ID A0A0L9VPL5_PHAAN Unreviewed; 1091 AA.
AC A0A0L9VPL5;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=Protein kinase domain-containing protein {ECO:0000259|PROSITE:PS50011};
GN ORFNames=LR48_Vigan11g001200 {ECO:0000313|EMBL:KOM56980.1};
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:KOM56980.1, 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 -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000256|ARBA:ARBA00008684}.
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 EMBL; CM003381; KOM56980.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0L9VPL5; -.
DR STRING; 3914.A0A0L9VPL5; -.
DR EnsemblPlants; KOM56980; KOM56980; LR48_Vigan11g001200.
DR Gramene; KOM56980; KOM56980; LR48_Vigan11g001200.
DR OMA; EFRACVA; -.
DR Proteomes; UP000053144; Chromosome 11.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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 Gene3D; 3.80.10.10; Ribonuclease Inhibitor; 4.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR001611; Leu-rich_rpt.
DR InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
DR InterPro; IPR032675; LRR_dom_sf.
DR InterPro; IPR013210; LRR_N_plant-typ.
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; PTHR45974:SF95; OS02G0153700 PROTEIN; 1.
DR PANTHER; PTHR45974; RECEPTOR-LIKE PROTEIN 55; 1.
DR Pfam; PF00560; LRR_1; 6.
DR Pfam; PF13855; LRR_8; 2.
DR Pfam; PF08263; LRRNT_2; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR PRINTS; PR00019; LEURICHRPT.
DR SMART; SM00369; LRR_TYP; 7.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF52058; L domain-like; 3.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS51450; LRR; 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|PROSITE-
KW ProRule:PRU10141}; Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Leucine-rich repeat {ECO:0000256|ARBA:ARBA00022614};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, 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 Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 21..40
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 721..745
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 808..1079
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT BINDING 837
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 1091 AA; 119289 MW; 3CC4CE08F0522F70 CRC64;
MPSPSSSSSA YSLYNSYMVS NFMVSIIVPL FLFSLFVVHV SSCSQIDKLS LLAFSGNIST
SPPFPSLNWS DSLDCCAWEG ITCDGDLRVT HLLLPSRGLT GFISPSLTNL SSLSHLNLSH
NRLSGGLQHQ LFSLLSHLVV LDLSYNHLSG ELPPFVGDNS GKNSSGAAIQ ELDLSSNFFN
GTLPNSLLEN LAAAAAGGSL VSLNVSNNSF IGHIPTSLFC INDRNSSSLR FLDYSSNDFD
GAIQPGLGAC SKLERFRAGF NFLSGPIPSD LFDAVSLTEI SLPLNRLTGT IGDGIVGLTN
LTVLELYSNH FTGFIPREIG KLSKLERLLL HVNNLTGTMP PSLMNCVNLV VLNLRVNLLE
GNLSAFNFSG FLSLTTLDLG NNYFIGGLPP TLYACKSLSA VRFASNQLEG EISPRILELE
SLSFLSISTN KLRNVTGALT ILRGLKNLST LMLSKNFFNE MIPQDVNIIE PGGFQKLQVL
GFGGCNFTGQ IPGWLVKLKK LEALDLSFNQ ISGPIPPWLG RLPQLFYMDL SFNLLTGVIP
VELTELPALA SQQANDKVER TYLELPVFAN ANNVSLLQYN QLSALPPAIY LGNNHLNGSI
PIEIGKLKAL LQLDVKNNSF SGDIPVQFSN LTNLEKLDLS GNQLSGEIPD SLRRLHFLSF
FSVAFNNIQG QIPTGGQFDT FSYSSFEGNS QLCGPVIQRS CSQQNTSTNT TAASHSSNKR
IMIALVITAS FGFGSLITVL TLWILSKRRV NPGGELDKIE MESISAYSNN GIHPEVDKEA
SLVVLFSNKN NETKDLTIFD ILKATENFSQ ANIIGCGGFG LVYKATLPNG TTVAIKKLSG
DLGLMEREFK AEVEALSTAQ HENLVALKGY CVHEGFRLLM YTYMENGSLD YWLHEKPDGA
SQLDWPTRLK IAQGASCGLA YLHQICEPHI VHRDIKSSNI LLNENFEAHV ADFGLSRLIL
PYHTHVTTEL VGTLGYIPPE YGQAWVATLR GDVYSLGVVM LELLTGRRPV DVCKPKMSRE
LVGWVQQMRI EGKQDQVFDP ILRGKGFEGE MLKVLDVACM CVSHNPFKRP SIREVVEWLK
NVASDNQPAQ K
//
