ID A0A0S3SRK8_PHAAN Unreviewed; 1016 AA.
AC A0A0S3SRK8;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=Protein kinase domain-containing protein {ECO:0000259|PROSITE:PS50011};
GN Name=Vigan.08G220700 {ECO:0000313|EMBL:BAT95472.1};
GN ORFNames=VIGAN_08220700 {ECO:0000313|EMBL:BAT95472.1};
OS Vigna angularis var. 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=157739 {ECO:0000313|EMBL:BAT95472.1, ECO:0000313|Proteomes:UP000291084};
RN [1] {ECO:0000313|EMBL:BAT95472.1, ECO:0000313|Proteomes:UP000291084}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Shumari {ECO:0000313|Proteomes:UP000291084};
RX PubMed=26616024; DOI=10.1038/srep16780;
RA Sakai H., Naito K., Ogiso-Tanaka E., Takahashi Y., Iseki K., Muto C.,
RA Satou K., Teruya K., Shiroma A., Shimoji M., Hirano T., Itoh T., Kaga A.,
RA Tomooka N.;
RT "The power of single molecule real-time sequencing technology in the de
RT novo assembly of a eukaryotic genome.";
RL Sci. Rep. 5:16780-16780(2015).
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000256|ARBA:ARBA00008684}.
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DR EMBL; AP015041; BAT95472.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0S3SRK8; -.
DR Proteomes; UP000291084; Chromosome 8.
DR GO; GO:0005886; C:plasma 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 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; IPR008271; Ser/Thr_kinase_AS.
DR PANTHER; PTHR48054:SF76; LRRNT_2 DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR48054; RECEPTOR KINASE-LIKE PROTEIN XA21; 1.
DR Pfam; PF00560; LRR_1; 7.
DR Pfam; PF13855; LRR_8; 1.
DR Pfam; PF08263; LRRNT_2; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00369; LRR_TYP; 6.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF52058; L domain-like; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR SUPFAM; SSF52047; RNI-like; 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};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000291084};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}; Signal {ECO:0000256|SAM:SignalP};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT SIGNAL 1..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..1016
FT /note="Protein kinase domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5006618553"
FT DOMAIN 706..981
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 981..1003
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 981..995
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 736
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 1016 AA; 110573 MW; 5CF6C7229DC18D32 CRC64;
MQLKTQFFFY FCCMFCFSYG FAAAANDEAS ALLSIKAGLI DPLNSLLDWK LLVKAKGKGA
AHCNWTGVQC NSAGVVDSLD LSRMNLSGIV SNEIQSLKSL TSLNLCCNEF SSSLSSIANL
TTLKTLDVSQ NFFTGDFPLG LGKALGLTTL NASSNNFSGF LPEDLGNVSS LETLDFRGSF
FEGSVPKSFS NLHRLKFLGL SGNNLTGEIP GELGQLSSLE CLILGYNEFE GGIPAEFGNL
TMLKYLDLAE GNLGGEIPAE LGKLKLLNTV FLYKNKLEGK IPPTIGTMTS LVQLDLSDNM
LSGNIPAEIS QLKNLQLLNF MRNRLSGPVP SGLGDLPQLE VLELWNNSLS GSLPRNLGKN
SPLLWLDVSS NLLSGEIPET LCTKGYLTKL ILFNNAFMGP IPASLSTCPS IVRVRIQNNF
LSGTIPVGLG KLRKLQRLEL ANNSLTGGIP NDIGSSTSLS FIDFSTNNLH SSLPSNILSI
SNLQTLIVSN NNLRGEIPDE FQDCPSLGVL DLSRNELSGG IPASLASCQK LVNLNLQNNQ
LTGEIPKALA SMPTLAILDL ANNSLIGQIP GNFGSSPALE TFNVSHNKLK GPVPENGVLR
TINPNDLAGN AGLCGAVLPP CVQISAYPLR RGNSYPKHII VGWIIGISSI LAIGVTTVVA
RSLYIRWYTE GLCFQERFYK GRKGWPWRLM AFQRLDFTSS DILSCIKDTN MIGMGATGVV
YKAEIPQSST IVAVKKLWRS GSDIEVGSSD DLVGEVNLLG RLRHRNIVRL LGFLYNDADV
MIVYEFMHNG NLGDALHGKQ AGRLLVDWVS RYNIALGIAE GLVYLHHDCH PPVIHRDIKS
NNILLDANLD ARIADFGLAK MMLRKNETVS MIAGSYGYIA PEYGYSLKVD EKIDIYSYGV
VLLELLTGKR PLEPEFGESI DIVGWIRRKI DKKSAHEALD PSVGNCRYVQ EEMILVLKIA
LLCTAKFPKD RPSMRDVRMM LGEAKPRRKS GRSSETFSAN KEMPANISKP AVNGLL
//
