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WRK62_ORYSI
ID   WRK62_ORYSI             Reviewed;         318 AA.
AC   B8BF91; Q6IEL9;
DT   07-SEP-2016, integrated into UniProtKB/Swiss-Prot.
DT   03-MAR-2009, sequence version 1.
DT   03-AUG-2022, entry version 74.
DE   RecName: Full=WRKY transcription factor WRKY62 {ECO:0000303|PubMed:15618416};
DE            Short=OsWRKY62 {ECO:0000303|PubMed:15618416};
DE   AltName: Full=XA21-binding protein 10 {ECO:0000303|PubMed:20118235};
GN   Name=WRKY62 {ECO:0000303|PubMed:15618416};
GN   Synonyms=XB10 {ECO:0000303|PubMed:20118235};
GN   ORFNames=OsI_31380 {ECO:0000312|EMBL:EEC84578.1};
OS   Oryza sativa subsp. indica (Rice).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX   NCBI_TaxID=39946;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=15047897; DOI=10.1104/pp.103.034967;
RA   Zhang Z.-L., Xie Z., Zou X., Casaretto J., Ho T.-H.D., Shen Q.J.;
RT   "A rice WRKY gene encodes a transcriptional repressor of the gibberellin
RT   signaling pathway in aleurone cells.";
RL   Plant Physiol. 134:1500-1513(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. 93-11;
RX   PubMed=15685292; DOI=10.1371/journal.pbio.0030038;
RA   Yu J., Wang J., Lin W., Li S., Li H., Zhou J., Ni P., Dong W., Hu S.,
RA   Zeng C., Zhang J., Zhang Y., Li R., Xu Z., Li S., Li X., Zheng H., Cong L.,
RA   Lin L., Yin J., Geng J., Li G., Shi J., Liu J., Lv H., Li J., Wang J.,
RA   Deng Y., Ran L., Shi X., Wang X., Wu Q., Li C., Ren X., Wang J., Wang X.,
RA   Li D., Liu D., Zhang X., Ji Z., Zhao W., Sun Y., Zhang Z., Bao J., Han Y.,
RA   Dong L., Ji J., Chen P., Wu S., Liu J., Xiao Y., Bu D., Tan J., Yang L.,
RA   Ye C., Zhang J., Xu J., Zhou Y., Yu Y., Zhang B., Zhuang S., Wei H.,
RA   Liu B., Lei M., Yu H., Li Y., Xu H., Wei S., He X., Fang L., Zhang Z.,
RA   Zhang Y., Huang X., Su Z., Tong W., Li J., Tong Z., Li S., Ye J., Wang L.,
RA   Fang L., Lei T., Chen C.-S., Chen H.-C., Xu Z., Li H., Huang H., Zhang F.,
RA   Xu H., Li N., Zhao C., Li S., Dong L., Huang Y., Li L., Xi Y., Qi Q.,
RA   Li W., Zhang B., Hu W., Zhang Y., Tian X., Jiao Y., Liang X., Jin J.,
RA   Gao L., Zheng W., Hao B., Liu S.-M., Wang W., Yuan L., Cao M.,
RA   McDermott J., Samudrala R., Wang J., Wong G.K.-S., Yang H.;
RT   "The genomes of Oryza sativa: a history of duplications.";
RL   PLoS Biol. 3:266-281(2005).
RN   [3]
RP   GENE FAMILY, AND NOMENCLATURE.
RX   PubMed=15618416; DOI=10.1104/pp.104.054312;
RA   Xie Z., Zhang Z.-L., Zou X., Huang J., Ruas P., Thompson D., Shen Q.J.;
RT   "Annotations and functional analyses of the rice WRKY gene superfamily
RT   reveal positive and negative regulators of abscisic acid signaling in
RT   aleurone cells.";
RL   Plant Physiol. 137:176-189(2005).
RN   [4]
RP   INDUCTION BY SALICYLIC ACID; MAGNAPORTHE GRISEA AND XANTHOMONAS ORYZAE.
RX   PubMed=16528562; DOI=10.1007/s00299-006-0138-1;
RA   Ryu H.-S., Han M., Lee S.-K., Cho J.-I., Ryoo N., Heu S., Lee Y.-H.,
RA   Bhoo S.H., Wang G.-L., Hahn T.-R., Jeon J.-S.;
RT   "A comprehensive expression analysis of the WRKY gene superfamily in rice
RT   plants during defense response.";
RL   Plant Cell Rep. 25:836-847(2006).
RN   [5]
RP   INTERACTION WITH XA21, AND INDUCTION BY XA21.
RX   PubMed=20118235; DOI=10.1074/jbc.m109.093427;
RA   Chen X., Chern M., Canlas P.E., Jiang C., Ruan D., Cao P., Ronald P.C.;
RT   "A conserved threonine residue in the juxtamembrane domain of the XA21
RT   pattern recognition receptor is critical for kinase autophosphorylation and
RT   XA21-mediated immunity.";
RL   J. Biol. Chem. 285:10454-10463(2010).
CC   -!- FUNCTION: Transcription repressor. Interacts specifically with the W
CC       box (5'-(T)TGAC[CT]-3'), a frequently occurring elicitor-responsive
CC       cis-acting element. Regulates, probably indirectly, the activation of
CC       defense-related genes during defense response (By similarity).
CC       Regulates negatively basal innate immunity and XA21-mediated defense
CC       against X.oryzae pv. oryzae (Xoo) (By similarity).
CC       {ECO:0000250|UniProtKB:Q6EPZ0, ECO:0000250|UniProtKB:Q6QHD1}.
CC   -!- SUBUNIT: Interacts with XA21 in the nucleus.
CC       {ECO:0000269|PubMed:20118235}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q6QHD1,
CC       ECO:0000255|PROSITE-ProRule:PRU00223}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=B8BF91-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=B8BF91-2; Sequence=VSP_058457;
CC   -!- INDUCTION: Might be activated by XA21 in the nucleus upon pathogen
CC       infection (PubMed:20118235). Induced by biotic elicitors (e.g. fungal
CC       chitin oligosaccharide) (By similarity). Induced by pathogen infection
CC       (e.g. M.grisea and X.oryzae pv. oryzae (Xoo)). Accumulates after
CC       treatment with benzothiadiazole (BTH) and salicylic acid (SA)
CC       (PubMed:16528562). Transactivated by WRKY45 (By similarity).
CC       {ECO:0000250|UniProtKB:Q6EPZ0, ECO:0000269|PubMed:16528562,
CC       ECO:0000303|PubMed:20118235}.
CC   -!- DOMAIN: The WRKY domain is required to bind DNA.
CC       {ECO:0000250|UniProtKB:Q6QHD1}.
CC   -!- SIMILARITY: Belongs to the WRKY group II-a family. {ECO:0000305}.
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DR   EMBL; BK005065; DAA05127.1; -; Genomic_DNA.
DR   EMBL; CM000134; EEC84578.1; -; Genomic_DNA.
DR   AlphaFoldDB; B8BF91; -.
DR   SMR; B8BF91; -.
DR   STRING; 39946.B8BF91; -.
DR   EnsemblPlants; BGIOSGA029757-TA; BGIOSGA029757-PA; BGIOSGA029757. [B8BF91-1]
DR   Gramene; BGIOSGA029757-TA; BGIOSGA029757-PA; BGIOSGA029757. [B8BF91-1]
DR   HOGENOM; CLU_047067_0_1_1; -.
DR   OMA; FMHALTY; -.
DR   Proteomes; UP000007015; Chromosome 9.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:InterPro.
DR   GO; GO:0043565; F:sequence-specific DNA binding; IEA:InterPro.
DR   GO; GO:0006952; P:defense response; IEA:UniProtKB-KW.
DR   GO; GO:1900425; P:negative regulation of defense response to bacterium; IEA:EnsemblPlants.
DR   GO; GO:0009617; P:response to bacterium; IEP:UniProtKB.
DR   GO; GO:0010200; P:response to chitin; ISS:UniProtKB.
DR   GO; GO:0009620; P:response to fungus; IEP:UniProtKB.
DR   GO; GO:0009751; P:response to salicylic acid; IEP:UniProtKB.
DR   Gene3D; 2.20.25.80; -; 1.
DR   InterPro; IPR003657; WRKY_dom.
DR   InterPro; IPR036576; WRKY_dom_sf.
DR   InterPro; IPR044810; WRKY_plant.
DR   PANTHER; PTHR31429; PTHR31429; 1.
DR   Pfam; PF03106; WRKY; 1.
DR   SMART; SM00774; WRKY; 1.
DR   SUPFAM; SSF118290; SSF118290; 1.
DR   PROSITE; PS50811; WRKY; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; ATP-binding; Coiled coil; DNA-binding;
KW   Nucleotide-binding; Nucleus; Plant defense; Reference proteome;
KW   Transcription; Transcription regulation.
FT   CHAIN           1..318
FT                   /note="WRKY transcription factor WRKY62"
FT                   /id="PRO_0000436957"
FT   DNA_BIND        138..204
FT                   /note="WRKY"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00223"
FT   REGION          1..27
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          65..86
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          100..136
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          29..49
FT                   /evidence="ECO:0000255"
FT   BINDING         259..266
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00289"
FT   VAR_SEQ         1..39
FT                   /note="Missing (in isoform 2)"
FT                   /id="VSP_058457"
SQ   SEQUENCE   318 AA;  33515 MW;  D5C96CAE89B5637C CRC64;
     MDDDGDGSSS PTDDSAAAGL LPLFSRSPAE DLEEKLRRAM EENARLTRAL DAILAGHHAH
     QRALLAPSLS PPPPSATARA PSVSTSCAAR EDAAPAVAAA AASTACPSRQ QPPTAEPRPK
     VRTVRVRADA ADATDANSMA ETVKDGYQWR KYGQKVTRDN PYPRAYFRCA FAPSCPVKKK
     LQRCAEDRSM LVATYEGEHN HALSTQTTEF VASGCTTSQH AGGSSSSPLP CSISINSSGR
     TITLDLTNQA GSGSIASCGV EAAAVSGELV TVLSPELRRH LVEEVVQVLK NDAEFVEAVT
     NAVAARVVDQ IPHIPVHL
 
 
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