ID A0A0L9VDP1_PHAAN Unreviewed; 637 AA.
AC A0A0L9VDP1;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE RecName: Full=Cysteine-rich receptor-like protein kinase 2 {ECO:0008006|Google:ProtNLM};
GN ORFNames=LR48_Vigan09g144300 {ECO:0000313|EMBL:KOM52784.1};
OS Phaseolus angularis (Azuki bean) (Vigna angularis).
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=3914 {ECO:0000313|EMBL:KOM52784.1, ECO:0000313|Proteomes:UP000053144};
RN [1] {ECO:0000313|Proteomes:UP000053144}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=cv. Jingnong 6 {ECO:0000313|Proteomes:UP000053144};
RX PubMed=26460024; DOI=10.1073/pnas.1420949112;
RA Yang K., Tian Z., Chen C., Luo L., Zhao B., Wang Z., Yu L., Li Y., Sun Y.,
RA Li W., Chen Y., Li Y., Zhang Y., Ai D., Zhao J., Shang C., Ma Y., Wu B.,
RA Wang M., Gao L., Sun D., Zhang P., Guo F., Wang W., Li Y., Wang J.,
RA Varshney R.K., Wang J., Ling H.Q., Wan P.;
RT "Genome sequencing of adzuki bean (Vigna angularis) provides insight into
RT high starch and low fat accumulation and domestication.";
RL Proc. Natl. Acad. Sci. U.S.A. 112:13213-13218(2015).
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004167}; Single-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004167}.
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DR EMBL; CM003379; KOM52784.1; -; Genomic_DNA.
DR RefSeq; XP_017435999.1; XM_017580510.1.
DR AlphaFoldDB; A0A0L9VDP1; -.
DR EnsemblPlants; KOM52784; KOM52784; LR48_Vigan09g144300.
DR GeneID; 108342714; -.
DR Gramene; KOM52784; KOM52784; LR48_Vigan09g144300.
DR KEGG; var:108342714; -.
DR OMA; IETALMC; -.
DR OrthoDB; 393015at2759; -.
DR Proteomes; UP000053144; Chromosome 9.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd14066; STKc_IRAK; 1.
DR Gene3D; 3.30.430.20; Gnk2 domain, C-X8-C-X2-C motif; 2.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR002902; GNK2.
DR InterPro; IPR038408; GNK2_sf.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR PANTHER; PTHR47973; CYSTEINE-RICH RECEPTOR-LIKE PROTEIN KINASE 3; 1.
DR PANTHER; PTHR47973:SF23; CYSTEINE-RICH RLK (RECEPTOR-LIKE KINASE) PROTEIN; 1.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF01657; Stress-antifung; 2.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS51473; GNK2; 2.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Kinase {ECO:0000256|ARBA:ARBA00022777}; Membrane {ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000053144};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..637
FT /note="Cysteine-rich receptor-like protein kinase 2"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5005596505"
FT TRANSMEM 265..284
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 29..132
FT /note="Gnk2-homologous"
FT /evidence="ECO:0000259|PROSITE:PS51473"
FT DOMAIN 138..242
FT /note="Gnk2-homologous"
FT /evidence="ECO:0000259|PROSITE:PS51473"
FT DOMAIN 322..609
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT BINDING 351
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 637 AA; 70467 MW; 90274BABC0896CB7 CRC64;
MLGLVKLLAL TLIWWSSSVE HADAATQKTR LINTGCSPFN ASNARSFLAN VNDSFSEMRA
EVSNQSKLFG TSQKSRGGTL TYTMFQCRNY LSKNDCLSCF DTASTQIRNC SKANGARVIY
NDCFLRYESE RFYQQTNELG SGVTCGNTSL KTTRDFKVVG QQALTEIQTA TPKTKGFYAA
TKTQVDDGSA IYAIAQCVET AAESDCLKCM QVAYNNLQSC LPNTDGTAYD AGCFMRYSTT
PFFAANQTID IRSYLKQGSS GKKGGIIGGV VGGFVLLLIL FFVWRMSRKR NKVHRGDILG
ATELRGPVNY KYNDLKAATK NFSAENKLGE GGFGAVYKGT LKNGKIVAIK KLVLGKSSKM
EDDFEGEVKL ISNVHHRNLV RLLGCCSKGE ERILVYEYMA NSSLDRFLFG AKGSLNWQQR
YDIILGTARG LAYLHEEFHV SIIHRDIKTG NILLDDDLQP KIADFGLARL LPGDRSHLST
KFAGTLGYTA PEYAMHGQLS EKADTYSYGI VVLEIISGQK STDVKNEEEC REYLLQRAWK
LYERGLQLEL VDEAIDPNEY DAEEVKKIIE IALLCTQASA ASRPTMSEVV VLLKSKSLME
HMRPTMPVFV DTNMINREGN SASSSNATVS ISVLSAR
//
