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Database: UniProt
Entry: A0A1U7LK81_NEOID
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ID   A0A1U7LK81_NEOID        Unreviewed;       181 AA.
AC   A0A1U7LK81;
DT   10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT   10-MAY-2017, sequence version 1.
DT   24-JAN-2024, entry version 17.
DE   RecName: Full=CDP-diacylglycerol--serine O-phosphatidyltransferase {ECO:0000256|ARBA:ARBA00017171};
DE            EC=2.7.8.8 {ECO:0000256|ARBA:ARBA00013174};
DE   AltName: Full=Phosphatidylserine synthase {ECO:0000256|ARBA:ARBA00032361};
GN   ORFNames=NEOLI_001293 {ECO:0000313|EMBL:OLL23054.1};
OS   Neolecta irregularis (strain DAH-3).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina; Neolectales;
OC   Neolectaceae; Neolecta.
OX   NCBI_TaxID=1198029 {ECO:0000313|EMBL:OLL23054.1, ECO:0000313|Proteomes:UP000186594};
RN   [1] {ECO:0000313|EMBL:OLL23054.1, ECO:0000313|Proteomes:UP000186594}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DAH-3 {ECO:0000313|EMBL:OLL23054.1,
RC   ECO:0000313|Proteomes:UP000186594};
RA   Cisse O., Nguyen A., Hewitt D.A., Jedd G., Stajich J.E.;
RT   "Evolutionary innovation and constraint leading to complex multicellularity
RT   in the Ascomycota.";
RL   Submitted (APR-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a CDP-1,2-diacyl-sn-glycerol + L-serine = a 1,2-diacyl-sn-
CC         glycero-3-phospho-L-serine + CMP + H(+); Xref=Rhea:RHEA:16913,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:33384, ChEBI:CHEBI:57262,
CC         ChEBI:CHEBI:58332, ChEBI:CHEBI:60377; EC=2.7.8.8;
CC         Evidence={ECO:0000256|ARBA:ARBA00000287};
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}.
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:OLL23054.1}.
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DR   EMBL; LXFE01002348; OLL23054.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1U7LK81; -.
DR   STRING; 1198029.A0A1U7LK81; -.
DR   OrthoDB; 1332156at2759; -.
DR   Proteomes; UP000186594; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016780; F:phosphotransferase activity, for other substituted phosphate groups; IEA:InterPro.
DR   GO; GO:0008654; P:phospholipid biosynthetic process; IEA:InterPro.
DR   Gene3D; 1.20.120.1760; -; 1.
DR   InterPro; IPR004533; CDP-diaglyc--ser_O-PTrfase.
DR   InterPro; IPR000462; CDP-OH_P_trans.
DR   InterPro; IPR043130; CDP-OH_PTrfase_TM_dom.
DR   InterPro; IPR048254; CDP_ALCOHOL_P_TRANSF_CS.
DR   NCBIfam; TIGR00473; pssA; 1.
DR   PANTHER; PTHR14269; CDP-DIACYLGLYCEROL--GLYCEROL-3-PHOSPHATE 3-PHOSPHATIDYLTRANSFERASE-RELATED; 1.
DR   PANTHER; PTHR14269:SF61; CDP-DIACYLGLYCEROL--SERINE O-PHOSPHATIDYLTRANSFERASE; 1.
DR   Pfam; PF01066; CDP-OH_P_transf; 1.
DR   PROSITE; PS00379; CDP_ALCOHOL_P_TRANSF; 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};
KW   Phospholipid biosynthesis {ECO:0000256|ARBA:ARBA00023209};
KW   Phospholipid metabolism {ECO:0000256|ARBA:ARBA00023264};
KW   Reference proteome {ECO:0000313|Proteomes:UP000186594};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU003750};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
SQ   SEQUENCE   181 AA;  19906 MW;  FCC61EC159FEF5EA CRC64;
     MSVFSSMRYC LGLPTDFSDL TLAMVLIPMG LFFDFMDGKV ARWRNRSSFL GQELDSLADL
     ISFGVAPAAC AFAIGFRTFA DTIVLSSFVL CGLSRLARFN VTVSSLPKDV SGKSKYFEGT
     PIPTTLGLVM TMAYWLKQNR VLDALPWGVK GSGMFEIHPI VCIFILHGSA MLSKTLRIPK
     L
//
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