ID A0A251VLZ7_HELAN Unreviewed; 855 AA.
AC A0A251VLZ7;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=Receptor-like serine/threonine-protein kinase {ECO:0000256|PIRNR:PIRNR000641};
DE EC=2.7.11.1 {ECO:0000256|PIRNR:PIRNR000641};
GN Name=B120 {ECO:0000313|EMBL:OTG36086.1};
GN ORFNames=HannXRQ_Chr01g0003751 {ECO:0000313|EMBL:OTG36086.1};
OS Helianthus annuus (Common sunflower).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; campanulids; Asterales; Asteraceae; Asteroideae;
OC Heliantheae alliance; Heliantheae; Helianthus.
OX NCBI_TaxID=4232 {ECO:0000313|EMBL:OTG36086.1, ECO:0000313|Proteomes:UP000215914};
RN [1] {ECO:0000313|Proteomes:UP000215914}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. SF193 {ECO:0000313|Proteomes:UP000215914};
RX PubMed=28538728; DOI=10.1038/nature22380;
RA Badouin H., Gouzy J., Grassa C.J., Murat F., Staton S.E., Cottret L.,
RA Lelandais-Briere C., Owens G.L., Carrere S., Mayjonade B., Legrand L.,
RA Gill N., Kane N.C., Bowers J.E., Hubner S., Bellec A., Berard A.,
RA Berges H., Blanchet N., Boniface M.C., Brunel D., Catrice O., Chaidir N.,
RA Claudel C., Donnadieu C., Faraut T., Fievet G., Helmstetter N., King M.,
RA Knapp S.J., Lai Z., Le Paslier M.C., Lippi Y., Lorenzon L., Mandel J.R.,
RA Marage G., Marchand G., Marquand E., Bret-Mestries E., Morien E.,
RA Nambeesan S., Nguyen T., Pegot-Espagnet P., Pouilly N., Raftis F.,
RA Sallet E., Schiex T., Thomas J., Vandecasteele C., Vares D., Vear F.,
RA Vautrin S., Crespi M., Mangin B., Burke J.M., Salse J., Munos S.,
RA Vincourt P., Rieseberg L.H., Langlade N.B.;
RT "The sunflower genome provides insights into oil metabolism, flowering and
RT Asterid evolution.";
RL Nature 546:148-152(2017).
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 -!- 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 EMBL; CM007890; OTG36086.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A251VLZ7; -.
DR EnsemblPlants; mRNA:HanXRQr2_Chr01g0006151; mRNA:HanXRQr2_Chr01g0006151; HanXRQr2_Chr01g0006151.
DR Gramene; mRNA:HanXRQr2_Chr01g0006151; mRNA:HanXRQr2_Chr01g0006151; HanXRQr2_Chr01g0006151.
DR InParanoid; A0A251VLZ7; -.
DR OMA; WRKRWEI; -.
DR OrthoDB; 2101463at2759; -.
DR Proteomes; UP000215914; Chromosome 1.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0030246; F:carbohydrate 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; IBA:GO_Central.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0048544; P:recognition of pollen; IEA:InterPro.
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; 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:SF248; RECEPTOR-LIKE SERINE_THREONINE-PROTEIN KINASE; 1.
DR Pfam; PF01453; B_lectin; 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|PROSITE-ProRule:PRU00076};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Kinase {ECO:0000256|PIRNR:PIRNR000641, ECO:0000313|EMBL:OTG36086.1};
KW Lectin {ECO:0000313|EMBL:OTG36086.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|PIRNR:PIRNR000641};
KW Reference proteome {ECO:0000313|Proteomes:UP000215914};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527,
KW ECO:0000256|PIRNR:PIRNR000641};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR000641}.
FT SIGNAL 1..27
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 28..855
FT /note="Receptor-like serine/threonine-protein kinase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5012513133"
FT DOMAIN 31..156
FT /note="Bulb-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50927"
FT DOMAIN 299..338
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 358..436
FT /note="Apple"
FT /evidence="ECO:0000259|PROSITE:PS50948"
FT DOMAIN 538..815
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
SQ SEQUENCE 855 AA; 95326 MW; 4B575C75A92A6D02 CRC64;
MGFITKTLTN LHIITIILLL HSSRVFPQST TSRLDQDQVL RDGEILVSPQ QIFELGFFSP
RNSSSRYVGI WYYGMQNRTV VWVANRDNPI PDNSGVFGIR NRSLIVSDGN SQVYWSSDSS
AARNDLNLSN LTMMLVDSGN LILSTVENAG REEDAIWRSC DHPTDTFLPN LRVYLNITEG
ISQQFVSWRT ANDPAKGNYS MGVDPRGSPQ VVVWDDRSNR RLWRSGHWNN QIFIGVPRMR
SLLLFGFRLV NVDDGLVYFT FENPNSGPLM RFLIQWNGAV QQMIYNQTIS RWTPMVSLPS
NGCEEYNKCG NFGICRPSTA PSQLCSCMRG FDPNPRFQDQ RNSGNWSGGC VRRTGLECSA
NGSTSDGFVE RMGVKLPDFA DRIAGDRGEC ENGCLQNCSC MGYAFVEGIG CLIWGDELID
VEEFEQGGET LFIRVADSDL VSGSNGGVSK TTVIAVSVTG AVVIGVLALL LWKYRNKVKA
CQIPCGGKKN GPLVSEVFNG QDISVEASEQ LEREMKECDG PPLPVFSSHA LEVATDGYAN
KNKLGQGGFG PVHKGILPGG QEIAVKRLAK SSGQGLEEFK NEMILIAKLQ HRNLVRLLGY
CIEGEERMLV YEYMPNKSLD SFLFDSVKKV ELDWKTRFKI IEGIARGLLY LHRDSRLRII
HRDLKVSNIL LDEEMNPKIS DFGMARIFGG NQNEANTNRV VGTYGYMSPE YAMEGLFSVK
SDVYSFGVLL LEIISGHRNN SFRSEDSTNL IRHAWKLWKE GKPEELIDPL ILDSCNRTEA
LQCIHVAMLC VQSSAVQRPT MSSVVFMLEG ENTSLPQPNE LDLTSLSSAE MDLIMEGREI
NVSSNDVTIT EVSGR
//
