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Database: UniProt
Entry: A0A1E1L5Y1_9HELO
LinkDB: A0A1E1L5Y1_9HELO
Original site: A0A1E1L5Y1_9HELO 
ID   A0A1E1L5Y1_9HELO        Unreviewed;       478 AA.
AC   A0A1E1L5Y1;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   24-JAN-2024, entry version 20.
DE   RecName: Full=CDP-diacylglycerol--glycerol-3-phosphate 3-phosphatidyltransferase {ECO:0000256|RuleBase:RU365024};
DE            EC=2.7.8.5 {ECO:0000256|RuleBase:RU365024};
GN   ORFNames=RCO7_05197 {ECO:0000313|EMBL:CZT05982.1};
OS   Rhynchosporium commune.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Helotiales; Ploettnerulaceae; Rhynchosporium.
OX   NCBI_TaxID=914237 {ECO:0000313|EMBL:CZT05982.1, ECO:0000313|Proteomes:UP000178129};
RN   [1] {ECO:0000313|EMBL:CZT05982.1, ECO:0000313|Proteomes:UP000178129}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UK7 {ECO:0000313|EMBL:CZT05982.1,
RC   ECO:0000313|Proteomes:UP000178129};
RA   Ploux O.;
RL   Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Functions in the biosynthesis of the anionic phospholipids
CC       phosphatidylglycerol and cardiolipin. {ECO:0000256|RuleBase:RU365024}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a CDP-1,2-diacyl-sn-glycerol + sn-glycerol 3-phosphate = 1,2-
CC         diacyl-sn-glycero-3-phospho-(1'-sn-glycero-3'-phosphate) + CMP +
CC         H(+); Xref=Rhea:RHEA:12593, ChEBI:CHEBI:15378, ChEBI:CHEBI:57597,
CC         ChEBI:CHEBI:58332, ChEBI:CHEBI:60110, ChEBI:CHEBI:60377; EC=2.7.8.5;
CC         Evidence={ECO:0000256|ARBA:ARBA00001566,
CC         ECO:0000256|RuleBase:RU365024};
CC   -!- PATHWAY: Phospholipid metabolism; phosphatidylglycerol biosynthesis;
CC       phosphatidylglycerol from CDP-diacylglycerol: step 1/2.
CC       {ECO:0000256|ARBA:ARBA00005042, ECO:0000256|RuleBase:RU365024}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000256|RuleBase:RU365024}.
CC   -!- SIMILARITY: Belongs to the CDP-alcohol phosphatidyltransferase class-II
CC       family. {ECO:0000256|ARBA:ARBA00010682, ECO:0000256|RuleBase:RU365024}.
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DR   EMBL; FJUW01000037; CZT05982.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1E1L5Y1; -.
DR   STRING; 914237.A0A1E1L5Y1; -.
DR   InParanoid; A0A1E1L5Y1; -.
DR   OrthoDB; 179003at2759; -.
DR   UniPathway; UPA00084; UER00503.
DR   Proteomes; UP000178129; Unassembled WGS sequence.
DR   GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0008444; F:CDP-diacylglycerol-glycerol-3-phosphate 3-phosphatidyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0032049; P:cardiolipin biosynthetic process; IEA:InterPro.
DR   CDD; cd09135; PLDc_PGS1_euk_1; 1.
DR   CDD; cd09137; PLDc_PGS1_euk_2; 1.
DR   Gene3D; 3.30.870.10; Endonuclease Chain A; 2.
DR   InterPro; IPR016270; PGS1.
DR   InterPro; IPR001736; PLipase_D/transphosphatidylase.
DR   PANTHER; PTHR12586:SF1; CDP-DIACYLGLYCEROL--GLYCEROL-3-PHOSPHATE 3-PHOSPHATIDYLTRANSFERASE, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR12586; CDP-DIACYLGLYCEROL--SERINE O-PHOSPHATIDYLTRANSFERASE; 1.
DR   PIRSF; PIRSF000850; Phospholipase_D_PSS; 2.
DR   SMART; SM00155; PLDc; 2.
DR   SUPFAM; SSF56024; Phospholipase D/nuclease; 1.
DR   PROSITE; PS50035; PLD; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|RuleBase:RU365024};
KW   Lipid biosynthesis {ECO:0000256|RuleBase:RU365024};
KW   Lipid metabolism {ECO:0000256|RuleBase:RU365024};
KW   Mitochondrion {ECO:0000256|RuleBase:RU365024};
KW   Nucleotide-binding {ECO:0000256|RuleBase:RU365024};
KW   Phospholipid biosynthesis {ECO:0000256|RuleBase:RU365024};
KW   Phospholipid metabolism {ECO:0000256|RuleBase:RU365024};
KW   Reference proteome {ECO:0000313|Proteomes:UP000178129};
KW   Transferase {ECO:0000256|RuleBase:RU365024}.
FT   DOMAIN          135..161
FT                   /note="PLD phosphodiesterase"
FT                   /evidence="ECO:0000259|PROSITE:PS50035"
SQ   SEQUENCE   478 AA;  52753 MW;  491CC2BEF4DA75B4 CRC64;
     MLGAFMNELD KIAPKFEIQG SQIDILRSPA EFYETLKVRL IPTLHMQKMG SADGKTEHEL
     ISTLQQALRA KPRLKLSILT DALRGTRESP EASCASLLAP LVSEFGPDRV EIRMYHTPNL
     TGLRKKYIPK RINEGWGLQH MKLYGVDDEI IISGANLSSD YFTNRQDRYH IFTSKEITEY
     FSKIHNAVSS LSFLVTPDAQ LPAGYTLEWP TSNLAPSPLS NPAKYISQSS TVLKSLIQPL
     NTSAQSPANP ANNTSVYPLS QLTQLLSPDT STELPAITSI LQTLSKPTFN TSSWTFTAGY
     FNPDPSLISL LLSTTSQHNT VITASPWANG FYGSKGVSGL LPAAYTLLSR RFLEAAQKSG
     RENAITLKEW RNGTVGEKDG WTYHAKGLWV SLNDEKNPSI SVVGSSNYTK RSYGLDLEVG
     TVIVTSDEGL KGRLGEERDN LGVYAERVGM KDFVKVERRV GIKVRVAMWI VKMVGGAL
//
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