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
//