ID W3WP39_PESFW Unreviewed; 386 AA.
AC W3WP39;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:ETS75670.1};
GN ORFNames=PFICI_12614 {ECO:0000313|EMBL:ETS75670.1};
OS Pestalotiopsis fici (strain W106-1 / CGMCC3.15140).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Xylariomycetidae; Xylariales; Sporocadaceae; Pestalotiopsis.
OX NCBI_TaxID=1229662 {ECO:0000313|EMBL:ETS75670.1, ECO:0000313|Proteomes:UP000030651};
RN [1] {ECO:0000313|Proteomes:UP000030651}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=W106-1 / CGMCC3.15140 {ECO:0000313|Proteomes:UP000030651};
RX PubMed=25623211; DOI=10.1186/s12864-014-1190-9;
RA Wang X., Zhang X., Liu L., Xiang M., Wang W., Sun X., Che Y., Guo L.,
RA Liu G., Guo L., Wang C., Yin W.B., Stadler M., Zhang X., Liu X.;
RT "Genomic and transcriptomic analysis of the endophytic fungus
RT Pestalotiopsis fici reveals its lifestyle and high potential for synthesis
RT of natural products.";
RL BMC Genomics 16:28-28(2015).
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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; KI912118; ETS75670.1; -; Genomic_DNA.
DR RefSeq; XP_007839386.1; XM_007841195.1.
DR AlphaFoldDB; W3WP39; -.
DR STRING; 1229662.W3WP39; -.
DR GeneID; 19277627; -.
DR KEGG; pfy:PFICI_12614; -.
DR eggNOG; KOG1617; Eukaryota.
DR HOGENOM; CLU_051314_0_0_1; -.
DR InParanoid; W3WP39; -.
DR OrthoDB; 5490365at2759; -.
DR Proteomes; UP000030651; 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:UP000030651};
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 316..334
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
SQ SEQUENCE 386 AA; 41655 MW; 5B92182824FB8769 CRC64;
MASPTLSCGG ARFAVARLAT GMTVPSLNSN RARLVSDPRG APVSLRHAQS IHYFSSATVL
RRLSRQRSQH ELAADRASEQ AAECIAARTA TASSSIGPGM THLDVPSLAV KRPIYGIMRN
TSLCRHFSFR TSCLERDGKG PKEQGPETAA GVTSTSAIRK VLPKALGSAL TPHENIYTIP
NLLTFSRIIA SPFIGYAILH DAHAWALGLF VYAGVSDLLD GWIARRWKLQ TVVGSIVDPM
ADKMLMTILT VCLAAKGALP IWLAGIILGR DVGLAISAIY YRWISLPPPK TFTRYWDFSL
PSAEVRPTTI SKYNTFLQLA LMGSTVVAPL VTGIEVGPAL IGLQYIVATT TIWSGLSYVF
SKDAVKILSD AKSKDNAANE DKSREQ
//
