ID A0A251MVE6_PRUPE Unreviewed; 1078 AA.
AC A0A251MVE6;
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=non-specific serine/threonine protein kinase {ECO:0000256|ARBA:ARBA00012513};
DE EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
GN ORFNames=PRUPE_8G043000 {ECO:0000313|EMBL:ONH90259.1};
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:ONH90259.1, ECO:0000313|Proteomes:UP000006882};
RN [1] {ECO:0000313|EMBL:ONH90259.1, 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 -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000256|ARBA:ARBA00008684}.
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DR EMBL; CM007658; ONH90259.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A251MVE6; -.
DR EnsemblPlants; ONH90259; ONH90259; PRUPE_8G043000.
DR Gramene; ONH90259; ONH90259; PRUPE_8G043000.
DR eggNOG; ENOG502QUMP; Eukaryota.
DR OrthoDB; 457890at2759; -.
DR Proteomes; UP000006882; Chromosome g8.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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; 6.
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; PTHR48056:SF69; LEUCINE-RICH REPEAT RECEPTOR PROTEIN KINASE EXS; 1.
DR PANTHER; PTHR48056; LRR RECEPTOR-LIKE SERINE/THREONINE-PROTEIN KINASE-RELATED; 1.
DR Pfam; PF00560; LRR_1; 9.
DR Pfam; PF13855; LRR_8; 2.
DR Pfam; PF08263; LRRNT_2; 1.
DR Pfam; PF00069; Pkinase; 1.
DR PRINTS; PR00019; LEURICHRPT.
DR SMART; SM00369; LRR_TYP; 10.
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; 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:UP000006882};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
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 713..734
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 781..1071
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT BINDING 810
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 1078 AA; 117305 MW; 40F42C9E3687135F CRC64;
MEQNRTHFLF SFTLLIYITM AKLLLVTSLS SDGQALLSLL PAKQSSSSSS VLSSWDPSSQ
TPCSWQGITC SPQNRVISLS LPNIFLNLSS LPPQLSSLSY LQLLNLSSTN ISGTIPPSFG
QLTHLRLLDL SANSLTGSIP PELGNLSALQ FLFLNSNRLS DKMPQQLANL TSLQVLCLQD
NLINGSIPSQ LGSLVSLQQF RVGGNPYISG EIPSQLGLLT NLTTFGAAAT GLSGTIPSTF
GNLVNLQTLA LYDTEIVGSI PPELGLCLEL RNLYLHMNKL TGSIPPQLGK LQKLTSLLLW
GNALSGPIPA EISNCSSLVI LDASANDLSG AIPRDIGKLV VLEQLHLSDN SLTGTIPSQL
SNCTSLTALQ LDKNQFSGTI PWQVGNLKSL QSFFLWGNLV SGTIPSSFGN CTELYALDLS
RNKLTGSIPE EIFSLKKLSK LLLLGNSLSG GLLPSVAHCQ SLVRLRLGEN QLSGQIPKEI
GQLQNLVFLD LYMNHFSGGL PVEIANITVL ELLDVHNNYI SGEIPSELGE LVNMEQLDLS
RNSFTGEIPW SFGNLSYLNK LIINNNLLTG SIPKSIRNLQ KLTLLDLSFN SLSGPIPPEI
GHVTSLTISL DLSSNSFTGE IPETMEGLTQ LQSLDLSHNM LFGNIKVLGS LTSLTSLNIS
CNNFSGPIPV TPFFRTLSSS SYLKNPHLCE SADGTTCSSS LMRKNGLKSA KTVALISVIL
ASVTIAVIAS WIVVMRNHRY MVKKSLGALA LSSGAEDFSY PWTFIPFQKL NFTIDNILDC
LKDENVIGKG CSGIVYKAEM QNGDLIAVKK LWKTKQEEEP IDSFAAEIQI LGHIRHRNIV
KLLGYCSNRS VKLLLYNFIP NGNLQQLLQG NRNLDWETRY KIAIGSAQGL AYLHHDCVPA
ILHRDVKCNN ILLDSKYEAY LADFGLAKLM NSPTYHHAMS RVAGSYGYIA PEYGYTMNIT
EKSDVYSYGV VLLEILSGRS AVQPQIGDGL HIVEWVKKKM GSFEPAVSIL DAKLQGLPDQ
MVQEMLQTLG IAMFCVNSSP AERPTMKEVV ALLMEVKSQP EEWGKTSQPL IKQSSAQS
//