(data stored in SCRATCH zone)

SWISSPROT: Q4WDE4_ASPFU

ID   Q4WDE4_ASPFU            Unreviewed;       238 AA.
AC   Q4WDE4;
DT   05-JUL-2005, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2005, sequence version 1.
DT   11-DEC-2019, entry version 74.
DE   SubName: Full=Phosphatidyl synthase {ECO:0000313|EMBL:EAL85594.1};
DE            EC=2.7.8.5 {ECO:0000313|EMBL:EAL85594.1};
GN   ORFNames=AFUA_6G04460 {ECO:0000313|EMBL:EAL85594.1};
OS   Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC
OS   A1100) (Aspergillus fumigatus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=330879 {ECO:0000313|EMBL:EAL85594.1, ECO:0000313|Proteomes:UP000002530};
RN   [1] {ECO:0000313|EMBL:EAL85594.1, ECO:0000313|Proteomes:UP000002530}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100
RC   {ECO:0000313|Proteomes:UP000002530};
RX   PubMed=16372009; DOI=10.1038/nature04332;
RA   Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S., Arroyo J.,
RA   Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J., Bowyer P.,
RA   Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.,
RA   Fedorova N., Fedorova N., Feldblyum T.V., Fischer R., Fosker N., Fraser A.,
RA   Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K.,
RA   Griffith-Jones S., Gwilliam R., Haas B., Haas H., Harris D., Horiuchi H.,
RA   Huang J., Humphray S., Jimenez J., Keller N., Khouri H., Kitamoto K.,
RA   Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafon A., Latge J.P.,
RA   Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L., Mohamoud Y.,
RA   Molina M., Monod M., Mouyna I., Mulligan S., Murphy L., O'Neil S.,
RA   Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L., Quail M.A.,
RA   Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U., Renauld H.,
RA   Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M., Ronning C.M.,
RA   Rutter S., Salzberg S.L., Sanchez M., Sanchez-Ferrero J.C., Saunders D.,
RA   Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F., Turner G.,
RA   Vazquez de Aldana C.R., Weidman J., White O., Woodward J., Yu J.H.,
RA   Fraser C., Galagan J.E., Asai K., Machida M., Hall N., Barrell B.,
RA   Denning D.W.;
RT   "Genomic sequence of the pathogenic and allergenic filamentous fungus
RT   Aspergillus fumigatus.";
RL   Nature 438:1151-1156(2005).
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:EAL85594.1}.
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DR   EMBL; AAHF01000012; EAL85594.1; -; Genomic_DNA.
DR   RefSeq; XP_747632.1; XM_742539.1.
DR   STRING; 746128.CADAFUBP00009120; -.
DR   EnsemblFungi; EAL85594; EAL85594; AFUA_6G04460.
DR   GeneID; 3505293; -.
DR   KEGG; afm:AFUA_6G04460; -.
DR   EuPathDB; FungiDB:Afu6g04460; -.
DR   HOGENOM; HOG000010898; -.
DR   InParanoid; Q4WDE4; -.
DR   KO; K08744; -.
DR   OMA; TSMIILR; -.
DR   OrthoDB; 1169813at2759; -.
DR   Proteomes; UP000002530; Chromosome 6.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR   GO; GO:0008808; F:cardiolipin synthase activity; IBA:GO_Central.
DR   GO; GO:0008444; F:CDP-diacylglycerol-glycerol-3-phosphate 3-phosphatidyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0032049; P:cardiolipin biosynthetic process; IBA:GO_Central.
DR   GO; GO:0046474; P:glycerophospholipid biosynthetic process; IBA:GO_Central.
DR   InterPro; IPR000462; CDP-OH_P_trans.
DR   InterPro; IPR004570; Phosphatidylglycerol_P_synth.
DR   Pfam; PF01066; CDP-OH_P_transf; 1.
DR   PIRSF; PIRSF000847; Phos_ph_gly_syn; 1.
DR   PROSITE; PS00379; CDP_ALCOHOL_P_TRANSF; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q4WDE4.
DR   SWISS-2DPAGE; Q4WDE4.
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002530};
KW   Transferase {ECO:0000256|RuleBase:RU003750, ECO:0000313|EMBL:EAL85594.1};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        31..48
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        55..73
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        93..117
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        165..184
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        196..214
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
SQ   SEQUENCE   238 AA;  25930 MW;  65A6AE6E5A4AE48F CRC64;
     MCSPQSGPKK SPILSKIPIP THENIYTVPN ILTFSRLVAA PLVGYFLVHD HHAAALSLFV
     YAGLTDLVDG YIARRYNLQT VVGTIIDPMA DKLLMTIGVA CLAVNGSIPV WLAVIILGRD
     VGLALSAIYY RWISLPPPKT MARYWDFSLP SAEVKPTGIS KVNTALQLVL VGSAIALPVI
     PEAVLDAWNL QDGMTALQYL VASTTIWSGL SYVFSKDAVK ILTKEEVQKR LARASRKK
//

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