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Database: UniProt
Entry: Q4WGM8_ASPFU
LinkDB: Q4WGM8_ASPFU
Original site: Q4WGM8_ASPFU 
ID   Q4WGM8_ASPFU            Unreviewed;       879 AA.
AC   Q4WGM8;
DT   05-JUL-2005, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2005, sequence version 1.
DT   27-MAR-2024, entry version 96.
DE   RecName: Full=Phospholipase {ECO:0000256|PIRNR:PIRNR009376};
DE            EC=3.1.4.4 {ECO:0000256|PIRNR:PIRNR009376};
GN   ORFNames=AFUA_7G05580 {ECO:0000313|EMBL:EAL86913.1};
OS   Aspergillus fumigatus (strain ATCC MYA-4609 / CBS 101355 / FGSC A1100 /
OS   Af293) (Neosartorya fumigata).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Fumigati.
OX   NCBI_TaxID=330879 {ECO:0000313|EMBL:EAL86913.1, ECO:0000313|Proteomes:UP000002530};
RN   [1] {ECO:0000313|EMBL:EAL86913.1, 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   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 1,2-diacyl-
CC         sn-glycero-3-phosphate + choline + H(+); Xref=Rhea:RHEA:14445,
CC         ChEBI:CHEBI:15354, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:57643, ChEBI:CHEBI:58608; EC=3.1.4.4;
CC         Evidence={ECO:0000256|PIRNR:PIRNR009376};
CC   -!- SIMILARITY: Belongs to the phospholipase D family.
CC       {ECO:0000256|PIRNR:PIRNR009376}.
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:EAL86913.1}.
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DR   EMBL; AAHF01000009; EAL86913.1; -; Genomic_DNA.
DR   RefSeq; XP_748951.1; XM_743858.1.
DR   AlphaFoldDB; Q4WGM8; -.
DR   STRING; 330879.Q4WGM8; -.
DR   EnsemblFungi; EAL86913; EAL86913; AFUA_7G05580.
DR   GeneID; 3506609; -.
DR   KEGG; afm:AFUA_7G05580; -.
DR   eggNOG; KOG1329; Eukaryota.
DR   HOGENOM; CLU_000690_2_2_1; -.
DR   InParanoid; Q4WGM8; -.
DR   OMA; EWRLDQI; -.
DR   OrthoDB; 335467at2759; -.
DR   Proteomes; UP000002530; Chromosome 7.
DR   GO; GO:0043231; C:intracellular membrane-bounded organelle; IBA:GO_Central.
DR   GO; GO:0070290; F:N-acylphosphatidylethanolamine-specific phospholipase D activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0004630; F:phospholipase D activity; IBA:GO_Central.
DR   GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR   GO; GO:0006654; P:phosphatidic acid biosynthetic process; IEA:InterPro.
DR   GO; GO:0009395; P:phospholipid catabolic process; IBA:GO_Central.
DR   CDD; cd09138; PLDc_vPLD1_2_yPLD_like_1; 1.
DR   CDD; cd09141; PLDc_vPLD1_2_yPLD_like_2; 1.
DR   Gene3D; 3.30.870.10; Endonuclease Chain A; 3.
DR   InterPro; IPR025202; PLD-like_dom.
DR   InterPro; IPR001736; PLipase_D/transphosphatidylase.
DR   InterPro; IPR016555; PLipase_D_euk.
DR   InterPro; IPR015679; PLipase_D_fam.
DR   PANTHER; PTHR18896:SF128; PHOSPHOLIPASE; 1.
DR   PANTHER; PTHR18896; PHOSPHOLIPASE D; 1.
DR   Pfam; PF00614; PLDc; 1.
DR   Pfam; PF13091; PLDc_2; 1.
DR   PIRSF; PIRSF009376; Phospholipase_D_euk; 2.
DR   SMART; SM00155; PLDc; 2.
DR   SUPFAM; SSF56024; Phospholipase D/nuclease; 2.
DR   PROSITE; PS50035; PLD; 2.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PIRNR:PIRNR009376};
KW   Lipid degradation {ECO:0000256|ARBA:ARBA00022963,
KW   ECO:0000256|PIRNR:PIRNR009376};
KW   Lipid metabolism {ECO:0000256|ARBA:ARBA00022963,
KW   ECO:0000256|PIRNR:PIRNR009376};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002530}.
FT   DOMAIN          203..230
FT                   /note="PLD phosphodiesterase"
FT                   /evidence="ECO:0000259|PROSITE:PS50035"
FT   DOMAIN          626..653
FT                   /note="PLD phosphodiesterase"
FT                   /evidence="ECO:0000259|PROSITE:PS50035"
FT   REGION          577..616
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        577..593
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   879 AA;  101073 MW;  A38A7A71078A2735 CRC64;
     MGKLKEKLEH EIDHLESALK DSHLHDAKAK AHHFKHKVGK FFNVVNPNHR HDEEHERETD
     KKRTAIAESH RYKSFAPVRE GNRVKWYVDA LDYLWAVSVA LEEAKEVIYI EDWWLSPELF
     LRRPPYSTQE WRLDQVLKHR AEAGVKIYVI VYKEVNQALT CNSAHTKHAL HSLCPEGTPG
     HGNIKVLRHP DHNIFENAAD MTFYWAHHEK FIVIDYAVAF IGGIDLCFGR WDAHQHPLAD
     VHPANLKDEI FPGQDWNNNR IMDFQSVADW QSNEVSKADY GRMPWHDVAM GLVGDCVYDI
     AEHFVLRWNF VKRDKYKRDH GVDWLLLEGR TGDDEDLVGV QRPKYPCGQY IQHPLNPLDT
     KPRGMQGTVR GQIIRSSGDW SSGILTEQSI QNAYCEIIRN AQHLVYIENQ FFITATGDQQ
     KPIINTIGGA IVDACVRAGK EGRKFRVIIV MPAIPGFAGD LRQSAATGTR AIMDYQYKSI
     LRGEHSIFGQ ISAQGVDPRE HVFLFNLRAY DRINKTSALE ELEKEAGVTY HDIQRGIAES
     IMSDSVHPVV GEEGDKHEVN YDDAEQEKEE RLARLRRYEE KQEGRRSEQY RSKDSVAHTT
     MLNGGKMSEE PWEGDPESEK ANFVQEELYV HGKVCIVDDR IAICGSANIN DRSQLGYHDS
     ELAIVVEDQD FIDSMMDGKP YRASRLAATL RRQLWREHLG LLPAQDYDAS KHPNAQPPNV
     CLNEILEGPE NDFVTDPLND DLWKTWTEQA TTNTEVYRML FRADPDDNIR TFEEYDNFRP
     QGGIKEGHLF DPYQPVKDVR EKLDQIKGHL VWMPLDFLKD AEMAEPGLAV NQITEASLLL
     TRFGRYFFAN LDAEHLYLIF CYLCPNSGVL RCNQDFDTI
//
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