ID A0A067BSE1_SAPPC Unreviewed; 444 AA.
AC A0A067BSE1;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 24-JAN-2024, entry version 44.
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 ORFNames=SPRG_14247 {ECO:0000313|EMBL:KDO19720.1};
OS Saprolegnia parasitica (strain CBS 223.65).
OC Eukaryota; Sar; Stramenopiles; Oomycota; Saprolegniales; Saprolegniaceae;
OC Saprolegnia.
OX NCBI_TaxID=695850 {ECO:0000313|EMBL:KDO19720.1, ECO:0000313|Proteomes:UP000030745};
RN [1] {ECO:0000313|EMBL:KDO19720.1, ECO:0000313|Proteomes:UP000030745}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 223.65 {ECO:0000313|EMBL:KDO19720.1,
RC ECO:0000313|Proteomes:UP000030745};
RX PubMed=23785293;
RA Jiang R.H., de Bruijn I., Haas B.J., Belmonte R., Lobach L., Christie J.,
RA van den Ackerveken G., Bottin A., Bulone V., Diaz-Moreno S.M., Dumas B.,
RA Fan L., Gaulin E., Govers F., Grenville-Briggs L.J., Horner N.R.,
RA Levin J.Z., Mammella M., Meijer H.J., Morris P., Nusbaum C., Oome S.,
RA Phillips A.J., van Rooyen D., Rzeszutek E., Saraiva M., Secombes C.J.,
RA Seidl M.F., Snel B., Stassen J.H., Sykes S., Tripathy S., van den Berg H.,
RA Vega-Arreguin J.C., Wawra S., Young S.K., Zeng Q., Dieguez-Uribeondo J.,
RA Russ C., Tyler B.M., van West P.;
RT "Distinctive expansion of potential virulence genes in the genome of the
RT oomycete fish pathogen Saprolegnia parasitica.";
RL PLoS Genet. 9:E1003272-E1003272(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|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; KK583337; KDO19720.1; -; Genomic_DNA.
DR RefSeq; XP_012209579.1; XM_012354189.1.
DR AlphaFoldDB; A0A067BSE1; -.
DR STRING; 695850.A0A067BSE1; -.
DR EnsemblProtists; KDO19720; KDO19720; SPRG_14247.
DR GeneID; 24136062; -.
DR KEGG; spar:SPRG_14247; -.
DR VEuPathDB; FungiDB:SPRG_14247; -.
DR OMA; FFAYMYF; -.
DR OrthoDB; 5481516at2759; -.
DR UniPathway; UPA00557; UER00614.
DR Proteomes; UP000030745; 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:UP000030745};
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 70..87
FT /note="Helical"
FT /evidence="ECO:0000256|PIRNR:PIRNR018269"
FT TRANSMEM 93..113
FT /note="Helical"
FT /evidence="ECO:0000256|PIRNR:PIRNR018269"
FT TRANSMEM 125..143
FT /note="Helical"
FT /evidence="ECO:0000256|PIRNR:PIRNR018269"
FT TRANSMEM 163..186
FT /note="Helical"
FT /evidence="ECO:0000256|PIRNR:PIRNR018269"
FT TRANSMEM 198..220
FT /note="Helical"
FT /evidence="ECO:0000256|PIRNR:PIRNR018269"
FT TRANSMEM 226..249
FT /note="Helical"
FT /evidence="ECO:0000256|PIRNR:PIRNR018269"
FT TRANSMEM 269..287
FT /note="Helical"
FT /evidence="ECO:0000256|PIRNR:PIRNR018269"
FT TRANSMEM 339..361
FT /note="Helical"
FT /evidence="ECO:0000256|PIRNR:PIRNR018269"
FT REGION 1..34
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 7..25
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 444 AA; 51552 MW; F6C23C42FBC2AACC CRC64;
MSSGAVVRRR REAKPRRRDE TDESSDSMVE QPATGWREPR WDFTTKAKDV TLLVDEDKAK
KWQSFKTRTI YTLLMIVAFL GIVFGLKQPG CCALVFVLQA IMYGELVALM FKHQVENEMP
MFRRLYYYWF LVCTFFVYGR ALMPHFEVHE FDRVFGLYFL EKGFIVQHHT AISFALYVVG
FVSFVFSLRK RKHYKYQFSQ FAFCHVALLM IVAQSTFMIS NMFEGLIWFL LPCSLIIVND
VFAYIFGFFW GRTPLIPKLS PKKTWEGFIG AYGATVLWSM GFSRFMAQYE MMVCPQVGFH
LAFKSCTPAQ IFVPLPLQAY PTLSQYVPEM LHDVTIAPIQ YHMVFFAIFA SIVAPFGGFF
ASGFKRAFKI KDFGTSIPGH GGVVDRMDCQ IIMGMFTFVY FTNFIQRPDR VSNILRVLER
LTNEEQLVVF QKFQHLLLES GILD
//
