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Database: UniProt
Entry: I1PJD0_ORYGL
LinkDB: I1PJD0_ORYGL
Original site: I1PJD0_ORYGL 
ID   I1PJD0_ORYGL            Unreviewed;       804 AA.
AC   I1PJD0;
DT   13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT   13-JUN-2012, sequence version 1.
DT   27-MAR-2024, entry version 57.
DE   RecName: Full=Receptor-like serine/threonine-protein kinase {ECO:0000256|PIRNR:PIRNR000641};
DE            EC=2.7.11.1 {ECO:0000256|PIRNR:PIRNR000641};
OS   Oryza glaberrima (African rice).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Oryzoideae; Oryzeae; Oryzinae; Oryza.
OX   NCBI_TaxID=4538 {ECO:0000313|EnsemblPlants:ORGLA04G0029900.1, ECO:0000313|Proteomes:UP000007306};
RN   [1] {ECO:0000313|Proteomes:UP000007306}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IRGC 96717 {ECO:0000313|Proteomes:UP000007306};
RA   Wing R.A., Yu Y., Rounsley S., Reddy-Marri P., Goicoechea J.L.,
RA   Sisneros N., Lee S., Song X., Angelova A., Kudrna D.P., de Baynast K.,
RA   Zuccolo A.;
RT   "The complete genome of Oryza glaberrima.";
RL   Submitted (JUN-2010) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EnsemblPlants:ORGLA04G0029900.1}
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         ECO:0000256|PIRNR:PIRNR000641};
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         ECO:0000256|PIRNR:PIRNR000641};
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-
CC       pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC       kinase family. {ECO:0000256|PIRNR:PIRNR000641}.
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DR   AlphaFoldDB; I1PJD0; -.
DR   STRING; 4538.I1PJD0; -.
DR   EnsemblPlants; ORGLA04G0029900.1; ORGLA04G0029900.1; ORGLA04G0029900.
DR   Gramene; ORGLA04G0029900.1; ORGLA04G0029900.1; ORGLA04G0029900.
DR   eggNOG; ENOG502QQEW; Eukaryota.
DR   HOGENOM; CLU_000288_116_2_1; -.
DR   OMA; QWNIRAQ; -.
DR   Proteomes; UP000007306; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
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:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   GO; GO:0051707; P:response to other organism; IEA:UniProt.
DR   CDD; cd01098; PAN_AP_plant; 1.
DR   Gene3D; 2.90.10.10; Bulb-type lectin domain; 2.
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; 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; IPR024171; SRK-like_kinase.
DR   PANTHER; PTHR47976; G-TYPE LECTIN S-RECEPTOR-LIKE SERINE/THREONINE-PROTEIN KINASE SD2-5; 1.
DR   PANTHER; PTHR47976:SF117; G-TYPE LECTIN S-RECEPTOR-LIKE SERINE_THREONINE-PROTEIN KINASE LECRK4; 1.
DR   Pfam; PF01453; B_lectin; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   PIRSF; PIRSF000641; SRK; 1.
DR   SMART; SM00108; B_lectin; 1.
DR   SMART; SM00220; S_TKc; 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; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PIRNR:PIRNR000641};
KW   EGF-like domain {ECO:0000256|ARBA:ARBA00022536};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|PIRNR:PIRNR000641};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|PIRNR:PIRNR000641}; Receptor {ECO:0000256|ARBA:ARBA00023170};
KW   Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527,
KW   ECO:0000256|PIRNR:PIRNR000641}; Signal {ECO:0000256|SAM:SignalP};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR000641};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           24..804
FT                   /note="Receptor-like serine/threonine-protein kinase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5003649036"
FT   DOMAIN          17..150
FT                   /note="Bulb-type lectin"
FT                   /evidence="ECO:0000259|PROSITE:PS50927"
FT   DOMAIN          514..790
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   BINDING         545
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   804 AA;  89753 MW;  21A2FA28280FAB1D CRC64;
     MAPPLFLLSL QLLVLLSSPS AQAQNISLGT SLTTQGPNNA WLSPSGDFAF GFRPIDGNSS
     FYLLAIWFNK ISDKTATWYA KTSEQEPQPI QVPSGSILQF TSTGVLSLRD PTNREVWNPG
     ATGAPYASML DTGNFVIAAA GGSTISWETF KNPTDTILVT QALSPGMKLR SRLLTTDYSN
     GRFLLNMETQ RAALYTMAVP SGNLYDPYWS TPIDENVTNQ VTNLVFNTTG RIYMSMKNGT
     QFNMTSGVIR SMEDYYHRAT LDPDGVFRQY VYPKKPSSMS QAWTAVSIQP ENICNAQTKV
     GSGTCGFNSY CMFDGSNNQT SCVCPEQYSF FDEVRKYRGC RPDFELQSCD LDEAASMAQY
     EFNLVNNVDW PQADYEWYTP IDMDECRRLC LIDCFCAVAV FHENTCWKKK LPLSNGIMGS
     GVQRTVLIKV PKSNSSQPEL RKSRKWKSDK KLWILGSSLL LGGSVIANFA LSSVLLFGTY
     CTITRKDVQP LQPSRDPGLP LKAFSYAELE KATDGFKEVL GTGASGIVYK GQLQDELGTY
     IAVKKIDKIQ HETEKEFAVE VQTIGRTYHK NLVRMLGFCN EGTERLLVYE FMVNGSLNRF
     LFSGVRPLWS LRVQLALGVA RGLLYLHEEC STQIIHCDIK PQNILLDDNF IAKISDFGLA
     KLLRTNQTQT YTGIRGTRGY VAPEWFKNVG ITAKVDVYSF GVILLELICC RQNVEMEAAE
     EEQSILTYWA NDCYRCGRVD LLVDGDDEAK LNIKKVERFV AVALWCLQEE PTMRPSILKV
     TQMLDGADAI PTPPDSSSVV NSFP
//
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