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Database: UniProt
Entry: J3NDE8_ORYBR
LinkDB: J3NDE8_ORYBR
Original site: J3NDE8_ORYBR 
ID   J3NDE8_ORYBR            Unreviewed;       833 AA.
AC   J3NDE8;
DT   03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT   03-OCT-2012, sequence version 1.
DT   24-JAN-2024, entry version 42.
DE   RecName: Full=non-specific serine/threonine protein kinase {ECO:0000256|ARBA:ARBA00012513};
DE            EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
OS   Oryza brachyantha (malo sina).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Oryzoideae; Oryzeae; Oryzinae; Oryza.
OX   NCBI_TaxID=4533 {ECO:0000313|EnsemblPlants:OB12G20060.1};
RN   [1] {ECO:0000313|EnsemblPlants:OB12G20060.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IRGC 101232 {ECO:0000313|EnsemblPlants:OB12G20060.1};
RX   PubMed=23481403;
RA   Chen J., Huang Q., Gao D., Wang J., Lang Y., Liu T., Li B., Bai Z.,
RA   Luis Goicoechea J., Liang C., Chen C., Zhang W., Sun S., Liao Y., Zhang X.,
RA   Yang L., Song C., Wang M., Shi J., Liu G., Liu J., Zhou H., Zhou W., Yu Q.,
RA   An N., Chen Y., Cai Q., Wang B., Liu B., Min J., Huang Y., Wu H., Li Z.,
RA   Zhang Y., Yin Y., Song W., Jiang J., Jackson S.A., Wing R.A., Wang J.,
RA   Chen M.;
RT   "Whole-genome sequencing of Oryza brachyantha reveals mechanisms underlying
RT   Oryza genome evolution.";
RL   Nat. Commun. 4:1595-1595(2013).
RN   [2] {ECO:0000313|EnsemblPlants:OB12G20060.1}
RP   IDENTIFICATION.
RG   EnsemblPlants;
RL   Submitted (APR-2013) to UniProtKB.
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:0000256|ARBA:ARBA00001433};
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:0000256|ARBA:ARBA00000775};
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr
CC       protein kinase family. {ECO:0000256|ARBA:ARBA00009903}.
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DR   AlphaFoldDB; J3NDE8; -.
DR   EnsemblPlants; OB12G20060.1; OB12G20060.1; OB12G20060.
DR   Gramene; OB12G20060.1; OB12G20060.1; OB12G20060.
DR   eggNOG; KOG0610; Eukaryota.
DR   HOGENOM; CLU_000288_39_3_1; -.
DR   OMA; CNVVTLA; -.
DR   Proteomes; UP000006038; Chromosome 12.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
DR   CDD; cd05574; STKc_phototropin_like; 1.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 2.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   PANTHER; PTHR45637; FLIPPASE KINASE 1-RELATED; 1.
DR   PANTHER; PTHR45637:SF86; SERINE/THREONINE-PROTEIN KINASE KIPK; 1.
DR   Pfam; PF00069; Pkinase; 2.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000006038}.
FT   DOMAIN          410..739
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   REGION          69..101
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          226..260
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          311..340
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        83..101
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        311..327
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   833 AA;  91827 MW;  FA8B63E75068ACD0 CRC64;
     MGSSGCSSEI VEFTEEFDDT APVSCSNLLH IKVKAEEKDG GCRDYPVEDD LEQLLKVIDS
     RTFRRTLSPG QAGADALRKN GQKKSARSGT PQTAGIRISS KQVNMKQALR RLCISQASEM
     AAMKRLSMSP GSSSSSEAGT IHRLYASLMV QSNDESHLHD DEKMNLIEIS ITPEKFSKNS
     SRATSEYSEE CDFETADGSA VTSLHSASST SAEIRKIRIQ DVISGDPIDS ESSMVENEKL
     DKKVSTATDG SSPRAPILSK PITTSRLVKP VFRCKTISKK KVKEEPPSLG TSSNSTKFCS
     SKESISLAST SCSSTSSITN PTSCVDEEKT NLGPEESGEK SLEWLGAEEK GECSQNSNSI
     SEYGCSTSIS DESQFGLCSY NNRPHMAKDL RWITIRELAL QQGSLGLDNF KLLKRLGCGD
     IGTVYLAELV DSDCLFALKV MDIEYLINRK KMLRAQAERE ILEMLDHPFL PTLYAHFTTD
     NLSCLVMEYC PGGDLHVLRQ RQPGRNFPEP AARFYVAEVL LALEYLHMLG VIYRDLKPEN
     ILVREDGHIM LSDFDLSLRC SVNPVLLRSS SVAANHQPRK LAGPCAESSC ISSSCQPSCA
     QTSCFMARPP LPKPRKPKSS HRKLPQLVVE PIDARSNSFV GTHEYLAPEI IKGDGHGSAV
     DWWTFGVFLY ELLYGKTPFR GPGNDETLAN VVSQNLKFPE NPSISSNAKD LIKGLLVKEP
     ENRLGSLRGA AEIKQHPFFE GLNWALIRSA APPETRPCDV VTLATAKKKK EGKCLEFRSN
     SEDLEFEVFY YKQFSCVYAN DNVSPATVNP GKQPDNGVLS FYRSLRNSTP RQI
//
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