ID A0A024VLA9_PLAFA Unreviewed; 667 AA.
AC A0A024VLA9;
DT 09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT 09-JUL-2014, sequence version 1.
DT 24-JAN-2024, entry version 33.
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=PFFCH_03312 {ECO:0000313|EMBL:ETW29262.1};
OS Plasmodium falciparum FCH/4.
OC Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Haemosporida;
OC Plasmodiidae; Plasmodium; Plasmodium (Laverania).
OX NCBI_TaxID=1036724 {ECO:0000313|EMBL:ETW29262.1, ECO:0000313|Proteomes:UP000030656};
RN [1] {ECO:0000313|EMBL:ETW29262.1, ECO:0000313|Proteomes:UP000030656}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FCH/4 {ECO:0000313|EMBL:ETW29262.1,
RC ECO:0000313|Proteomes:UP000030656};
RG The Broad Institute Genome Sequencing Platform;
RG The Broad Institute Genome Sequencing Center for Infectious Disease;
RA Neafsey D., Hoffman S., Volkman S., Rosenthal P., Walker B., Young S.K.,
RA Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W.,
RA Alvarado L., Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J.,
RA Goldberg J., Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A.,
RA Ireland A., Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W.,
RA Priest M., Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J.,
RA Nusbaum C., Birren B.;
RT "The Genome Annotation of Plasmodium falciparum FCH/4.";
RL Submitted (FEB-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ETW29262.1, ECO:0000313|Proteomes:UP000030656}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FCH/4 {ECO:0000313|EMBL:ETW29262.1,
RC ECO:0000313|Proteomes:UP000030656};
RG The Broad Institute Genome Sequencing Platform;
RG The Broad Institute Genome Sequencing Center for Infectious Disease;
RA Neafsey D., Cheeseman I., Volkman S., Adams J., Walker B., Young S.K.,
RA Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Dewar J., Goldberg J., Griggs A.,
RA Gujja S., Hansen M., Howarth C., Imamovic A., Larimer J., McCowan C.,
RA Murphy C., Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T.,
RA Sisk P., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Plasmodium falciparum FCH/4.";
RL Submitted (FEB-2013) to the EMBL/GenBank/DDBJ databases.
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|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|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; KI927981; ETW29262.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A024VLA9; -.
DR EnsemblProtists; ETW29262; ETW29262; PFFCH_03312.
DR UniPathway; UPA00557; UER00614.
DR Proteomes; UP000030656; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
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 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 PROSITE; PS01315; CDS; 1.
PE 3: Inferred from homology;
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 Phospholipid biosynthesis {ECO:0000256|ARBA:ARBA00023209};
KW Phospholipid metabolism {ECO:0000256|ARBA:ARBA00023264};
KW Reference proteome {ECO:0000313|Proteomes:UP000030656};
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 267..298
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 319..338
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 350..374
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 386..405
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 411..436
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 448..470
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 527..549
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT REGION 1..117
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 637..667
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..21
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 22..85
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 86..117
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 667 AA; 77990 MW; 030234D73B64D71F CRC64;
MPRKNSKTMT NKCANSNSND FIEDKVLDDK KRKKSTESST VDEKGDIIKR RSKSKSLDDS
NGGIENMDKV KVSNNNRKKK SETMINNDNN NDNDDIKSMN HMNSMTHTNS TNHTNNMDNM
DNMDNVNNMD DVNNMNNVNN MKNNINDEVY KLGSFEYEEE CKKRNIRNSE CKRRRNLKDM
KYFKDIKPLK DFVNLKNSNN NNNTNQHNSG IFSNFTRFYG YNNKNSFNSN RSKQSTCSNS
NLQNNMNLVN SESFESKLQT FKVRSQWTFI LILLYFIILA AGHFYCSILV LILVTTLYKE
IISLKSIENK DKKLPEIFYI RWYWFFLTIM TLGIPWVIPK LKHQIPLYKF LLTYHSINMF
ILAFVGFVWF ILSLRKFSLK YQFSQIGIIL LSSLFIVTQS LMHIANIYSG MIWFIVPVSS
VVINDIFAYV FGILFGKTRL IQLSPKKTVE GYVGSSIITI VWGILITYFL QRYKFFICPQ
KYITFQPFVS WNYIDCDINP IFQQKVYEVP KQISQILSIK NIYYSKMIFH GLMLSLFAAF
LAPFGGFFAS GFKRALKIKD FGKSIPGHGG VTDRFDCQIF IGMFTYIYMK TFVKIKGGIY
SYDLIIESIQ KLDHKEIIRL FNQLKNIVDK KRRKQCTDNN TNDIHTRKDK RSNIDKPCTD
KNKIPNK
//
