ID A0A218XK17_PUNGR Unreviewed; 1097 AA.
AC A0A218XK17;
DT 27-SEP-2017, integrated into UniProtKB/TrEMBL.
DT 27-SEP-2017, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE RecName: Full=Protein kinase domain-containing protein {ECO:0000259|PROSITE:PS50011};
GN ORFNames=CDL15_Pgr027853 {ECO:0000313|EMBL:OWM85066.1};
OS Punica granatum (Pomegranate).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Myrtales; Lythraceae; Punica.
OX NCBI_TaxID=22663 {ECO:0000313|EMBL:OWM85066.1, ECO:0000313|Proteomes:UP000197138};
RN [1] {ECO:0000313|Proteomes:UP000197138}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Dabenzi {ECO:0000313|Proteomes:UP000197138};
RX PubMed=28654223; DOI=10.1111/tpj.13625;
RA Qin G., Xu C., Ming R., Tang H., Guyot R., Kramer E.M., Hu Y., Yi X.,
RA Qi Y., Xu X., Gao Z., Pan H., Jian J., Tian Y., Yue Z., Xu Y.;
RT "The pomegranate (Punica granatum L.) genome and the genomics of
RT punicalagin biosynthesis.";
RL Plant J. 91:1108-1128(2017).
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000256|ARBA:ARBA00008684}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OWM85066.1}.
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; MTKT01001287; OWM85066.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A218XK17; -.
DR Proteomes; UP000197138; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
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; 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; 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; PTHR48054:SF27; PROTEIN KINASE DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR48054; RECEPTOR KINASE-LIKE PROTEIN XA21; 1.
DR Pfam; PF00560; LRR_1; 12.
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; 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, ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; 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 7..26
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 712..736
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 773..1062
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT BINDING 802
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 1097 AA; 119622 MW; 5C5D91BB57214E3C CRC64;
MSRDHGITAT PAITIFAILI LNITLLPSVS SALNLEGHAL LSWLSTFNSS PSSSFFASWN
QTHRNPCRWD FIQCSPGGFV SGIAISSVYI PTGFPTQVLS FFHLSSLVIK GVNLTGEIPP
AIGNLSKLTV LDLSYNGLIG KIPPEIGKLS RLESLALNTN FLEGEIPRSI GNCSALARLE
IFDNQLSGRI PVEIGMLGSL EIFRAGGNPG IFGEIPSEIS SCVELNFLGL SDTGISGPIP
DSLGELKKLR TLSVYTANLT GEIPKSISNC SALEDLFLYQ NRILGSIPEE LFWLRNLKRV
LLWQNELVGQ VPRNIGNCSG LLVVDLSVNS LSGEIPPSLA NLASLEELLL SENEFSGEFP
SFIGEILSLK QLELDNNALS GEIPPSIGKL ENLFLFFAWQ NRLKGRIPGE LANCQQLQAL
DLSHNSLAGP IPSQLFGLKN LSQLLLISNS LSGGIPPEIG NCTSLTRLRL GSNQLTGRVP
PEIGLLYSLS FLELSENRIT GPIPPEIGNC VKLEMVDLHA NEIMGTIPSS LERLERLNVL
DISSNHLTGP IPGNLGKLTS LNKLVISRNN ISGSIPPSLG LCKDLQLLDI SFNRLAGPIP
YEIGQLQGLD IMLNLSWNSL SGPIPSSFSK LSNLANLDFS HNDLSGTLEV LGKLDNLVSL
DVSYNKFSGL LPNTKFFQNL PAAAYAGNQD LCIDSNGNKC SGAINGTKPA RNLLICVFLG
ITMTVLIVST GMYLYLRIYG AKLRRSDEES DLEWHFTPFQ KLNFSVTDIV TKLSDSNVVG
KGCSGLVYRV ETSTKQVIAV KKLWPPNNEG RPDPERDLFS SEVRILGSIR HKNIVRLLGC
CNRGKSQLLL FDYISNGSLS GLLHEKNQVC LDWDVRYQII LGAAHGLAYL HHDCIPPIIH
RDIKTNNILV GPQFEAYLAD FGLAKLVNTS EYSVASKTIA GSYGYMAPEY GYSFKITEKS
DVYSFGIVLL EVLTGMQPTD TRIPDGAHIV SWVNRELREK RRDFTTILDP QLLSRSGTQT
QEMLQVLGVS LLCVSPIPEE RPAMKDVVAM LKEIRHEVHE EIEKPCLNGK SLGTNPEAAV
HCSSFSRSSE PLIASTS
//
