(data stored in SCRATCH zone)

SWISSPROT: Q757U6_ASHGO

ID   Q757U6_ASHGO            Unreviewed;       433 AA.
AC   Q757U6;
DT   05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2004, sequence version 1.
DT   11-DEC-2019, entry version 97.
DE   RecName: Full=Phosphatidate cytidylyltransferase {ECO:0000256|PIRNR:PIRNR018269, ECO:0000256|RuleBase:RU003938};
DE            EC=2.7.7.41 {ECO:0000256|PIRNR:PIRNR018269, ECO:0000256|RuleBase:RU003938};
GN   ORFNames=AGOS_AEL084W {ECO:0000313|EMBL:AAS52601.1};
OS   Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056)
OS   (Yeast) (Eremothecium gossypii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX   NCBI_TaxID=284811 {ECO:0000313|EMBL:AAS52601.1, ECO:0000313|Proteomes:UP000000591};
RN   [1] {ECO:0000313|EMBL:AAS52601.1, ECO:0000313|Proteomes:UP000000591}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056
RC   {ECO:0000313|Proteomes:UP000000591};
RX   PubMed=15001715; DOI=10.1126/science.1095781;
RA   Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S.,
RA   Mohr C., Pohlmann R., Luedi P., Choi S., Wing R.A., Flavier A.,
RA   Gaffney T.D., Philippsen P.;
RT   "The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces
RT   cerevisiae genome.";
RL   Science 304:304-307(2004).
RN   [2] {ECO:0000313|Proteomes:UP000000591}
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056
RC   {ECO:0000313|Proteomes:UP000000591};
RX   PubMed=23749448; DOI=10.1534/g3.112.002881;
RA   Dietrich F.S., Voegeli S., Kuo S., Philippsen P.;
RT   "Genomes of Ashbya fungi isolated from insects reveal four mating-type
RT   loci, numerous translocations, lack of transposons, and distinct gene
RT   duplications.";
RL   G3 (Bethesda) 3:1225-1239(2013).
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|PIRNR:PIRNR018269,
CC         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|PIRNR:PIRNR018269, ECO:0000256|RuleBase:RU003938}.
CC   -!- SIMILARITY: Belongs to the CDS family. {ECO:0000256|PIRNR:PIRNR018269,
CC       ECO:0000256|RuleBase:RU003938}.
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DR   EMBL; AE016818; AAS52601.1; -; Genomic_DNA.
DR   RefSeq; NP_984777.1; NM_210131.1.
DR   STRING; 33169.AAS52601; -.
DR   EnsemblFungi; AAS52601; AAS52601; AGOS_AEL084W.
DR   GeneID; 4620967; -.
DR   KEGG; ago:AGOS_AEL084W; -.
DR   HOGENOM; HOG000209582; -.
DR   InParanoid; Q757U6; -.
DR   KO; K00981; -.
DR   OMA; VVQAHFI; -.
DR   UniPathway; UPA00557; UER00614.
DR   Proteomes; UP000000591; Chromosome V.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IBA:GO_Central.
DR   GO; GO:0070319; C:Golgi to plasma membrane transport vesicle; IEA:EnsemblFungi.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-UniRule.
DR   GO; GO:0004605; F:phosphatidate cytidylyltransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0016024; P:CDP-diacylglycerol biosynthetic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0046488; P:phosphatidylinositol metabolic process; IEA:EnsemblFungi.
DR   GO; GO:0006658; P:phosphatidylserine metabolic process; IEA:EnsemblFungi.
DR   InterPro; IPR000374; PC_trans.
DR   InterPro; IPR016720; PC_Trfase_euk.
DR   PANTHER; PTHR13773; PTHR13773; 1.
DR   PIRSF; PIRSF018269; PC_trans_euk; 1.
DR   PROSITE; PS01315; CDS; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q757U6.
DR   SWISS-2DPAGE; Q757U6.
KW   Lipid biosynthesis {ECO:0000256|PIRNR:PIRNR018269};
KW   Lipid metabolism {ECO:0000256|PIRNR:PIRNR018269};
KW   Membrane {ECO:0000256|PIRNR:PIRNR018269};
KW   Nucleotidyltransferase {ECO:0000256|PIRNR:PIRNR018269,
KW   ECO:0000256|RuleBase:RU003938};
KW   Phospholipid biosynthesis {ECO:0000256|PIRNR:PIRNR018269};
KW   Phospholipid metabolism {ECO:0000256|PIRNR:PIRNR018269};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000591};
KW   Transferase {ECO:0000256|PIRNR:PIRNR018269, ECO:0000256|RuleBase:RU003938};
KW   Transmembrane {ECO:0000256|PIRNR:PIRNR018269,
KW   ECO:0000256|RuleBase:RU003938};
KW   Transmembrane helix {ECO:0000256|PIRNR:PIRNR018269}.
FT   TRANSMEM        52..79
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|PIRNR:PIRNR018269"
FT   TRANSMEM        146..163
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|PIRNR:PIRNR018269"
FT   TRANSMEM        170..193
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|PIRNR:PIRNR018269"
FT   TRANSMEM        199..220
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|PIRNR:PIRNR018269"
FT   TRANSMEM        241..259
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|PIRNR:PIRNR018269"
FT   TRANSMEM        313..335
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|PIRNR:PIRNR018269"
FT   REGION          1..21
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..15
FT                   /note="Polyampholyte"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   433 AA;  49374 MW;  C4ED545D2B4AEAE2 CRC64;
     MTDKDSRKED MGENLTSDGE VASVKDKVAT NPNGDPRLLE DSKVYNFVVR TIWTLIMIAG
     FFITLAMGHF WCVILILGCQ IATFQECIAV TAESGREKNL PLTRTLNWYF LFTTIYYLDG
     KSLYKLFRHY TINYRVLGFI AANHKFISYC MLVFGFVVFV CSLRKGFLKF QFASLCVTHM
     VLLLVVFQAH LIINNVLNGL IWFLLPCGLV IVNDIFAYLC GITFGRTKLI AISPKKTLEG
     FLGAWFFTGL AALVLTRLLT PYTYMTCPVQ NIHTNVFSPL NCETNPVFIP QTYRLPPIIF
     DRFNVSTITF KPIYMHAFNL ATFASLFAPF GGFFASGLKR TFKVKDFGHS IPGHGGITDR
     VDCQFMMGSF MNLYYETFIS EKRITVETVL STILMNFDER QILQLIAALN RVLWENGKMA
     GDNYERISEL YNI
//

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