UniProt: W6LE03

Database: UniProt
Entry: W6LE03_9TRYP

LinkDB:  W6LE03_9TRYP 
Original site:  W6LE03_9TRYP

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Ontology (3)   
   GO (3)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (3)   
   InterPro (1)   
   Pfam (1)   
   PROSITE (1)   
Literature (1)   
   PubMed (1)   
All databases (9)   

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ID   W6LE03_9TRYP            Unreviewed;       469 AA.
AC   W6LE03;
DT   16-APR-2014, integrated into UniProtKB/TrEMBL.
DT   16-APR-2014, sequence version 1.
DT   27-MAR-2024, entry version 32.
DE   RecName: Full=Phosphatidate cytidylyltransferase {ECO:0000256|ARBA:ARBA00012487, ECO:0000256|RuleBase:RU003938};
DE            EC=2.7.7.41 {ECO:0000256|ARBA:ARBA00012487, ECO:0000256|RuleBase:RU003938};
GN   ORFNames=GSHART1_T00004324001 {ECO:0000313|EMBL:CCW67751.1};
OS   Phytomonas sp. Hart1.
OC   Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC   Trypanosomatida; Trypanosomatidae; Phytomonas.
OX   NCBI_TaxID=223615 {ECO:0000313|EMBL:CCW67751.1, ECO:0000313|Proteomes:UP000053358};
RN   [1] {ECO:0000313|EMBL:CCW67751.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Hart1 {ECO:0000313|EMBL:CCW67751.1};
RA   Genoscope - CEA;
RL   Submitted (MAY-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:CCW67751.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Hart1 {ECO:0000313|EMBL:CCW67751.1};
RX   PubMed=24516393; DOI=10.1371/journal.pgen.1004007;
RA   Porcel B.M., Denoeud F., Opperdoes F., Noel B., Madoui M.A.,
RA   Hammarton T.C., Field M.C., Da Silva C., Couloux A., Poulain J.,
RA   Katinka M., Jabbari K., Aury J.M., Campbell D.A., Cintron R., Dickens N.J.,
RA   Docampo R., Sturm N.R., Koumandou V.L., Fabre S., Flegontov P., Lukes J.,
RA   Michaeli S., Mottram J.C., Szoor B., Zilberstein D., Bringaud F.,
RA   Wincker P., Dollet M.;
RT   "The Streamlined Genome of Phytomonas spp. Relative to Human Pathogenic
RT   Kinetoplastids Reveals a Parasite Tailored for Plants.";
RL   PLoS Genet. 10:e1004007-e1004007(2014).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 1,2-diacyl-sn-glycero-3-phosphate + CTP + H(+) = a CDP-1,2-
CC         diacyl-sn-glycerol + diphosphate; Xref=Rhea:RHEA:16229,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:33019, ChEBI:CHEBI:37563,
CC         ChEBI:CHEBI:58332, ChEBI:CHEBI:58608; EC=2.7.7.41;
CC         Evidence={ECO:0000256|RuleBase:RU003938};
CC   -!- PATHWAY: Phospholipid metabolism; CDP-diacylglycerol biosynthesis; CDP-
CC       diacylglycerol from sn-glycerol 3-phosphate: step 3/3.
CC       {ECO:0000256|ARBA:ARBA00005119, ECO:0000256|RuleBase:RU003938}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC   -!- SIMILARITY: Belongs to the CDS family. {ECO:0000256|ARBA:ARBA00010185,
CC       ECO:0000256|RuleBase:RU003938}.
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DR   EMBL; HF955201; CCW67751.1; -; Genomic_DNA.
DR   AlphaFoldDB; W6LE03; -.
DR   EnsemblProtists; CCW67751; CCW67751; GSHART1_T00004324001.
DR   OrthoDB; 168087at2759; -.
DR   UniPathway; UPA00557; UER00614.
DR   Proteomes; UP000053358; Unassembled WGS sequence.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR   GO; GO:0004605; F:phosphatidate cytidylyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0016024; P:CDP-diacylglycerol biosynthetic process; IEA:UniProtKB-UniPathway.
DR   InterPro; IPR000374; PC_trans.
DR   PANTHER; PTHR46382; PHOSPHATIDATE CYTIDYLYLTRANSFERASE; 1.
DR   PANTHER; PTHR46382:SF1; PHOSPHATIDATE CYTIDYLYLTRANSFERASE; 1.
DR   Pfam; PF01148; CTP_transf_1; 1.
DR   PROSITE; PS01315; CDS; 1.
PE   3: Inferred from homology;
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW   Lipid biosynthesis {ECO:0000256|ARBA:ARBA00022516};
KW   Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695,
KW   ECO:0000256|RuleBase:RU003938};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053358};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU003938};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW   ECO:0000256|RuleBase:RU003938};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        6..39
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        148..168
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        235..255
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        261..282
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        363..385
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        401..421
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
SQ   SEQUENCE   469 AA;  52324 MW;  856B6132CAC54C1B CRC64;
     MQTRTITILT MGPLCIFFLT WSKHTATLLV LACLFIGGLE WSGLKRHLKV ALLAPNEFLN
     RTSPMKLEGV PQGKFSKADH SVEHKTMYSG SYNSRSSSRY LSPPLSFPDG IPLTPKEYAV
     PVIPLSAYSI FKYLGWSLLA LAASHCEAVY VTVFALYILI FVCVTLMARS RLRDNVECAV
     ELLTSWFCSG IIEPKGSDPN LSMEKTSKDA QQRYFLLLEL HVISERQPAE QFLDICLDFF
     GVMWLSGLVF FLFLYDVPRL GLPWFTSVLL SNFFNDITAL LVGNGIRKLR TKYSHIYDST
     LNVDSSDCYF DKKASTKCRP ELQSGGNGKK KLRSDSSFFV RYILSSPHSL CPTISPNKSI
     EGAVFGVIMN AISFSASLYF CYRFVLDYPD VNIISPKFQS ISVWFVLGIF VGIAGVLGDL
     LQSLLKRVAR VKDTGIIIPG HGGILDRIDG VLLAFPFTYC ALSVLRALS
//

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