ID A0A0L9U0H6_PHAAN Unreviewed; 684 AA.
AC A0A0L9U0H6;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE RecName: Full=Cysteine-rich receptor-like protein kinase {ECO:0008006|Google:ProtNLM};
GN ORFNames=LR48_Vigan02g232200 {ECO:0000313|EMBL:KOM36172.1};
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:KOM36172.1, 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; CM003372; KOM36172.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0L9U0H6; -.
DR EnsemblPlants; KOM36172; KOM36172; LR48_Vigan02g232200.
DR Gramene; KOM36172; KOM36172; LR48_Vigan02g232200.
DR OMA; NDHRLES; -.
DR Proteomes; UP000053144; Chromosome 2.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
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; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR PANTHER; PTHR27002:SF844; CYSTEINE-RICH RECEPTOR-LIKE PROTEIN KINASE 27-RELATED; 1.
DR PANTHER; PTHR27002; RECEPTOR-LIKE SERINE/THREONINE-PROTEIN KINASE SD1-8; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 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}; Coiled coil {ECO:0000256|SAM:Coils};
KW 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 Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
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..38
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 39..684
FT /note="Cysteine-rich receptor-like protein kinase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5005595142"
FT TRANSMEM 285..306
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 40..143
FT /note="Gnk2-homologous"
FT /evidence="ECO:0000259|PROSITE:PS51473"
FT DOMAIN 149..256
FT /note="Gnk2-homologous"
FT /evidence="ECO:0000259|PROSITE:PS51473"
FT DOMAIN 352..628
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 663..684
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 308..338
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 663..677
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 380
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 684 AA; 77110 MW; B173661BDF4585A5 CRC64;
MIIRKASVKV VGCSDYVMGA VSCMLLFFLC CLIPEASAQY LFLNCDNNNG NYTANGTYST
NLNTLLSTLS SNTEINYGFY NFSHGQNSDR VNAIGLCRGD VEQNPCRSCL KDAGGNITEL
CPNQKQAAIY YDNCMLRYSN DSIFGVLDIS PHFYMWNSNN ATGAAEFNQV LQNLLRELRD
KAASGDSRRK YATNNDTTTN FQAIYGLVQC TPDLTQTQCN DCLDEAISRI PTCCNDKRGG
RVVGPSCNIR YEDYRFYEQT TIIDPETPPP TINTSTEESS NTTTIVIAVV VPTVAVVFLI
CLFICLRRRK ARKNLEVKKE EREEEDEDED EIKIAESLQF NFDTIRVATE DFSDSNKLGQ
GGFGAVYRGK LSNGQIIAVK RLSRDSGQGD VEFKNEVVLV VKLQHRNLVR LLGFCLEGRE
RLLVYEFVPN KSLDYFIFDP AMKAQLDWEK RYKIIRGIAR GLLYLHEDSQ LRIIHRDLKA
SNILLDEEMN PKIADFGMAR LVLLDQTQAN TSRIVGTYGY MAPEYAMHGQ FSVKSDVFSF
GVLILEIVSG QRNSGINNGE NMEDLLSFAW RNWKEGKALN IVDPSLNNNS RNEMLRCIHI
GLLCVQENLV DRPTMATIIL MLNSHSLSLA IPAEPAFYMN SRTRSFPGMQ SWEYNSREMG
SSEPILKSAQ ESENEASITE LYPR
//
