OSK3_ORYSI
ID OSK3_ORYSI Reviewed; 508 AA.
AC A2XFF4;
DT 02-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT 20-MAR-2007, sequence version 1.
DT 03-AUG-2022, entry version 97.
DE RecName: Full=Serine/threonine protein kinase OSK3 {ECO:0000250|UniProtKB:Q852Q0};
DE Short=OsK3 {ECO:0000250|UniProtKB:Q852Q0};
DE EC=2.7.11.1 {ECO:0000250|UniProtKB:Q852Q0};
GN Name=OSK3 {ECO:0000250|UniProtKB:Q852Q0};
GN ORFNames=OsI_11096 {ECO:0000312|EMBL:EAY89564.1};
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 [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).
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; EC=2.7.11.1;
CC Evidence={ECO:0000250|UniProtKB:Q852Q0};
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 EC=2.7.11.1; Evidence={ECO:0000250|UniProtKB:Q852Q0};
CC -!- SUBUNIT: Interacts with HDR1. {ECO:0000250|UniProtKB:Q852Q0}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q852Q1}.
CC -!- TISSUE SPECIFICITY: Strongly expressed in immature seeds. Mostly
CC expressed in panicles, and to a lower extent, in leaf sheaths.
CC {ECO:0000250|UniProtKB:Q852Q0}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
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DR EMBL; CM000128; EAY89564.1; -; Genomic_DNA.
DR AlphaFoldDB; A2XFF4; -.
DR SMR; A2XFF4; -.
DR STRING; 39946.A2XFF4; -.
DR iPTMnet; A2XFF4; -.
DR PRIDE; A2XFF4; -.
DR EnsemblPlants; BGIOSGA012387-TA; BGIOSGA012387-PA; BGIOSGA012387.
DR Gramene; BGIOSGA012387-TA; BGIOSGA012387-PA; BGIOSGA012387.
DR HOGENOM; CLU_000288_59_3_1; -.
DR OMA; TRTITYC; -.
DR Proteomes; UP000007015; Chromosome 3.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
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:0006468; P:protein phosphorylation; IEA:InterPro.
DR InterPro; IPR028375; KA1/Ssp2_C.
DR InterPro; IPR001772; KA1_dom.
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; IPR015940; UBA.
DR Pfam; PF02149; KA1; 1.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF00627; UBA; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF103243; SSF103243; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS50032; KA1; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
DR PROSITE; PS50030; UBA; 1.
PE 3: Inferred from homology;
KW ATP-binding; Kinase; Nucleotide-binding; Nucleus; Reference proteome;
KW Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..508
FT /note="Serine/threonine protein kinase OSK3"
FT /id="PRO_0000438040"
FT DOMAIN 17..269
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 290..330
FT /note="UBA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00212"
FT DOMAIN 459..507
FT /note="KA1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00565"
FT ACT_SITE 140
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 23..31
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 46
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ SEQUENCE 508 AA; 58250 MW; E935262080B39A59 CRC64;
MDGNAKGGGH SEALKNYNLG RTLGIGSFGK VKIAEHKLTG HRVAIKILNR RQMRNMEMEE
KAKREIKILR LFIHPHIIRL YEVIYTPTDI YVVMEYCKFG ELFDYIVEKG RLQEDEARRI
FQQIISGVEY CHRNMVVHRD LKPENLLLDS KYNVKLADFG LSNVMHDGHF LKTSCGSPNY
AAPEVISGKL YAGPEVDVWS CGVILYALLC GTLPFDDENI PNLFKKIKGG IYTLPSHLSA
LARDLIPRML VVDPMKRITI REIREHQWFQ IRLPRYLAVP PPDTAQQAKM IDEDTLQDVV
NLGYGKDHVC ESLRNRLQNE ATVAYYLLLD NRFRATSGYL GADYQESLER NFNRFASSES
ASSNTRHYLP GSSDPHASGL RPHYPVERKW ALGLQSRAQP REIMIEVLKA LQDLNVSWKK
NGQYNMKCRW SVGTQATDML DVNNSFVDDS IIMDNGDVNG RLPAVIKFEI QLYKTRDEKY
LLDMQRVTGP QLLFLDFCAD FLTKLRVL
