PUB70_ORYSJ
ID PUB70_ORYSJ Reviewed; 805 AA.
AC Q5WA76;
DT 07-JUN-2017, integrated into UniProtKB/Swiss-Prot.
DT 07-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=U-box domain-containing protein 70 {ECO:0000303|PubMed:19825583};
DE Short=OsPUB70 {ECO:0000303|PubMed:19825583};
DE AltName: Full=Plant U-box protein 70 {ECO:0000305};
DE AltName: Full=Receptor-like cytoplasmic kinase 197 {ECO:0000303|PubMed:19825577};
DE Short=OsRLCK197 {ECO:0000303|PubMed:19825577};
DE Includes:
DE RecName: Full=E3 ubiquitin ligase {ECO:0000305};
DE EC=2.3.2.27 {ECO:0000305};
DE AltName: Full=RING-type E3 ubiquitin transferase {ECO:0000305};
DE Includes:
DE RecName: Full=Serine/threonine-protein kinase {ECO:0000305};
DE EC=2.7.11.- {ECO:0000305};
GN Name=PUB70 {ECO:0000303|PubMed:19825583};
GN Synonyms=RLCK197 {ECO:0000303|PubMed:19825577};
GN OrderedLocusNames=Os06g0163000 {ECO:0000312|EMBL:BAF18807.1},
GN LOC_Os06g06760 {ECO:0000305};
GN ORFNames=OsJ_20227 {ECO:0000312|EMBL:EEE65144.1},
GN P0681F10.40 {ECO:0000312|EMBL:BAD67644.1};
OS Oryza sativa subsp. japonica (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=39947;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=16100779; DOI=10.1038/nature03895;
RG International rice genome sequencing project (IRGSP);
RT "The map-based sequence of the rice genome.";
RL Nature 436:793-800(2005).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=18089549; DOI=10.1093/nar/gkm978;
RG The rice annotation project (RAP);
RT "The rice annotation project database (RAP-DB): 2008 update.";
RL Nucleic Acids Res. 36:D1028-D1033(2008).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=24280374; DOI=10.1186/1939-8433-6-4;
RA Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R.,
RA Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L.,
RA Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H.,
RA Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.;
RT "Improvement of the Oryza sativa Nipponbare reference genome using next
RT generation sequence and optical map data.";
RL Rice 6:4-4(2013).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=12869764; DOI=10.1126/science.1081288;
RG The rice full-length cDNA consortium;
RT "Collection, mapping, and annotation of over 28,000 cDNA clones from
RT japonica rice.";
RL Science 301:376-379(2003).
RN [6]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=19825577; DOI=10.1093/mp/ssn047;
RA Vij S., Giri J., Dansana P.K., Kapoor S., Tyagi A.K.;
RT "The receptor-like cytoplasmic kinase (OsRLCK) gene family in rice:
RT organization, phylogenetic relationship, and expression during development
RT and stress.";
RL Mol. Plant 1:732-750(2008).
RN [7]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=19825583; DOI=10.1093/mp/ssn044;
RA Zeng L.R., Park C.H., Venu R.C., Gough J., Wang G.L.;
RT "Classification, expression pattern, and E3 ligase activity assay of rice
RT U-box-containing proteins.";
RL Mol. Plant 1:800-815(2008).
RN [8]
RP FUNCTION, AND INTERACTION WITH MODD.
RX PubMed=27468891; DOI=10.1105/tpc.16.00171;
RA Tang N., Ma S., Zong W., Yang N., Lv Y., Yan C., Guo Z., Li J., Li X.,
RA Xiang Y., Song H., Xiao J., Li X., Xiong L.;
RT "MODD mediates deactivation and degradation of OsbZIP46 to negatively
RT regulate ABA signaling and drought resistance in rice.";
RL Plant Cell 28:2161-2177(2016).
CC -!- FUNCTION: Functions as an E3 ubiquitin ligase. Is recruited by MODD to
CC promote ubiquitination of BZIP46, a positive regulator of abscisic acid
CC (ABA) signaling and drought stress tolerance.
CC {ECO:0000269|PubMed:27468891}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine +
CC [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-
CC cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.;
CC EC=2.3.2.27;
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBUNIT: Interacts with MODD. {ECO:0000269|PubMed:27468891}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000305}.
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DR EMBL; AB026295; BAD67644.1; -; Genomic_DNA.
DR EMBL; AP008212; BAF18807.1; -; Genomic_DNA.
DR EMBL; AP014962; BAS96304.1; -; Genomic_DNA.
DR EMBL; CM000143; EEE65144.1; -; Genomic_DNA.
DR EMBL; AK069245; BAG91337.1; -; mRNA.
DR RefSeq; XP_015644198.1; XM_015788712.1.
DR AlphaFoldDB; Q5WA76; -.
DR SMR; Q5WA76; -.
DR STRING; 4530.OS06T0163000-03; -.
DR PaxDb; Q5WA76; -.
DR PRIDE; Q5WA76; -.
DR EnsemblPlants; Os06t0163000-01; Os06t0163000-01; Os06g0163000.
DR EnsemblPlants; Os06t0163000-03; Os06t0163000-03; Os06g0163000.
DR GeneID; 4340220; -.
DR Gramene; Os06t0163000-01; Os06t0163000-01; Os06g0163000.
DR Gramene; Os06t0163000-03; Os06t0163000-03; Os06g0163000.
DR KEGG; osa:4340220; -.
DR eggNOG; KOG0548; Eukaryota.
DR HOGENOM; CLU_020505_0_0_1; -.
DR InParanoid; Q5WA76; -.
DR OMA; MHYTEAM; -.
DR OrthoDB; 933764at2759; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000000763; Chromosome 6.
DR Proteomes; UP000007752; Chromosome 6.
DR Proteomes; UP000059680; Chromosome 6.
DR ExpressionAtlas; Q5WA76; baseline and differential.
DR GO; GO:0043229; C:intracellular organelle; IEA:UniProt.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IEA:InterPro.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR Gene3D; 1.25.40.10; -; 2.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR InterPro; IPR019734; TPR_repeat.
DR InterPro; IPR003613; Ubox_domain.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF04564; U-box; 1.
DR SMART; SM00220; S_TKc; 1.
DR SMART; SM00028; TPR; 4.
DR SMART; SM00504; Ubox; 1.
DR SUPFAM; SSF48452; SSF48452; 2.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
DR PROSITE; PS50005; TPR; 4.
DR PROSITE; PS50293; TPR_REGION; 2.
DR PROSITE; PS51698; U_BOX; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Coiled coil; Kinase; Nucleotide-binding; Reference proteome;
KW Repeat; Serine/threonine-protein kinase; TPR repeat; Transferase;
KW Ubl conjugation pathway.
FT CHAIN 1..805
FT /note="U-box domain-containing protein 70"
FT /id="PRO_0000440563"
FT REPEAT 15..48
FT /note="TPR 1"
FT /evidence="ECO:0000255"
FT REPEAT 49..82
FT /note="TPR 2"
FT /evidence="ECO:0000255"
FT REPEAT 90..127
FT /note="TPR 3"
FT /evidence="ECO:0000255"
FT REPEAT 129..153
FT /note="TPR 4"
FT /evidence="ECO:0000255"
FT REPEAT 154..187
FT /note="TPR 5"
FT /evidence="ECO:0000255"
FT REPEAT 189..221
FT /note="TPR 6"
FT /evidence="ECO:0000255"
FT REPEAT 222..255
FT /note="TPR 7"
FT /evidence="ECO:0000255"
FT DOMAIN 445..711
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 730..804
FT /note="U-box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01034"
FT REGION 136..160
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 341..417
FT /evidence="ECO:0000255"
FT ACT_SITE 567
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 451..459
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 472
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ SEQUENCE 805 AA; 91026 MW; 7AC38262550DB598 CRC64;
MEAEDDERAE AEAEARREKE AGNAAYRKLY LETAVRHYTR GALLDPRDIS FLTNRAAAYL
LMSKYKECVR DCDEAVEKGR ELRADNKLVA RALARKASAL LKLAACAADY DPAIRALQQS
LAEHYSEETL AKLGEAEEAR KEIEERERLD QEAADHHRDR GNDFFKQKRY QEAAMHYTEA
MKKNPKDPRV FSNRAQCHIY LGALPEGLED ADKCIALDPT FLKGYLRKAK VQLLMGNYEI
ALATYVEGLK CDPNNLEVLD GLRRCAACIK RANGGDSRAE DLREILGDLH LNDDLCNKLQ
KSMDEAAVLK KEASDERLKR IESERLARTL EDLYLSQVQQ RKETEESLSR VQQEFEQLKI
QQDEVTVELQ RVNEQNENLL GQLSDSREHF EWLLSEHDQL LRERDNAVRE VEELRQKRGQ
MLSVLVTAMH CEFSSSEVES ATENFSNSLK IGEGGFGCVY KGILRNMTVA IKVLRPDSLQ
GQSQFEQEVS ILSRVRHPHL VTLLGACSES STLVYEFLPN GSLEDFLMCS DKRQTLTWQA
RIRIIAEICS ALIFLHKNKP HPVVHGDLKP ANILLGVNLV SKLSDFGISR LLIQSSTNNT
TLYRTMHPVG TPLYMDPEFL STGELTPQSD VYSFGIVVLR LLTGKPPVGI KNIVEDAMEK
GDLNSVIDTS VGEWPHLHIE QLAYLALRCT ELSRRCRPDL SGEVWAIVEA IRDAALSSPS
SSRSAQDQNS PPSYFICPIS QDIMDDPHIA ADGFTYEAEA IRSWLCNGHD TSPMTNLLLE
HEELIPNRAL RSAIQEWLQQ HSMSL
