ID A0A0E0L4C9_ORYPU Unreviewed; 898 AA.
AC A0A0E0L4C9;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 27-MAR-2024, entry version 48.
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 punctata (Red rice).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza.
OX NCBI_TaxID=4537 {ECO:0000313|EnsemblPlants:OPUNC05G19470.1};
RN [1] {ECO:0000313|EnsemblPlants:OPUNC05G19470.1}
RP NUCLEOTIDE SEQUENCE.
RA Wing R.;
RT "Oryza genome evolution.";
RL Submitted (AUG-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblPlants:OPUNC05G19470.1}
RP IDENTIFICATION.
RG EnsemblPlants;
RL Submitted (APR-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}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00076}.
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DR AlphaFoldDB; A0A0E0L4C9; -.
DR STRING; 4537.A0A0E0L4C9; -.
DR EnsemblPlants; OPUNC05G19470.1; OPUNC05G19470.1; OPUNC05G19470.
DR Gramene; OPUNC05G19470.1; OPUNC05G19470.1; OPUNC05G19470.
DR eggNOG; ENOG502QQQ3; Eukaryota.
DR HOGENOM; CLU_000288_116_5_1; -.
DR OMA; SSTWRAG; -.
DR Proteomes; UP000026962; Chromosome 5.
DR GO; GO:0016020; C:membrane; 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: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; 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; IPR000719; Prot_kinase_dom.
DR InterPro; IPR021820; S-locus_recpt_kinase_C.
DR InterPro; IPR000858; S_locus_glycoprot_dom.
DR InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR InterPro; IPR024171; SRK-like_kinase.
DR PANTHER; PTHR32444; BULB-TYPE LECTIN DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR32444:SF118; INACTIVE G-TYPE LECTIN S-RECEPTOR-LIKE SERINE_THREONINE-PROTEIN KINASE SRK-RELATED; 1.
DR Pfam; PF01453; B_lectin; 1.
DR Pfam; PF11883; DUF3403; 1.
DR Pfam; PF08276; PAN_2; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR Pfam; PF00954; S_locus_glycop; 1.
DR PIRSF; PIRSF000641; SRK; 1.
DR SMART; SM00108; B_lectin; 1.
DR SMART; SM00473; PAN_AP; 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; PS50026; EGF_3; 1.
DR PROSITE; PS50948; PAN; 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 Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW EGF-like domain {ECO:0000256|ARBA:ARBA00022536, ECO:0000256|PROSITE-
KW ProRule:PRU00076}; Kinase {ECO:0000256|PIRNR:PIRNR000641};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|PIRNR:PIRNR000641}; Receptor {ECO:0000256|ARBA:ARBA00023170};
KW Reference proteome {ECO:0000313|Proteomes:UP000026962};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527,
KW ECO:0000256|PIRNR:PIRNR000641}; Signal {ECO:0000256|ARBA:ARBA00022729};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR000641};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 505..528
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 82..209
FT /note="Bulb-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50927"
FT DOMAIN 350..386
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 405..489
FT /note="Apple"
FT /evidence="ECO:0000259|PROSITE:PS50948"
FT DOMAIN 580..867
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 37..59
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 44..58
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 898 AA; 97482 MW; 618FDD377756B188 CRC64;
MLPTRTSWAE QAVTRNAAQL PLDKTTPHRI NGNILVPPGK AHSERVTPSR RAHHDEPTMA
SHQLSSVLLL MLLAPATSRA RDSIAPGEPL LAGNEKLVSA GAGGFALGFF TPPGSNDTYV
GVWYARVSPR TVVWVANRAD PVPGPVEGNA GATLSVSRGC ELAVADANST VVWSVSPAAA
TGPCTARIRD DGNLVVTDAR GLVAWQGFDH PTDTLLPGMR IGVDFAAGKN MTLTAWKSPS
DPSPSQVVVA MDTSGDPEVF VWNGPNKVWR SGPWDGVQFT GVPDTVTYKI FSFSFVNSAR
EVTYSFQVPN ASIMSRLVLN SSGAAAGVGL LQRWTWVEAA GAWNLYWYAP KDQCDAVSPC
GANGVCDTNS LPVCSCLRGF APRSPAAWAL RDGRDGCARE TPLDCANGTD GFAVVRHAKA
PDTTAATVDY DSGLQLCRRR CLGNCSCTAY ANANLSAPPG RRGCVMWSGG LEDIRVYPAF
GQDLYVRLAA ADLDSTSKSK KKTHIIIAVV VSICALAIIL TLTGMYIWRT KKTKARRRGP
SNWSGGLHSR DLYSEGNSHG DDLDLPLFDL ETIASATDGF SADNKLGEGG FGPVYKGTLE
DGQEIAVKTL SKTSVQGLDE FRNEVMLIAK LQHRNLVQLI GYNVCGQEKM LIYEFMENKS
LDCFLFDKSK SKLLDWQIRY HIIEGIARGL LYLHQDSRYR IIHRDLKTSN ILLDKEMTPK
ISDFGMARMF GSDDTEINTV RVVGTYGYMA PEYAMDGVFS VKSDVFSFGV IVLEIISGKR
NRGVYSYSSH LNLLAHAWSS WNEGNSLDLV DETLNGSFNS EEVLKCLKVG LLCVQENPDD
RPLMSQVLLM LARADAASLP DPRQPGFVAR RAATEDTSSS RPDCSFVDSM TITMIKGR
//
