ID A0A251PVG1_PRUPE Unreviewed; 855 AA.
AC A0A251PVG1;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=Protein kinase domain-containing protein {ECO:0000259|PROSITE:PS50011};
GN ORFNames=PRUPE_3G049500 {ECO:0000313|EMBL:ONI15551.1};
OS Prunus persica (Peach) (Amygdalus persica).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Rosales; Rosaceae; Amygdaloideae; Amygdaleae; Prunus.
OX NCBI_TaxID=3760 {ECO:0000313|EMBL:ONI15551.1, ECO:0000313|Proteomes:UP000006882};
RN [1] {ECO:0000313|EMBL:ONI15551.1, ECO:0000313|Proteomes:UP000006882}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nemared {ECO:0000313|Proteomes:UP000006882};
RX PubMed=23525075; DOI=10.1038/ng.2586;
RA Verde I., Abbott A.G., Scalabrin S., Jung S., Shu S., Marroni F.,
RA Zhebentyayeva T., Dettori M.T., Grimwood J., Cattonaro F., Zuccolo A.,
RA Rossini L., Jenkins J., Vendramin E., Meisel L.A., Decroocq V.,
RA Sosinski B., Prochnik S., Mitros T., Policriti A., Cipriani G., Dondini L.,
RA Ficklin S., Goodstein D.M., Xuan P., Del Fabbro C., Aramini V., Copetti D.,
RA Gonzalez S., Horner D.S., Falchi R., Lucas S., Mica E., Maldonado J.,
RA Lazzari B., Bielenberg D., Pirona R., Miculan M., Barakat A., Testolin R.,
RA Stella A., Tartarini S., Tonutti P., Arus P., Orellana A., Wells C.,
RA Main D., Vizzotto G., Silva H., Salamini F., Schmutz J., Morgante M.,
RA Rokhsar D.S.;
RT "The high-quality draft genome of peach (Prunus persica) identifies unique
RT patterns of genetic diversity, domestication and genome evolution.";
RL Nat. Genet. 45:487-494(2013).
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DR EMBL; CM007653; ONI15551.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A251PVG1; -.
DR STRING; 3760.A0A251PVG1; -.
DR EnsemblPlants; ONI15551; ONI15551; PRUPE_3G049500.
DR Gramene; ONI15551; ONI15551; PRUPE_3G049500.
DR eggNOG; KOG1187; Eukaryota.
DR OrthoDB; 472728at2759; -.
DR Proteomes; UP000006882; Chromosome g3.
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 CDD; cd14066; STKc_IRAK; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
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; PTHR47989; OS01G0750732 PROTEIN; 1.
DR PANTHER; PTHR47989:SF45; PROTEIN KINASE DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
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}; Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000006882};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Signal {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..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..855
FT /note="Protein kinase domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5012151434"
FT TRANSMEM 369..392
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 463..740
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 73..137
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 324..346
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 118..137
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 327..341
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 491
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 855 AA; 92834 MW; 82BB9BC9DDAF74A7 CRC64;
MGRQLNLLLV QMCLIVGVLP FHGSAEHAVS PKSPLSFGWK RHEKLVALPP RKAFQHILPS
DYSPDKASHP HSAIWPSSIA VPPTSSEGPA KKWVHGPISS PSISHHKHHH KSKKFHSSAP
EPTYSRQGPA VSPLQSPFSS TSSWAAAAPS PTTLTSHYNM PVFPPTVSPV GSSLKNTKAP
PPSPILALPP PPPSEDCSSI TCTEPLTYTP LGSSCGCVRP IQVQLQLGVA IYTFFPLVSE
LAEEIAASVA LNHSQVRIMG ADAVSQQLEK SAVLINLVPT GITFDGTTAF QIYDKFWRRQ
VSIKPSLFGD YEVFYVHYPG LPPSPPSASS SISTTDDGPY TGKDNNGRAI KPFGVDVPRR
KRDGLGKSMI AVIVVSSFTA FLLCVGVVWL LLLKCGSCHS HQLEKFPQTL TSSPTKLSGA
PRSVMFGSMR GSGSTSLSSG TLNYTGSAKT FTLNDMERAT NNFDASRILG EGGFGLVYSG
ILDDGREVAV KVLKREDHHG SREFLAEVEM LSRLHHRNLV KLIGICTEGH TRCLVYELVP
NGSVESHLHG IDKETDPLDW DARIKIALGA ARGLAYLHED SNPRVIHRDF KASNILLEYD
CTPKVSDFGL ARAALEEGKR HISTHVMGTF GYLAPEYAMT GHLLVKSDVY SYGVVLLELL
SGRKPVDLSQ PPGQENLVAW ARPLLTSKEG LEMIIDPALK PSDISWDSVT KVAAIASMCI
QPEVSHRPFM GEVVQALKLV CNEFKETQEV GASTSCGQDD LFIHIDSGSL EASQSQQEQE
LPGFGAGHGT KIPSTSDLLS APVGLEVEGQ EFGSFRRYSS SGPLRTGKRK QFWQRLRSLS
RGSMSEHGFP MKLWL
//
