GenomeNet

Database: UniProt
Entry: A0A1S3VED7_VIGRR
LinkDB: A0A1S3VED7_VIGRR
Original site: A0A1S3VED7_VIGRR 
ID   A0A1S3VED7_VIGRR        Unreviewed;       836 AA.
AC   A0A1S3VED7;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   27-MAR-2024, entry version 33.
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=LOC106774288 {ECO:0000313|RefSeq:XP_014516721.1};
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_014516721.1};
RN   [1] {ECO:0000313|RefSeq:XP_014516721.1}
RP   IDENTIFICATION.
RC   TISSUE=Leaf {ECO:0000313|RefSeq:XP_014516721.1};
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|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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   RefSeq; XP_014516721.1; XM_014661235.2.
DR   AlphaFoldDB; A0A1S3VED7; -.
DR   STRING; 3916.A0A1S3VED7; -.
DR   EnsemblPlants; Vradi01g10270.1; Vradi01g10270.1; Vradi01g10270.
DR   GeneID; 106774288; -.
DR   Gramene; Vradi01g10270.1; Vradi01g10270.1; Vradi01g10270.
DR   KEGG; vra:106774288; -.
DR   OrthoDB; 364069at2759; -.
DR   Proteomes; UP000087766; Chromosome 1.
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; 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: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..21
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           22..836
FT                   /note="Receptor-like serine/threonine-protein kinase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5010387125"
FT   TRANSMEM        424..448
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          29..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          796..836
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   836 AA;  90570 MW;  8B58EC149053002A CRC64;
     MFLKIQFFFL ILFLAATVAT AIDPGSTLSA SSTSNQTWSS PRGTFSLGFI SVQPPTTPPS
     FIAAISYTGG DPVVWSAGHG AAVDSGGSLQ FLSSGNLRLV NGSGSTVWES ATAGATSAAL
     EDSGNLVISN GTSTLWTSFD NPTDTLVQSQ NFSVGKVLTS ESYFFSLSGI GNLTLKWNNS
     IEYWTQGLNS SVNVSLESPV LSLTSIGLLE LSDVNLGTPV LVAYSSDYDL NANVFRVLKL
     DNDGNLRIYS TNLGGGTSTV RWAAVANQCE VYAYCGNYGV CGYNDSSTVC GCPSENFEMV
     DPNNGRKGCR RKLSLDSCQG TATMLTLDHA VVLSYPPTTT SETFFIGLSA CRTNCLSSSS
     ACFASTSLSD GTGQCVLRSL DFVSGYQDPS LPSTSYFKVC PPLAPNPPPS SAGTVRERRS
     KVPAWVVVVV VLGTLFVLLA LEGGLWMWCC RNNKRFGALS AQYALLEYAS GAPVQFSYKE
     LQQATKGFKE KLGAGGFGAV YRGTLVNKTV VAVKQLEGIE QGEKQFRMEV ATISSTHHLN
     LVRLIGFCSE GRHRLLVYEF MKNGSLDNFL FQTENHSGKL LNWEYRYNIA LGTARGITYL
     HEECRDCIVH CDIKPENILL DENYVSKVSD FGLAKLINPK DHRHRTLTSV RGTRGYLAPE
     WLANLPITSK SDVYSYGMVL LEIVSGRRNF DVSEETNRKK FSIWAYEEFE RGNISAILDK
     RLAGQEVDME QVRRAIQASF WCIQEQPSQR PTMSRVLQML EGVTEVEKPP APKSVMEGTV
     SGTSTYLSSN ASAFSTLGVS PPGPSSTSSF QISGVSTFNS GRTPEKATSS LLQSDT
//
DBGET integrated database retrieval system