ID A0A251PID9_PRUPE Unreviewed; 1017 AA.
AC A0A251PID9;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=non-specific serine/threonine protein kinase {ECO:0000256|ARBA:ARBA00012513};
DE EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
GN ORFNames=PRUPE_4G069300 {ECO:0000313|EMBL:ONI10810.1};
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:ONI10810.1, ECO:0000313|Proteomes:UP000006882};
RN [1] {ECO:0000313|EMBL:ONI10810.1, 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).
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-
CC pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.
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DR EMBL; CM007654; ONI10810.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A251PID9; -.
DR EnsemblPlants; ONI10810; ONI10810; PRUPE_4G069300.
DR Gramene; ONI10810; ONI10810; PRUPE_4G069300.
DR eggNOG; ENOG502QUIV; Eukaryota.
DR OrthoDB; 991910at2759; -.
DR Proteomes; UP000006882; Chromosome g4.
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; IBA:GO_Central.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd14066; STKc_IRAK; 1.
DR Gene3D; 2.60.120.430; Galactose-binding lectin; 1.
DR Gene3D; 3.80.10.10; Ribonuclease Inhibitor; 3.
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; IPR032675; LRR_dom_sf.
DR InterPro; IPR021720; Malectin_dom.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR PANTHER; PTHR48006; LEUCINE-RICH REPEAT-CONTAINING PROTEIN DDB_G0281931-RELATED; 1.
DR PANTHER; PTHR48006:SF66; PROTEIN KINASE DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF00560; LRR_1; 3.
DR Pfam; PF11721; Malectin; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF52058; L domain-like; 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 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:UP000006882};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}; Signal {ECO:0000256|SAM:SignalP};
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 SIGNAL 1..34
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 35..1017
FT /note="non-specific serine/threonine protein kinase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5012897016"
FT TRANSMEM 614..636
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 672..953
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 973..1017
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 700
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 1017 AA; 113115 MW; A31A0DCC2FA9A39B CRC64;
MARGVSCIAP KTIMNLIMLI SVLCLCTKLV EVEARASRLP PAEEEALEEI AKQLGKTDWN
FNINPCNNNT NWDTPKSTAN PLYNNTLECN CSYRGGFCHV VGIFLKGQDL AGVLPPSVAK
LPYITQVDFT RNYLSGPIPS EWASTKLEHL SVNVNNLSGQ IPSFLGNIKT LIYLNLQTNL
FSGTVPHELG NLVNLELFIL SSNYLTGELP VAFTNLTKLR EFRISSNNFT GRIPDYLGNF
KQLEKLEIQA SGLHGPIPSS ISVLSNLKEL RVSDLNGGGS KFPNLSNITG MTDLMLRSCN
LYGPIPAYIS TMENLKKLDL SFNKLEGNIN TPDYEHLQHV QYLYLTSNWL NGSVPEWIKI
RDNRYLTDIS YNNFSESSEP PTCPETLNVF KSFSAQRNLS FGVCLKNFQC PEDKSSLHIN
CGGKQTTIEG VTFEDDQDQG GAAKFFPQRP IWGTSSTGHF WDSASNATAY IANNVSILRM
NNAELYTNAR INPLSLTYYA RCFRNGNYTV KLHFSEITIR GNRSFRSVGR RIFDIYIQEK
LVWKDFEIKK EAHGVDKELI KECKAVEVKN KTLEIRFHWS GKGTTASPKT GTYGALISAI
SVEPEFKKSK VPTIVGASVG ALVLFLIFLI FGILWWKGCL DCKISREKAL RGLDLQTGFF
TFKQIKAATN NFDPINKIGE GGFGSVYKGI LLDGTIIAVK QLSSKSKQGN REFVNEIGMI
SGLQHPNLVR LYGCCVESNQ LLLVYEYMEN NSLARALFVP EESPLKLDWP TRQNICIGIA
RGLAFLHEES ALKIVHRDIK TTNILLDRDL NSKISDFGLA KLDEEENTHI STRVAGTIGY
MAPEYALWGY LTYKADVYSF GVVALEIVAG KNNMKYRPNE NFVCLVDWAL VLQQKGELLE
LVDPRLGSDV SEEEAIRMIK VALLCINAAP ALRPTMSAVV SMLEGRTAVH ELVTDPSTYG
DELRLTALTN QFDHSSSQNP SQTQSLVPSS SDAPWIGSSA TTTSSDLYKI NPSTSSY
//
