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Database: UniProt
Entry: V7C4R4_PHAVU
LinkDB: V7C4R4_PHAVU
Original site: V7C4R4_PHAVU 
ID   V7C4R4_PHAVU            Unreviewed;       838 AA.
AC   V7C4R4;
DT   19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT   19-FEB-2014, 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};
GN   ORFNames=PHAVU_004G085800g {ECO:0000313|EMBL:ESW23901.1};
OS   Phaseolus vulgaris (Kidney bean) (French bean).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC   NPAAA clade; indigoferoid/millettioid clade; Phaseoleae; Phaseolus.
OX   NCBI_TaxID=3885 {ECO:0000313|EMBL:ESW23901.1, ECO:0000313|Proteomes:UP000000226};
RN   [1] {ECO:0000313|Proteomes:UP000000226}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. G19833 {ECO:0000313|Proteomes:UP000000226};
RX   PubMed=24908249; DOI=10.1038/ng.3008;
RA   Schmutz J., McClean P.E., Mamidi S., Wu G.A., Cannon S.B., Grimwood J.,
RA   Jenkins J., Shu S., Song Q., Chavarro C., Torres-Torres M., Geffroy V.,
RA   Moghaddam S.M., Gao D., Abernathy B., Barry K., Blair M., Brick M.A.,
RA   Chovatia M., Gepts P., Goodstein D.M., Gonzales M., Hellsten U.,
RA   Hyten D.L., Jia G., Kelly J.D., Kudrna D., Lee R., Richard M.M.,
RA   Miklas P.N., Osorno J.M., Rodrigues J., Thareau V., Urrea C.A., Wang M.,
RA   Yu Y., Zhang M., Wing R.A., Cregan P.B., Rokhsar D.S., Jackson S.A.;
RT   "A reference genome for common bean and genome-wide analysis of dual
RT   domestications.";
RL   Nat. Genet. 46:707-713(2014).
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|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|PIRNR:PIRNR000641};
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004251};
CC       Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004251}.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC       kinase family. {ECO:0000256|PIRNR:PIRNR000641}.
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DR   EMBL; CM002291; ESW23901.1; -; Genomic_DNA.
DR   RefSeq; XP_007151907.1; XM_007151845.1.
DR   AlphaFoldDB; V7C4R4; -.
DR   STRING; 3885.V7C4R4; -.
DR   EnsemblPlants; ESW23901; ESW23901; PHAVU_004G085800g.
DR   GeneID; 18632440; -.
DR   Gramene; ESW23901; ESW23901; PHAVU_004G085800g.
DR   KEGG; pvu:PHAVU_004G085800g; -.
DR   eggNOG; ENOG502QRWA; Eukaryota.
DR   OMA; QEPYMTM; -.
DR   OrthoDB; 364069at2759; -.
DR   PhylomeDB; V7C4R4; -.
DR   Proteomes; UP000000226; Chromosome 4.
DR   GO; GO:0005886; C:plasma 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:0048544; P:recognition of pollen; IEA:InterPro.
DR   CDD; cd00028; B_lectin; 1.
DR   CDD; cd14066; STKc_IRAK; 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; IPR000858; S_locus_glycoprot_dom.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   InterPro; IPR024171; SRK-like_kinase.
DR   PANTHER; PTHR47974; OS07G0415500 PROTEIN; 1.
DR   PANTHER; PTHR47974:SF9; RECEPTOR-LIKE SERINE_THREONINE-PROTEIN KINASE; 1.
DR   Pfam; PF01453; B_lectin; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   Pfam; PF00954; S_locus_glycop; 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; 2.
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   Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW   Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|PIRNR:PIRNR000641};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|PIRNR:PIRNR000641};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000226};
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};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           22..838
FT                   /note="Receptor-like serine/threonine-protein kinase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5004754977"
FT   TRANSMEM        424..448
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          19..141
FT                   /note="Bulb-type lectin"
FT                   /evidence="ECO:0000259|PROSITE:PS50927"
FT   DOMAIN          143..261
FT                   /note="Bulb-type lectin"
FT                   /evidence="ECO:0000259|PROSITE:PS50927"
FT   DOMAIN          486..763
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   REGION          797..838
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         514
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   838 AA;  90765 MW;  15436181F0808451 CRC64;
     MFLKIQFLFL TLFLAATVAT AIDPGSTLSA SSTSNQTWSS PSGTFSLRFI SVQPPTTPPS
     FIAAIVYTGG NPVVWSAGNG TAVDSGGSLR FLSSGSLRLV NGSGATVWDS GTAGATSAAL
     EESGKLVISN GTSPLWSSFD NPTDTLVPSQ NFSVGKVLTS ESYVFSLNGI GNLSLKWNSS
     IVYWTQGLNS SVNVSLESPV LTLTSIGLLE LSDVKLSSPV LVAYSSDYDL NADVFRVLKL
     DNDGNLRIYS TNKGGGTSTV RWAAVADQCK VYAYCGNYGV CSYNDSSTVC GCPSENFEMV
     DPNDGRKGCK RKASLDSCQG SATMLTLDHA VVLSYLPEAS SETFFIGLSA CRTNCLSGST
     ACFASTSLSD GTGQCVIRSV DFVSGYQDPS LPGTSYFKVC PPLAPNPPSS SAETVRERGS
     KVPAWVVVVV VLGTLLGLVA LEGGLWMWCC RNNKRFGGLS AQYALLEYAS GAPVQFSYKE
     LQQATKGFKE KLGAGGFGAV YRGTLVNKTV VAVKQLEGIE QGEKQFRMEV ATISSTHHLN
     LVRLIGFCSE GRHRLLVYEF MKNGSLDNFL FLTEQHSGKL LNWDYRYNIA LGTARGITYL
     HEECRDCIVH CDIKPENILL DENYVSKVSD FGLAKLINPK DHRHRTLTSV RGTRGYLAPE
     WLANLPITSK SDVYSYGMVL LEIVSGRRNF DVSEETNRKK FSIWAYEEFE KGNISEILDK
     RLARQEVDME QVRRAIQASF WCIQEQPSQR PTMSRVLQML EGVTQFEKPP APKSVVMEGT
     VSGTSTYLSS NASAFSTVGV SPPGPSSTSS FQISNNVSTF NSERNPEKPT STLLQSDT
//
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