ID A0A0E0R5M4_ORYRU Unreviewed; 2734 AA.
AC A0A0E0R5M4;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 27-MAR-2024, entry version 41.
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 rufipogon (Brownbeard rice) (Asian wild rice).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza.
OX NCBI_TaxID=4529 {ECO:0000313|EnsemblPlants:ORUFI11G06440.4, ECO:0000313|Proteomes:UP000008022};
RN [1] {ECO:0000313|Proteomes:UP000008022}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=cv. W1943 {ECO:0000313|Proteomes:UP000008022};
RA Zhao Q.;
RL Submitted (JUN-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblPlants:ORUFI11G06440.4}
RP IDENTIFICATION.
RG EnsemblPlants;
RL Submitted (JUN-2015) 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 -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-
CC pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.
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DR EnsemblPlants; ORUFI11G06440.4; ORUFI11G06440.4; ORUFI11G06440.
DR Gramene; ORUFI11G06440.4; ORUFI11G06440.4; ORUFI11G06440.
DR Proteomes; UP000008022; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0048544; P:recognition of pollen; IEA:InterPro.
DR GO; GO:0051707; P:response to other organism; IEA:UniProt.
DR CDD; cd00028; B_lectin; 3.
DR CDD; cd01098; PAN_AP_plant; 3.
DR CDD; cd14066; STKc_IRAK; 2.
DR Gene3D; 2.90.10.10; Bulb-type lectin domain; 3.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 3.
DR InterPro; IPR001480; Bulb-type_lectin_dom.
DR InterPro; IPR036426; Bulb-type_lectin_dom_sf.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR003609; Pan_app.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR000858; S_locus_glycoprot_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR PANTHER; PTHR47974; OS07G0415500 PROTEIN; 1.
DR PANTHER; PTHR47974:SF19; RECEPTOR-LIKE SERINE_THREONINE-PROTEIN KINASE; 1.
DR Pfam; PF01453; B_lectin; 3.
DR Pfam; PF08276; PAN_2; 3.
DR Pfam; PF00069; Pkinase; 3.
DR Pfam; PF00954; S_locus_glycop; 3.
DR SMART; SM00108; B_lectin; 3.
DR SMART; SM00473; PAN_AP; 3.
DR SMART; SM00220; S_TKc; 3.
DR SUPFAM; SSF51110; alpha-D-mannose-specific plant lectins; 3.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 3.
DR PROSITE; PS50927; BULB_LECTIN; 3.
DR PROSITE; PS50948; PAN; 3.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 2.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 3.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 3.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW EGF-like domain {ECO:0000256|ARBA:ARBA00022536};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Receptor {ECO:0000256|ARBA:ARBA00023170};
KW Reference proteome {ECO:0000313|Proteomes:UP000008022};
KW Signal {ECO:0000256|ARBA:ARBA00022729};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 448..468
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 684..708
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1433..1457
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2211..2235
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 245..390
FT /note="Bulb-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50927"
FT DOMAIN 586..669
FT /note="Apple"
FT /evidence="ECO:0000259|PROSITE:PS50948"
FT DOMAIN 741..1015
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 1036..1181
FT /note="Bulb-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50927"
FT DOMAIN 1335..1418
FT /note="Apple"
FT /evidence="ECO:0000259|PROSITE:PS50948"
FT DOMAIN 1437..1729
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 1765..1909
FT /note="Bulb-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50927"
FT DOMAIN 2113..2196
FT /note="Apple"
FT /evidence="ECO:0000259|PROSITE:PS50948"
FT DOMAIN 2268..2542
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 2559..2591
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 769
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
FT BINDING 2296
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 2734 AA; 305020 MW; 83623DDF03ED493C CRC64;
MWWTEKLAGV SRDVVHDGGS DPYQCVMLWV MYAVMCRVQV LKIHNLDQID IEVYKGMPLV
SPHLTKIELS GIELKNCFLN FSSCPALKEL YFTKNCGFDS VYEILSRYEV SDDSESVLLG
GLTEAENLKL IAGPNIEYKS MVELETEEND NPLWKPAAIS EHLKVVKVHC KEVDEGVYKI
GKWLSTLDKK SQQHLLLTHP CCCLSNPSSA TFSNISMSPL HTHLGFFLLL LLFSLHNPSC
SAAANDTLAA GQVLAVGEKL VSRNGKFALG FYKPALPEGI ASKYGNITSP GWYLAIWFNK
IPVCTTVWVA NRERPITDLE IKLTQLKFSQ NGSSLAIIIN RATEYTVWSR QIANRTAQAK
TSMNTSAILL DSGNLVIESI PDVYLWQSFD EPTDLALPGA KFGWNKVTRL HRTGISKKNL
IDPGLGPYSV QLNERGIILW RRDPYMEYWT WSSVQLTNML IPLLNSLLEM NAQTKGFLTP
NYTNNNEEEY FMYHSSDESS SSFVSIDMSG QLKLSIWSQA NQSWQEVYAQ PPDPCTPFAT
CGPFSVCNGN SDLFCDCMES FSQKSPQDWE LKDRTAGCFR NTPLDCPSNK SSTDMFHTIT
RVALPANPKK IEDATTQSKC AESCLSNCSC NAYAYKDSTC FVWHSELLNV KLHDSIESLS
EDTLYLRLAA KDMPATTKNK QKPVVVAVTA ASIAGFGLLM LMLFFLIWRN KFKCCGVTLH
HNQGNSGIIA FRYTDLSHAT KNFSEKLGSG GFGSVFKGVL RDSTTIAVKR LDGSHQGEKQ
FRAEVSSLGL IQHINLVKLI GFCCEGDKRL LVYEHMVNGS LDAHLFHSNG AVLDWNTRHQ
IAIGVARGLS YLHESCRECI IHCDIKPENI LLEASFAPKI ADFGMAAFVG RDFSRVLTTF
RGTKGYLAPE WLSGVAITPK VDVYSFGMVL LEIISGRRNL SEAYTSNHYH FDYFPVQAIS
KLHEGSVQNL LDPELHGDFN LEEAERVCKV ACWCIQEDEI DRPTMGEVVR FLEGLQEVDM
PPMPRLLAAI TESLLFEQIE SSNLLAVGEK LISRNGKFAL GFFKPTLPED AGSKYKNIAS
PGWYLAIWFN EIPVCTTVWV ANRERPIADH ELKLAQLKFS QDGSSLAIII NRATESTAWS
TQIANRTAQA KTSMNTSEIL LDSGNLVIES LPDVYLWQSF DDATNLVLPG AKLGWNKVTG
LHCTSISKKN LIDPGLSSYS VQLNERGIVL WRRDPYMKYL TWSSTLMSGQ LKLSIWSQAN
QYWQEVYAHP TYPCASFATC GPFSFCIATC GPFGVCDGNR KPFCDCMEGF SPKSPQDWEL
MDRTAGCFRN TPLDCSSNRS STDMFLAIGR GVLPTNHKRV EDATTQSKCE EACLSNCSCI
AYAYEDSTCY AWHGELLNLR LQDSIESLSE DTLYLRLAAK DMPASTKNKR KPFPAAVTIA
SIIGFGLLML LLLFLIWQNK LKCRGVPLHH TQGSSGIGVL SDSTTIVVKR LDGLHQGEKQ
FRAEMRSLRL IQHINLVKLI GFCYEDDKRL LVYEHMINGP LDAHLFHSNG AIIDWSTRHQ
IAIGVARGLS YLHESCHECI IHCDIKPENI LVEASFAPKI ADFGMAAFVG RDFSRVLTTF
RGTKGYLAPE WLSGVAITPK VDVYSFGMKS YNEGGIYPKH TPATIIILII FLCKPSANFM
REVCRICLIQ NYMVISIWKR LKGFVKLLVG ASKKMKLIGQ QWVKWFAFLR VYRSRYFNIF
MPPLYRYLGL LLAISLHTPS CSTANDTLAA GQVLVVSEKL ISRNGKFALG FFKPALPEGT
ANTYGNVTSP GWYLAIWFNN IPVCTTVWVA NRERPITEPE LKLVQMKISE DGSSLVIINH
AIKSIVWSTQ ITNGTAQAKT GVNTSAILLD SGNLVIESLP DVYLWQSFDY PTDLVLPGAK
IGWNKVTGLC RTCTSKKNLI DPGLGSYSVQ LNSRGIILWH RDPYIEYWTW SSIQMTYTLM
PLLNSLLTMN SEARGFLTPT YVNNDEEEYL MYHSSDESSS SFVSIDMSGQ VKLNIWSQAN
QSWAEVHAEP WAQVYAQPPD PCTPFATCGP FGICNGNSEQ FCDCMESFSQ KSPQDWKLKD
RSASCIRNTP LDCPSNRSST DMFQTIARVT LPANPEKLED ATTQSKCAEV CLSNCSCNAY
AYKDSVCSVW HSELLNVKLR DNIESLSEDT LYLRLAAKDM PASTKNKRKP VIAVVTTASI
VGFGLLMLVM FFLIWRIKFN CCGVPLHHNQ GNSGIIAFKY TDLSHATKNF SQKLGSGGFG
SVFKGVLSDS TTIAVKRLDG LHQGEKQFRA EVSSLGLIHH INLVKLIGFC YEGDKRLLVY
ERMINGSLDA HLFHSNGTIL DWSTRHQIAI GVARGLFYLH ESCHKCIIHC DIKPENILLE
ASFAPKIADF GMAAFVGRDF SRVLTSFRGT KGYLAPEWLS GVAITPKVDV YSFGMVLLEI
ISGRRNLSEA YTSKHYHFDY FPMQAMSKLH GGSVQDLLDP KLNGDFNLEE AERICKVACW
CIQENEFDRP TMGEVVHILE GLQEVEMPPT PRLFADISEK VSYAPPTPTP PAKQRRRRPD
PRPSYCTAPA SLSPRAAARA SARLLDCTST WSVVSRLFAS RAHSVPFARH LFDGMPPKRK
GLTSKKMAEA REEGGIDVLP DALLQHILSF LSADEAVKTS ASYPAAGATP PLEIHAHPAY
CQNGGQMGLG ELRGFQQVCQ HPTTLPWKRA SKHV
//
