ID A0A1I8NQD6_STOCA Unreviewed; 541 AA.
AC A0A1I8NQD6;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 24-JAN-2024, entry version 29.
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 Name=106086009 {ECO:0000313|EnsemblMetazoa:SCAU001121-PA};
OS Stomoxys calcitrans (Stable fly) (Conops calcitrans).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Muscoidea;
OC Muscidae; Stomoxys.
OX NCBI_TaxID=35570 {ECO:0000313|EnsemblMetazoa:SCAU001121-PA, ECO:0000313|Proteomes:UP000095300};
RN [1] {ECO:0000313|EnsemblMetazoa:SCAU001121-PA}
RP IDENTIFICATION.
RC STRAIN=USDA {ECO:0000313|EnsemblMetazoa:SCAU001121-PA};
RG EnsemblMetazoa;
RL Submitted (MAY-2020) 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|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 RefSeq; XP_013105966.1; XM_013250512.1.
DR AlphaFoldDB; A0A1I8NQD6; -.
DR STRING; 35570.A0A1I8NQD6; -.
DR EnsemblMetazoa; SCAU001121-RA; SCAU001121-PA; SCAU001121.
DR KEGG; scac:106086009; -.
DR VEuPathDB; VectorBase:SCAU001121; -.
DR OrthoDB; 5481516at2759; -.
DR UniPathway; UPA00557; UER00614.
DR Proteomes; UP000095300; 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 GO; GO:0071897; P:DNA biosynthetic process; IEA:UniProt.
DR Gene3D; 3.30.70.270; -; 1.
DR InterPro; IPR043502; DNA/RNA_pol_sf.
DR InterPro; IPR000374; PC_trans.
DR InterPro; IPR016720; PC_Trfase_euk.
DR InterPro; IPR043128; Rev_trsase/Diguanyl_cyclase.
DR PANTHER; PTHR13773; PHOSPHATIDATE CYTIDYLYLTRANSFERASE; 1.
DR PANTHER; PTHR13773:SF8; PHOSPHATIDATE CYTIDYLYLTRANSFERASE, PHOTORECEPTOR-SPECIFIC; 1.
DR Pfam; PF01148; CTP_transf_1; 1.
DR SUPFAM; SSF56672; DNA/RNA polymerases; 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 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 177..196
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 232..249
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 276..294
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 306..323
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 329..354
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 375..401
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 439..461
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT REGION 1..47
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 16..47
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 541 AA; 61676 MW; F2BD4722D7833E5A CRC64;
MAEVRRRKVE EAGDDATNTQ LGSSAGTSAE AEKRNSSAAE SSDHVSGRPP INTLLLCAGE
TILPFTVMPF GLCNAAQRLW DKVIPSAIRD CVFQVEKKSD FTVLGRPLYH FTVMPFDLCN
AAQKLCRSID KVIPSAIRDR VFDYLDDLLI VSPSFDTHLV LLVEGSSNMT RARWKNWVIR
GIFTWIMICG FCLIIYGGPL ALMITTLLVQ VKCFEEIISI GYHVYRINGL PWFRSLSWYF
LLTSNYFFYG ENLVDYFGVA INRVEYLKFM VTYHRFLSFA LYCIGFVWFV LSLVKKYYLR
QFSLFAWTHV SLLIVVTQSY LIIQNIFEGL IWFIVPVSMI VCNDVMAYMF GFFFGKTPLI
KLSPKKTWEG FIGGGFATVI FGLIFSYILC NFQYFVCPIV YSEELGSMSM NCEPSYLFTP
QEYSLSVFGI GKSFRMYPFV WHSISLSLFS SIIGPFGGFF ASGFKRAFKI KDFGDVIPGH
GGIMDRFDCQ FLMATFVNVY ISSFIRTPSP AKLLTQIYNL KIEQQFQILQ SLKESLGDVL
N
//
