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Database: UniProt
Entry: A0A0N5AZ93_9BILA
LinkDB: A0A0N5AZ93_9BILA
Original site: A0A0N5AZ93_9BILA 
ID   A0A0N5AZ93_9BILA        Unreviewed;       215 AA.
AC   A0A0N5AZ93;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   27-MAR-2024, entry version 28.
DE   RecName: Full=CDP-diacylglycerol--inositol 3-phosphatidyltransferase {ECO:0000256|ARBA:ARBA00013212, ECO:0000256|PIRNR:PIRNR000848};
DE            EC=2.7.8.11 {ECO:0000256|ARBA:ARBA00013212, ECO:0000256|PIRNR:PIRNR000848};
OS   Syphacia muris.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Spirurina; Oxyuridomorpha; Oxyuroidea; Oxyuridae; Syphacia.
OX   NCBI_TaxID=451379 {ECO:0000313|Proteomes:UP000046393, ECO:0000313|WBParaSite:SMUV_0001031501-mRNA-1};
RN   [1] {ECO:0000313|WBParaSite:SMUV_0001031501-mRNA-1}
RP   IDENTIFICATION.
RG   WormBaseParasite;
RL   Submitted (FEB-2017) to UniProtKB.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a CDP-1,2-diacyl-sn-glycerol + myo-inositol = a 1,2-diacyl-sn-
CC         glycero-3-phospho-(1D-myo-inositol) + CMP + H(+);
CC         Xref=Rhea:RHEA:11580, ChEBI:CHEBI:15378, ChEBI:CHEBI:17268,
CC         ChEBI:CHEBI:57880, ChEBI:CHEBI:58332, ChEBI:CHEBI:60377; EC=2.7.8.11;
CC         Evidence={ECO:0000256|PIRNR:PIRNR000848};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946};
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC   -!- SIMILARITY: Belongs to the CDP-alcohol phosphatidyltransferase class-I
CC       family. {ECO:0000256|PIRNR:PIRNR000848}.
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DR   AlphaFoldDB; A0A0N5AZ93; -.
DR   STRING; 451379.A0A0N5AZ93; -.
DR   WBParaSite; SMUV_0001031501-mRNA-1; SMUV_0001031501-mRNA-1; SMUV_0001031501.
DR   Proteomes; UP000046393; Unplaced.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0003881; F:CDP-diacylglycerol-inositol 3-phosphatidyltransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0008654; P:phospholipid biosynthetic process; IEA:UniProtKB-KW.
DR   Gene3D; 1.20.120.1760; -; 1.
DR   InterPro; IPR000462; CDP-OH_P_trans.
DR   InterPro; IPR043130; CDP-OH_PTrfase_TM_dom.
DR   InterPro; IPR014387; CDP_diag_ino_3_P_euk.
DR   PANTHER; PTHR15362:SF4; CDP-DIACYLGLYCEROL--INOSITOL 3-PHOSPHATIDYLTRANSFERASE; 1.
DR   PANTHER; PTHR15362; PHOSPHATIDYLINOSITOL SYNTHASE; 1.
DR   Pfam; PF01066; CDP-OH_P_transf; 1.
DR   PIRSF; PIRSF000848; CDP_diag_ino_3_P; 1.
PE   3: Inferred from homology;
KW   Lipid biosynthesis {ECO:0000256|PIRNR:PIRNR000848};
KW   Lipid metabolism {ECO:0000256|ARBA:ARBA00023098,
KW   ECO:0000256|PIRNR:PIRNR000848};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|PIRNR:PIRNR000848};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Phospholipid biosynthesis {ECO:0000256|PIRNR:PIRNR000848};
KW   Phospholipid metabolism {ECO:0000256|PIRNR:PIRNR000848};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR000848};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        6..26
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        142..163
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        169..187
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
SQ   SEQUENCE   215 AA;  24428 MW;  42471767123AAEC0 CRC64;
     MTTENVWLFY PNLIGYCRII LGLLSFEAMM YAPIRAAVFY TISVGLDAVD GELARRYKQC
     MLFACSRYGA MLDQLTDRCS TLGLIITLAL FYPKYILLFQ LSAVIDIASH WLHLHASDLT
     HLTTHKTSNN PILHLYYTSR KFLFFMCAGN EAFYWLLYVN HFWSGPGIFG IHLIPILAAV
     VCPVAIVKSM ISLVHLVTAS QTVVNHDVTL RQKQQ
//
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