ID B0WRX4_CULQU Unreviewed; 452 AA.
AC B0WRX4;
DT 08-APR-2008, integrated into UniProtKB/TrEMBL.
DT 08-APR-2008, sequence version 1.
DT 24-JAN-2024, entry version 86.
DE RecName: Full=Phosphatidate cytidylyltransferase {ECO:0000256|ARBA:ARBA00012487, ECO:0000256|PIRNR:PIRNR018269};
DE EC=2.7.7.41 {ECO:0000256|ARBA:ARBA00012487, ECO:0000256|PIRNR:PIRNR018269};
GN Name=6042325 {ECO:0000313|EnsemblMetazoa:CPIJ009904-PA};
GN ORFNames=CpipJ_CPIJ009904 {ECO:0000313|EMBL:EDS33584.1};
OS Culex quinquefasciatus (Southern house mosquito) (Culex pungens).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC Culicinae; Culicini; Culex; Culex.
OX NCBI_TaxID=7176;
RN [1] {ECO:0000313|EMBL:EDS33584.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JHB {ECO:0000313|EMBL:EDS33584.1};
RG The Broad Institute Genome Sequencing Platform;
RA Atkinson P.W., Hemingway J., Christensen B.M., Higgs S., Kodira C.,
RA Hannick L., Megy K., O'Leary S., Pearson M., Haas B.J., Mauceli E.,
RA Wortman J.R., Lee N.H., Guigo R., Stanke M., Alvarado L., Amedeo P.,
RA Antoine C.H., Arensburger P., Bidwell S.L., Crawford M., Camaro F.,
RA Devon K., Engels R., Hammond M., Howarth C., Koehrsen M., Lawson D.,
RA Montgomery P., Nene V., Nusbaum C., Puiu D., Romero-Severson J.,
RA Severson D.W., Shumway M., Sisk P., Stolte C., Zeng Q., Eisenstadt E.,
RA Fraser-Liggett C., Strausberg R., Galagan J., Birren B., Collins F.H.;
RT "Annotation of Culex pipiens quinquefasciatus.";
RL Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblMetazoa:CPIJ009904-PA}
RP IDENTIFICATION.
RC STRAIN=JHB {ECO:0000313|EnsemblMetazoa:CPIJ009904-PA};
RG EnsemblMetazoa;
RL Submitted (FEB-2021) to UniProtKB.
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|ARBA:ARBA00001698,
CC ECO:0000256|PIRNR:PIRNR018269, ECO:0000256|RuleBase:RU003938};
CC -!- PATHWAY: Lipid metabolism. {ECO:0000256|ARBA:ARBA00005189}.
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|PIRNR:PIRNR018269,
CC 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|PIRNR:PIRNR018269, ECO:0000256|RuleBase:RU003938}.
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DR EMBL; DS232062; EDS33584.1; -; Genomic_DNA.
DR RefSeq; XP_001851458.1; XM_001851406.1.
DR AlphaFoldDB; B0WRX4; -.
DR STRING; 7176.B0WRX4; -.
DR EnsemblMetazoa; CPIJ009904-RA; CPIJ009904-PA; CPIJ009904.
DR KEGG; cqu:CpipJ_CPIJ009904; -.
DR VEuPathDB; VectorBase:CPIJ009904; -.
DR VEuPathDB; VectorBase:CQUJHB017354; -.
DR eggNOG; KOG1440; Eukaryota.
DR HOGENOM; CLU_023471_0_1_1; -.
DR InParanoid; B0WRX4; -.
DR OMA; FFAYMYF; -.
DR OrthoDB; 5481516at2759; -.
DR UniPathway; UPA00557; UER00614.
DR Proteomes; UP000002320; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004605; F:phosphatidate cytidylyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0016024; P:CDP-diacylglycerol biosynthetic process; IEA:UniProtKB-UniRule.
DR InterPro; IPR000374; PC_trans.
DR InterPro; IPR016720; PC_Trfase_euk.
DR PANTHER; PTHR13773; PHOSPHATIDATE CYTIDYLYLTRANSFERASE; 1.
DR PANTHER; PTHR13773:SF8; PHOSPHATIDATE CYTIDYLYLTRANSFERASE, PHOTORECEPTOR-SPECIFIC; 1.
DR Pfam; PF01148; CTP_transf_1; 1.
DR PIRSF; PIRSF018269; PC_trans_euk; 1.
DR PROSITE; PS01315; CDS; 1.
PE 3: Inferred from homology;
KW Lipid biosynthesis {ECO:0000256|ARBA:ARBA00022516,
KW ECO:0000256|PIRNR:PIRNR018269};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098,
KW ECO:0000256|PIRNR:PIRNR018269};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|PIRNR:PIRNR018269};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695,
KW ECO:0000256|PIRNR:PIRNR018269};
KW Phospholipid biosynthesis {ECO:0000256|ARBA:ARBA00023209,
KW ECO:0000256|PIRNR:PIRNR018269};
KW Phospholipid metabolism {ECO:0000256|ARBA:ARBA00023264,
KW ECO:0000256|PIRNR:PIRNR018269};
KW Reference proteome {ECO:0000313|Proteomes:UP000002320};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR018269};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|PIRNR:PIRNR018269};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|PIRNR:PIRNR018269}.
FT TRANSMEM 90..109
FT /note="Helical"
FT /evidence="ECO:0000256|PIRNR:PIRNR018269"
FT TRANSMEM 145..162
FT /note="Helical"
FT /evidence="ECO:0000256|PIRNR:PIRNR018269"
FT TRANSMEM 189..207
FT /note="Helical"
FT /evidence="ECO:0000256|PIRNR:PIRNR018269"
FT TRANSMEM 219..236
FT /note="Helical"
FT /evidence="ECO:0000256|PIRNR:PIRNR018269"
FT TRANSMEM 242..268
FT /note="Helical"
FT /evidence="ECO:0000256|PIRNR:PIRNR018269"
FT TRANSMEM 280..302
FT /note="Helical"
FT /evidence="ECO:0000256|PIRNR:PIRNR018269"
FT TRANSMEM 348..370
FT /note="Helical"
FT /evidence="ECO:0000256|PIRNR:PIRNR018269"
FT REGION 1..53
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..33
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 452 AA; 52007 MW; 7ECD8F2873F970D4 CRC64;
MSAEAEIRRR NIGEGDSLGE SSLKPDDKGQ KPAQESTTAE SSDHIDSEEE KLPEEKYVEE
MSKTLPQGTN KTPEVLGQAL SGLPDRWRNW VIRGIFTWIM ISGFCLIIYG GPLALMITAL
AVQVKCFEEI ISIGYSVYRI HGLPWFRSLS WYFLVSSNYF FYGENLVDYF GVAVNRVDSL
RFLVKYHRFL SFCLYIIGFV WFVLSLVKRY YMKQFSLFAW THVALLIVVT QSYFIIQNIF
EGLIWFIVPV SMIVCNDVMA YMFGFFFGRT PLIKLSPKKT WEGFIGGGFA TVVFGLLFSY
WLCQFQYFVC PIEYSESAGR MTIECEPSYL FQPQEYSIGS TTITMYPFML HSLSLSIFSS
VIGPFGGFFA SGFKRAFKIK DFGDMIPGHG GIMDRFDCQF LMATFVNVYI SSFIPFNSTF
FLQVYSLKPE QQLQLFNQLK DNLEERNIIN LN
//
