GenomeNet

Database: UniProt
Entry: A0A218WUX4_PUNGR
LinkDB: A0A218WUX4_PUNGR
Original site: A0A218WUX4_PUNGR 
ID   A0A218WUX4_PUNGR        Unreviewed;       904 AA.
AC   A0A218WUX4;
DT   27-SEP-2017, integrated into UniProtKB/TrEMBL.
DT   27-SEP-2017, sequence version 1.
DT   27-MAR-2024, entry version 18.
DE   RecName: Full=Protein kinase domain-containing protein {ECO:0000259|PROSITE:PS50011};
GN   ORFNames=CDL15_Pgr005427 {ECO:0000313|EMBL:OWM76463.1};
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:OWM76463.1, 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   -!- 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:OWM76463.1}.
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; MTKT01003181; OWM76463.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A218WUX4; -.
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: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; 3.80.10.10; Ribonuclease Inhibitor; 1.
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; IPR024788; Malectin-like_Carb-bd_dom.
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; PTHR45631; OS07G0107800 PROTEIN-RELATED; 1.
DR   PANTHER; PTHR45631:SF187; PROTEIN KINASE DOMAIN-CONTAINING PROTEIN; 1.
DR   Pfam; PF13855; LRR_8; 1.
DR   Pfam; PF12819; Malectin_like; 1.
DR   Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR   PRINTS; PR00019; LEURICHRPT.
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}; 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        536..559
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          590..866
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   REGION          1..30
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          51..70
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         618
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   904 AA;  99437 MW;  BF25F4025022AFF6 CRC64;
     MPPNGGASEL SHHHPKRACR SHKRSSATLV QPATSPWTVV AVRQSTTFQI SLPLSPRERG
     RSGKNHNGGG PVVSHHSFGF ISIDCGALNA YPNNDLQIYY ETDDGYIDSG VSKQVSSDGM
     GDGVRASAKT LREFPDGFRN CYTIPPTTTD EGHGKYLIRA SFLYDNYDNQ NRTPKFNLFI
     GVNYWTTVDF PDPGSYVHKE IIHVVPPTAD AIQVCLVNTG NGTPFISSLE LRQLADTMYL
     SDDQFPTLAL YIRTDMGYTA DESMFRHPSD SYDRFWDVDD MDNDGTLSSA WNGTSPPTLD
     RTNDAYKVPI EVLGTFVTVE SSYNLSLSWK AHVPGASKWI SYLHFAEMEN LSSPREFTIY
     SNDAFIKTIS LDYLVPMTVP TNQFTSDIGF KFKFVANSLS SASSVPPIIN AVELYYLLDI
     STRPTDLNDG NSTAKNFGRN LSSYGLKGKI ADSLTNLTAL TSLDLSSNQL TGPIPELLAK
     LPNLNILNLS GNNLTGPIPE SLQKKKYDGK LELSVAGNPN LRLEDSGKLK KKRSSFVVPV
     IAAGSGLVVI LSIALAIIWR FKITKGKGQE GTIKLRNRPF TFNEVLKITD NFKTVIGKGG
     FGKVYLGTLA NGTNVAVKML SQTSKQGRKE FQAEAELLMI VHHRNLVSLV GYCDDAKNMA
     LIYELMVNGN LRQHLSDQSC NAQVLTWNER LRITIDAAQG LDYLHNGCKP PIIHRDLKTL
     NILLNESRQA KIADFGLSKA FAAENDSSIS TRPAGTPGYL DPEYQSSGSL NRKSDVYSFG
     VILLELITGH PAMIRSASGS IHILHWATPI IERGDIHSIV DPRLDGKFSV NSAWKMVEIA
     MSCVQTTAVK RPDISCVLAE LKDCWAIETA SERSQMMGSS KSRSMGSFQM TSMAVDCDSL
     PFAR
//
DBGET integrated database retrieval system