ID A0A1S3VPK8_VIGRR Unreviewed; 784 AA.
AC A0A1S3VPK8;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 31.
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=LOC106777264 {ECO:0000313|RefSeq:XP_014520316.1};
OS Vigna radiata var. radiata (Mung bean) (Phaseolus aureus).
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; Vigna.
OX NCBI_TaxID=3916 {ECO:0000313|Proteomes:UP000087766, ECO:0000313|RefSeq:XP_014520316.1};
RN [1] {ECO:0000313|RefSeq:XP_014520316.1}
RP IDENTIFICATION.
RC TISSUE=Leaf {ECO:0000313|RefSeq:XP_014520316.1};
RG RefSeq;
RL Submitted (NOV-2023) 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 -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000256|PIRNR:PIRNR000641}.
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DR RefSeq; XP_014520316.1; XM_014664830.2.
DR AlphaFoldDB; A0A1S3VPK8; -.
DR GeneID; 106777264; -.
DR KEGG; vra:106777264; -.
DR OrthoDB; 339619at2759; -.
DR Proteomes; UP000087766; Chromosome 11.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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; cd00053; EGF; 1.
DR Gene3D; 2.90.10.30; -; 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; 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; PTHR47976; G-TYPE LECTIN S-RECEPTOR-LIKE SERINE/THREONINE-PROTEIN KINASE SD2-5; 1.
DR PANTHER; PTHR47976:SF62; LECTIN KINASE FAMILY PROTEIN; 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; 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 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:UP000087766};
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..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..784
FT /note="Receptor-like serine/threonine-protein kinase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5010363516"
FT TRANSMEM 435..458
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 28..142
FT /note="Bulb-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50927"
FT DOMAIN 497..784
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT BINDING 528
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 784 AA; 87585 MW; EDF115D6067FA002 CRC64;
MAAQFLGLSV AMLLFFNVPS IAISIELGSG IVAGSATSSS WRSSSGEYAF GFYHLVSGRY
LVGIWFDKIL EKTLVWSANR DNPVEIGSFI NLTRSGQFVI QPLNGASFSI YEGTNTASAE
MKDDGNFVLK NSFSSVIWQS FDSPTDTLLL GQTLNTSRKL YSNANGSVDY STGQYSLEIQ
QSDGNIVLKA YRFTDSAYWW SDTAQNTGVR IIFDNTTAFL YAVNATNQII FNMTTEVVGP
IEDYYHRVLV DDKGNFQKLI YHKENGSEWR SVWQAVTKPC TVTALCGVYG FCNTSGSDTQ
TYSCGCLPGY TPLDPTAPSK GCYLSEVKDL CAANSSASNF EVEVKEIQDA DIPNSGYFFL
DLKVLDRMDL ESCKKELMHD CLCMVAVLDG SACHKKKWPI INAIRIIPDT SNRVMLIKVP
LLDNNKDNER DSSSVVVLVV ALISCSLLAV LFAATAIYHH PVCQHLMHKQ APPKPKTKPM
DINLRVFSFQ QLREATNGFK DKLGRGAYGT VFGGVLNLED QQVDVAVKQL EEVDDRGDKE
FVTEVQVIAL TYHRNLVGLV GFCNEQSHRL LVYEKMENGT LSNFLFGGDR PSWESRVRIV
LEIARGLLYL HEECDQQIIH CDIKPQNVLL DSSYTAKISD FGLAKLLMKD KTRTNTNARG
TMGYMAPEWL KNAPVTTKVD IYSFGVVLLE IIFCRRHIEL HEIENGTMGD DMILVDWVLY
LVMERNLRAA VIDDVEVESD FSRFERMAMV GLWCINPNPN LRPSMKIVVQ MLEGNVEVGV
PPLH
//
