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Database: UniProt
Entry: A0A158QD55_HYMDI
LinkDB: A0A158QD55_HYMDI
Original site: A0A158QD55_HYMDI 
ID   A0A158QD55_HYMDI        Unreviewed;       990 AA.
AC   A0A158QD55;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   03-JUL-2019, entry version 16.
DE   RecName: Full=Diacylglycerol kinase {ECO:0000256|RuleBase:RU361128};
DE            Short=DAG kinase {ECO:0000256|RuleBase:RU361128};
DE            EC=2.7.1.107 {ECO:0000256|RuleBase:RU361128};
OS   Hymenolepis diminuta (Rat tapeworm).
OC   Eukaryota; Metazoa; Platyhelminthes; Cestoda; Eucestoda;
OC   Cyclophyllidea; Hymenolepididae; Hymenolepis.
OX   NCBI_TaxID=6216 {ECO:0000313|Proteomes:UP000046397, ECO:0000313|WBParaSite:HDID_0000246301-mRNA-1};
RN   [1] {ECO:0000313|Proteomes:UP000046397, ECO:0000313|WBParaSite:HDID_0000246301-mRNA-1}
RP   NUCLEOTIDE SEQUENCE.
RG   Helminth Genomes Consortium;
RL   Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|WBParaSite:HDID_0000246301-mRNA-1}
RP   IDENTIFICATION.
RG   WormBaseParasite;
RL   Submitted (APR-2016) to UniProtKB.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 1,2-diacyl-sn-glycerol + ATP = a 1,2-diacyl-sn-glycero-
CC         3-phosphate + ADP + H(+); Xref=Rhea:RHEA:10272,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:17815, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:58608, ChEBI:CHEBI:456216; EC=2.7.1.107;
CC         Evidence={ECO:0000256|RuleBase:RU361128};
CC   -!- SIMILARITY: Belongs to the eukaryotic diacylglycerol kinase
CC       family. {ECO:0000256|RuleBase:RU361128}.
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DR   WBParaSite; HDID_0000246301-mRNA-1; HDID_0000246301-mRNA-1; HDID_0000246301.
DR   Proteomes; UP000046397; Genome Assembly.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004143; F:diacylglycerol kinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0003951; F:NAD+ kinase activity; IEA:InterPro.
DR   GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR   GO; GO:0007205; P:protein kinase C-activating G protein-coupled receptor signaling pathway; IEA:InterPro.
DR   CDD; cd00029; C1; 1.
DR   Gene3D; 3.40.50.10330; -; 1.
DR   InterPro; IPR017438; ATP-NAD_kinase_N.
DR   InterPro; IPR037607; DGK.
DR   InterPro; IPR000756; Diacylglycerol_kin_accessory.
DR   InterPro; IPR001206; Diacylglycerol_kinase_cat_dom.
DR   InterPro; IPR016064; NAD/diacylglycerol_kinase_sf.
DR   InterPro; IPR002219; PE/DAG-bd.
DR   InterPro; IPR000159; RA_dom.
DR   InterPro; IPR029071; Ubiquitin-like_domsf.
DR   PANTHER; PTHR11255; PTHR11255; 2.
DR   Pfam; PF00130; C1_1; 1.
DR   Pfam; PF00609; DAGK_acc; 1.
DR   Pfam; PF00781; DAGK_cat; 1.
DR   Pfam; PF00788; RA; 2.
DR   SMART; SM00109; C1; 2.
DR   SMART; SM00045; DAGKa; 1.
DR   SMART; SM00046; DAGKc; 1.
DR   SMART; SM00314; RA; 2.
DR   SUPFAM; SSF111331; SSF111331; 1.
DR   SUPFAM; SSF54236; SSF54236; 1.
DR   PROSITE; PS50146; DAGK; 1.
DR   PROSITE; PS50200; RA; 1.
DR   PROSITE; PS00479; ZF_DAG_PE_1; 2.
DR   PROSITE; PS50081; ZF_DAG_PE_2; 2.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|RuleBase:RU361128};
KW   Complete proteome {ECO:0000313|Proteomes:UP000046397};
KW   Kinase {ECO:0000256|RuleBase:RU361128};
KW   Nucleotide-binding {ECO:0000256|RuleBase:RU361128};
KW   Reference proteome {ECO:0000313|Proteomes:UP000046397};
KW   Transferase {ECO:0000256|RuleBase:RU361128}.
FT   DOMAIN        6     54       Phorbol-ester/DAG-type.
FT                                {ECO:0000259|PROSITE:PS50081}.
FT   DOMAIN      243    294       Phorbol-ester/DAG-type.
FT                                {ECO:0000259|PROSITE:PS50081}.
FT   DOMAIN      367    458       Ras-associating. {ECO:0000259|PROSITE:
FT                                PS50200}.
FT   DOMAIN      676    814       DAGKc. {ECO:0000259|PROSITE:PS50146}.
FT   REGION      108    132       Disordered. {ECO:0000256|MobiDB-lite:
FT                                A0A158QD55}.
FT   REGION      187    232       Disordered. {ECO:0000256|MobiDB-lite:
FT                                A0A158QD55}.
FT   COMPBIAS    108    130       Polar. {ECO:0000256|MobiDB-lite:
FT                                A0A158QD55}.
FT   COMPBIAS    187    205       Polar. {ECO:0000256|MobiDB-lite:
FT                                A0A158QD55}.
FT   COMPBIAS    215    232       Pro-rich. {ECO:0000256|MobiDB-lite:
FT                                A0A158QD55}.
SQ   SEQUENCE   990 AA;  110061 MW;  8F2BB310C7FA30CF CRC64;
     LQDPMAHCWS EVGHFKRKFC NVCRKRLDDL LSVRCEICEY YTHYECLEFV SADCKVCSIS
     TPSKDKERSP TLIRKPSVPM PFQGISQFCN LTDIPELNSA LEMITGSTNS GGAGTESAAT
     NTSGITSDPF VPSRPGTGGM AAFAAYAMRS AAIQAAAAAT NVITTAATTT ATSCSVNSAG
     AFSPSISNTA TTSSSPLSPL TQSAGLGGNV GMGAPSNPPP SPVSPQAPPP LPFTITPQID
     RPVHHWREGN LPANSKCSSC KKTCWSAECL TGMRCEWCGV TVHYTCFRNL PVECDYGSLR
     DIMLPPQAVS IPRTSLLMEH IIGLPKPQPD FFPGFPALMD EFTSSGESLE ESGFDRRANR
     DKTDRDFDDY VRVYDGMDRY RRHQCRYLSL GKNVSVRKVI ELSLKAFQLP PDEENDFYLV
     EINERDGSEH RLDSNTSFKR QLQFETRRPQ IILRYVEREE NRDYINVYPG SLTYAYSSQS
     LSESAFDSAF LSHCREYADI SVPSIQVSIT PETSAHDVLV LSLHRLGVGY LDAKKFNLVE
     TVVDRGLVER VLHPTDRPWE IIDNVRLESV RALRLTRFYI RSVKDPYGQG VSLFVGNLKK
     GLSQRLYEII LLERLGYQNK WDAIEVIYYD FGSLVVIYSN AEKADEAYRL LKNSTFEDRP
     ILAMILPRIK PEFILEGTQP LLVFVNVKSG GCQGLELITS FRKLLNPHQV FNLDNGGPLP
     GLHCFRHLFR FKILVCGGDG TVGWALSCLD NVGQDAACPT PPMAILPIGT GNDLARVLHW
     GPGYTGTEDP LQILRDVVEA EEIRLDRWTV VIKPDQVESD AQKKQLQIEA NACNTNEDTS
     RIFVMNNYFG LGIDADLNLD FHLAREENPA KFNSRIHNKS VYFKMGLRKM VNQTKCKDLH
     QNVLIEVDGK QLDLPPIEGI IILNILSWGA GANPWGMEKD EAFAKPTHYD GLLEVVGVTG
     VVHMGQIFSG LRTGTRLAQG GHVRSWSCFK
//
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