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Database: UniProt
Entry: A0A317XN95_9BASI
LinkDB: A0A317XN95_9BASI
Original site: A0A317XN95_9BASI 
ID   A0A317XN95_9BASI        Unreviewed;       348 AA.
AC   A0A317XN95;
DT   10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT   10-OCT-2018, sequence version 1.
DT   27-MAR-2024, entry version 19.
DE   RecName: Full=CDP-diacylglycerol--glycerol-3-phosphate 3-phosphatidyltransferase {ECO:0008006|Google:ProtNLM};
GN   ORFNames=BCV70DRAFT_200703 {ECO:0000313|EMBL:PWY99793.1};
OS   Testicularia cyperi.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC   Ustilaginomycetes; Ustilaginales; Anthracoideaceae; Testicularia.
OX   NCBI_TaxID=1882483 {ECO:0000313|EMBL:PWY99793.1, ECO:0000313|Proteomes:UP000246740};
RN   [1] {ECO:0000313|EMBL:PWY99793.1, ECO:0000313|Proteomes:UP000246740}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MCA 3645 {ECO:0000313|EMBL:PWY99793.1,
RC   ECO:0000313|Proteomes:UP000246740};
RX   PubMed=29771364; DOI=10.1093/molbev/msy072;
RA   Kijpornyongpan T., Mondo S.J., Barry K., Sandor L., Lee J., Lipzen A.,
RA   Pangilinan J., LaButti K., Hainaut M., Henrissat B., Grigoriev I.V.,
RA   Spatafora J.W., Aime M.C.;
RT   "Broad genomic sampling reveals a smut pathogenic ancestry of the fungal
RT   clade Ustilaginomycotina.";
RL   Mol. Biol. Evol. 0:0-0(2018).
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; KZ819194; PWY99793.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A317XN95; -.
DR   STRING; 1882483.A0A317XN95; -.
DR   InParanoid; A0A317XN95; -.
DR   Proteomes; UP000246740; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0030572; F:phosphatidyltransferase activity; IEA:UniProt.
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   PANTHER; PTHR14269:SF60; CARDIOLIPIN SYNTHASE (CMP-FORMING); 1.
DR   PANTHER; PTHR14269; CDP-DIACYLGLYCEROL--GLYCEROL-3-PHOSPHATE 3-PHOSPHATIDYLTRANSFERASE-RELATED; 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, ECO:0000256|SAM:Phobius};
KW   Phospholipid biosynthesis {ECO:0000256|ARBA:ARBA00023209};
KW   Phospholipid metabolism {ECO:0000256|ARBA:ARBA00023264};
KW   Reference proteome {ECO:0000313|Proteomes:UP000246740};
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        75..97
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        140..163
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        197..214
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        275..295
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   REGION          1..53
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          228..258
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          313..348
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        14..37
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        313..332
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        333..348
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   348 AA;  37034 MW;  C24BA0E36D11B493 CRC64;
     MSSLRRQTKD DKSKPSSGSV PVSTSPSSSS SLSPSSQPPS QPSSPATPPP QQQLSEDILT
     VPNLLTMLRL ALTPYIGYLV TTHQFVPAVT LLFFAAVTDL LDGWIARRTS RYTVFGSIAD
     PAADKALVTT MVVSLALGGM LPWTMAGIIL ARDVALIISA FVIRYRTLAQ PKTLKRYFNP
     RLPSATVTPT QISKYNTFLQ LLLVGILTLY PILYPGQPSP QLFPDGFSNP TTITTTTTTT
     TSDAEQVDPS TSSSSSFSSQ VQASWSTKQI IDASITALMW ITAITTIWSG IGYLGGAGSS
     KSFKSGSLLQ KVQNVSSKVS NTTARLKSSA SRTPTKPPPP SPPPSSSS
//
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