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Database: UniProt
Entry: A0A218WGP1_PUNGR
LinkDB: A0A218WGP1_PUNGR
Original site: A0A218WGP1_PUNGR 
ID   A0A218WGP1_PUNGR        Unreviewed;       913 AA.
AC   A0A218WGP1;
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_Pgr017907 {ECO:0000313|EMBL:OWM72024.1};
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:OWM72024.1, 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:OWM72024.1}.
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DR   EMBL; MTKT01004293; OWM72024.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A218WGP1; -.
DR   Proteomes; UP000197138; Unassembled WGS sequence.
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   CDD; cd14066; STKc_IRAK; 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; 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; PTHR45974:SF134; PROTEIN KINASE DOMAIN-CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR45974; RECEPTOR-LIKE PROTEIN 55; 1.
DR   Pfam; PF00560; LRR_1; 3.
DR   Pfam; PF13855; LRR_8; 1.
DR   Pfam; PF08263; LRRNT_2; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00369; LRR_TYP; 5.
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   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   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        515..539
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          581..855
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   REGION          863..913
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         609
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   913 AA;  100494 MW;  4470614BABF80144 CRC64;
     MPVGAQNNSV TDPLEVKALR DIRRRLKDPN GNLTNWNSGD PCTSTWTGVI CFNRTLDDGY
     LHVQELDFMW NNISGSIPKE IGNITSLELL LLNGNQLTGP LPEELGYFPK LDRIQIDQNQ
     ISGPLPKSFA NLNKTKHFHM NNNSISGQIP PELSRLPSLV HFLLDNNNLS GYLPPEFSEL
     PKLLILQVDN NNFEGTTIPP SYSNMSKLLK MSLRNCSLEG PIPDLSRIPQ LGYLDLSSNR
     LNGSIPQSEL SENITTIDLS DNNLSGNISD IFSGLPNLQR LSLANNSLDG SVPSSIWENK
     TLNATERKTL DFRNNKFSNI SGSTVLPPNV SVWLQGNPVC TATNLVQLCG TQNDDGDTWQ
     GAANSSSIAE CHPQACPPPY EYSVLSPVPC FCTAPLLVGY RLKSPGFSYF PPYKGIFEEY
     LSSGLSLYPY QLQVLSSLWQ KGPRLAMYVK LFPVYNNDSR IFNESEIHRI RTMFTGWNIG
     DSDLFGPYEL LNFTLRGPYE QENNARQSSG ISKGAIAGIV VGTIAGAVIL SALVSLLILR
     MHLRDHYVLS KRRRSSASMS IKIEGVRGFT YEEMGLATNN FDSSTQVGQG GYGKVYRGVL
     ADGTIVAIKR AQEGSLQGDK EFLTEIQLLS RVHHRNLVSL IGYCDEEDEQ LLVYEFMPNG
     TLRDHLSVRS KEPLSFAMRL SIALGSAKGI LYLHTEANPP IFHRDIKASN ILLDSKFTAK
     VADFGLSRLA PVPDIEGALP DHVSTVVKGT PGYLDPEYFL THKLTDKSDV YSLGVVFLEL
     LTGMQPISHG KNIVREVNLA NQSGMIFSII DGRMGCYPSE CVEKFLKLAL KCCQDETDSR
     PSMADVVREL ENIWLMTPES LSNAKNAESP AKGATPTTPP SSSSFSLTKD PHVSSDVSGS
     DLLSGVVPSI TPR
//
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