GenomeNet

Database: UniProt
Entry: A0A0V0YCJ2_TRIPS
LinkDB: A0A0V0YCJ2_TRIPS
Original site: A0A0V0YCJ2_TRIPS 
ID   A0A0V0YCJ2_TRIPS        Unreviewed;       734 AA.
AC   A0A0V0YCJ2;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   27-MAR-2024, entry version 28.
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};
DE   Flags: Fragment;
GN   Name=Dgkq {ECO:0000313|EMBL:KRX97481.1};
GN   ORFNames=T4E_5600 {ECO:0000313|EMBL:KRX97481.1};
OS   Trichinella pseudospiralis (Parasitic roundworm).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC   Trichinellida; Trichinellidae; Trichinella.
OX   NCBI_TaxID=6337 {ECO:0000313|EMBL:KRX97481.1, ECO:0000313|Proteomes:UP000054815};
RN   [1] {ECO:0000313|EMBL:KRX97481.1, ECO:0000313|Proteomes:UP000054815}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ISS141 {ECO:0000313|EMBL:KRX97481.1};
RA   Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT   "Evolution of Trichinella species and genotypes.";
RL   Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 1,2-diacyl-sn-glycerol + ATP = a 1,2-diacyl-sn-glycero-3-
CC         phosphate + ADP + H(+); Xref=Rhea:RHEA:10272, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:17815, ChEBI:CHEBI:30616, ChEBI:CHEBI:58608,
CC         ChEBI:CHEBI:456216; EC=2.7.1.107;
CC         Evidence={ECO:0000256|ARBA:ARBA00001383,
CC         ECO:0000256|RuleBase:RU361128};
CC   -!- SIMILARITY: Belongs to the eukaryotic diacylglycerol kinase family.
CC       {ECO:0000256|ARBA:ARBA00009280, ECO:0000256|RuleBase:RU361128}.
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:KRX97481.1}.
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; JYDU01000031; KRX97481.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0V0YCJ2; -.
DR   Proteomes; UP000054815; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004143; F:ATP-dependent diacylglycerol kinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   GO; GO:0007205; P:protein kinase C-activating G protein-coupled receptor signaling pathway; IEA:InterPro.
DR   Gene3D; 2.60.200.40; -; 1.
DR   Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR000073; AB_hydrolase_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   PANTHER; PTHR11255; DIACYLGLYCEROL KINASE; 1.
DR   PANTHER; PTHR11255:SF54; DIACYLGLYCEROL KINASE THETA; 1.
DR   Pfam; PF00561; Abhydrolase_1; 1.
DR   Pfam; PF00609; DAGK_acc; 1.
DR   Pfam; PF00781; DAGK_cat; 1.
DR   PRINTS; PR00111; ABHYDROLASE.
DR   SMART; SM00045; DAGKa; 1.
DR   SMART; SM00046; DAGKc; 1.
DR   SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
DR   SUPFAM; SSF111331; NAD kinase/diacylglycerol kinase-like; 1.
DR   PROSITE; PS50146; DAGK; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU361128};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|RuleBase:RU361128};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU361128};
KW   Reference proteome {ECO:0000313|Proteomes:UP000054815};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU361128}.
FT   DOMAIN          64..202
FT                   /note="DAGKc"
FT                   /evidence="ECO:0000259|PROSITE:PS50146"
FT   REGION          411..452
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        420..452
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:KRX97481.1"
SQ   SEQUENCE   734 AA;  81497 MW;  A42CDFC0409AD3C2 CRC64;
     LFAFQARPFS AIGPIYFEYG SLVMTFNSPK VATKVCLKLQ DVSYEERKLL VLCLPNIQAH
     MIPADVEPLV VLVNMRSGGC QGADLIRSFR KLLNPFQVFD VMNGGPLVAL YVFRNVPKYK
     ILVCGGDGTA GWVLQCLDIV GQDSVCSSPP CALLPLGTGN DLARVLRWGS GYTGQEDPLQ
     ILKDIIEADE VRLDRWTVVF HPQEPSSELS CALEQNPDRA LPMNNPEEQT SMIIMNNYFG
     IGLDAEVCLG FDKARKLNPD KFNSRIHNKG VYARIGLKKM VNRKLCRDIQ RKIKLEVDGR
     VFELPSLEGI IILNIMSWGS GSNPWGPEKE EVGFTKPNHD DGLLEVIGIT GIVHLGQMQA
     GFSSGIRLAQ GGHVKITTFT DMPVHVDGEP QMLPPGTFTI LKSALKATML KKSKNKRRQT
     TDANATTSTM TTTLQRESSS QAASLPSSLS SGPVLQAEPD DDYFLPLAYK TYFGRHDSSK
     GSLIILHGLF GHKGNWRSLG AALSQKLNRK VFAVDLRNHG DSPHHSSMTV PEMADDVIAL
     IKDLNIAGDQ LGIIGHSMGG KVAAHLALHQ PSLLGKLLLE DMIPKRIDQP QDKVLLCIKA
     LNQCELPQMD LTKARQTVYQ QLFSVIKDAE TTHFLLTSLM LDKHGKPVWK FNISAIENNL
     QEMFFYEIES KNTFEGPTFV VHGKRSDYVK PADVPFMLNF FPKLRFQCIA EAGHWVHADR
     PSEFLSAAVD FFRR
//
DBGET integrated database retrieval system