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Database: UniProt
Entry: G1QR39_NOMLE
LinkDB: G1QR39_NOMLE
Original site: G1QR39_NOMLE 
ID   G1QR39_NOMLE            Unreviewed;       716 AA.
AC   G1QR39;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   28-FEB-2018, sequence version 2.
DT   27-MAR-2024, entry version 82.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSNLEP00000003407.2};
GN   Name=PRKD2 {ECO:0000313|Ensembl:ENSNLEP00000003407.2};
OS   Nomascus leucogenys (Northern white-cheeked gibbon) (Hylobates leucogenys).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hylobatidae;
OC   Nomascus.
OX   NCBI_TaxID=61853 {ECO:0000313|Ensembl:ENSNLEP00000003407.2, ECO:0000313|Proteomes:UP000001073};
RN   [1] {ECO:0000313|Ensembl:ENSNLEP00000003407.2, ECO:0000313|Proteomes:UP000001073}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG   Gibbon Genome Sequencing Consortium;
RL   Submitted (OCT-2012) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSNLEP00000003407.2}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946};
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004370}.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. CAMK Ser/Thr
CC       protein kinase family. PKD subfamily. {ECO:0000256|ARBA:ARBA00008582}.
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DR   EMBL; ADFV01102176; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; ADFV01102177; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; ADFV01102178; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; ADFV01102179; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; ADFV01102180; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; ADFV01102181; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; ADFV01102182; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; ADFV01102183; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; ADFV01102184; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; ADFV01102185; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   AlphaFoldDB; G1QR39; -.
DR   STRING; 61853.ENSNLEP00000003407; -.
DR   Ensembl; ENSNLET00000003574.3; ENSNLEP00000003407.2; ENSNLEG00000002792.3.
DR   eggNOG; KOG4236; Eukaryota.
DR   GeneTree; ENSGT00950000183024; -.
DR   HOGENOM; CLU_009772_1_0_1; -.
DR   InParanoid; G1QR39; -.
DR   OMA; WVVHYSS; -.
DR   TreeFam; TF314320; -.
DR   Proteomes; UP000001073; Chromosome 17.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004697; F:diacylglycerol-dependent serine/threonine kinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:2000573; P:positive regulation of DNA biosynthetic process; IEA:Ensembl.
DR   GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; IEA:Ensembl.
DR   GO; GO:0032743; P:positive regulation of interleukin-2 production; IEA:Ensembl.
DR   GO; GO:0050862; P:positive regulation of T cell receptor signaling pathway; IEA:Ensembl.
DR   GO; GO:0036211; P:protein modification process; IEA:UniProt.
DR   CDD; cd20795; C1_PKD_rpt1; 1.
DR   CDD; cd01239; PH_PKD; 1.
DR   CDD; cd14082; STKc_PKD; 1.
DR   Gene3D; 3.30.60.20; -; 1.
DR   Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR046349; C1-like_sf.
DR   InterPro; IPR020454; DAG/PE-bd.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR002219; PE/DAG-bd.
DR   InterPro; IPR011993; PH-like_dom_sf.
DR   InterPro; IPR001849; PH_domain.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   PANTHER; PTHR22968; PROTEIN KINASE C, MU; 1.
DR   PANTHER; PTHR22968:SF12; SERINE_THREONINE-PROTEIN KINASE D2; 1.
DR   Pfam; PF00130; C1_1; 1.
DR   Pfam; PF00169; PH; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   PRINTS; PR00008; DAGPEDOMAIN.
DR   SMART; SM00109; C1; 1.
DR   SMART; SM00233; PH; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF57889; Cysteine-rich domain; 1.
DR   SUPFAM; SSF50729; PH domain-like; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS50003; PH_DOMAIN; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
DR   PROSITE; PS00479; ZF_DAG_PE_1; 1.
DR   PROSITE; PS50081; ZF_DAG_PE_2; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW   ProRule:PRU10141}; Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000001073};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   DOMAIN          138..188
FT                   /note="Phorbol-ester/DAG-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50081"
FT   DOMAIN          271..383
FT                   /note="PH"
FT                   /evidence="ECO:0000259|PROSITE:PS50003"
FT   DOMAIN          425..690
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   REGION          1..35
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          217..247
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        13..35
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         454
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   716 AA;  78988 MW;  04A61ADFA88BDA22 CRC64;
     MAATSSYPAG LPGSPGPGSP PPPGGLELQS PPPLLPQIPA PGSGVSFHIQ IGLTREFVLL
     PAASELAHVK QLACSIVDQK FPECGFYGLY DKILLFKHDP TSANLLQLVR SAGDIQEGDL
     VEVVLSASAT FEDFQIRPHA LTVHSYRAPA FCDHCGEMLF GLVRQGLKCD DCKFNCHKRC
     ATRVPNDCLG EALINGDVPM EEATDFSEAD KSALMDESED SGVIPGSHSE NALHASEEEE
     GEGGKAQSSL GYIPLMRVVQ SVRHTTRKSS TTLREGWVVH YSNKDTLRKR HYWRLDCKCI
     TLFQNNTTNR YYKEIPLSEI LTVESAQNFS LVPPGTNPHC FEIVTANATY FVGEMPGGAP
     GGPSGQGAEA ARGWETAIRQ ALMPVILQDA PSAPGHAPHR QASLSISVSN SQIQENVDIA
     TVYQIFPDEV LGSGQFGVVY GGKHRKTGRD VAVKVIDKLR FPTKESQLRN EVSILQSLRH
     PGIVNLECMF ETPEKVFVVM EKLHGDMLEM ILSSEKGRLP ERLTKFLITQ ILVALRHLHF
     KNIVHCDLKP ENVLLASADP FPQVKLCDFG FARIIGEKSF RRSVVGTPAY LAPEVLLNQG
     YNRSLDMWSV GVIMYVSLSG TFPFNEDEDI NDQIQNAAFM YPASPWSHIS AGGAWGAPTP
     WAAIDLINNL LQVKMRKRYS VDKSLSHPWL QEYQTWLDLR ELEGKMGERY ITHESD
//
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