ID A0A094ZQ69_SCHHA Unreviewed; 201 AA.
AC A0A094ZQ69;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=CDP-diacylglycerol--inositol 3-phosphatidyltransferase {ECO:0000256|ARBA:ARBA00013212};
DE EC=2.7.8.11 {ECO:0000256|ARBA:ARBA00013212};
DE Flags: Fragment;
GN ORFNames=MS3_04539 {ECO:0000313|EMBL:KGB36252.1};
OS Schistosoma haematobium (Blood fluke).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes; Trematoda;
OC Digenea; Strigeidida; Schistosomatoidea; Schistosomatidae; Schistosoma.
OX NCBI_TaxID=6185 {ECO:0000313|EMBL:KGB36252.1};
RN [1] {ECO:0000313|EMBL:KGB36252.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=22246508; DOI=10.1038/ng.1065;
RA Young N.D., Jex A.R., Li B., Liu S., Yang L., Xiong Z., Li Y.,
RA Cantacessi C., Hall R.S., Xu X., Chen F., Wu X., Zerlotini A., Oliveira G.,
RA Hofmann A., Zhang G., Fang X., Kang Y., Campbell B.E., Loukas A.,
RA Ranganathan S., Rollinson D., Rinaldi G., Brindley P.J., Yang H., Wang J.,
RA Wang J., Gasser R.B.;
RT "Whole-genome sequence of Schistosoma haematobium.";
RL Nat. Genet. 44:221-225(2012).
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|ARBA:ARBA00001936};
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|RuleBase:RU003750}.
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DR EMBL; KL250757; KGB36252.1; -; Genomic_DNA.
DR RefSeq; XP_012796017.1; XM_012940563.1.
DR AlphaFoldDB; A0A094ZQ69; -.
DR STRING; 6185.A0A094ZQ69; -.
DR EnsemblMetazoa; XM_012940563.2; XP_012796017.2; MS3_0020134.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0003881; F:CDP-diacylglycerol-inositol 3-phosphatidyltransferase activity; IEA:UniProtKB-EC.
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; IPR048254; CDP_ALCOHOL_P_TRANSF_CS.
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.
DR PROSITE; PS00379; CDP_ALCOHOL_P_TRANSF; 1.
PE 3: Inferred from homology;
KW Lipid biosynthesis {ECO:0000256|ARBA:ARBA00023209};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Phospholipid biosynthesis {ECO:0000256|ARBA:ARBA00023209};
KW Phospholipid metabolism {ECO:0000256|ARBA:ARBA00023264};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU003750};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 23..44
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 121..144
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 156..178
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KGB36252.1"
FT NON_TER 201
FT /evidence="ECO:0000313|EMBL:KGB36252.1"
SQ SEQUENCE 201 AA; 22957 MW; E8045AD893655821 CRC64;
GYIRIVLLFQ ACYFMKTNCE LTLLTYIISC LLDAVDGCAA RALNQSTKFG AMLDMIVDRC
STMCLLACLT YFYPSYMLFF QFSMIVDIAS HWLHLHSSVL SGKSSHKFID LKANRFLKLY
YTNRVILFLM CAGNELFYTT LYIYHFYTGP KIFASGLWGI VICLTAPIAF LKMLISLIQL
HAACMNMVSL DELERSQNKA D
//
