ID Q2RAY8_ORYSJ Unreviewed; 1267 AA.
AC Q2RAY8;
DT 24-JAN-2006, integrated into UniProtKB/TrEMBL.
DT 24-JAN-2006, sequence version 1.
DT 27-MAR-2024, entry version 113.
DE RecName: Full=non-specific serine/threonine protein kinase {ECO:0000256|ARBA:ARBA00012513};
DE EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
GN OrderedLocusNames=LOC_Os11g03820 {ECO:0000313|EMBL:ABA91378.1};
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 {ECO:0000313|EMBL:ABA91378.1};
RN [1] {ECO:0000313|EMBL:ABA91378.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16188032; DOI=10.1186/1741-7007-3-20;
RG The rice chromosomes 11 and 12 sequencing consortia;
RT "The sequence of rice chromosomes 11 and 12, rich in disease resistance
RT genes and recent gene duplications.";
RL BMC Biol. 3:20-20(2005).
RN [2] {ECO:0000313|EMBL:ABA91378.1}
RP NUCLEOTIDE SEQUENCE.
RA Buell C.R., Wing R.A., McCombie W.A., Ouyang S.;
RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:ABA91378.1}
RP NUCLEOTIDE SEQUENCE.
RA Buell R.;
RL Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
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}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00076}.
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DR EMBL; DP000010; ABA91378.1; -; Genomic_DNA.
DR AlphaFoldDB; Q2RAY8; -.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
DR GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
DR GO; GO:0003723; F:RNA binding; IEA:InterPro.
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; 1.
DR CDD; cd00054; EGF_CA; 1.
DR CDD; cd01098; PAN_AP_plant; 1.
DR CDD; cd14066; STKc_IRAK; 1.
DR Gene3D; 2.90.10.10; Bulb-type lectin domain; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR001480; Bulb-type_lectin_dom.
DR InterPro; IPR036426; Bulb-type_lectin_dom_sf.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR003609; Pan_app.
DR InterPro; IPR021099; PORR_domain.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR000858; S_locus_glycoprot_dom.
DR PANTHER; PTHR47974:SF31; NON-SPECIFIC SERINE_THREONINE PROTEIN KINASE; 1.
DR PANTHER; PTHR47974; OS07G0415500 PROTEIN; 1.
DR Pfam; PF01453; B_lectin; 1.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF11955; PORR; 2.
DR Pfam; PF00954; S_locus_glycop; 1.
DR SMART; SM00108; B_lectin; 1.
DR SUPFAM; SSF51110; alpha-D-mannose-specific plant lectins; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS50927; BULB_LECTIN; 1.
DR PROSITE; PS50026; EGF_3; 1.
DR PROSITE; PS50948; PAN; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
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|PROSITE-ProRule:PRU00076};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Lectin {ECO:0000313|EMBL:ABA91378.1};
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 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 425..442
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 454..476
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 919..944
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 489..607
FT /note="Bulb-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50927"
FT DOMAIN 741..777
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 791..871
FT /note="Apple"
FT /evidence="ECO:0000259|PROSITE:PS50948"
FT DOMAIN 981..1260
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT BINDING 1010
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 1267 AA; 146067 MW; B28C3575B0126191 CRC64;
MASIAFGQRN LRVFPLRRHI WDAVFQHGPY NCTIQRRWKK PVDSARTRQE GRTRDHKLDK
LMIQLKNLRL ALDLHELISQ QRNGFASLQL LSRWRHEVGL NIEIGAFLKK YPHIFYIYVH
PVKRNECCKV TPKMAELIAE EDAVIRENEP AIVKRLKKLL MLMKDGTLNM HALWLIRREL
GLPDDYRCSI LTNHQSDFSL GSPDTLTLVT RDETGFKIEN GFREKLGNWQ RLPYTKAYDK
NDLHPIHNVG RLEKRIVGIL HELLSLTVEK MIPLERLSHF RRPFGMEVNL RELILKHLGI
FYISTKGSTQ HVLLRESYSK GCLVDPNPVY NVFQREGALH HRLRAVLSLN YEQAAVEYSK
EVRKRWDIIW KRQQMPTERE LYVNNGILMS NSHDCFRFVE VDYEFGLPKT CITLTKLDCS
FQANIIYSRC ILGMFVLAIY SSSDHLSKTA TMDAPFLSTS LAVLATLFLL ALPLSAATHD
ILPLKSSLFV EEYETNILQS SDGTFSCGFY NITNAYNITS AFTFSIWYSN SADKAIVWSA
NRGRPVHSRR SEITLRKDGN IVLTDYDGTV VWQTDGKFPN VRYVQLLNTG NLVLKNSSGN
IVWQSFDSPT DTLLPTQRIL ATTKLVSTTG LQVPSHYTFR FSDQSILSLI YDDTNVSGVY
WPDPDYQYYE NNRNLYNSTR IGSLDDYGEF FSSDLAKHQA RVASDRSLGI KRRLTLDYDG
NLRLYSLNNS DGTWTISWIA QPQTCMTHGL CGPYGICHYS PTPRCSCPPG YKMRNPGNWT
QGCKPIVEIA CDGKQNVTFL QLRNTDFWGS DQQRIEKVPW EVCWNTCISD CTCKGFQYQE
GNGTCYPKSF LFNGRTFPTP FVRTMYIKLP SSLDVSKKPI PQSSIHDYTL SGLDCDHLNT
ITTEAVRNMN KIGGEEPKWF YFYGFIGVFF IVEVFFFAFA WFFVLRKEMR SSQVWIAEEG
YRVMTSHFRM YSHRELVKAT ERFKHELGWG GSGVVYKGIL DDDRAVVIKK LENVTQNREE
FQDELHVISR INHMNLVRIY GFCSERFHRL LVLEYVENGS LANVLFNSKI LLDWKQRFNI
ALGVAKGLAY LHHECLEWVI HCNLKPENIL LDENLEPKIT DFGLAKLLSR SGSNQNVSRA
RGTIGYIAPE WISGLPITAK VDVYSYGVVL LELVSGRRVF DLIVGEDKTK VHEMLKKFIK
MICYRLDNEK SLWLAEFVDF RVGDEFNYLQ AKTLVKLAVS CLEEDRKKRP TMESIVESLL
SVDLARS
//
