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Database: UniProt
Entry: A0A183T015_SCHSO
LinkDB: A0A183T015_SCHSO
Original site: A0A183T015_SCHSO 
ID   A0A183T015_SCHSO        Unreviewed;       447 AA.
AC   A0A183T015;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   24-JAN-2024, entry version 25.
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=SSLN_LOCUS9813 {ECO:0000313|EMBL:VDL96198.1};
OS   Schistocephalus solidus (Tapeworm).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes; Cestoda;
OC   Eucestoda; Diphyllobothriidea; Diphyllobothriidae; Schistocephalus.
OX   NCBI_TaxID=70667 {ECO:0000313|Proteomes:UP000050788, ECO:0000313|WBParaSite:SSLN_0001017701-mRNA-1};
RN   [1] {ECO:0000313|WBParaSite:SSLN_0001017701-mRNA-1}
RP   IDENTIFICATION.
RG   WormBaseParasite;
RL   Submitted (JUN-2016) to UniProtKB.
RN   [2] {ECO:0000313|EMBL:VDL96198.1, ECO:0000313|Proteomes:UP000275846}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NST_G2 {ECO:0000313|EMBL:VDL96198.1,
RC   ECO:0000313|Proteomes:UP000275846};
RG   Pathogen Informatics;
RL   Submitted (NOV-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Functions in the biosynthesis of the anionic phospholipids
CC       phosphatidylglycerol and cardiolipin. {ECO:0000256|ARBA:ARBA00003537,
CC       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; UYSU01035466; VDL96198.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A183T015; -.
DR   STRING; 70667.A0A183T015; -.
DR   WBParaSite; SSLN_0001017701-mRNA-1; SSLN_0001017701-mRNA-1; SSLN_0001017701.
DR   UniPathway; UPA00084; UER00503.
DR   Proteomes; UP000050788; Unplaced.
DR   Proteomes; UP000275846; 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; 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   Pfam; PF00614; PLDc; 1.
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:UP000275846};
KW   Transferase {ECO:0000256|RuleBase:RU365024}.
FT   DOMAIN          101..127
FT                   /note="PLD phosphodiesterase"
FT                   /evidence="ECO:0000259|PROSITE:PS50035"
SQ   SEQUENCE   447 AA;  49716 MW;  2CECB3E569B4600F CRC64;
     MCPSRDGVSA LESAVKERSN YGLSVHLLVE STRSTRPASL TRRYVGSVHR NKTNEDTQAP
     ASSMQLLSRL ANLPGVTVSL YHSHKLRGWV RRLLPERVNE TVGLQHIKAY VFDDTVIIGG
     ANLSDEYFTT RQDRAWVFSD LPPLADFYAG LTDVISSLSY HLMPDGSFSA ASLDVDPVEA
     DTLVYVETFR TRLNAYLSGV RAALSSPRHL TTETMVLPLV QAGAYGVNQE HSLLLHILRR
     LPSLASHCSL YLTSGYFCPT DEMQDCLGHL LSSRPDSTLN LLCAAPEANS FFRSNGLSGG
     IPKAYRESLI AFLCRLAKAL PVVSAIASSG RLRVGEYFRA GWTFHAKGLW VETGVCQGNS
     TTAAAPATLT WIGSSNYGYR SRDRDLESQV LVCTSNAGLR QAIRAERAVI WDARYYRPVT
     LQDLSRQTEH RLQWYLRWIL PLLRRIM
//
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