ID A0A218X9C3_PUNGR Unreviewed; 652 AA.
AC A0A218X9C3;
DT 27-SEP-2017, integrated into UniProtKB/TrEMBL.
DT 27-SEP-2017, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=non-specific serine/threonine protein kinase {ECO:0000256|ARBA:ARBA00012513};
DE EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
GN Name=LOC116192501 {ECO:0000313|RefSeq:XP_031376917.1};
GN ORFNames=CDL15_Pgr007314 {ECO:0000313|EMBL:OWM81276.1};
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:OWM81276.1, 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).
RN [2] {ECO:0000313|EMBL:OWM81276.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC TISSUE=Fresh leaf {ECO:0000313|EMBL:OWM81276.1};
RA Xu C.;
RT "The pomegranate genome and the genomics of punicalagin biosynthesis.";
RL Submitted (JUN-2017) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|RefSeq:XP_031376917.1}
RP IDENTIFICATION.
RC TISSUE=Leaf {ECO:0000313|RefSeq:XP_031376917.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
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DR EMBL; MTKT01002214; OWM81276.1; -; Genomic_DNA.
DR RefSeq; XP_031376917.1; XM_031521057.1.
DR OrthoDB; 294771at2759; -.
DR Proteomes; UP000197138; Unassembled WGS sequence.
DR Proteomes; UP000515151; Chromosome 1.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0030247; F:polysaccharide binding; IEA:InterPro.
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; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR011009; Kinase-like_dom_sf.
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 InterPro; IPR032872; WAK_assoc_C.
DR InterPro; IPR025287; WAK_GUB.
DR PANTHER; PTHR27002:SF844; CYSTEINE-RICH RECEPTOR-LIKE PROTEIN KINASE 27-RELATED; 1.
DR PANTHER; PTHR27002; RECEPTOR-LIKE SERINE/THREONINE-PROTEIN KINASE SD1-8; 1.
DR Pfam; PF13947; GUB_WAK_bind; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR Pfam; PF14380; WAK_assoc; 1.
DR SMART; SM00220; S_TKc; 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};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|RefSeq:XP_031376917.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Receptor {ECO:0000313|RefSeq:XP_031376917.1};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Signal {ECO:0000256|SAM:SignalP};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..652
FT /note="non-specific serine/threonine protein kinase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5041166280"
FT TRANSMEM 261..282
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 321..595
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 617..652
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 617..643
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 349
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 652 AA; 73635 MW; 0A86697708E30989 CRC64;
MMSSFFFSFL FFTVLVLPLQ YGDASEGNDQ YLECSRRFVC GDNINVTYPF WGEDRPWHCG
LEGFQLLCEG ESTSMVFEEQ RYRVFNINQT DRTMNLSRDD LVKDPCLYDH YPNTTIDNHT
LLHYSETVQN ISIFYGCSDP DSDPSTKMIG EFSCPYPGDP AAVAIFKENP LSERPHPELN
SCRTHIKVPV LRSSEMLRFF LSGFVMEYSV DEACSGCELS NGICGRTNGS SYGFSCYCND
KPYPISCPHR DGNSNNTVRT VIVVVAPIAA ACLLASILYV YFRRVRKPFE CVERNAAMDE
ITTAESLQYD FETVRAATNN FSEENKLGQG GFGAVYRGKL ANGQEIAVKR LSRGLGQGDQ
EFKTEVLLVA RLQHRNLVRL LGFCVSGDER LLIYEFLPNS SLDRFIFDPV KRPQLDWQWR
QMIIGGVARG LVYLHEDSRL RIIHRDLKAS NVLLDANMTP KISDFGLARL FRVDATHMAT
SRIVGTYGYM APEYALYGQF SLKSDVFSFG VLVLEIVSGQ RWNCFRNGET IEDLLAIVWR
NWREGTVSNI MDPSLRDGPR TEMQRCIHIG LLCVQEHAAN RPNMVSVLLM LNSFSISLPV
PSQPALYMQS NMDSSVPFSA MNNSRETRPD GSESKSLGGS INEASITDVY PR
//
