ID G3J7Y8_CORMM Unreviewed; 458 AA.
AC G3J7Y8;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 24-JAN-2024, entry version 54.
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=CCM_01859 {ECO:0000313|EMBL:EGX97199.1};
OS Cordyceps militaris (strain CM01) (Caterpillar fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Cordycipitaceae; Cordyceps.
OX NCBI_TaxID=983644 {ECO:0000313|EMBL:EGX97199.1, ECO:0000313|Proteomes:UP000001610};
RN [1] {ECO:0000313|EMBL:EGX97199.1, ECO:0000313|Proteomes:UP000001610}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CM01 {ECO:0000313|EMBL:EGX97199.1,
RC ECO:0000313|Proteomes:UP000001610};
RX PubMed=22112802; DOI=10.1186/gb-2011-12-11-r116;
RA Zheng P., Xia Y., Xiao G., Xiong C., Hu X., Zhang S., Zheng H., Huang Y.,
RA Zhou Y., Wang S., Zhao G.P., Liu X., St Leger R.J., Wang C.;
RT "Genome sequence of the insect pathogenic fungus Cordyceps militaris, a
RT valued traditional Chinese medicine.";
RL Genome Biol. 12:RESEARCH116.1-RESEARCH116.21(2011).
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; JH126399; EGX97199.1; -; Genomic_DNA.
DR RefSeq; XP_006667076.1; XM_006667013.1.
DR AlphaFoldDB; G3J7Y8; -.
DR STRING; 983644.G3J7Y8; -.
DR GeneID; 18163888; -.
DR KEGG; cmt:CCM_01859; -.
DR VEuPathDB; FungiDB:CCM_01859; -.
DR eggNOG; KOG1440; Eukaryota.
DR HOGENOM; CLU_023471_1_1_1; -.
DR InParanoid; G3J7Y8; -.
DR OMA; FFAYMYF; -.
DR OrthoDB; 5481516at2759; -.
DR UniPathway; UPA00557; UER00614.
DR Proteomes; UP000001610; 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:UP000001610};
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 69..88
FT /note="Helical"
FT /evidence="ECO:0000256|PIRNR:PIRNR018269"
FT TRANSMEM 94..116
FT /note="Helical"
FT /evidence="ECO:0000256|PIRNR:PIRNR018269"
FT TRANSMEM 128..148
FT /note="Helical"
FT /evidence="ECO:0000256|PIRNR:PIRNR018269"
FT TRANSMEM 168..185
FT /note="Helical"
FT /evidence="ECO:0000256|PIRNR:PIRNR018269"
FT TRANSMEM 197..215
FT /note="Helical"
FT /evidence="ECO:0000256|PIRNR:PIRNR018269"
FT TRANSMEM 221..247
FT /note="Helical"
FT /evidence="ECO:0000256|PIRNR:PIRNR018269"
FT TRANSMEM 259..277
FT /note="Helical"
FT /evidence="ECO:0000256|PIRNR:PIRNR018269"
FT TRANSMEM 336..358
FT /note="Helical"
FT /evidence="ECO:0000256|PIRNR:PIRNR018269"
FT REGION 1..59
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 11..35
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 43..59
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 458 AA; 51900 MW; 37AEF4903EF0A85F CRC64;
MSRPKRGVRF SHKSSNGSGS EGRRSSFSDV SEDGSPSRSK PYLRLETVDE KPPTPEEKRA
EYEKKKANFW TRTLWTFVMM GIFFGALFMG HIYIITIITA VQIISFKEVI AIANVPSRAR
SLRSTKSLNW YWLATTMYFL YGESVIYYFK HIVLVDKVLL PLATHHRFIS FILYVFGFVC
FVASLKAGHY KFQFTNFAWT HMALYLIVVQ AHFVMNNILE GMIWFFLPAA LVITNDIFAY
ICGIAFGRTQ LIKLSPKKTV EGFVGAWIMT VLFGIFLSNL MMKSKFFICP VNDLGANIFT
GLECNPNPVF LPATYEIPQF FFLPQHRTIT LTFAPIQLHT FILASFASLI APFGGFFASG
LKRSFKIKDF GDSIPGHGGM TDRMDCQFIM GFFAYMYYHT FIAVYKVDLG IVLETAITRL
GPDDQVELVK SMCRYLGNQG IVPEALSACI EHAMAAGQ
//
