFGDINDNHVGININGMRSIKFAPAGYYDQEGQFKDLSLISGSLLRVTILYSQMEKQLNVTLSSPEEAYYPNKPLLSLNQDLSPYILENMYVGFSASTGSVRAMHYMLSWFVHGGVDVPNLDLGIPTFPPYPKEKSLVYRIVLVTSLALVLFVALVASALSIFFYRRHKKVKEVLEEWEIQCGPHRFAYKELFKATKGFKQLLGKGGFGQVFKGTLPGSDAEIAVKRISHDSKQGMQEFLAEISTIGRLRHQNLVRLQGYCRYKEELYLVYDFMPNGSLDKYLYHRANQEQLTWNQRFKIIKDIASALCYLHHEWVQVVIHRDIKPANVLIDHQMNARLGDFGLAKLYDQGYDPQTSRVAGTFWYIAPELIRSGRATTGTDVYAFGLFMLEVSCGRRLIERRTASDEVVLAEWTLKCWENGDILEAVNDGIRHEDNREQLELVLKLGVLCSHQAVAIRPDMSKVVQILGGDLQLPDNLLDIVKAEKVRMWSETSESVLGVLTSQGSIGTLTLTEPFTSRGR
2.7.11.1
null
defense response to bacterium [GO:0042742]; defense response to oomycetes [GO:0002229]; phosphorylation [GO:0016310]
plasma membrane [GO:0005886]
ATP binding [GO:0005524]; carbohydrate binding [GO:0030246]; protein serine kinase activity [GO:0106310]; transmembrane receptor protein serine/threonine kinase activity [GO:0004675]
PF00139;PF00069;
2.60.120.200;1.10.510.10;
Protein kinase superfamily, Ser/Thr protein kinase family; Leguminous lectin family
null
SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q9LSR8}; 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: Involved in resistance response to the pathogenic oomycetes Phytophthora infestans and Phytophthora capsici and to the pathogenic bacteria Pseudomonas syringae. {ECO:0000269|PubMed:25083911}.
Arabidopsis thaliana (Mouse-ear cress)
O22850
GPX3_ARATH
MPRSSRWVNQRATSKIKKFILFLGVAFVFYLYRYPSSPSTVEQSSTSIYNISVKDIEGKDVSLSKFTGKVLLIVNVASKCGLTHGNYKEMNILYAKYKTQGFEILAFPCNQFGSQEPGSNMEIKETVCNIFKAEFPIFDKIEVNGKNTCPLYNFLKEQKGGLFGDAIKWNFAKFLVDRQGNVVDRYAPTTSPLEIEKDIVKLLASA
1.11.1.9
null
abscisic acid-activated signaling pathway [GO:0009738]; cellular response to water deprivation [GO:0042631]; response to hydrogen peroxide [GO:0042542]
cytosol [GO:0005829]; endoplasmic reticulum [GO:0005783]; endosome [GO:0005768]; Golgi apparatus [GO:0005794]; mitochondrion [GO:0005739]; trans-Golgi network [GO:0005802]
glutathione peroxidase activity [GO:0004602]
PF00255;
3.40.30.10;
Glutathione peroxidase family
null
SUBCELLULAR LOCATION: Mitochondrion {ECO:0000305}.
CATALYTIC ACTIVITY: Reaction=2 glutathione + H2O2 = glutathione disulfide + 2 H2O; Xref=Rhea:RHEA:16833, ChEBI:CHEBI:15377, ChEBI:CHEBI:16240, ChEBI:CHEBI:57925, ChEBI:CHEBI:58297; EC=1.11.1.9;
null
null
null
null
FUNCTION: May constitute a glutathione peroxidase-like protective system against oxidative stresses. Involved positively in abscisic acid (ABA) signaling pathway that regulates numerous ABA responses, such as stomatal closure, seed germination and inhibition of vegetative growth. Oxidizes and represses target proteins (e.g. the phosphatase activity of ABI1 and ABI2) when oxidized by H(2)O(2), probably after ABA signaling. Modulates the calcium channel activity in guard cells in response to ABA or H(2)O(2). Confers tolerance to drought stress, by enhancing the ABA-dependent stomatal closure. {ECO:0000269|PubMed:16998070}.
Arabidopsis thaliana (Mouse-ear cress)
O22854
ETFQO_ARATH
MHRFLVKLSSSSSPFSNQLRSLKNQRLILPLLPSSKPFTSSSVSPPPSPLNASNRFGYPYSADLFRNLSPLNPNSRILGVNGITSSRCISSEAVRESIEYDVLIVGAGPAGLSAAIRLKQLSQEKNIDLSVCVVEKGAEVGGHIISGNVFEPLALDELLPHWRQEHAPIEIPASSDKFWFLTKDRAFSLPSPFDNKGNYVISLSQLVRWLGGKAEELGTEIYPGFSASEVLFDASDKVVGIATKDMGISKDGSKKENFQPGVDIKGRVTLFAEGCRGSLSERIIKKYKLREEVNAQHQTYALGIKEVWEIDESKHNPGEVIHTLGWPLDPKTYGGSFLYHMNDRQVALGLVVALNYHNPFLNPYEEFQKLKHHPAIKGILEGGTVLQYGARTLNEGGFQSIPYPVFPGGAIIGCSAGFLNVPKIKGTHTAMKSGMLAAEAAFGALHEGLNMNTYWDNLRDSWVWKELYAARNYRPAFEYGLLPGLAISAMEHYVLKGKVPFTLKHGKADHEATDLARKWTPIVYPKPDGVLSFDVPTSLYRSNTNHDHDQPSHLRLRDPKIPEKVNFPEYAAPESRYCPARVYEYIEDEEGKPKLQINAQNCLHCKACDIKDPKQNIEWTVPEGGGGPAYSLM
1.5.5.1
COFACTOR: Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; Evidence={ECO:0000250}; Note=Binds 1 [4Fe-4S] cluster. {ECO:0000250}; COFACTOR: Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250};
alternative respiration [GO:0010230]; leucine catabolic process [GO:0006552]; response to absence of light [GO:0009646]
cytosol [GO:0005829]; mitochondrial inner membrane [GO:0005743]; mitochondrion [GO:0005739]
4 iron, 4 sulfur cluster binding [GO:0051539]; electron-transferring-flavoprotein dehydrogenase activity [GO:0004174]; metal ion binding [GO:0046872]
PF05187;PF21162;PF13450;
3.30.70.20;3.30.9.90;3.50.50.60;
ETF-QO/FixC family
null
SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000305|PubMed:16055629}.
CATALYTIC ACTIVITY: Reaction=a ubiquinone + reduced [electron-transfer flavoprotein] = a ubiquinol + H(+) + oxidized [electron-transfer flavoprotein]; Xref=Rhea:RHEA:24052, Rhea:RHEA-COMP:9565, Rhea:RHEA-COMP:9566, Rhea:RHEA-COMP:10685, Rhea:RHEA-COMP:10686, ChEBI:CHEBI:15378, ChEBI:CHEBI:16389, ChEBI:CHEBI:17976, ChEBI:CHEBI:57692, ChEBI:CHEBI:58307; EC=1.5.5.1;
null
null
null
null
FUNCTION: Accepts electrons from ETF and reduces ubiquinone. May act downstream of IVD and D2HGDH in the degradation of phytol or chlorophyll during dark-induced senescence and sugar starvation. {ECO:0000269|PubMed:16055629, ECO:0000269|PubMed:20501910}.
Arabidopsis thaliana (Mouse-ear cress)
O22873
BZP18_ARATH
MEDPSNPQPNQSNLSQCPPLATAPTPAPVRGPYHRRAHSEVQFRLPEDLDLSEPFGGFDELGSEDDLFCSYMDIEKLGSGSGSASDSAGPSAPRSDNPFSAENGGAEAGNSRPRHRHSLSVDGSSTLESIEAKKAMAPDKLAELWVVDPKRAKRIIANRQSAARSKERKARYILELERKVQTLQTEATTLSAQLSLFQRDTTGLSSENTELKLRLQVMEQQAKLRDALNEQLKKEVERLKFATGEVSPADAYNLGMAHMQYQQQPQQSFFQHHHQQQTDAQNLQQMTHQFHLFQPNNNQNQSSRTNPPTAHQLMHHATSNAPAQSHSYSEAMHEDHLGRLQGLDISSCGRGSNFGRSDTVSESSSTM
null
null
null
cytoplasm [GO:0005737]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; perinuclear region of cytoplasm [GO:0048471]
chromatin DNA binding [GO:0031490]; DNA-binding transcription factor activity [GO:0003700]; protein self-association [GO:0043621]; transcription cis-regulatory region binding [GO:0000976]
PF00170;
1.20.5.170;
null
null
SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00978}. Nucleus, nucleoplasm {ECO:0000269|PubMed:27896439}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:27896439}. Cytoplasm {ECO:0000269|PubMed:27896439}.
null
null
null
null
null
FUNCTION: Transcription factor that may participate with bZIP34 in the gametophytic control of pollen development. {ECO:0000269|PubMed:27896439}.
Arabidopsis thaliana (Mouse-ear cress)
O22893
GOLS1_ARATH
MAPGLTQTADAMSTVTITKPSLPSVQDSDRAYVTFLAGNGDYVKGVVGLAKGLRKVKSAYPLVVAMLPDVPEEHRRILVDQGCIVREIEPVYPPENQTQFAMAYYVINYSKLRIWKFVEYSKMIYLDGDIQVYENIDHLFDLPDGYLYAVMDCFCEKTWSHTPQYKIRYCQQCPDKVQWPKAELGEPPALYFNAGMFLYEPNLETYEDLLRTLKITPPTPFAEQDFLNMYFKKIYKPIPLVYNLVLAMLWRHPENVELGKVKVVHYCAAGSKPWRYTGKEANMEREDIKMLVKKWWDIYDDESLDYKKPVTVVDTEVDLVNLKPFITALTEAGRLNYVTAPSAA
2.4.1.123
COFACTOR: Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240; Evidence={ECO:0000250};
galactose metabolic process [GO:0006012]; response to abscisic acid [GO:0009737]; response to cold [GO:0009409]; response to heat [GO:0009408]; response to oxidative stress [GO:0006979]; response to salt stress [GO:0009651]; response to water deprivation [GO:0009414]
cytoplasm [GO:0005737]
inositol 3-alpha-galactosyltransferase activity [GO:0047216]; metal ion binding [GO:0046872]
PF01501;
null
Glycosyltransferase 8 family, Galactosyltransferase subfamily
null
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CATALYTIC ACTIVITY: Reaction=myo-inositol + UDP-alpha-D-galactose = alpha-D-galactosyl-(1->3)-1D-myo-inositol + H(+) + UDP; Xref=Rhea:RHEA:12464, ChEBI:CHEBI:15378, ChEBI:CHEBI:17268, ChEBI:CHEBI:17505, ChEBI:CHEBI:58223, ChEBI:CHEBI:66914; EC=2.4.1.123; Evidence={ECO:0000269|PubMed:11846875};
null
null
null
null
FUNCTION: Galactinol synthase involved in the biosynthesis of raffinose family oligosaccharides (RFOs) that function as osmoprotectants. Promotes plant stress tolerance such as heat, chilling, salinity and methylviologen (MV), a superoxide radical generating drug, by mediating raffinose accumulation, an osmoprotective substance. {ECO:0000269|PubMed:15466240, ECO:0000269|PubMed:18502973}.
Arabidopsis thaliana (Mouse-ear cress)
O22898
LACS1_ARATH
MKSFAAKVEEGVKGIDGKPSVGPVYRNLLSEKGFPPIDSEITTAWDIFSKSVEKFPDNNMLGWRRIVDEKVGPYMWKTYKEVYEEVLQIGSALRAAGAEPGSRVGIYGVNCPQWIIAMEACAAHTLICVPLYDTLGSGAVDYIVEHAEIDFVFVQDTKIKGLLEPDCKCAKRLKAIVSFTNVSDELSHKASEIGVKTYSWIDFLHMGREKPEDTNPPKAFNICTIMYTSGTSGDPKGVVLTHQAVATFVVGMDLYMDQFEDKMTHDDVYLSFLPLAHILDRMNEEYFFRKGASVGYYHGNLNVLRDDIQELKPTYLAGVPRVFERIHEGIQKALQELNPRRRFIFNALYKHKLAWLNRGYSHSKASPMADFIAFRKIRDKLGGRIRLLVSGGAPLSPEIEEFLRVTCCCFVVQGYGLTETLGGTALGFPDEMCMLGTVGIPAVYNEIRLEEVSEMGYDPLGENPAGEICIRGQCMFSGYYKNPELTEEVMKDGWFHTGDIGEILPNGVLKIIDRKKNLIKLSQGEYVALEHLENIFGQNSVVQDIWVYGDSFKSMLVAVVVPNPETVNRWAKDLGFTKPFEELCSFPELKEHIISELKSTAEKNKLRKFEYIKAVTVETKPFDVERDLVTATLKNRRNNLLKYYQVQIDEMYRKLASKKI
6.2.1.3
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
cutin biosynthetic process [GO:0010143]; fatty acid metabolic process [GO:0006631]; wax biosynthetic process [GO:0010025]
endoplasmic reticulum [GO:0005783]; membrane [GO:0016020]
ATP binding [GO:0005524]; long-chain fatty acid-CoA ligase activity [GO:0004467]; very long-chain fatty acid-CoA ligase activity [GO:0031957]
PF00501;
3.40.50.12780;
ATP-dependent AMP-binding enzyme family
null
SUBCELLULAR LOCATION: Endoplasmic reticulum {ECO:0000269|PubMed:20237894}.
CATALYTIC ACTIVITY: Reaction=a long-chain fatty acid + ATP + CoA = a long-chain fatty acyl-CoA + AMP + diphosphate; Xref=Rhea:RHEA:15421, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:57560, ChEBI:CHEBI:83139, ChEBI:CHEBI:456215; EC=6.2.1.3; Evidence={ECO:0000269|PubMed:12177484};
null
PATHWAY: Lipid metabolism; fatty acid metabolism.
null
null
FUNCTION: Activation of long-chain fatty acids for both synthesis of cellular lipids, and degradation via beta-oxidation. Acts in both the wax and cutin pathways. Preferentially uses palmitate, palmitoleate, linoleate and eicosenoate. Seems to have a specific activity against very long-chain fatty acid (VLCFA) class with acids longer than 24 carbons (C(24)). {ECO:0000269|PubMed:12228482, ECO:0000269|PubMed:19392700, ECO:0000269|PubMed:20237894}.
Arabidopsis thaliana (Mouse-ear cress)
O22901
BH151_ARATH
MGVTLEGQRKESIWVLMRRQRARRALVKKIMIRPRKSVEASRRPCRAIHRRVKTLKELVPNTKTSEGLDGLFRQTADYILALEMKVKVMQTMVQVLTETNCV
null
null
cell differentiation [GO:0030154]; regulation of DNA-templated transcription [GO:0006355]; regulation of root development [GO:2000280]
nucleus [GO:0005634]
DNA-binding transcription factor activity [GO:0003700]; protein dimerization activity [GO:0046983]; transcription cis-regulatory region binding [GO:0000976]
null
null
null
null
SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00981, ECO:0000269|PubMed:21074051}.
null
null
null
null
null
FUNCTION: Transcription factor that modulates the balance between cellular proliferation and differentiation in root growth. Does not act through cytokinin and auxin signaling, but by repressing peroxidase expression in the elongation zone. {ECO:0000269|PubMed:21074051}.
Arabidopsis thaliana (Mouse-ear cress)
O22914
CP121_ARATH
MTTIAAAGLNVATPRVVVRPVARVLGPVRLNYPWKFGSMKRMVVVKATSEGEISEKVEKSIQEAKETCADDPVSGECVAAWDEVEELSAAASHARDKKKAGGSDPLEEYCNDNPETDECRTYDN
null
null
negative regulation of reductive pentose-phosphate cycle [GO:0080153]; reductive pentose-phosphate cycle [GO:0019253]; response to sucrose [GO:0009744]
chloroplast [GO:0009507]; chloroplast envelope [GO:0009941]; chloroplast stroma [GO:0009570]; cytosol [GO:0005829]; protein-containing complex [GO:0032991]
copper ion binding [GO:0005507]; mRNA binding [GO:0003729]; nickel cation binding [GO:0016151]
PF02672;
null
CP12 family
PTM: Contains two disulfide bonds; only the oxidized protein, with two disulfide bonds, is active in complex formation. The C-terminal disulfide is involved in the interaction with GAPDH and the N-terminal disulfide mediates the binding of PRK with this binary complex.
SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000269|PubMed:18431481, ECO:0000269|PubMed:20399532}.
null
null
null
null
null
FUNCTION: Acts as a linker essential in the assembly of a core complex of PRK/GAPDH. Coordinates the reversible inactivation of chloroplast enzymes GAPDH and PRK during darkness in photosynthetic tissues. {ECO:0000269|PubMed:20399532}.
Arabidopsis thaliana (Mouse-ear cress)
O22921
WRK25_ARATH
MSSTSFTDLLGSSGVDCYEDDEDLRVSGSSFGGYYPERTGSGLPKFKTAQPPPLPISQSSHNFTFSDYLDSPLLLSSSHSLISPTTGTFPLQGFNGTTNNHSDFPWQLQSQPSNASSALQETYGVQDHEKKQEMIPNEIATQNNNQSFGTERQIKIPAYMVSRNSNDGYGWRKYGQKQVKKSENPRSYFKCTYPDCVSKKIVETASDGQITEIIYKGGHNHPKPEFTKRPSQSSLPSSVNGRRLFNPASVVSEPHDQSENSSISFDYSDLEQKSFKSEYGEIDEEEEQPEMKRMKREGEDEGMSIEVSKGVKEPRVVVQTISDIDVLIDGFRWRKYGQKVVKGNTNPRSYYKCTFQGCGVKKQVERSAADERAVLTTYEGRHNHDIPTALRRS
null
null
cellular heat acclimation [GO:0070370]; cellular response to heat [GO:0034605]; response to cold [GO:0009409]; response to osmotic stress [GO:0006970]; response to salt stress [GO:0009651]
nucleus [GO:0005634]
DNA-binding transcription factor activity [GO:0003700]; metal ion binding [GO:0046872]; sequence-specific DNA binding [GO:0043565]
PF03106;
2.20.25.80;
WRKY group I family
PTM: Phosphorylated by MPK4. {ECO:0000305|PubMed:15990873}.
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:18839316}.
null
null
null
null
null
FUNCTION: Transcription factor. Interacts specifically with the W box (5'-(T)TGAC[CT]-3'), a frequently occurring elicitor-responsive cis-acting element (By similarity). Functions with WRKY33 as positive regulator of salt stress response and abscisic acid (ABA) signaling (PubMed:18839316). Plays a partial role in heat stress tolerance (PubMed:19125253). Functions with WRKY26 and WRKY33 as positive regulator of plant thermotolerance by partially participating in ethylene-response signal transduction pathway (PubMed:21336597). {ECO:0000250|UniProtKB:Q9SI37, ECO:0000269|PubMed:18839316, ECO:0000269|PubMed:19125253, ECO:0000269|PubMed:21336597}.
Arabidopsis thaliana (Mouse-ear cress)
O22932
CIPKB_ARATH
MPEIEIAAGSGDNNDALFGKYELGKLLGCGAFAKVFHARDRRTGQSVAVKILNKKKLLTNPALANNIKREISIMRRLSHPNIVKLHEVMATKSKIFFAMEFVKGGELFNKISKHGRLSEDLSRRYFQQLISAVGYCHARGVYHRDLKPENLLIDENGNLKVSDFGLSALTDQIRPDGLLHTLCGTPAYVAPEILSKKGYEGAKVDVWSCGIVLFVLVAGYLPFNDPNVMNMYKKIYKGEYRFPRWMSPDLKRFVSRLLDINPETRITIDEILKDPWFVRGGFKQIKFHDDEIEDQKVESSLEAVKSLNAFDLISYSSGLDLSGLFAGCSNSSGESERFLSEKSPEMLAEEVEGFAREENLRMKKKKEEEYGFEMEGQNGKFGIGICISRLNDLLVVVEARRRGGDGDCYKEMWNGKLRVQLIRVCDQTSSTNAAI
2.7.11.1
COFACTOR: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000269|PubMed:17483306}; Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:17483306};
protein phosphorylation [GO:0006468]; response to calcium ion [GO:0051592]; response to pH [GO:0009268]; signal transduction [GO:0007165]
null
ATP binding [GO:0005524]; protein kinase activity [GO:0004672]; 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.
null
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. Acts as a negative regulator of the plasma membrane proton pump AHA2 by preventing its interaction with 14-3-3 protein. {ECO:0000269|PubMed:17483306}.
Arabidopsis thaliana (Mouse-ear cress)
O22943
STL1_ARATH
MLVQDRAAPSPAKPPKSQIRELPTHQQIRRRFSEPKNLDFSTWFSENLSRIAVFSLLIVTIVAFFFLYNTTDTASLLCFQSQSTQFLQSLSRPQIKWNSIPVVPDKTSPYANFQTEKWIVVSVTKYPTEELKSLVKIRGWQVLAIGNSATPKDWSLKGSIFLSLDAQAELGYRVLDHLPYDSFVRKSVGYLFAIQHGAKKIYDADDRGEVIDGDLGKHFDVELVGLDSKQEPILQYSHENPNRTVVNPYIHFGQRSVWPRGLPLENVGEINHEEYYTEVFGGKQFIQQGISNGLPDVDSVFYFTRKTTLEAFDIRFDEHSPKVALPQGVMVPVNSFNTLYHSSAFWGLMLPVSVSSMASDVLRGYWGQRLLWELGGYVAVYPPTAHRFDRIEAYPFVEEKDLHVNVGRLIKFLLAWRSEKHSFFETVLDLSFAMAEEGFWTEQDLKFTAAWLQDLIAVGYQQPRLMSLELDRPRASIGHGDRKEFVPRKLPSVHLGVEETGTVSTEIGNLIRWRKNFGNVVLVMFCNGPVERTALEWRLLYGRIFKTVVILSSQKNSDLYVEEAKLDHIYKHLPKIFDRYSSAEGFLFVEDDTVLNYWNLLQADKSKIWTTDKVSKSWTSVKPTGNSDWFSVQAELVKKTVSTMPAHFQVNYKDATKNNHETLTVCSSEVFYVPKRLVTDFIDLVDLVGDMDLHYKVAVPMFFLSMDSPQNFDPVLGSMVYKRKSASFNTSSSLYSAKAPAVHPWSISSEQDFIKLVQQMAEGDPLLMELV
2.4.-.-
null
plant-type cell wall cellulose biosynthetic process [GO:0052324]; regulation of plant-type cell wall cellulose biosynthetic process [GO:2001009]
endosome [GO:0005768]; Golgi apparatus [GO:0005794]; Golgi membrane [GO:0000139]; trans-Golgi network [GO:0005802]
glycosyltransferase activity [GO:0016757]; identical protein binding [GO:0042802]
PF03385;
null
STELLO family
null
SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000269|PubMed:27277162}; Single-pass type II membrane protein {ECO:0000255}.
null
null
null
null
null
FUNCTION: Probable glycosyltransferase regulating the assembly and trafficking of cellulose synthase complexes. {ECO:0000269|PubMed:27277162}.
Arabidopsis thaliana (Mouse-ear cress)
O22975
LPAAT_ARATH
MNLSRFASRLRMAEEISKTKVGSSSTASVADSSAAASAATNAAKSRWKILWPNSLRWIPTSTDYIIAAEKRLLSILKTPYVQEQVSIGSGPPGSKIRWFRSTSNESRYINTVTFDAKEGAPTLVMVHGYGASQGFFFRNFDALASRFRVIAIDQLGWGGSSRPDFTCRSTEETEAWFIDSFEEWRKAQNLSNFILLGHSFGGYVAAKYALKHPEHVQHLILVGSAGFSAEADAKSEWLTKFRATWKGAVLNHLWESNFTPQKLVRGLGPWGPGLVNRYTTARFGAHSEGTGLTEEEAKLLTDYVYHTLAAKASGELCLKYIFSFGAFARKPLLQSASEWKVPTTFIYGMNDWMNYQGAVEARKSMKVPCEIIRVPQGGHFVFIDNPIGFHSAVLYACRKFISQDSSHDQQLLDGLRLV
2.3.1.51
null
cardiolipin acyl-chain remodeling [GO:0035965]; cellular response to hypoxia [GO:0071456]; fatty acid homeostasis [GO:0055089]; lipid homeostasis [GO:0055088]; phosphatidic acid biosynthetic process [GO:0006654]; phospholipid homeostasis [GO:0055091]; triglyceride homeostasis [GO:0070328]
lipid droplet [GO:0005811]; mitochondrial inner membrane [GO:0005743]
1-acylglycerol-3-phosphate O-acyltransferase activity [GO:0003841]; lipase activity [GO:0016298]; lysophosphatidic acid acyltransferase activity [GO:0042171]; phospholipase A2 activity [GO:0004623]
PF00561;
3.40.50.1820;
Peptidase S33 family, ABHD4/ABHD5 subfamily
null
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:20876112}. Note=Does not associate with endogenous lipid droplets.
CATALYTIC ACTIVITY: Reaction=a 1-acyl-sn-glycero-3-phosphate + an acyl-CoA = a 1,2-diacyl-sn-glycero-3-phosphate + CoA; Xref=Rhea:RHEA:19709, ChEBI:CHEBI:57287, ChEBI:CHEBI:57970, ChEBI:CHEBI:58342, ChEBI:CHEBI:58608; EC=2.3.1.51; Evidence={ECO:0000269|PubMed:19700561};
null
null
null
null
FUNCTION: Lysophosphatidic acid acyltransferase which functions in phosphatidic acid biosynthesis. Is highly specific for lysophosphatidic acid and able to use different acyl-CoA donors. May regulate neutral lipid accumulation and participate in the regulation of lipid turnover in vegetative cells. Possesses additional triacylglycerol lipase and phospholipase A2 activities in vitro. Is not active as esterase or lysophospholipase. {ECO:0000269|PubMed:19700561, ECO:0000269|PubMed:20876112}.
Arabidopsis thaliana (Mouse-ear cress)
O22993
FTSI1_ARATH
MASIDNVFSLGTRFSIPENPKRSILKHATTSSFSARTQTRWRAPILRRSFTVLCELKTGSSSSGETNNSPAADDFVTRVLKENPSQVEPRYRVGDKLYNLKEREDLSKGTNAATGAFEFIKRKFDSKKKTETDKSEESVYLSDILREYKGKLYVPEQVFGPELSEEEEFEKNVKDLPKMSLEDFRKAMENDKVKLLTSKEVSGVSYTSGYRGFIVDLKEIPGVKSLQRTKWSMKLEVGEAQALLKEYTGPQYEIERHMTSWVGKVADFPNPVASSISSRVMVELGMVTAVIAAAAVVVGGFLASAVFAVTSFAFVTTVYVVWPIAKPFLKLFVGVFLGVLEKSWDYIVDVLADGGIFSRISDFYTFGGVASSLEMLKPILLVVMTMVLLVRFTLSRRPKNFRKWDLWQGIAFSQSKAEARVDGSTGVKFADVAGIDEAVDELQELVKYLKNPDLFDKMGIKPPHGVLLEGPPGCGKTLVAKAIAGEAGVPFYQMAGSEFVEVLVGVGSARIRDLFKRAKVNKPSVIFIDEIDALATRRQGIFKENSDQLYNAATQERETTLNQLLIELDGFDTGKGVIFLGATNRRDLLDPALLRPGRFDRKIRVRPPNAKGRLDILKIHASKVKMSDSVDLSSYASNLPGWSGAKLAQLVQEAALVAVRKTHNSILQSDMDDAVDRLTVGPTRIGLELGHQGQCRRATTEVGVAITSHLLLRYENAKIERCDRVSIIPRGQTLSQVVFHRLDDESYMFGRLPQLLHRLQVLLGGRAAEEVIYGSDTSKASVDYLSDASWLARKILTIWNLENPMVIHGEPPPWRKRPQFVGPRLDFEGSLYDDYDLVEPPVNFNMDDEVAHRSEELISQMYNKTVSLLRQNQTALLKTVKVLLNQKEISGEAIDFILDHYPPQTPLNSLLQEQNPGSLPFVPEHLRRESGDFVLVNHSTDVNAQV
null
null
chloroplast fission [GO:0010020]; chloroplast organization [GO:0009658]; embryo development ending in seed dormancy [GO:0009793]; plastid fission [GO:0043572]; protein import into chloroplast stroma [GO:0045037]; proteolysis [GO:0006508]
chloroplast [GO:0009507]; chloroplast envelope [GO:0009941]; chloroplast inner membrane [GO:0009706]; chloroplast thylakoid [GO:0009534]; cytosol [GO:0005829]; plastid [GO:0009536]; Ycf2/FtsHi complex [GO:0062091]
ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; ATP-dependent peptidase activity [GO:0004176]; chloroplast protein-transporting ATPase activity [GO:0016464]; metalloendopeptidase activity [GO:0004222]
PF00004;PF17862;PF01434;
1.10.8.60;3.40.50.300;1.20.58.760;
AAA ATPase family; Peptidase M41 family
null
SUBCELLULAR LOCATION: Plastid, chloroplast inner membrane {ECO:0000269|PubMed:22900897}; Multi-pass membrane protein {ECO:0000269|PubMed:22900897}.
null
null
null
null
null
FUNCTION: Functions in chloroplast biogenesis and chloroplast division (PubMed:10417716, PubMed:22900897). Required for plastid development during embryogenesis (PubMed:22900897, PubMed:24964212). Might be involved in chaperone functions or play a structural role in the thylakoid FtsH complex (PubMed:12185496). {ECO:0000269|PubMed:10417716, ECO:0000269|PubMed:22900897, ECO:0000269|PubMed:24964212, ECO:0000303|PubMed:12185496}.
Arabidopsis thaliana (Mouse-ear cress)
O23044
PER3_ARATH
MNCLIAIALSVSFFLVGIVGPIQAQLQMNFYANSCPNAEKIVQDFVSNHVSNAPSLAAALIRMHFHDCFVRGCDGSVLINSTSGNAERDATPNLTVRGFGFIDAIKSVLEAQCPGIVSCADIIALASRDAVVFTGGPNWSVPTGRRDGRISNAAEALANIPPPTSNITNLQTLFANQGLDLKDLVLLSGAHTIGVSHCSSFTNRLYNFTGRGGQDPALDSEYAANLKSRKCPSLNDNKTIVEMDPGSRKTFDLSYYQLVLKRRGLFQSDSALTTNPTTLSNINRILTGSVGSFFSEFAKSMEKMGRINVKTGSAGVVRRQCSVANS
1.11.1.7
COFACTOR: Name=heme b; Xref=ChEBI:CHEBI:60344; Evidence={ECO:0000255|PROSITE-ProRule:PRU00297}; Note=Binds 1 heme b (iron(II)-protoporphyrin IX) group per subunit. {ECO:0000255|PROSITE-ProRule:PRU00297}; COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000255|PROSITE-ProRule:PRU00297}; Note=Binds 2 calcium ions per subunit. {ECO:0000255|PROSITE-ProRule:PRU00297};
hydrogen peroxide catabolic process [GO:0042744]; hyperosmotic salinity response [GO:0042538]; response to cold [GO:0009409]; response to desiccation [GO:0009269]; response to oxidative stress [GO:0006979]
endoplasmic reticulum [GO:0005783]; extracellular region [GO:0005576]; plant-type cell wall [GO:0009505]; plasmodesma [GO:0009506]
heme binding [GO:0020037]; lactoperoxidase activity [GO:0140825]; metal ion binding [GO:0046872]; peroxidase activity [GO:0004601]
PF00141;
1.10.520.10;1.10.420.10;
Peroxidase family, Classical plant (class III) peroxidase subfamily
null
SUBCELLULAR LOCATION: Secreted {ECO:0000255|PROSITE-ProRule:PRU00297}.
CATALYTIC ACTIVITY: Reaction=2 a phenolic donor + H2O2 = 2 a phenolic radical donor + 2 H2O; Xref=Rhea:RHEA:56136, ChEBI:CHEBI:15377, ChEBI:CHEBI:16240, ChEBI:CHEBI:139520, ChEBI:CHEBI:139521; EC=1.11.1.7;
null
null
null
null
FUNCTION: Removal of H(2)O(2), oxidation of toxic reductants, biosynthesis and degradation of lignin, suberization, auxin catabolism, response to environmental stresses such as wounding, pathogen attack and oxidative stress. These functions might be dependent on each isozyme/isoform in each plant tissue.
Arabidopsis thaliana (Mouse-ear cress)
O23066
C86A2_ARATH
MDVSNTMLLVAVVAAYWLWFQRISRWLKGPRVWPVLGSLPGLIEQRDRMHDWITENLRACGGTYQTCICAVPFLAKKQGLVTVTCDPKNIEHMLKTRFDNYPKGPTWQAVFHDFLGQGIFNSDGDTWLFQRKTAALEFTTRTLRQAMGRWVNRGIKLRFCPILETAQNNYEPVDLQDLILRLTFDNICGLAFGKDTRTCAPGLPENGFASAFDRATEASLQRFILPEFLWRLKKWLGLGLEVSLSRSLGEIDGYLDAVINTRKQELLSQRESGVQRHDDLLSRFMKKKDQSYSETFLRHVALNFILAGRDTSSVALSWFFWLITTHPTVEDKIVREICSVLIETRGTDVSSWTAEPLEFDEVDRLVYLKAALSETLRLYPSVPEDSKHVVNDDILPDGTFVPAGSSVTYSIYAAGRMKSTWGEDCLEFKPERWISPDDGKFVNHDQYRFVAFNAGPRICLGKDLAYLQMKTIAAAVLLRHRLTVAPGHKVEQKMSLTLFMKNGLLVNVHKRDLEVMMKSLVPKERNDVVVLNGKCNGGIGEGVAVNAAVAVAV
1.14.14.1
COFACTOR: Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250};
defense response [GO:0006952]; fatty acid metabolic process [GO:0006631]
membrane [GO:0016020]
alkane 1-monooxygenase activity [GO:0018685]; aromatase activity [GO:0070330]; heme binding [GO:0020037]; iron ion binding [GO:0005506]
PF00067;
1.10.630.10;
Cytochrome P450 family
null
SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}.
CATALYTIC ACTIVITY: Reaction=an organic molecule + O2 + reduced [NADPH--hemoprotein reductase] = an alcohol + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:17149, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:30879, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:142491; EC=1.14.14.1;
null
null
null
null
FUNCTION: Catalyzes the omega-hydroxylation of various fatty acids (FA). Acts on saturated and unsaturated fatty acids with chain lengths from C12 to C18. Plays a major role in the biosynthesis of extracellular lipids. Involved in the biosynthesis of hydroxylated fatty acids required for cutin biosynthesis, cuticle development and repression of bacterial type III gene expression. {ECO:0000269|PubMed:15241470, ECO:0000269|PubMed:15709153, ECO:0000269|PubMed:17427946}.
Arabidopsis thaliana (Mouse-ear cress)
O23078
PLDB2_ARATH
MENYGWNYPYYPYRPPRPNPPYPAPPHHHGSMSHSGPLDHHHPPMSYYASFDYQHQPPPPYPPVSYYASFSSHSDLSYSGRLDSSGHGFTSTASPHSPGMHIVPFGKASLKVLLLHGNLDIWVSCANNLPNLDLFHKTLGVVFGGMTNMIEGQLSKKITSDPYVSISVAGAVIGRTYVISNSENPVWQQHFYVPVAHHAAEVHFVVKDSDAVGSQLIGIVTIPVEQIYSGARIEGTYSIRDSNGKPCKPGATLSLSIQYTSMNKLSVYHSGVGAGPYYQGVPGTYFPLREGGSVTLYQDAHVPEGMLPGIKLGNGMCYEHGKCWHDMFHAICQARRLIYITGWSVWHNVRLVRDKEDPSSECRLGELLRSKSQEGVRVLLLVWDDPTSQNILGYMTDGVMGTHDEETRRFFKDSSVQVLLCPRNAGKRHSWVKQREVGTIYTHHQKNLIVDADAGGNRRKIVAFVGGLDLCDGRYDTPQHPLFRTLQTDHNGDYHNPTFTGNVSGCPREPWHDLHSKIDGPAAYDVLTNFEERWLKAAKPHRINKLKTSYDDALLRIDRIPDILRVLDAPTVSANDPEAWHVQIFRSIDSNSVKGFPKDPKYATSKNLVCGKNVLIDMSIHTAYVKAIRAAQHFIYIENQYFIGSSYDWNAHKDIGANNLIPMEIALKIADKIRAKERFAAYIVIPMWPEGVPTGAATQRILYWQHKTMQMMYGTIYNALVEAGLEDEYSPQDYLNFFCLGNREMVNGNNESGTGSASNENTPQGLCRKSRRFMIYVHSKGMVVDDEYVVIGSANINQRSMEGTRDTEIAMGAYQPQHTWARRQSGPRGQIYGYRMSLWAEHMALLDDCFVEPESLGCVRKVRTVAEENWEQFRSEEVSEMRGHLMKYPVEVDRKGKVRPLPGSEEFPDVGGNVVGSFLAIQENLTI
3.1.4.4
COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250|UniProtKB:Q38882}; Note=Ca(2+). Requires micromolar level (PIP2-dependent). {ECO:0000250|UniProtKB:Q38882};
phosphatidylcholine metabolic process [GO:0046470]; phospholipid catabolic process [GO:0009395]
cytoplasm [GO:0005737]; plasma membrane [GO:0005886]
calcium ion binding [GO:0005509]; N-acylphosphatidylethanolamine-specific phospholipase D activity [GO:0070290]; phospholipase D activity [GO:0004630]
PF00168;PF12357;PF00614;
2.60.40.150;3.30.870.10;
Phospholipase D family, C2-PLD subfamily
null
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q38882}. Membrane {ECO:0000250|UniProtKB:Q38882}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q38882}.
CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 1,2-diacyl-sn-glycero-3-phosphate + choline + H(+); Xref=Rhea:RHEA:14445, ChEBI:CHEBI:15354, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57643, ChEBI:CHEBI:58608; EC=3.1.4.4; Evidence={ECO:0000250|UniProtKB:Q38882};
null
null
null
null
FUNCTION: Hydrolyzes glycerol-phospholipids at the terminal phosphodiesteric bond to generate phosphatidic acids (PA). Plays an important role in various cellular processes, including phytohormone action, vesicular trafficking, secretion, cytoskeletal arrangement, meiosis, tumor promotion, pathogenesis, membrane deterioration and senescence. Can use phosphatidylserine or N-acylphosphatidylethanolamine as substrates.
Arabidopsis thaliana (Mouse-ear cress)
O23141
SPE2_ARATH
MPALACVDTSFVPPAYAFSDTAGDVFIPASSPTSAAVVVDRWSPSLSSSLYRIDGWGAPYFIANSSGNISVRPHGSETLPHQDIDLLKIVKKVTGPKSSGGLGLQLPLIVRFPDVLKNRLECLQSAFDYAIKSQGYDSHYQGVYPVKCNQDRFVVEDIVKFGSSFRFGLEAGSKPEILLAMSCLCKGSPDAFLVCNGFKDAEYISLALLGRKLALNTVIVLEQEEELDLVIELSQKMNVRPVIGLRAKLRTKHSGHFGSTSGEKGKFGLTTTQIVRVVRKLRQSGMLDCLQLLHFHIGSQIPSTSLLSDGVAEAAQLYCELVRLGAHMKVIDIGGGLGIDYDGSKSGESDLSVAYSLEEYAEAVVASVRVVCDRSSVKHPVICSESGRAIVSHHSVLIFEAVSADKPMVHQATPGDIQFLLEGNEEARANYEDLYAAVMRGDHESCLLYVDQLKQRCVEGFKEGVLSIEQLASVDGLCEWVLKAIGASDPVHTYNINLSVFTSIPDLWGIDQLFPIVPIHKLDQRPGARGILSDLTCDSDGKINKFIGGESSLPLHELDKNGSGGRYFLGMFLGGAYEEALGGVHNLFGGPSVVRVSQSDGPHSFAVTRAVPGQSSADVLRAMQHEPELMFQTLKHRAEEMMHTKGGSEGENEEEEEDDEFNNVAASLDRSFHNMPYLATEQASPSNSLSAAISNLGFYYCDEDVYDYISA
4.1.1.19
COFACTOR: Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
arginine catabolic process [GO:0006527]; polyamine biosynthetic process [GO:0006596]; putrescine biosynthetic process [GO:0009446]; response to abscisic acid [GO:0009737]; response to cold [GO:0009409]; response to jasmonic acid [GO:0009753]; response to osmotic stress [GO:0006970]; response to oxidative stress [GO:0006979]; response to salt stress [GO:0009651]; response to wounding [GO:0009611]; spermidine biosynthetic process [GO:0008295]
chloroplast [GO:0009507]; cytosol [GO:0005829]
arginine decarboxylase activity [GO:0008792]; protein homodimerization activity [GO:0042803]
PF02784;
1.20.58.930;3.20.20.10;
Orn/Lys/Arg decarboxylase class-II family, SpeA subfamily
null
SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000269|PubMed:28109885, ECO:0000269|PubMed:28716421}. Cytoplasm, cytosol {ECO:0000269|PubMed:28109885}. Note=Localizes mainly in the chloroplast. {ECO:0000269|PubMed:28109885}.
CATALYTIC ACTIVITY: Reaction=H(+) + L-arginine = agmatine + CO2; Xref=Rhea:RHEA:17641, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:32682, ChEBI:CHEBI:58145; EC=4.1.1.19; Evidence={ECO:0000305|PubMed:14684170};
null
PATHWAY: Amine and polyamine biosynthesis; agmatine biosynthesis; agmatine from L-arginine: step 1/1. {ECO:0000305}.
null
null
FUNCTION: Required for the biosynthesis of putrescine. Catalyzes the first step of polyamine (PA) biosynthesis to produce putrescine from arginine (PubMed:14684170, PubMed:15733873, PubMed:16045477, PubMed:25409942). Is a major contributor to basal arginine decarboxylase (ADC) activity and putrescine biosynthesis (PubMed:25409942). Accumulation of putrescine plays a positive role in salt stress tolerance (PubMed:14684170). Accumulation of putrescine plays a positive role in freezing tolerance (PubMed:18701673). Production of PA is essential for normal seed development (PubMed:15733873). Controls PA homeostasis which is crucial for normal plant growth and development (PubMed:27014322). {ECO:0000269|PubMed:14684170, ECO:0000269|PubMed:15733873, ECO:0000269|PubMed:16045477, ECO:0000269|PubMed:18701673, ECO:0000269|PubMed:25409942, ECO:0000269|PubMed:27014322}.
Arabidopsis thaliana (Mouse-ear cress)
O23144
PPI1_ARATH
MGVEVVNSGGFEVAPAPFEGKPEKNGKLDQGKGDDAPINFGSVGELPKNAEENNNKVVNSDAPKNAAEEWPVAKQIHSFYLVKYRSYADPKIKAKLDLADKELEKLNKARTGVLDKLRAKRAERSELFDLLDPLKSERKGFNTMFDEKRKEMEPLQQALGKLRSNDGGSARGPAICSSEEELNSMIYSYQYRIQHESIPLTEEKQILKEIRLLEGTRDKVIANAAMRAKIKESMGQKDDIQGQVKLMGAGLDGVKKERQAISARINELSEKLKATKDEITVLENELKTVSEKRDKAYSNIHDLRRQRDETNSEYYQNRTVLNKARDLAAQKNISELEALANAEVEKFISLWCSKKNFREDYEKRILQSLDSRQLSRDGRMRNPDEKPLIAPEAAPSKATPSETEVVPKAKAKPQPKEEPVSAPKPDATVAQNTEKAKDAVKVKNVADDDDDEVYGLGKPQKEEKPVDAATAKEMRKQEEIAKAKQAMERKKKLAEKAAAKAAIRAQKEAEKKEKKEQEKKAKKKTGGNTETETEEVPEASEEEIEAPVQEEKPQKEKVFKEKPIRNRTRGRGPETIPRAILKRKKSTNYWVYAAPAALVVLLLLVLGYYYVL
null
null
regulation of proton transport [GO:0010155]
cytosol [GO:0005829]; endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]; plasma membrane [GO:0005886]; plasmodesma [GO:0009506]
mRNA binding [GO:0003729]
null
null
Plant Proton pump-interactor protein family
null
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:19796364}; Single-pass membrane protein {ECO:0000255}. Endoplasmic reticulum membrane {ECO:0000269|PubMed:19796364}; Single-pass membrane protein {ECO:0000255}.
null
null
null
null
null
FUNCTION: Promotes AHA1 plasma membrane ATPase activity by binding to a site different from the 14-3-3 binding site. {ECO:0000269|PubMed:12182706, ECO:0000269|PubMed:16279950}.
Arabidopsis thaliana (Mouse-ear cress)
O23147
ADPG1_ARATH
MARCCRHLAVFLCVLLMLSLCKALSSNVDDGYGHEDGSFESDSLLKLNNDDVLSLISSDETTLEASTVSVSNFGAKGDGKTDDTQAFKKAWKKACSTNGVTTFLVPKGKTYLLKSTRFRGPCKSLRNFQILGTLSASTKRSDYKDKNHWLILEDVNNLSIDGGSTGIINGNGKTWWQNSCKIDKSKPCTKAPTALTLYNLKNLNVKNLRVKNAQQIQISIEKCNKVEVSNVEITAPGDSPNTDGIHITNTQNIRVSNSDIGTGDDCISIEDGTQNLQIFDLTCGPGHGISIGSLGDDNSKAYVSGINVDGAKFSESDNGVRIKTYQGGSGTAKNIKFQNIRMENVKNPIIIDQDYCDKDKCEDQESAVQVKNVVYKNISGTSATDVAITLNCSEKYPCQGIVLENVKIKGGTASCKNANVKNQGTVSPKCS
3.2.1.15
null
anther dehiscence [GO:0009901]; cell wall modification involved in abscission [GO:0009830]; fruit dehiscence [GO:0010047]; pectin catabolic process [GO:0045490]
cytoplasm [GO:0005737]; extracellular region [GO:0005576]
polygalacturonase activity [GO:0004650]
PF00295;
2.160.20.10;
Glycosyl hydrolase 28 family
null
SUBCELLULAR LOCATION: Secreted, cell wall {ECO:0000269|PubMed:11485203}. Cytoplasm {ECO:0000269|PubMed:11485203}. Note=Released to the cell wall during maturation of the dehiscence zone.
CATALYTIC ACTIVITY: Reaction=(1,4-alpha-D-galacturonosyl)n+m + H2O = (1,4-alpha-D-galacturonosyl)n + (1,4-alpha-D-galacturonosyl)m.; EC=3.2.1.15;
null
null
null
null
FUNCTION: Polygalacturonase involved in cell separation in the final stages of pod shatter and in anther dehiscence. Not involved in floral organ abscission. {ECO:0000269|PubMed:17928369, ECO:0000269|PubMed:19168715}.
Arabidopsis thaliana (Mouse-ear cress)
O23160
MYB73_ARATH
MSNPTRKNMERIKGPWSPEEDDLLQRLVQKHGPRNWSLISKSIPGRSGKSCRLRWCNQLSPEVEHRAFSQEEDETIIRAHARFGNKWATISRLLNGRTDNAIKNHWNSTLKRKCSVEGQSCDFGGNGGYDGNLGEEQPLKRTASGGGGVSTGLYMSPGSPSGSDVSEQSSGGAHVFKPTVRSEVTASSSGEDPPTYLSLSLPWTDETVRVNEPVQLNQNTVMDGGYTAELFPVRKEEQVEVEEEEAKGISGGFGGEFMTVVQEMIRTEVRSYMADLQRGNVGGSSSGGGGGGSCMPQSVNSRRVGFREFIVNQIGIGKME
null
null
glucosinolate metabolic process [GO:0019760]; negative regulation of response to salt stress [GO:1901001]; positive regulation of auxin mediated signaling pathway [GO:0010929]; regulation of DNA-templated transcription [GO:0006355]
nucleus [GO:0005634]
DNA-binding transcription factor activity [GO:0003700]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]; transcription cis-regulatory region binding [GO:0000976]
PF00249;
1.10.10.60;
null
null
SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00625, ECO:0000269|PubMed:23809151}.
null
null
null
null
null
FUNCTION: Transcription factor that functions in salt stress response. Acts as a negative regulator of NHX7/SOS1 and CBL4/SOS3 induction in response to salt stress (PubMed:23809151). In response to auxin, activates the transcription of the auxin-responsive gene IAA19. The IAA19 transcription activation by MYB73 is enhanced by direct interaction between MYB73 and PYL8 (PubMed:24894996). {ECO:0000269|PubMed:23809151, ECO:0000269|PubMed:24894996}.
Arabidopsis thaliana (Mouse-ear cress)
O23166
TR164_ARATH
MARLVFSLNLPSSHGFNLSPRNLQSFFVTQTGAPRFRAVRCKPNPESSETKQEKLVIDNGETSSASKEVESSSSVADSSSSSSSGFPESPNKDINRRVAAVTVIAALSLFVSTRLDFGISLKDLTASALPYEEALSNGKPTVVEFYADWCEVCRELAPDVYKIEQQYKDKVNFVMLNVDNTKWEQELDEFGVEGIPHFAFLDREGNEEGNVVGRLPRQYLVENVNALAAGKQSIPYARAVGQYSSSESRKVHQVTDPLSHG
null
null
cytochrome b6f complex assembly [GO:0010190]
chloroplast [GO:0009507]; chloroplast thylakoid [GO:0009534]; chloroplast thylakoid membrane [GO:0009535]; plasma membrane [GO:0005886]; thylakoid lumen [GO:0031977]
oxidoreductase activity, acting on a sulfur group of donors, disulfide as acceptor [GO:0016671]
PF00085;
3.40.30.10;
Thioredoxin family
null
SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane {ECO:0000269|PubMed:11701887, ECO:0000269|PubMed:16997915}; Peripheral membrane protein {ECO:0000269|PubMed:11701887, ECO:0000269|PubMed:16997915}; Lumenal side {ECO:0000269|PubMed:11701887, ECO:0000269|PubMed:16997915}.
null
null
null
null
null
FUNCTION: Thiol-disulfide oxidoreductase that participates in various redox reactions in the chloroplast. Mediates the reduction of PSI-N in the thylakoid lumen. May interact and probably reduce other target proteins of the thylakoid membrane, such as FTSH2, FTSH8, LHCB5, atpA, atpB, atpE, petA and petC. Involved in the biogenesis of the plastid cytochrome b6f complex. Reducing equivalents are provided by stromal M-type thioredoxins and probably transduced through the thylakoid membrane by CCDA. Possesses low insulin disulfide bonds reducing activity. {ECO:0000269|PubMed:11701887, ECO:0000269|PubMed:16997915}.
Arabidopsis thaliana (Mouse-ear cress)
O23171
MES9_ARATH
MKHYVLVHGGCHGAWCWYKVKPMLEHSGHRVTVFDLTAHGVNMSRVEDIQTLEDFAKPLLEVLESFGSDDKVVLVAHSLGGIPAALAADMFPSKISVAVFVTSFMPDTTNPPSYVFEKFLGSITEEERMDFELGSYGTDDHPLKTAFLGPNYLKNMYLLSPIEDYELAKMLMRVTPAITSNLTGTKSLTAQGYGSISRVYIVCGEDKGIRVDFQRWMIENSPVKEVMEIKDADHMPMFSKPHELCDRLLKIADKYP
3.1.1.-
null
defense response to fungus [GO:0050832]; innate immune response [GO:0045087]; jasmonic acid metabolic process [GO:0009694]; oxylipin biosynthetic process [GO:0031408]; salicylic acid metabolic process [GO:0009696]; systemic acquired resistance [GO:0009627]
null
hydrolase activity, acting on ester bonds [GO:0016788]; methyl indole-3-acetate esterase activity [GO:0080030]; methyl jasmonate esterase activity [GO:0080032]; methyl salicylate esterase activity [GO:0080031]
PF12697;
3.40.50.1820;
AB hydrolase superfamily, Methylesterase family
null
null
CATALYTIC ACTIVITY: Reaction=H2O + methyl (indol-3-yl)acetate = (indol-3-yl)acetate + H(+) + methanol; Xref=Rhea:RHEA:32919, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17790, ChEBI:CHEBI:30854, ChEBI:CHEBI:72782; Evidence={ECO:0000269|PubMed:18467465}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:32920; Evidence={ECO:0000269|PubMed:18467465}; CATALYTIC ACTIVITY: Reaction=H2O + methyl (-)-jasmonate = H(+) + jasmonate + methanol; Xref=Rhea:RHEA:55372, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15929, ChEBI:CHEBI:17790, ChEBI:CHEBI:58431; Evidence={ECO:0000269|PubMed:18467465}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:55373; Evidence={ECO:0000269|PubMed:18467465}; CATALYTIC ACTIVITY: Reaction=H2O + methyl salicylate = H(+) + methanol + salicylate; Xref=Rhea:RHEA:33611, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17790, ChEBI:CHEBI:30762, ChEBI:CHEBI:31832; Evidence={ECO:0000269|PubMed:18467465}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33612; Evidence={ECO:0000269|PubMed:18467465};
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=147.1 uM for methyl salicylate (MeSA) {ECO:0000269|PubMed:18643994}; Vmax=25.88 nmol/min/ug enzyme with methyl salicylate (MeSA) as substrate {ECO:0000269|PubMed:18643994};
PATHWAY: Plant hormone biosynthesis. {ECO:0000269|PubMed:18467465}.; PATHWAY: Lipid metabolism; oxylipin biosynthesis. {ECO:0000269|PubMed:18467465}.
null
null
FUNCTION: Methylesterase shown to have carboxylesterase activity, methyl indole-3-acetic acid (MeIAA) esterase activity, methyl salicylate (MeSA) esterase activity and methyl jasmonate (MeJA) esterase activity in vitro. Required to convert methyl salicylate (MeSA) to salicylic acid (SA) as part of the signal transduction pathways that activate systemic acquired resistance in systemic tissue. MeSA is believed to be an inactive form that needs to be demethylated to exert a biological effect. {ECO:0000269|PubMed:18467465, ECO:0000269|PubMed:18643994}.
Arabidopsis thaliana (Mouse-ear cress)
O23179
PLP1_ARATH
MENKSPSKKNKPPSCGSLVTILSLDGGGVRGIIAGVILAFLEKQLQELDGEEARLADYFDVIAGTSTGGLVTAMLTVPDETGRPHFAAKDIVPFYLEHCPKIFPQPTGVLALLPKLPKLLSGPKYSGKYLRNLLSKLLGETRLHQTLTNIVIPTFDIKKLQPTIFSSYQLLVDPSLDVKVSDICIGTSAAPTFFPPHYFSNEDSQGNKTEFNLVDGAVTANNPTLVAMTAVSKQIVKNNPDMGKLKPLGFDRFLVISIGTGSTKREEKYSAKKAAKWGIISWLYDDGSTPILDITMESSRDMIHYHSSVVFKALQSEDKYLRIDDDTLEGDVSTMDLATKSNLENLQKIGEKMLTNRVMQMNIDTGVYEPVAENITNDEQLKRYAKILSDERKLRRLRSDTMIKDSSNESQEIK
3.1.1.-
null
defense response [GO:0006952]; lateral root formation [GO:0010311]; lipid catabolic process [GO:0016042]
cytoplasm [GO:0005737]
acylglycerol lipase activity [GO:0047372]; phospholipase activity [GO:0004620]
PF01734;
3.40.1090.10;
Patatin family
PTM: Phosphorylated at Ser-399 by CPK3. Phosphorylation enhances PLP1 activity towards phosphatidylcholine. {ECO:0000269|PubMed:20053799}.
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12226489}.
null
null
null
BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.0. {ECO:0000269|PubMed:12226489};
null
FUNCTION: Possesses non-specific lipolytic acyl hydrolase (LAH) activity. Catalyzes the hydrolysis of the neutral lipids monogalactosyldiacylglycerol (MGDG), digalactosyldiacylglycerol (DGDG) and phosphatidylglycerol (PG), and less efficiently the polar lipids phosphatidylcholine (PC) and phosphatidylinositol (PI), but not the storage lipid triacylglycerol (TAG). May play a role in root development. {ECO:0000269|PubMed:12226489, ECO:0000269|PubMed:20053799}.
Arabidopsis thaliana (Mouse-ear cress)
O23180
PLP5_ARATH
MENESPSKKNMPPSCGTLVTILSLDGGGVRGIIAGVILAYLEKQLQELDGEHVRVADYFDVIAGTSTGGLVTAMLTAPDENGRPRFAAKEIVPFYLEHCPKIFPQPTGVLALLPKLPKLLSGPKYSGNYLRTTLGKLLGETKLRQTLTNVVIPTFDIKTLQPTIFSSYQALTDPSLDVKVSDICIGTSAAPTYFPPYYFSNEDSQGKTRHFNLVDGGVTANNPTLVAMTAVTKQIVNNNPDMGTLNPLGYDQFLVISIGTGSAKKEERYSAKKAAKWGIISWLYEDGTTPILDITFESSRDIVHYHSSVVFKALQSEDKYLRIDDDTLEGDASTLDLSTKSNLENLIKLGEKMLTNRVMQMNIDTGTYEPAAENINNDEQLKRFAKILSEERKLRRKRSDKMTKDSSIGSQEIK
3.1.1.-
null
defense response [GO:0006952]; lateral root formation [GO:0010311]; lipid catabolic process [GO:0016042]
null
acylglycerol lipase activity [GO:0047372]; phospholipase activity [GO:0004620]
PF01734;
3.40.1090.10;
Patatin family
PTM: Phosphorylated at Ser-399 by CPK3. Phosphorylation enhances PLP5 activity towards phosphatidylcholine. {ECO:0000269|PubMed:20053799}.
null
null
null
null
null
null
FUNCTION: Possesses non-specific lipolytic acyl hydrolase (LAH) activity. Catalyzes the hydrolysis of the neutral lipids monogalactosyldiacylglycerol (MGDG), digalactosyldiacylglycerol (DGDG) and phosphatidylglycerol (PG), and less efficiently the polar lipids phosphatidylcholine (PC) and phosphatidylinositol (PI), but not the storage lipid triacylglycerol (TAG). May play a role in root development. {ECO:0000269|PubMed:20053799}.
Arabidopsis thaliana (Mouse-ear cress)
O23181
PLP3_ARATH
MDTERGSISSSEISRTAHLQDRTVACLPPSYGQLVTILSIDGGGIRGIIPGTILAYLESQLQELDGEEARLVDYFDVISGTSTGGLIVAMLTAQDQSGGHSRNSNRPLFEAKEIVPFYLKHSPKIFPQPRGIFCGWGETIVRLVGGPKFNGKYLHDLVEGFLGDTKLTQSLTNVVIPCFDIKKLQPVIFSSYQAVNNQAMNAKLSDICISTSAAPTFFPAHRFTNEDSEGIKHEFNLIDGGIAANNPTLCAIAEVTKQIIKKNPVMGDISPLDFTRFLVISIGTGSIRNQEKYNAKMASKWGLMCWVFESGSTPILDCYSEAIHDMVDYQSSVVFQALRSEKNYLRIDDDSLKGDLGSVDISTEKNMEGLVEVGEALLKKRVSRVNLESGHYQPISENVTNEEALKRFAKVLSEERKLRESRSPKLKI
3.1.1.-
null
defense response [GO:0006952]; lipid catabolic process [GO:0016042]; response to abscisic acid [GO:0009737]
cytoplasm [GO:0005737]
acylglycerol lipase activity [GO:0047372]; phospholipase activity [GO:0004620]
PF01734;
3.40.1090.10;
Patatin family
null
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12226489}.
null
null
null
null
null
FUNCTION: Possesses non-specific lipolytic acyl hydrolase (LAH) activity. Catalyzes the hydrolysis of the neutral lipids monogalactosyldiacylglycerol (MGDG), digalactosyldiacylglycerol (DGDG) and phosphatidylglycerol (PG), and less efficiently the polar lipids phosphatidylcholine (PC) and phosphatidylinositol (PI), but not the storage lipid triacylglycerol (TAG). May play a role in root development. {ECO:0000269|PubMed:20053799}.
Arabidopsis thaliana (Mouse-ear cress)
O23212
U2A2A_ARATH
MSEFEDHEGNGTVADAIYDEENGGRDGEIEDQLDSKPKRESRDHERETSRSKDREREKGRDKDRERDSEVSRRSRDRDGEKSKERSRDKDRDHRERHHRSSRHRDHSRERGERRERGGRDDDDYRRSRDRDHDRRRDDRGGRRSRRSRSRSKDRSERRTRSRSPSKSKQRVSGFDMAPPASAMLAAGAAVTGQVPPAPPTLPGAGMFPNMFPLPTGQSFGGLSMMPIQAMTQQATRHARRVYVGGLSPTANEQSVATFFSQVMAAVGGNTAGPGDAVVNVYINHEKKFAFVEMRSVEEASNAMSLDGIIFEGAPVKVRRPSDYNPSLAATLGPSQPSPHLNLAAVGLTPGASGGLEGPDRIFVGGLPYYFTESQVRELLESFGGLKGFDLVKDRETGNSKGYAFCVYQDLSVTDIACAALNGIKMGDKTLTVRRANQGTMLQKPEQENVLLHAQQQIAFQRVMLQPGAVATTVVCLTQVVTEDELRDDEEYGDIMEDMRQEGGKFGALTNVVIPRPSPNGEPVAGLGKVFLKYADTDGSTRARFGMNGRKFGGNEVVAVYYPEDKFEQGDYGA
null
null
mRNA splicing, via spliceosome [GO:0000398]
commitment complex [GO:0000243]; nuclear speck [GO:0016607]; nucleus [GO:0005634]; U2-type prespliceosome [GO:0071004]; U2AF complex [GO:0089701]
mRNA binding [GO:0003729]; poly-pyrimidine tract binding [GO:0008187]; pre-mRNA 3'-splice site binding [GO:0030628]
PF00076;
3.30.70.330;
Splicing factor SR family
null
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:24580679}.
null
null
null
null
null
FUNCTION: Necessary for the splicing of pre-mRNA. {ECO:0000250}.
Arabidopsis thaliana (Mouse-ear cress)
O23240
D2HDH_ARATH
MMMQKLRRSGEFIRFGCKSLISSRPNKDSVSRSVSGFVNHYKSKGKLFELSDGNYKTELHHPCISRNVGMLLQQYKCFGSSAASLIQRNPLFSSLDSKDVSYFKEILGEKNVVEDKERLETANTDWMHKYKGSSKLMLLPKNTQEVSQILEYCDSRRLAVVPQGGNTGLVGGSVPVFDEVIVNVGLMNKILSFDEVSGVLVCEAGCILENLATFLDTKGFIMPLDLGAKGSCHIGGNVSTNAGGLRLIRYGSLHGTVLGLEAVTANGNVLDMLGTLRKDNTGYDLKHLFIGSEGSLGIVTKVSILTQPKLSSVNLAFIACKDYLSCQKLLVEAKRNLGEILSAFEFLDNNSMDLVLNHLDGVRNPVSSSENFYILIETTGSDETNDREKLEAFLLKSLEKGLVSDGVIAQDINQASSFWRIREGITEALQKAGAVYKYDLSLPVEEIYNIVNDLRGRLGDLANVMGYGHLGDGNLHLNISAAEYNDKLLGLIEPYVYEWTSKHRGSISAEHGLGVMKANEIFYSKSPETVALMASIKKLLDPKGILNPYKVLPHSLFSN
1.1.99.39
COFACTOR: Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000269|PubMed:19586914}; Note=Binds 1 FAD per monomer. {ECO:0000269|PubMed:19586914};
alternative respiration [GO:0010230]; lactate oxidation [GO:0019516]; nitrogen compound metabolic process [GO:0006807]; photorespiration [GO:0009853]; respiratory electron transport chain [GO:0022904]
mitochondrion [GO:0005739]; plasma membrane [GO:0005886]
(R)-2-hydroxyglutarate dehydrogenase activity [GO:0051990]; 2-hydroxyglutarate dehydrogenase activity [GO:0047545]; FAD binding [GO:0071949]
PF02913;PF01565;
3.30.465.10;3.30.70.2190;3.30.70.2740;3.30.43.10;
FAD-binding oxidoreductase/transferase type 4 family
null
SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:19586914, ECO:0000269|PubMed:21296880, ECO:0000305|PubMed:25732537}.
CATALYTIC ACTIVITY: Reaction=(R)-2-hydroxyglutarate + A = 2-oxoglutarate + AH2; Xref=Rhea:RHEA:38295, ChEBI:CHEBI:13193, ChEBI:CHEBI:15801, ChEBI:CHEBI:16810, ChEBI:CHEBI:17499; EC=1.1.99.39; Evidence={ECO:0000269|PubMed:19586914};
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=584 uM for (R)-2-hydroxyglutarate (with DCIP as acceptor molecule) {ECO:0000269|PubMed:19586914}; Note=Very low activity toward D-lactate, D-2-hydroxybutyrate and meso-tartrate. Does not efficiently use cytochrome c as electron acceptor and is not able to transfer electrons to NAD or NADP.;
null
BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8.5-9.5. {ECO:0000269|PubMed:19586914};
null
FUNCTION: Catalyzes the oxidation of (R)-2-hydroxyglutarate to 2-oxoglutarate. May be involved in the catabolism of propionyl-CoA derived from beta-oxidation. Involved in degradation of lysine for the supply of carbon and electrons to the ETF/ETFQO complex during dark-induced sugar starvation. {ECO:0000269|PubMed:19586914, ECO:0000269|PubMed:20501910, ECO:0000269|PubMed:21296880}.
Arabidopsis thaliana (Mouse-ear cress)
O23249
CKS1_ARATH
MGQIQYSEKYFDDTFEYRHVVLPPEVAKLLPKNRLLSENEWRAIGVQQSRGWVHYAVHRPEPHIMLFRRPLNYQQQQENQAQNMLVK
null
null
cell division [GO:0051301]; DNA endoreduplication [GO:0042023]; mitotic cell cycle [GO:0000278]; regulation of cell cycle [GO:0051726]; regulation of mitotic cell cycle [GO:0007346]
cyclin-dependent protein kinase holoenzyme complex [GO:0000307]; cytoplasm [GO:0005737]; peroxisome [GO:0005777]; SCF ubiquitin ligase complex [GO:0019005]
cyclin-dependent protein serine/threonine kinase activator activity [GO:0061575]; histone binding [GO:0042393]; protein kinase binding [GO:0019901]; ubiquitin binding [GO:0043130]
PF01111;
3.30.170.10;
CKS family
null
null
null
null
null
null
null
FUNCTION: Associates with cyclin-dependent kinases (CDKs) and plays an essential role in the regulation of the cell cycle that affects plant growth rate. May inhibit both the G1/S and G2/M phases. {ECO:0000269|PubMed:11319029}.
Arabidopsis thaliana (Mouse-ear cress)
O23252
IF4E1_ARATH
MAVEDTPKSVVTEEAKPNSIENPIDRYHEEGDDAEEGEIAGGEGDGNVDESSKSGVPESHPLEHSWTFWFDNPAVKSKQTSWGSSLRPVFTFSTVEEFWSLYNNMKHPSKLAHGADFYCFKHIIEPKWEDPICANGGKWTMTFPKEKSDKSWLYTLLALIGEQFDHGDEICGAVVNIRGKQERISIWTKNASNEAAQVSIGKQWKEFLDYNNSIGFIIHEDAKKLDRNAKNAYTA
null
null
defense response [GO:0006952]; response to virus [GO:0009615]
cytoplasm [GO:0005737]; cytoplasmic stress granule [GO:0010494]; cytosol [GO:0005829]; eukaryotic translation initiation factor 4F complex [GO:0016281]; nucleolus [GO:0005730]; nucleus [GO:0005634]; P-body [GO:0000932]
RNA 7-methylguanosine cap binding [GO:0000340]; translation initiation factor activity [GO:0003743]
PF01652;
3.30.760.10;
Eukaryotic initiation factor 4E family
PTM: According to the redox status, the Cys-133-Cys-171 disulfide bridge may have a role in regulating protein function by affecting its ability to bind capped mRNA. {ECO:0000250|UniProtKB:P29557}.
SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:K0P2S0}. Cytoplasm {ECO:0000250|UniProtKB:K0P2S0}.
null
null
null
null
null
FUNCTION: Component of the protein complex eIF4F, which is involved in the recognition of the mRNA cap, ATP-dependent unwinding of 5'-terminal secondary structure and recruitment of mRNA to the ribosome (PubMed:9680993). Recognizes and binds the 7-methylguanosine-containing mRNA cap during an early step in the initiation of protein synthesis and facilitates ribosome binding by inducing the unwinding of the mRNAs secondary structures (By similarity). Key component of recessive resistance to potyviruses (PubMed:29504210, PubMed:30784179). {ECO:0000250|UniProtKB:P48599, ECO:0000269|PubMed:9680993, ECO:0000305|PubMed:29504210, ECO:0000305|PubMed:30784179}.; FUNCTION: (Microbial infection) Susceptibility host factor required for viral infection by recruiting viral RNAs to the host ribosomal complex via an interaction with viral genome-linked protein (VPg). {ECO:0000305|PubMed:29504210, ECO:0000305|PubMed:30784179}.
Arabidopsis thaliana (Mouse-ear cress)
O23254
GLYC4_ARATH
MEPVSSWGNTSLVSVDPEIHDLIEKEKRRQCRGIELIASENFTSFAVIEALGSALTNKYSEGIPGNRYYGGNEFIDEIENLCRSRALEAFHCDPAAWGVNVQPYSGSPANFAAYTALLQPHDRIMGLDLPSGGHLTHGYYTSGGKKISATSIYFESLPYKVNFTTGYIDYDKLEEKALDFRPKLLICGGSAYPRDWDYARFRAIADKVGALLLCDMAHISGLVAAQEAANPFEYCDVVTTTTHKSLRGPRAGMIFYRKGPKPPKKGQPEGAVYDFEDKINFAVFPALQGGPHNHQIGALAVALKQANTPGFKVYAKQVKANAVALGNYLMSKGYQIVTNGTENHLVLWDLRPLGLTGNKVEKLCDLCSITLNKNAVFGDSSALAPGGVRIGAPAMTSRGLVEKDFEQIGEFLSRAVTLTLDIQKTYGKLLKDFNKGLVNNKDLDQLKADVEKFSASYEMPGFLMSEMKYKD
2.1.2.1
COFACTOR: Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; Evidence={ECO:0000269|PubMed:31873125};
cellular response to leukemia inhibitory factor [GO:1990830]; circadian rhythm [GO:0007623]; folic acid metabolic process [GO:0046655]; glycine biosynthetic process from serine [GO:0019264]; L-serine catabolic process [GO:0006565]; protein homotetramerization [GO:0051289]; purine nucleobase biosynthetic process [GO:0009113]; tetrahydrofolate interconversion [GO:0035999]
cytosol [GO:0005829]; nucleus [GO:0005634]; plasma membrane [GO:0005886]; plasmodesma [GO:0009506]
cobalt ion binding [GO:0050897]; glycine hydroxymethyltransferase activity [GO:0004372]; mRNA 5'-UTR binding [GO:0048027]; mRNA regulatory element binding translation repressor activity [GO:0000900]; protein homodimerization activity [GO:0042803]; pyridoxal phosphate binding [GO:0030170]; salicylic acid binding [GO:1901149]; serine binding [GO:0070905]; zinc ion binding [GO:0008270]
PF00464;
3.90.1150.10;3.40.640.10;
SHMT family
null
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CATALYTIC ACTIVITY: Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + glycine + H2O = (6S)-5,6,7,8-tetrahydrofolate + L-serine; Xref=Rhea:RHEA:15481, ChEBI:CHEBI:15377, ChEBI:CHEBI:15636, ChEBI:CHEBI:33384, ChEBI:CHEBI:57305, ChEBI:CHEBI:57453; EC=2.1.2.1; Evidence={ECO:0000269|PubMed:31873125};
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=2.56 mM for L-serine (at pH 6.5 and 30 degrees Celsius) {ECO:0000269|PubMed:31873125}; KM=0.54 mM for L-serine (at pH 7.0 and 30 degrees Celsius) {ECO:0000269|PubMed:31873125}; KM=0.3 mM for L-serine (at pH 8.0 and 30 degrees Celsius) {ECO:0000269|PubMed:31873125}; KM=0.24 mM for L-serine (at pH 8.5 and 30 degrees Celsius) {ECO:0000269|PubMed:31873125}; KM=0.2 mM for L-serine (at pH 9.5 and 30 degrees Celsius) {ECO:0000269|PubMed:31873125}; KM=7.87 uM for (6S)-5,6,7,8-tetrahydrofolate (at pH 6.5 and 30 degrees Celsius) {ECO:0000269|PubMed:31873125}; KM=14.97 uM for (6S)-5,6,7,8-tetrahydrofolate (at pH 7.0 and 30 degrees Celsius) {ECO:0000269|PubMed:31873125}; KM=23.83 uM for (6S)-5,6,7,8-tetrahydrofolate (at pH 8.0 and 30 degrees Celsius) {ECO:0000269|PubMed:31873125}; KM=33.75 uM for (6S)-5,6,7,8-tetrahydrofolate (at pH 8.5 and 30 degrees Celsius) {ECO:0000269|PubMed:31873125}; KM=49.24 uM for (6S)-5,6,7,8-tetrahydrofolate (at pH 9.5 and 30 degrees Celsius) {ECO:0000269|PubMed:31873125};
PATHWAY: One-carbon metabolism; tetrahydrofolate interconversion. {ECO:0000305}.
null
null
FUNCTION: Catalyzes the interconversion of serine and glycine with the conversion of tetrahydrofolate (THF) into 5,10-methylene-THF. {ECO:0000269|PubMed:31873125}.
Arabidopsis thaliana (Mouse-ear cress)
O23255
SAHH1_ARATH
MALLVEKTSSGREYKVKDMSQADFGRLELELAEVEMPGLMACRTEFGPSQPFKGARITGSLHMTIQTAVLIETLTALGAEVRWCSCNIFSTQDHAAAAIARDSAAVFAWKGETLQEYWWCTERALDWGPGGGPDLIVDDGGDATLLIHEGVKAEEIFEKTGQVPDPTSTDNPEFQIVLSIIKEGLQVDPKKYHKMKERLVGVSEETTTGVKRLYQMQQNGTLLFPAINVNDSVTKSKFDNLYGCRHSLPDGLMRATDVMIAGKVAVICGYGDVGKGCAAAMKTAGARVIVTEIDPICALQALMEGLQVLTLEDVVSEADIFVTTTGNKDIIMVDHMRKMKNNAIVCNIGHFDNEIDMLGLETYPGVKRITIKPQTDRWVFPETKAGIIVLAEGRLMNLGCATGHPSFVMSCSFTNQVIAQLELWNEKASGKYEKKVYVLPKHLDEKVALLHLGKLGARLTKLSKDQSDYVSIPIEGPYKPPHYRY
3.13.2.1
COFACTOR: Name=NAD(+); Xref=ChEBI:CHEBI:57540; Evidence={ECO:0000250|UniProtKB:P23526}; Note=Binds 1 NAD(+) per subunit. {ECO:0000250|UniProtKB:P23526};
DNA methylation-dependent heterochromatin formation [GO:0006346]; embryo development ending in seed dormancy [GO:0009793]; one-carbon metabolic process [GO:0006730]; post-transcriptional gene silencing [GO:0016441]; S-adenosylmethionine cycle [GO:0033353]
cytosol [GO:0005829]; plant-type vacuole [GO:0000325]; plasma membrane [GO:0005886]; plasmodesma [GO:0009506]; vacuole [GO:0005773]
adenosylhomocysteinase activity [GO:0004013]; copper ion binding [GO:0005507]; mRNA binding [GO:0003729]
PF05221;PF00670;
3.40.50.1480;3.40.50.720;
Adenosylhomocysteinase family
null
null
CATALYTIC ACTIVITY: Reaction=H2O + S-adenosyl-L-homocysteine = adenosine + L-homocysteine; Xref=Rhea:RHEA:21708, ChEBI:CHEBI:15377, ChEBI:CHEBI:16335, ChEBI:CHEBI:57856, ChEBI:CHEBI:58199; EC=3.13.2.1; Evidence={ECO:0000269|PubMed:15659630};
null
PATHWAY: Amino-acid biosynthesis; L-homocysteine biosynthesis; L-homocysteine from S-adenosyl-L-homocysteine: step 1/1. {ECO:0000269|PubMed:15659630}.
null
null
FUNCTION: Essential protein during embryogenesis (PubMed:15266054). Adenosylhomocysteine is a competitive inhibitor of S-adenosyl-L-methionine-dependent methyl transferase reactions; therefore adenosylhomocysteinase may play a key role in the control of methylations via regulation of the intracellular concentration of adenosylhomocysteine (PubMed:15659630). Required for DNA methylation-dependent gene silencing (PubMed:15659630). {ECO:0000269|PubMed:15266054, ECO:0000269|PubMed:15659630}.
Arabidopsis thaliana (Mouse-ear cress)
O23273
DNMT4_ARATH
MEMETKAGKQKKRSVDSDDDVSKERRPKRAAACTNFKEKSLRISDKSETVEAKKEQILAEEIVAIQLTSSLESNDDPRPNRRLTDFVLHDSEGVPQPVEMLELGDIFIEGVVLPLGDEKKEEKGVRFQSFGRVENWNISGYEDGSPVIWISTALADYDCRKPSKKYKKLYDYFFEKACACVEVFKSLSKNPDTSLDELLAAVSRSMSGSKIFSSGGAIQEFVISQGEFIYNQLAGLDETAKNHETCFVENRVLVSLRDHESNKIHKALSNVALRIDESKVVTSDHLVDGAEDEDVKYAKLIQEEEYRKSMERSRNKRSSTTSGGSSRFYIKISEDEIADDYPLPSYYKNTKEETDELVLFEAGYEVDTRDLPCRTLHNWTLYNSDSRMISLEVLPMRPCAEIDVTVFGSGVVAEDDGSGFCLDDSESSTSTQSNDHDGMNIFLSQIKEWMIEFGAEMIFVTLRTDMAWYRLGKPSKQYAPWFGTVMKTVRVGISIFNMLMRESRVAKLSYANVIKRLCGLEENDKAYISSKLLDVERYVVVHGQIILQLFEEYPDKDIKRCPFVTSLASKMQDIHHTKWIIKKKKKILQKGKNLNPRAGIAPVVSRMKAMQATTTRLVNRIWGEFYSIYSPEVPSEAINAENVEEEELEEVEEEDENEEDDPEENELEAVEIQNSPTPKKIKGISEDMEIKWDGEILGKTSAGEPLYGRAFVGGDVVVVGSAVILEVDDQDDTQLICFVEFMFESSNHSKMLHGKLLQRGSETVLGMAANERELFLTNECLTVQLKDIKGTVSLEIRSRLWGHQYRKENIDVDKLDRARAEERKTNGLPTDYYCKSLYSPERGGFFSLPRNDMGLGSGFCSSCKIRENEEERSKTKLNDSKTGFLSNGIEYHNGDFVYVLPNYITKDGLKKGSRRTTLKCGRNVGLKAFVVCQLLDVIVLEESRKASKASFQVKLTRFYRPEDISEEKAYASDIQELYYSQDTYILPPEAIQGKCEVRKKSDMPLCREYPILDHIFFCEVFYDSSTGYLKQFPANMKLKFSTIKDETLLREKKGKGVETGTSSGMLMKPDEVPKEKPLATLDIFAGCGGLSHGLENAGVSTTKWAIEYEEPAGHAFKQNHPEATVFVDNCNVILRAIMEKCGDVDDCVSTVEAAELAAKLDENQKSTLPLPGQVDFINGGPPCQGFSGMNRFSHGSWSKVQCEMILAFLSFADYFRPKYFLLENVKKFVTYNKGRTFQLTMASLLEMGYQVRFGILEAGTYGVSQPRKRVIIWAASPEEVLPEWPEPMHVFDNPGSKISLPRGLRYDAGCNTKFGAPFRSITVRDTIGDLPPVENGESKINKEYGTTPASWFQKKIRGNMSVLTDHICKGLNELNLIRCKKIPKRPGADWRDLPDENVTLSNGLVEKLRPLALSKTAKNHNEWKGLYGRLDWQGNLPISITDPQPMGKVGMCFHPEQDRIITVRECARSQGFPDSYEFSGTTKHKHRQIGNAVPPPLAFALGRKLKEALYLKSSLQHQS
2.1.1.37
null
chromatin organization [GO:0006325]; DNA-mediated transformation [GO:0009294]; methylation [GO:0032259]
nucleus [GO:0005634]
chromatin binding [GO:0003682]; DNA (cytosine-5-)-methyltransferase activity [GO:0003886]; DNA binding [GO:0003677]
PF01426;PF00145;PF12047;
2.30.30.490;3.90.120.10;3.40.50.150;
Class I-like SAM-binding methyltransferase superfamily, C5-methyltransferase family
null
SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CATALYTIC ACTIVITY: Reaction=a 2'-deoxycytidine in DNA + S-adenosyl-L-methionine = a 5-methyl-2'-deoxycytidine in DNA + H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:13681, Rhea:RHEA-COMP:11369, Rhea:RHEA-COMP:11370, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:85452, ChEBI:CHEBI:85454; EC=2.1.1.37; Evidence={ECO:0000255|PROSITE-ProRule:PRU10018};
null
null
null
null
FUNCTION: Maintains chromatin CpG methylation that plays a role in genomic imprinting, regulation of embryogenesis and seed viability. Required for proper patterns of CG DNA methylation in dividing cells (By similarity). {ECO:0000250}.
Arabidopsis thaliana (Mouse-ear cress)
O23299
ECI2_ARATH
MCTLEKRGDLFLLTLTGDGEHRFHPDTIATILSLLEQAKSQSTRGSILITTANGKFFSNGFDLAWAQTAGSKTGAANRLHQMVESFKPVVAALLDLPMPTIAALNGHAAAAGLILALSHDYVFMRKDRGVLYMSEVDIGLSMPDYFSALVRAKIGTSAARRELLLSGKKIRGEEAVGLGIVDSAAYDSEEGVVVASVRLGEKLAAKKWSGEVYASIRKSLYPELCGILGLETRVFATPKL
5.3.3.8
null
fatty acid beta-oxidation [GO:0006635]; fatty acid catabolic process [GO:0009062]; indolebutyric acid metabolic process [GO:0080024]; response to indolebutyric acid [GO:0080026]; root hair elongation [GO:0048767]
peroxisome [GO:0005777]
delta(3)-delta(2)-enoyl-CoA isomerase activity [GO:0004165]
PF00378;
null
Enoyl-CoA hydratase/isomerase family
null
SUBCELLULAR LOCATION: Peroxisome {ECO:0000269|PubMed:17951448, ECO:0000269|PubMed:18657232}.
CATALYTIC ACTIVITY: Reaction=a (3Z)-enoyl-CoA = a 4-saturated (2E)-enoyl-CoA; Xref=Rhea:RHEA:45900, ChEBI:CHEBI:85097, ChEBI:CHEBI:85489; EC=5.3.3.8; Evidence={ECO:0000269|PubMed:18657232}; CATALYTIC ACTIVITY: Reaction=a (3E)-enoyl-CoA = a 4-saturated (2E)-enoyl-CoA; Xref=Rhea:RHEA:45228, ChEBI:CHEBI:58521, ChEBI:CHEBI:85097; EC=5.3.3.8; Evidence={ECO:0000269|PubMed:18657232};
null
PATHWAY: Lipid metabolism; fatty acid beta-oxidation. {ECO:0000305}.
null
null
FUNCTION: Able to isomerize both 3-cis and 3-trans double bonds into the 2-trans form in a range of enoyl-CoA species. Essential for the beta oxidation of unsaturated fatty acids (PubMed:18657232). Involved with IBR1 and IBR3 in the peroxisomal beta-oxidation of indole-3-butyric acid (IBA) to form indole-3-acetic acid (IAA), a biologically active auxin (PubMed:20562230). {ECO:0000269|PubMed:18657232, ECO:0000269|PubMed:20562230}.
Arabidopsis thaliana (Mouse-ear cress)
O23304
BLUS1_ARATH
MARNKLEFPLDAEAYEIICKIGVGVSASVYKAICIPMNSMVVAIKAIDLDQSRADFDSLRRETKTMSLLSHPNILNAYCSFTVDRCLWVVMPFMSCGSLHSIVSSSFPSGLPENCISVFLKETLNAISYLHDQGHLHRDIKAGNILVDSDGSVKLADFGVSASIYEPVTSSSGTTSSSLRLTDIAGTPYWMAPEVVHSHTGYGFKADIWSFGITALELAHGRPPLSHLPPLKSLLMKITKRFHFSDYEINTSGSSKKGNKKFSKAFREMVGLCLEQDPTKRPSAEKLLKHPFFKNCKGLDFVVKNVLHSLSNAEQMFMESQILIKSVGDDDEEEEEEDEEIVKNRRISGWNFREDDLQLSPVFPATESDSSESSPREEDQSKDKKEDDNVTITGYELGLGLSNEEAKNQEGEVVGFDKDLVLEKLKVLKKSLEHQRARVSIIIEALSGDKEEKSREEELLEMVEKLKIELETEKLKTLRADKDSVLG
2.7.11.1
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
phosphorylation [GO:0016310]; regulation of stomatal opening [GO:1902456]
cytosol [GO:0005829]
ATP binding [GO:0005524]; metal ion binding [GO:0046872]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activator activity [GO:0043539]; protein serine/threonine kinase activity [GO:0004674]
PF00069;
1.10.510.10;
Protein kinase superfamily, STE Ser/Thr protein kinase family, STE20 subfamily
PTM: Phosphorylated at Ser-348 by both PHOT1 and PHOT2. {ECO:0000269|PubMed:23811955}.
SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:23811955}.
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: Ser/Thr protein kinase mediating a primary step for phototropin signaling in guard cells. Essential for stomatal opening. {ECO:0000269|PubMed:23811955}.
Arabidopsis thaliana (Mouse-ear cress)
O23310
NFYB3_ARATH
MADSDNDSGGHKDGGNASTREQDRFLPIANVSRIMKKALPANAKISKDAKETVQECVSEFISFITGEASDKCQREKRKTINGDDLLWAMTTLGFEDYVEPLKVYLQKYREVEGEKTTTAGRQGDKEGGGGGGGAGSGSGGAPMYGGGMVTTMGHQFSHHFS
null
null
positive regulation of DNA-templated transcription [GO:0045893]; response to heat [GO:0009408]; response to water deprivation [GO:0009414]
CCAAT-binding factor complex [GO:0016602]; cytosol [GO:0005829]; nucleus [GO:0005634]
DNA-binding transcription activator activity, RNA polymerase II-specific [GO:0001228]; DNA-binding transcription factor activity [GO:0003700]; protein heterodimerization activity [GO:0046982]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]
PF00808;
1.10.20.10;
NFYB/HAP3 subunit family
null
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:25490919}. Cytoplasm, cytosol {ECO:0000269|PubMed:25490919}. Note=Present in both cytoplasm and nucleus under nonstress conditions but translocates in the nucleus upon heat stress. {ECO:0000269|PubMed:25490919}.
null
null
null
null
null
FUNCTION: Component of the NF-Y/HAP transcription factor complex (By similarity). The NF-Y complex stimulates the transcription of various genes by recognizing and binding to a CCAAT motif in promoters (By similarity). Promotes the expression of heat stress-inducible genes by contributing to the formation of a heat stress-specific transcriptional complex with NF-Y subunits (e.g. DPB3-1, NF-YA2 and NF-YB3) and DREB2A at the promoter of target genes, thus promoting heat tolerance (PubMed:25490919). {ECO:0000250|UniProtKB:Q84W66, ECO:0000269|PubMed:25490919}.
Arabidopsis thaliana (Mouse-ear cress)
O23349
AO1_ARATH
MNTSILAILFLIQCVFTLGLHFHPLDPLTPQEINKTSFIVKKSHLGNLKDLTFHYLDLEEPNKSHVLQWLSPNPSKKPPPPRRRSFVVVRAGGQTYELIIDLTTSKIASSRIYTGHGFPSFTFIELFKASKLPLTYPPFKKSILDRSLNISEVSCIPFTVGWYGETTTRRELKASCFYRDGSVNVFTRPIEGITVTIDVDSMQVIKYSDRFRKPIPDKEGNDFRTKHRPFPFFCNVSDTGFKILGNRVKWANWKFHVGFTARAGVTISTASVLDPRTKRFRRVMYRGHVSETFVPYMDPTYEWYYRTFMDIGEFGFGRSAVNLQPLIDCPQNAAFLDGHVAGPDGTAQKMTNVMCVFEKNGYGASFRHTEINVPGQVITSGEAEISLVVRMVATLGNYDYIVDWEFKKNGAIRVGVDLTGVLEVKATSYTSNDQITENVYGTLVAKNTIAVNHDHYLTYYLDLDVDGNGNSLVKAKLKTVRVTEVNKTSSRRKSYWTVVKETAKTEADGRVRLGSDPVELLIVNPNKKTKIGNTVGYRLIPEHLQATSLLTDDDYPELRAGYTKYPVWVTAYDRSERWAGGFYSDRSRGDDGLAVWSSRNREIENKDIVMWYNVGFHHIPYQEDFPVMPTLHGGFTLRPSNFFDNDPLIG
1.4.3.21
COFACTOR: Name=L-topaquinone; Xref=ChEBI:CHEBI:79027; Evidence={ECO:0000250|UniProtKB:P46883}; Note=Contains 1 topaquinone per subunit. {ECO:0000250|UniProtKB:P46883}; COFACTOR: Name=Cu cation; Xref=ChEBI:CHEBI:23378; Evidence={ECO:0000250|UniProtKB:P46883}; Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250|UniProtKB:P12807}; Note=Binds 1 copper ion per subunit (By similarity). Can also use zinc ion as cofactor (By similarity). {ECO:0000250|UniProtKB:P12807, ECO:0000250|UniProtKB:P46883}; COFACTOR: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250|UniProtKB:Q43077}; Note=Binds 1 Mn(2+) ion per subunit. {ECO:0000250|UniProtKB:Q43077};
amine metabolic process [GO:0009308]; jasmonic acid mediated signaling pathway [GO:0009867]; protoxylem development [GO:0090059]; regulation of programmed cell death [GO:0043067]; response to jasmonic acid [GO:0009753]
extracellular region [GO:0005576]
aliphatic amine oxidase activity [GO:0052595]; copper ion binding [GO:0005507]; primary amine oxidase activity [GO:0008131]; quinone binding [GO:0048038]
PF01179;PF02727;PF02728;
3.10.450.40;2.70.98.20;
Copper/topaquinone oxidase family
PTM: Topaquinone (TPQ) is generated by copper-dependent autoxidation of a specific tyrosyl residue. {ECO:0000250|UniProtKB:P46883}.
SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:H2A0M3}.
CATALYTIC ACTIVITY: Reaction=a primary methyl amine + H2O + O2 = an aldehyde + H2O2 + NH4(+); Xref=Rhea:RHEA:16153, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:17478, ChEBI:CHEBI:28938, ChEBI:CHEBI:228804; EC=1.4.3.21; Evidence={ECO:0000269|PubMed:9681017};
null
null
null
null
FUNCTION: Oxidizes preferentially the aliphatic diamine putrescine with production of the corresponding aldehyde, ammonia and hydrogen peroxide. May be involved in the regulation of developmental programmed cell death (PCD) in both vascular tissue and the root cap (PubMed:9681017). Required for jasmonic acid-(MeJA) mediated early protoxylem differentiation associated with putrescine levels reduction and H(2)O(2) accumulation in roots (PubMed:25883242). {ECO:0000269|PubMed:25883242, ECO:0000269|PubMed:9681017}.
Arabidopsis thaliana (Mouse-ear cress)
O23372
ATXR3_ARATH
MSDGGVACMPLLNIMEKLPIVEKTTLCGGNESKTAATTENGHTSIATKVPESQPANKPSASSQPVKKKRIVKVIRKVVKRRPKQPQKQADEQLKDQPPSQVVQLPAESQLQIKEQDKKSEFKGGTSGVKEVENGGDSGFKDEVEEGELGTLKLHEDLENGEISPVKSLQKSEIEKGEIVGESWKKDEPTKGEFSHLKYHKGYVERRDFSADKNWKGGKEEREFRSWRDPSDEIEKGEFIPDRWQKMDTGKDDHSYIRSRRNGVDREKTWKYEYEYERTPPGGRFVNEDIYHQREFRSGLDRTTRISSKIVIEENLHKNEYNNSSNFVKEYSSTGNRLKRHGAEPDSIERKHSYADYGDYGSSKCRKLSDDCSRSLHSDHYSQHSAERLYRDSYPSKNSSLEKYPRKHQDASFPAKAFSDKHGHSPSRSDWSPHDRSRYHENRDRSPYARERSPYIFEKSSHARKRSPRDRRHHDYRRSPSYSEWSPHDRSRPSDRRDYIPNFMEDTQSDRNRRNGHREISRKSGVRERRDCQTGTELEIKHKYKESNGKESTSSSKELQGKNILYNNSLLVEKNSVCDSSKIPVPCATGKEPVQVGEAPTEELPSMEVDMDICDTPPHEPMASDSSLGKWFYLDYYGTEHGPARLSDLKALMEQGILFSDHMIKHSDNNRWLVNPPEAPGNLLEDIADTTEAVCIEQGAGDSLPELVSVRTLPDGKEIFVENREDFQIDMRVENLLDGRTITPGREFETLGEALKVNVEFEETRRCVTSEGVVGMFRPMKRAIEEFKSDDAYGSESDEIGSWFSGRWSCKGGDWIRQDEASQDRYYKKKIVLNDGFPLCLMQKSGHEDPRWHHKDDLYYPLSSSRLELPLWAFSVVDERNQTRGVKASLLSVVRLNSLVVNDQVPPIPDPRAKVRSKERCPSRPARPSPASSDSKRESVESHSQSTASTGQDSQGLWKTDTSVNTPRDRLCTVDDLQLHIGDWFYTDGAGQEQGPLSFSELQKLVEKGFIKSHSSVFRKSDKIWVPVTSITKSPETIAMLRGKTPALPSACQGLVVSETQDFKYSEMDTSLNSFHGVHPQFLGYFRGKLHQLVMKTFKSRDFSAAINDVVDSWIHARQPKKESEKYMYQSSELNSCYTKRARLMAGESGEDSEMEDTQMFQKDELTFEDLCGDLTFNIEGNRSAGTVGIYWGLLDGHALARVFHMLRYDVKSLAFASMTCRHWKATINSYKDISRQVDLSSLGPSCTDSRLRSIMNTYNKEKIDSIILVGCTNVTASMLEEILRLHPRISSVDITGCSQFGDLTVNYKNVSWLRCQNTRSGELHSRIRSLKQTTDVAKSKGLGGDTDDFGNLKDYFDRVEKRDSANQLFRRSLYKRSKLYDARRSSAILSRDARIRRWAIKKSEHGYKRVEEFLASSLRGIMKQNTFDFFALKVSQIEEKMKNGYYVSHGLRSVKEDISRMCREAIKDELMKSWQDGSGLSSATKYNKKLSKTVAEKKYMSRTSDTFGVNGASDYGEYASDREIKRRLSKLNRKSFSSESDTSSELSDNGKSDNYSSASASESESDIRSEGRSQDLRIEKYFTADDSFDSVTEEREWGARMTKASLVPPVTRKYEVIEKYAIVADEEEVQRKMRVSLPEDYGEKLNAQRNGIEELDMELPEVKEYKPRKLLGDEVLEQEVYGIDPYTHNLLLDSMPGELDWSLQDKHSFIEDVVLRTLNRQVRLFTGSGSTPMVFPLRPVIEELKESAREECDIRTMKMCQGVLKEIESRSDDKYVSYRKGLGVVCNKEGGFGEEDFVVEFLGEVYPVWKWFEKQDGIRSLQENKTDPAPEFYNIYLERPKGDADGYDLVVVDAMHMANYASRICHSCRPNCEAKVTAVDGHYQIGIYSVRAIEYGEEITFDYNSVTESKEEYEASVCLCGSQVCRGSYLNLTGEGAFQKVLKDWHGLLERHRLMLEACVLNSVSEEDYLELGRAGLGSCLLGGLPDWMIAYSARLVRFINFERTKLPEEILKHNLEEKRKYFSDIHLDVEKSDAEVQAEGVYNQRLQNLAVTLDKVRYVMRHVFGDPKNAPPPLERLTPEETVSFVWNGDGSLVDELLQSLSPHLEEGPLNELRSKIHGHDPSGSADVLKELQRSLLWLRDEIRDLPCTYKCRNDAAADLIHIYAYTKCFFKVREYQSFISSPVHISPLDLGAKYADKLGESIKEYRKTYGENYCLGQLIYWYNQTNTDPDLTLVKATRGCLSLPDVASFYAKAQKPSKHRVYGPKTVKTMVSQMSKQPQRPWPKDKIWTFKSTPRVFGSPMFDAVLNNSSSLDRELLQWLRNRRHVFQATWDS
2.1.1.354
null
carpel development [GO:0048440]; circadian rhythm [GO:0007623]; epigenetic regulation of gene expression [GO:0040029]; methylation [GO:0032259]; post-embryonic development [GO:0009791]; stamen development [GO:0048443]; vegetative to reproductive phase transition of meristem [GO:0010228]
nucleus [GO:0005634]
histone H3K4 methyltransferase activity [GO:0042800]; histone H3K4 trimethyltransferase activity [GO:0140999]; metal ion binding [GO:0046872]
PF14237;PF19633;PF00856;
2.170.270.10;
Class V-like SAM-binding methyltransferase superfamily, Histone-lysine methyltransferase family, TRX/MLL subfamily
null
SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00768}.
CATALYTIC ACTIVITY: Reaction=L-lysyl(4)-[histone H3] + 3 S-adenosyl-L-methionine = 3 H(+) + N(6),N(6),N(6)-trimethyl-L-lysyl(4)-[histone H3] + 3 S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:60260, Rhea:RHEA-COMP:15537, Rhea:RHEA-COMP:15547, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:61961; EC=2.1.1.354; Evidence={ECO:0000269|PubMed:20937886};
null
null
null
null
FUNCTION: Histone methyltransferase specifically required for trimethylation of 'Lys-4' of histone H3 (H3K4me3) and is crucial for both sporophyte and gametophyte development (PubMed:20937886, PubMed:21037105). Function as a diurnal 'writer' to counteract the nocturne 'eraser' demethylase activity of JMJ14 thus orchestrating the circadian rythm of histone modifications (e.g. H3K4me3) and modulating the rythmic expression of diurnal target genes; this mechanism relies also on the circadian clock oscillators CCA1 and LHY (PubMed:31429787). {ECO:0000269|PubMed:20937886, ECO:0000269|PubMed:21037105, ECO:0000269|PubMed:31429787}.
Arabidopsis thaliana (Mouse-ear cress)
O23393
BIA1_ARATH
MEAKLEVTGKEVIKPASPSPRDRLQLSILDLYCPGIYVSTIFFYDLITESSEVFSENLKLSLSETLSRFYPLAGRIEGLSISCNDEGAVFTEARTDLLLPDFLRNLNTDSLSGFLPTLAAGESPAAWPLLSVKVTFFGSGSGVAVSVSVSHKICDIASLVTFVKDWATTTAKGKSNSTIEFAETTIYPPPPSHMYEQFPSTDSDSNITSKYVLKRFVFEPSKIAELKHKAASESVPVPTRVEAIMSLIWRCARNSSRSNLLIPRQAVMWQAMDIRLRIPSSVAPKDVIGNLQSGFSLKKDAESEFEIPEIVATFRKNKERVNEMIKESLQGNTIGQSLLSLMAETVSESTEIDRYIMSSWCRKPFYEVDFGSGSPVWVGYASHTIYDNMVGVVLIDSKEGDGVEAWISLPEEDMSVFVDDQELLAYAVLNPPVVA
2.3.1.-
null
brassinosteroid homeostasis [GO:0010268]; brassinosteroid mediated signaling pathway [GO:0009742]; brassinosteroid metabolic process [GO:0016131]; regulation of brassinosteroid biosynthetic process [GO:0010422]; regulation of flavonoid biosynthetic process [GO:0009962]; response to absence of light [GO:0009646]; response to brassinosteroid [GO:0009741]
cytosol [GO:0005829]
acyltransferase activity [GO:0016746]
PF02458;
3.30.559.10;
Plant acyltransferase family
null
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:22544867, ECO:0000269|PubMed:22956280}.
null
null
null
null
null
FUNCTION: Monitors brassinosteroids (BR) responses and homeostasis, particularly in the root and hypocotyl in darkness (PubMed:22544867, PubMed:22956280). Promotes flavonoid biosynthesis (PubMed:22956280). {ECO:0000269|PubMed:22544867, ECO:0000269|PubMed:22956280}.
Arabidopsis thaliana (Mouse-ear cress)
O23403
PPD1_ARATH
MASSAFAFPSYIITKGASTDSFKSTSLSSSRSLVTDFHLLFSRPISSGPKYQSAKSAKPESPVAINCLTDAKQVCAVGRRKSMMMGLLMSGLIVSQANLPTAFASTPVFREYIDTFDGYSFKYPQNWIQVRGAGADIFFRDPVVLDENLSVEFSSPSSSNYTSLEDLGSPEEVGKRVLRQYLTEFMSTRLGVKRQANILSTSSRVADDGKLYYQVEVNIKSYANNNELAVMPQDRVARLEWNRRYLAVLGVENDRLYSIRLQTPEKVFLEEEKDLRRVMDSFRVEKI
null
null
photosystem I assembly [GO:0048564]
chloroplast [GO:0009507]; chloroplast stroma [GO:0009570]; chloroplast thylakoid lumen [GO:0009543]; chloroplast thylakoid membrane [GO:0009535]; extrinsic component of membrane [GO:0019898]; photosystem II oxygen evolving complex [GO:0009654]; thylakoid [GO:0009579]; thylakoid lumen [GO:0031977]
calcium ion binding [GO:0005509]
PF01789;PF20928;
3.40.1000.10;
PsbP family
null
SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid lumen {ECO:0000269|PubMed:11719511, ECO:0000269|PubMed:23221595}. Note=Associates primarily with stroma-exposed thylakoids. {ECO:0000269|PubMed:23221595}.
null
null
null
null
null
FUNCTION: Photosystem I assembly factor that assists the proper folding and integration of PsaB and PsaA into the thylakoid membrane. {ECO:0000269|PubMed:23221595}.
Arabidopsis thaliana (Mouse-ear cress)
O23404
PPDK1_ARATH
MLYIRKKMTSMIVKTTPELFKGNGVFRTDHLGENRMVSRSNRLGDGSNRFPRTGTIHCQRLSIAKTGLHRETKARAILSPVSDPAASIAQKRVFTFGKGRSEGNKGMKSLLGGKGANLAEMASIGLSVPPGLTISTEACQQYQIAGKKLPEGLWEEILEGLSFIERDIGASLADPSKPLLLSVRSGAAISMPGMMDTVLNLGLNDQVVVGLAAKSGERFAYDSFRRFLDMFGDVVMGIPHAKFEEKLERMKERKGVKNDTDLSAADLKELVEQYKSVYLEAKGQEFPSDPKKQLELAIEAVFDSWDSPRANKYRSINQITGLKGTAVNIQCMVFGNMGDTSGTGVLFTRNPSTGEKKLYGEFLVNAQGEDVVAGIRTPEDLDTMKRFMPEAYAELVENCNILERHYKDMMDIEFTVQEERLWMLQCRAGKRTGKGAVKIAVDMVGEGLVEKSSAIKMVEPQHLDQLLHPQFHDPSGYREKVVAKGLPASPGAAVGQVVFTAEEAEAWHSQGKTVILVRTETSPDDVGGMHAAEGILTARGGMTSHAAVVARGWGKCCIAGCSEIRVDENHKVLLIGDLTINEGEWISMNGSTGEVILGKQALAPPALSPDLETFMSWADAIRRLKVMANADTPEDAIAARKNGAQGIGLCRTEHMFFGADRIKAVRKMIMAVTTEQRKASLDILLPYQRSDFEGIFRAMDGLPVTIRLLDPPLHEFLPEGDLDNIVHELAEETGVKEDEVLSRIEKLSEVNPMLGFRGCRLGISYPELTEMQARAIFEAAASMQDQGVTVIPEIMVPLVGTPQELGHQVDVIRKVAKKVFAEKGHTVSYKVGTMIEIPRAALIADEIAKEAEFFSFGTNDLTQMTFGYSRDDVGKFLPIYLAKGILQHDPFEVLDQQGVGQLIKMATEKGRAARPSLKVGICGEHGGDPSSVGFFAEAGLDYVSCSPFRVPIARLAAAQVVVA
2.7.9.1
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:P11155};
phosphorylation [GO:0016310]; photosynthesis [GO:0015979]; pyruvate metabolic process [GO:0006090]
chloroplast [GO:0009507]; chloroplast stroma [GO:0009570]; cytosol [GO:0005829]
ATP binding [GO:0005524]; kinase activity [GO:0016301]; metal ion binding [GO:0046872]; pyruvate, phosphate dikinase activity [GO:0050242]
PF00391;PF02896;PF01326;
1.20.80.30;3.30.1490.20;3.30.470.20;3.20.20.60;3.50.30.10;1.10.189.10;
PEP-utilizing enzyme family
PTM: Phosphorylation of Thr-543 in the dark inactivates the enzyme. Dephosphorylation upon light stimulation reactivates the enzyme. {ECO:0000250|UniProtKB:P11155}.
SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000269|PubMed:16915520}. Cytoplasm {ECO:0000269|PubMed:16915520}. Note=Isoform 1 is targeted to the chloroplast while isoform 2 is found in the cytoplasm.
CATALYTIC ACTIVITY: Reaction=ATP + phosphate + pyruvate = AMP + diphosphate + H(+) + phosphoenolpyruvate; Xref=Rhea:RHEA:10756, ChEBI:CHEBI:15361, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:43474, ChEBI:CHEBI:58702, ChEBI:CHEBI:456215; EC=2.7.9.1; Evidence={ECO:0000269|PubMed:21414960, ECO:0000269|PubMed:21883547};
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=17 uM for pyruvate {ECO:0000269|PubMed:21414960}; KM=292 uM for phosphoenolpyruvate {ECO:0000269|PubMed:21414960};
null
null
null
FUNCTION: Formation of phosphoenolpyruvate. May be involved in regulating the flux of carbon into starch and fatty acids of seeds and in the remobilization of nitrogen reserves in senescing leaves. {ECO:0000269|PubMed:15272878, ECO:0000269|PubMed:16915520, ECO:0000269|PubMed:21414960, ECO:0000269|PubMed:21883547}.
Arabidopsis thaliana (Mouse-ear cress)
O23463
CMTA5_ARATH
MAGVDSGKLIGSEIHGFHTLQDLDIQTMLDEAYSRWLRPNEIHALLCNHKFFTINVKPVNLPKSGTIVLFDRKMLRNFRKDGHNWKKKKDGKTIKEAHEHLKVGNEERIHVYYAHGEDTPTFVRRCYWLLDKSQEHIVLVHYRETHEVHAAPATPGNSYSSSITDHLSPKIVAEDTSSGVHNTCNTGFEVRSNSLGSRNHEIRLHEINTLDWDELLVPADISNQSHPTEEDMLYFTEQLQTAPRGSVKQGNHLAGYNGSVDIPSFPGLEDPVYQNNNSCGAGEFSSQHSHCGVDPNLQRRDFSATVTDQPGDALLNNGYGSQDSFGRWVNNFISDSPGSVDDPSLEAVYTPGQDSSTPPTVFHSHSDIPEQVFNITDVSPAWAYSTEKTKILVTGFFHDSFQHLGRSNLICICGELRVPAEFLQMGVYRCFLPPQSPGVVNLYLSVDGNKPISQLFSFEHRSVQFIEKAIPQDDQLYKWEEFEFQVRLAHLLFTSSNKISVLTSKISPENLLEAKKLASRTSHLLNSWAYLMKSIQANEVPFDQARDHLFELTLKNRLKEWLLEKVIENRNTKEYDSKGLGVIHLCAVLGYTWSILLFSWANISLDFRDKQGWTALHWAAYYGREKMVAALLSAGARPNLVTDPTKEFLGGCTAADLAQQKGYDGLAAFLAEKCLVAQFKDMQTAGNISGNLETIKAEKSSNPGNANEEEQSLKDTLAAYRTAAEAAARIQGAFREHELKVRSSAVRFASKEEEAKNIIAAMKIQHAFRNFEVRRKIAAAARIQYRFQTWKMRREFLNMRKKAIRIQAAFRGFQVRRQYQKITWSVGVLEKAILRWRLKRKGFRGLQVSQPDEKEGSEAVEDFYKTSQKQAEERLERSVVKVQAMFRSKKAQQDYRRMKLAHEEAQLEYDGMQELDQMATEES
null
null
cellular response to cold [GO:0070417]; regulation of DNA-templated transcription [GO:0006355]; regulation of transcription by RNA polymerase II [GO:0006357]; response to cold [GO:0009409]
nucleus [GO:0005634]
calmodulin binding [GO:0005516]; DNA-binding transcription factor activity [GO:0003700]; double-stranded DNA binding [GO:0003690]; sequence-specific DNA binding [GO:0043565]; transcription coregulator activity [GO:0003712]
PF12796;PF03859;PF00612;
1.20.5.190;1.25.40.20;2.60.40.10;
CAMTA family
null
SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00767, ECO:0000269|PubMed:14581622, ECO:0000269|PubMed:28351986}.
null
null
null
null
null
FUNCTION: Transcription activator (PubMed:14581622). Binds to the DNA consensus sequence 5'-[ACG]CGCG[GTC]-3' (By similarity). Regulates transcriptional activity in response to calcium signals (Probable). Binds calmodulin in a calcium-dependent manner (By similarity). Involved in response to cold. Contributes together with CAMTA3 to the positive regulation of the cold-induced expression of DREB1A/CBF3, DREB1B/CBF1 and DREB1C/CBF2 (PubMed:28351986). {ECO:0000250|UniProtKB:Q8GSA7, ECO:0000269|PubMed:14581622, ECO:0000269|PubMed:28351986, ECO:0000305|PubMed:11925432}.
Arabidopsis thaliana (Mouse-ear cress)
O23507
1MMP_ARATH
MSRNLIYRRNRALCFVLILFCFPYRFGARNTPEAEQSTAKATQIIHVSNSTWHDFSRLVDVQIGSHVSGVSELKRYLHRFGYVNDGSEIFSDVFDGPLESAISLYQENLGLPITGRLDTSTVTLMSLPRCGVSDTHMTINNDFLHTTAHYTYFNGKPKWNRDTLTYAISKTHKLDYLTSEDVKTVFRRAFSQWSSVIPVSFEEVDDFTTADLKIGFYAGDHGDGLPFDGVLGTLAHAFAPENGRLHLDAAETWIVDDDLKGSSEVAVDLESVATHEIGHLLGLGHSSQESAVMYPSLRPRTKKVDLTVDDVAGVLKLYGPNPKLRLDSLTQSEDSIKNGTVSHRFLSGNFIGYVLLVVGLILFL
3.4.24.-
COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250|UniProtKB:P03956}; COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250|UniProtKB:P03956}; Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000250|UniProtKB:P03956};
collagen catabolic process [GO:0030574]; extracellular matrix organization [GO:0030198]; proteolysis [GO:0006508]
extracellular matrix [GO:0031012]; plasma membrane [GO:0005886]; side of membrane [GO:0098552]
metalloendopeptidase activity [GO:0004222]; zinc ion binding [GO:0008270]
PF00413;PF01471;
3.40.390.10;
Peptidase M10A family, Matrix metalloproteinases (MMPs) subfamily
null
SUBCELLULAR LOCATION: Cell membrane {ECO:0000255}; Lipid-anchor, GPI-anchor {ECO:0000255}; Extracellular side {ECO:0000305}.
null
null
null
BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7-8. {ECO:0000269|PubMed:24156403};
BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 45-55 degrees Celsius. {ECO:0000269|PubMed:24156403};
FUNCTION: Matrix metalloproteinases (MMPs) or matrixins may play a role in the degradation and remodeling of the extracellular matrix (ECM) during development or in response to stresses (PubMed:10574937). Can cleave myelin basic protein as well as fluorigenic peptide substrates, McaPLANvaDpaAR-NH(2) and McaPChaGNvaHADpa-NH(2) 4-fold more efficiently than McaPLGLDpaAR-NH(2) (QF24) (PubMed:10574937). Active on myelin basic protein (MBP) and, to some extent, on McaPLGLDpaAR-NH(2) (QF24) and beta-casein (PubMed:24156403). {ECO:0000269|PubMed:10574937, ECO:0000269|PubMed:24156403, ECO:0000303|PubMed:10574937}.
Arabidopsis thaliana (Mouse-ear cress)
O23512
MES16_ARATH
MGGEGGAEPVIHFVFVHGASHGAWCWYKLTTLLDAAGFKSTSVDLTGAGISLIDSNIVFDSDQYNRPLFSLLSDLPPHHKVILVGHSIGGGSVTEALCKFTDKISMAIYLAASMVQPGSIPSPHLSNIHVGEEDIWEYTYGEGTDKPPTGVLMKPEFIRHYYYSQSPLEDVTLSSKLLRPAPMRAFQDLDKLPPNPEAEKVPRVYIKTAKDNLFDSVRQDLLVENWPPSQLYVLEDSDHSAFFSVPTTLFAYLLRAVSFLQR
3.1.1.-
null
chlorophyll a catabolic process [GO:0033310]; chlorophyll catabolic process [GO:0015996]; jasmonic acid metabolic process [GO:0009694]; leaf senescence [GO:0010150]; oxylipin biosynthetic process [GO:0031408]; salicylic acid metabolic process [GO:0009696]
cytoplasm [GO:0005737]
hydrolase activity, acting on ester bonds [GO:0016788]; methyl indole-3-acetate esterase activity [GO:0080030]; methyl jasmonate esterase activity [GO:0080032]; methyl salicylate esterase activity [GO:0080031]; pheophorbidase activity [GO:0035560]; primary fluorescent dioxobilin-type chlorophyll catabolite methylesterase activity [GO:0106372]; protein homodimerization activity [GO:0042803]
PF12697;
3.40.50.1820;
AB hydrolase superfamily, Methylesterase family
null
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:22147518}.
CATALYTIC ACTIVITY: Reaction=H2O + methyl (indol-3-yl)acetate = (indol-3-yl)acetate + H(+) + methanol; Xref=Rhea:RHEA:32919, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17790, ChEBI:CHEBI:30854, ChEBI:CHEBI:72782; Evidence={ECO:0000269|PubMed:18467465}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:32920; Evidence={ECO:0000269|PubMed:18467465}; CATALYTIC ACTIVITY: Reaction=H2O + methyl (-)-jasmonate = H(+) + jasmonate + methanol; Xref=Rhea:RHEA:55372, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15929, ChEBI:CHEBI:17790, ChEBI:CHEBI:58431; Evidence={ECO:0000269|PubMed:18467465}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:55373; Evidence={ECO:0000269|PubMed:18467465}; CATALYTIC ACTIVITY: Reaction=H2O + primary fluorescent dioxobilin-type chlorophyll catabolite = H(+) + methanol + O13(4)-desmethyl pFDCC; Xref=Rhea:RHEA:67176, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17790, ChEBI:CHEBI:167885, ChEBI:CHEBI:167889; Evidence={ECO:0000269|PubMed:23723324}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67177; Evidence={ECO:0000269|PubMed:23723324};
null
PATHWAY: Plant hormone biosynthesis. {ECO:0000269|PubMed:18467465}.; PATHWAY: Lipid metabolism; oxylipin biosynthesis. {ECO:0000269|PubMed:18467465}.; PATHWAY: Porphyrin-containing compound metabolism; chlorophyll degradation. {ECO:0000269|PubMed:22147518, ECO:0000269|PubMed:23723324}.
null
null
FUNCTION: Involved in the chlorophyll breakdown by its action in fluorescent chlorophyll catabolites (FCCs) demethylation (PubMed:22147518, PubMed:23723324, PubMed:24302623). Demethylates the C13(2)-carboxymethyl group present at the isocyclic ring of chlorophyll (PubMed:22147518). Uses primary fluorescent dioxobilin-type chlorophyll catabolite (pFDCC) as substrate to produce O13(4)-desmethyl pFDCC (PubMed:23723324, PubMed:24302623). Also able to catalyze pheophorbides in vitro (PubMed:22147518). Methylesterase shown to have carboxylesterase activity, methyl indole-3-acetic acid (MeIAA) esterase activity and methyl jasmonate (MeJA) esterase activity in vitro (PubMed:18467465, PubMed:27109476). {ECO:0000269|PubMed:18467465, ECO:0000269|PubMed:22147518, ECO:0000269|PubMed:23723324, ECO:0000269|PubMed:24302623, ECO:0000269|PubMed:27109476}.
Arabidopsis thaliana (Mouse-ear cress)
O23523
RGGA_ARATH
MATLNPFDLLDDDAEDPSQLAVAIEKIDKSKKSGQVSSLPAKSAPKLPSKPLPPAQAVREARSDAPRGGGGRGGFNRGRGGYNRDDGNNGYSGGYTKPSGEGDVSKSSYERRGGGGAPRGSFRGEGGGPGGGRRGGFSNEGGDGERPRRAFERRSGTGRGSDFKRDGSGRGNWGTPGEEIAAETEAVAGVETEKDVGEKPAVDDVAADANKEDTVVEEKEPEDKEMTLDEYEKILEEKKKALQSLTTSERKVDTKVFESMQQLSNKKSNDEIFIKLGSDKDKRKDDKEEKAKKAVSINEFLKPAEGGNYYRGGRGGRGRGGRGRGGVSSGESGGYRNEAAPAIGDAAQFPSLGGK
null
null
abscisic acid-activated signaling pathway [GO:0009738]; cellular response to osmotic stress [GO:0071470]; cellular response to salt stress [GO:0071472]; regulation of abscisic acid-activated signaling pathway [GO:0009787]; regulation of translation [GO:0006417]; response to abscisic acid [GO:0009737]; response to osmotic stress [GO:0006970]; response to salt stress [GO:0009651]
cytoplasm [GO:0005737]; cytosol [GO:0005829]; nucleus [GO:0005634]; perinuclear region of cytoplasm [GO:0048471]
mRNA binding [GO:0003729]
PF04774;PF09598;
6.10.140.1040;
SERBP1-HABP4 family
null
SUBCELLULAR LOCATION: Cytoplasm, perinuclear region {ECO:0000269|PubMed:25783413}. Nucleus {ECO:0000250|UniProtKB:Q9SQ56, ECO:0000255|PROSITE-ProRule:PRU00768}.
null
null
null
null
null
FUNCTION: Ribosome-binding protein that acts as a regulator of mRNA translation by promoting ribosome inactivation (By similarity). Binds RNA (PubMed:25783413). Regulates responses to abscisic acid (ABA) (PubMed:25783413). Promotes stomata closure in drought conditions (PubMed:25783413). Involved in resistance to salt and drought stresses via the accumulation of Pro (PubMed:25783413). {ECO:0000250|UniProtKB:Q5XJA5, ECO:0000269|PubMed:25783413}.
Arabidopsis thaliana (Mouse-ear cress)
O23530
SNC1_ARATH
MMDTSKDDDMEIASSSGSRRYDVFPSFRGEDVRDSFLSHLLKELRGKAITFIDDEIERSRSIGPELLSAIKESRIAIVIFSKNYASSTWCLNELVEIHKCYTNLNQMVIPIFFHVDASEVKKQTGEFGKVFEETCKAKSEDEKQSWKQALAAVAVMAGYDLRKWPSEAAMIEELAEDVLRKTMTPSDDFGDLVGIENHIEAIKSVLCLESKEARIMVGIWGQSGIGKSTIGRALYSKLSIQFHHRAFITYKSTSGSDVSGMKLRWEKELLSEILGQKDIKIEHFGVVEQRLKQQKVLILLDDVDSLEFLKTLVGKAEWFGSGSRIIVITQDRQLLKAHEIDLIYEVEFPSEHLALTMLCRSAFGKDSPPDDFKELAFEVAKLAGNLPLGLSVLGSSLKGRTKEWWMEMMPRLRNGLNGDIMKTLRVSYDRLHQKDQDMFLYIACLFNGFEVSYVKDLLKDNVGFTMLTEKSLIRITPDGYIEMHNLLEKLGREIDRAKSKGNPGKRRFLTNFEDIHEVVTEKTGTETLLGIRLPFEEYFSTRPLLIDKESFKGMRNLQYLEIGYYGDLPQSLVYLPLKLRLLDWDDCPLKSLPSTFKAEYLVNLIMKYSKLEKLWEGTLPLGSLKEMNLRYSNNLKEIPDLSLAINLEELDLVGCKSLVTLPSSIQNATKLIYLDMSDCKKLESFPTDLNLESLEYLNLTGCPNLRNFPAIKMGCSDVDFPEGRNEIVVEDCFWNKNLPAGLDYLDCLTRCMPCEFRPEQLAFLNVRGYKHEKLWEGIQSLGSLEGMDLSESENLTEIPDLSKATKLESLILNNCKSLVTLPSTIGNLHRLVRLEMKECTGLEVLPTDVNLSSLETLDLSGCSSLRSFPLISTNIVWLYLENTAIEEIPSTIGNLHRLVRLEMKKCTGLEVLPTDVNLSSLETLDLSGCSSLRSFPLISESIKWLYLENTAIEEIPDLSKATNLKNLKLNNCKSLVTLPTTIGNLQKLVSFEMKECTGLEVLPIDVNLSSLMILDLSGCSSLRTFPLISTNIVWLYLENTAIEEIPSTIGNLHRLVKLEMKECTGLEVLPTDVNLSSLMILDLSGCSSLRTFPLISTRIECLYLQNTAIEEVPCCIEDFTRLTVLMMYCCQRLKTISPNIFRLTRLELADFTDCRGVIKALSDATVVATMEDHVSCVPLSENIEYIWDKLYRVAYLQEHFSFRNCFKLDRDARELILRSCFKPVALPGEEIPKYFTYRAYGDSLTVIVPQSSLSQNFLRFKACVVVEPLSKGKGFYPFLKVNVGFNGKQYQKSFSKDAELELCKTDHLFFCSFKFRSEDLPSKLNFNDVEFKFCCSNRIKECGVRLMYVSQEENNQQTTRSEKRMRMTSGTSEEDINLPYGLIVADTGLAALNMELSLGQGEPSSSTSLEGEALCVDYMITEEQDKGIPILFPVSGN
3.2.2.6
null
defense response to bacterium [GO:0042742]; response to auxin [GO:0009733]; systemic acquired resistance, salicylic acid mediated signaling pathway [GO:0009862]
cytoplasm [GO:0005737]; cytosol [GO:0005829]; endoplasmic reticulum [GO:0005783]; intracellular membrane-bounded organelle [GO:0043231]; nucleus [GO:0005634]
ADP binding [GO:0043531]; ATP binding [GO:0005524]; NAD+ nucleosidase activity [GO:0003953]; NAD+ nucleotidase, cyclic ADP-ribose generating [GO:0061809]; nucleotide binding [GO:0000166]
PF20160;PF07725;PF00931;PF01582;
1.10.8.430;3.40.50.300;3.80.10.10;3.40.50.10140;
Disease resistance TIR-NB-LRR family
PTM: [Isoform 2]: Met-1 is specifically acetylated by N-terminal acetyltransferase complex A (NatA). The NatA-mediated acetylation serves as a degradation signal. {ECO:0000269|PubMed:25966763}.; PTM: [Isoform 1]: Met-1 is specifically acetylated by N-terminal acetyltransferase complex B (NatB). The NatB-mediated acetylation stabilizes SNC1. {ECO:0000269|PubMed:25966763}.
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:21079790}. Microsome {ECO:0000269|PubMed:21079790}. Nucleus {ECO:0000269|PubMed:21079790, ECO:0000269|PubMed:22454454}. Note=Restricted to microsomes when interacting with SRFR1. Accumulates in nucleus at 22 degrees Celsius, but not at 28 degrees Celsius. Nuclear accumulation is enhanced by abscisic acid deficiency. {ECO:0000269|PubMed:21079790, ECO:0000269|PubMed:22454454}.
CATALYTIC ACTIVITY: Reaction=H2O + NAD(+) = ADP-D-ribose + H(+) + nicotinamide; Xref=Rhea:RHEA:16301, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17154, ChEBI:CHEBI:57540, ChEBI:CHEBI:57967; EC=3.2.2.6; Evidence={ECO:0000305|PubMed:31439792}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16302; Evidence={ECO:0000305|PubMed:31439792};
null
null
null
null
FUNCTION: Disease resistance protein of the TIR-NB-LRR-type (PubMed:14576290). Part of the RPP5 locus that contains a cluster of several paralogous disease resistance (R) genes (PubMed:14576290). Resistance proteins guard the plant against pathogens that contain an appropriate avirulence protein via an indirect interaction with this avirulence protein (PubMed:14576290). That triggers a defense system including the hypersensitive response, which restricts the pathogen growth (PubMed:14576290). Probably acts as a NAD(+) hydrolase (NADase): in response to activation, catalyzes cleavage of NAD(+) into ADP-D-ribose (ADPR) and nicotinamide; NAD(+) cleavage triggering a defense system that promotes cell death (PubMed:31439792). Expression regulated by MOS1 at chromatin level (PubMed:20647385). Nuclear localization of SNC1 is essential for its activity (PubMed:22454454). ABA deficiency can rescue high-temperature inhibition of SNC1-mediated defense responses (PubMed:22454454). {ECO:0000269|PubMed:14576290, ECO:0000269|PubMed:20647385, ECO:0000269|PubMed:22454454, ECO:0000269|PubMed:31439792}.
Arabidopsis thaliana (Mouse-ear cress)
O23553
BAM3_ARATH
MELTLNSSSSLIKRKDAKSSRNQESSSNNMTFAKMKPPTYQFQAKNSVKEMKFTHEKTFTPEGETLEKWEKLHVLSYPHSKNDASVPVFVMLPLDTVTMSGHLNKPRAMNASLMALKGAGVEGVMVDAWWGLVEKDGPMNYNWEGYAELIQMVQKHGLKLQVVMSFHQCGGNVGDSCSIPLPPWVLEEISKNPDLVYTDKSGRRNPEYISLGCDSVPVLRGRTPIQVYSDFMRSFRERFEGYIGGVIAEIQVGMGPCGELRYPSYPESNGTWRFPGIGEFQCYDKYMKSSLQAYAESIGKTNWGTSGPHDAGEYKNLPEDTEFFRRDGTWNSEYGKFFMEWYSGKLLEHGDQLLSSAKGIFQGSGAKLSGKVAGIHWHYNTRSHAAELTAGYYNTRNHDGYLPIAKMFNKHGVVLNFTCMEMKDGEQPEHANCSPEGLVKQVQNATRQAGTELAGENALERYDSSAFGQVVATNRSDSGNGLTAFTYLRMNKRLFEGQNWQQLVEFVKNMKEGGHGRRLSKEDTTGSDLYVGFVKGKIAENVEEAALV
3.2.1.2
null
maltose biosynthetic process [GO:0000024]; response to cold [GO:0009409]; starch catabolic process [GO:0005983]
chloroplast stroma [GO:0009570]; cytosol [GO:0005829]
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:10652124, ECO:0000269|PubMed:16698902, ECO:0000269|PubMed:18390594}.
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 6-7. {ECO:0000269|PubMed:18390594, ECO:0000269|PubMed:19664588};
null
FUNCTION: Beta-amylase activity. No alpha-amylase activity. Involved in cold resistance. Mediates the accumulation of maltose upon freezing stress, thus contributing to the protection of the photosynthetic electron transport chain. Plays a role in the circadian-regulated starch degradation and maltose metabolism in chloroplasts, especially at night. More active on phosphorylated glucan. Interacts directly with starch or other alpha-1,4-glucan. {ECO:0000269|PubMed:10652124, ECO:0000269|PubMed:16055686, ECO:0000269|PubMed:16297066, ECO:0000269|PubMed:17631522, ECO:0000269|PubMed:18390594, ECO:0000269|PubMed:19664588}.
Arabidopsis thaliana (Mouse-ear cress)
O23627
SYGM1_ARATH
MRIFSTFVFHRRQQIFNLRQFQTTTILRNPISIAPIQIPMDATEQSLRQSLSEKSSSVEAQGNAVRALKASRAAKPEIDAAIEQLNKLKLEKSTVEKELQSIISSSGNGSLNREAFRKAVVNTLERRLFYIPSFKIYSGVAGLFDYGPPGCAIKSNVLSFWRQHFILEENMLEVDCPCVTPEVVLKASGHVDKFTDLMVKDEKTGTCYRADHLLKDYCTEKLEKDLTISAEKAAELKDVLAVMEDFSPEQLGAKIREYGITAPDTKNPLSDPYPFNLMFQTSIGPSGLIPGYMRPETAQGIFVNFKDLYYYNGKKLPFAAAQIGQAFRNEISPRQGLLRVREFTLAEIEHFVDPENKSHPKFSDVAKLEFLMFPREEQMSGQSAKKLCLGEAVAKGTVNNETLGYFIGRVYLFLTRLGIDKERLRFRQHLANEMAHYAADCWDAEIESSYGWIECVGIADRSAYDLRAHSDKSGTPLVAEEKFAEPKEVEKLVITPVKKELGLAFKGNQKNVVESLEAMNEEEAMEMKATLESKGEVEFYVCTLKKSVNIKKNMVSISKEKKKEHQRVFTPSVIEPSFGIGRIIYCLYEHCFSTRPSKAGDEQLNLFRFPPLVAPIKCTVFPLVQNQQFEEVAKVISKELASVGISHKIDITGTSIGKRYARTDELGVPFAITVDSDTSVTIRERDSKDQVRVTLKEAASVVSSVSEGKMTWQDVWATFPHHSSAAADE
2.7.7.-; 6.1.1.14
null
diadenosine tetraphosphate biosynthetic process [GO:0015966]; mitochondrial glycyl-tRNA aminoacylation [GO:0070150]
chloroplast [GO:0009507]; cytosol [GO:0005829]; endosome [GO:0005768]; Golgi apparatus [GO:0005794]; mitochondrion [GO:0005739]; nucleus [GO:0005634]; trans-Golgi network [GO:0005802]
ATP binding [GO:0005524]; glycine-tRNA ligase activity [GO:0004820]; protein dimerization activity [GO:0046983]; transferase activity [GO:0016740]
PF03129;PF00587;PF00458;
3.30.40.230;3.30.720.200;3.40.50.800;1.10.287.10;
Class-II aminoacyl-tRNA synthetase family
null
SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:11278923}. Cytoplasm, cytosol {ECO:0000269|PubMed:11278923}.
CATALYTIC ACTIVITY: Reaction=ATP + glycine + tRNA(Gly) = AMP + diphosphate + glycyl-tRNA(Gly); Xref=Rhea:RHEA:16013, Rhea:RHEA-COMP:9664, Rhea:RHEA-COMP:9683, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57305, ChEBI:CHEBI:78442, ChEBI:CHEBI:78522, ChEBI:CHEBI:456215; EC=6.1.1.14; Evidence={ECO:0000269|PubMed:11278923}; CATALYTIC ACTIVITY: Reaction=2 ATP + H(+) = diphosphate + P(1),P(4)-bis(5'-adenosyl) tetraphosphate; Xref=Rhea:RHEA:34935, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:58141; Evidence={ECO:0000250|UniProtKB:P41250};
null
null
null
null
FUNCTION: Catalyzes the ATP-dependent ligation of glycine to the 3'-end of its cognate tRNA, via the formation of an aminoacyl-adenylate intermediate (Gly-AMP). Also produces diadenosine tetraphosphate (Ap4A), a universal pleiotropic signaling molecule needed for cell regulation pathways, by direct condensation of 2 ATPs. Thereby, may play a special role in Ap4A homeostasis. {ECO:0000250|UniProtKB:P41250}.
Arabidopsis thaliana (Mouse-ear cress)
O23628
H2AV1_ARATH
MAGKGGKGLVAAKTMAANKDKDKDKKKPISRSARAGIQFPVGRIHRQLKTRVSAHGRVGATAAVYTASILEYLTAEVLELAGNASKDLKVKRITPRHLQLAIRGDEELDTLIKGTIAGGGVIPHIHKSLINKTTKE
null
null
detection of temperature stimulus [GO:0016048]; negative regulation of DNA-templated transcription [GO:0045892]; regulation of DNA methylation [GO:0044030]; regulation of gene expression [GO:0010468]; response to osmotic stress [GO:0006970]
nucleosome [GO:0000786]; nucleus [GO:0005634]
DNA binding [GO:0003677]; protein heterodimerization activity [GO:0046982]; structural constituent of chromatin [GO:0030527]
PF00125;PF16211;
1.10.20.10;
Histone H2A family
null
SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Chromosome {ECO:0000250}.
null
null
null
null
null
FUNCTION: Variant histone H2A which may replace conventional H2A in a subset of nucleosomes. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling (By similarity). {ECO:0000250}.
Arabidopsis thaliana (Mouse-ear cress)