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Database: UniProt
Entry: A0A1R1XG81_9FUNG
LinkDB: A0A1R1XG81_9FUNG
Original site: A0A1R1XG81_9FUNG 
ID   A0A1R1XG81_9FUNG        Unreviewed;       391 AA.
AC   A0A1R1XG81;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   24-JAN-2024, entry version 23.
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=AYI70_g2400 {ECO:0000313|EMBL:OMJ23229.1}, AYI70_g8372
GN   {ECO:0000313|EMBL:OMJ13639.1};
OS   Smittium culicis.
OC   Eukaryota; Fungi; Fungi incertae sedis; Zoopagomycota; Kickxellomycotina;
OC   Harpellomycetes; Harpellales; Legeriomycetaceae; Smittium.
OX   NCBI_TaxID=133412 {ECO:0000313|EMBL:OMJ13639.1, ECO:0000313|Proteomes:UP000187283};
RN   [1] {ECO:0000313|EMBL:OMJ13639.1, ECO:0000313|Proteomes:UP000187283}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GSMNP {ECO:0000313|EMBL:OMJ13639.1,
RC   ECO:0000313|Proteomes:UP000187283};
RA   Mah S.A., Swanson W.J., Moy G.W., Vacquier V.D.;
RL   Submitted (JAN-2017) 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|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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:OMJ13639.1}.
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DR   EMBL; LSSN01003406; OMJ13639.1; -; Genomic_DNA.
DR   EMBL; LSSN01000581; OMJ23229.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1R1XG81; -.
DR   STRING; 133412.A0A1R1XG81; -.
DR   UniPathway; UPA00557; UER00614.
DR   Proteomes; UP000187283; 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; 2.
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:UP000187283};
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        52..69
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|PIRNR:PIRNR018269"
FT   TRANSMEM        107..125
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|PIRNR:PIRNR018269"
FT   TRANSMEM        145..166
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|PIRNR:PIRNR018269"
FT   TRANSMEM        178..196
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|PIRNR:PIRNR018269"
FT   TRANSMEM        202..228
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|PIRNR:PIRNR018269"
FT   TRANSMEM        240..260
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|PIRNR:PIRNR018269"
FT   TRANSMEM        272..292
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|PIRNR:PIRNR018269"
FT   REGION          1..40
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        17..38
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   391 AA;  44825 MW;  B2DA32B1706309C9 CRC64;
     MKNKHLTPRK SEKTSSPSIR RSPQLNKSSK NTPAPSPAPE SKRNWINWNV RAFYTLIMIL
     SFISVIAAGT LPTLLLVFSL QLLIFKELIS ISTVANKERH LPWMRALNWY FLLITTNALY
     GKVFYKYAMR IRIEFLTEII QFCTINHRFV NFALYVFGFV WFVASLRPNY YKYQFTQFSW
     TLMLLFFVVY QSHFMVDSIL EGLFWFLIPV SFVIVNDIFA YVFGFFFGRH SLTRLSPKKT
     WEGFIGGAIS TVVFAFMFGY NIATVTLLPV QLHSIFLAMF ASLIAPFGGF FASGVKRAFK
     IKDFGNTIPG HGGVTDRFDC QFIMAFFSYV YYSTFIKGST ISITSIMAVI VSKMTHQDQI
     QLYHSLGNHL SAIDSTSILT ASFEAVKTKL V
//
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