ID   MEP1_ASPFU              Reviewed;         322 AA.
AC   Q4WJ01;
DT   05-APR-2011, integrated into UniProtKB/Swiss-Prot.
DT   05-APR-2011, sequence version 2.
DT   03-AUG-2022, entry version 73.
DE   RecName: Full=Extracellular metalloprotease AFUA_1G07730;
DE            EC=3.4.24.-;
DE   Flags: Precursor;
GN   ORFNames=AFUA_1G07730;
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;
OC   Aspergillus subgen. Fumigati.
OX   NCBI_TaxID=330879;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100;
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.W., Bowyer P.,
RA   Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.L.,
RA   Fedorova N., Fedorova N.D., Feldblyum T.V., Fischer R., Fosker N.,
RA   Fraser A., Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K.,
RA   Griffith-Jones S., Gwilliam R., Haas B.J., Haas H., Harris D.E.,
RA   Horiuchi H., Huang J., Humphray S., Jimenez J., Keller N., Khouri H.,
RA   Kitamoto K., Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafton A.,
RA   Latge J.-P., Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L.,
RA   Mohamoud Y., Molina M., Monod M., Mouyna I., Mulligan S., Murphy L.D.,
RA   O'Neil S., Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L.,
RA   Quail M.A., Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U.,
RA   Renauld H., Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M.,
RA   Ronning C.M., Rutter S., Salzberg S.L., Sanchez M., Sanchez-Ferrero J.C.,
RA   Saunders D., Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F.,
RA   Turner G., Vazquez de Aldana C.R., Weidman J., White O., Woodward J.R.,
RA   Yu J.-H., Fraser C.M., Galagan J.E., Asai K., Machida M., Hall N.,
RA   Barrell B.G., Denning D.W.;
RT   "Genomic sequence of the pathogenic and allergenic filamentous fungus
RT   Aspergillus fumigatus.";
RL   Nature 438:1151-1156(2005).
CC   -!- FUNCTION: Secreted metalloproteinase that allows assimilation of
CC       proteinaceous substrates. Plays a pivotal role as a pathogenicity
CC       determinant during infections and contributes to the ability of the
CC       pathogen to persist within the mammalian host (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the peptidase M43B family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=EAL88481.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AAHF01000007; EAL88481.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; XP_750519.1; XM_745426.1.
DR   AlphaFoldDB; Q4WJ01; -.
DR   SMR; Q4WJ01; -.
DR   GeneID; 3507778; -.
DR   KEGG; afm:AFUA_1G07730; -.
DR   eggNOG; ENOG502S6EM; Eukaryota.
DR   HOGENOM; CLU_048726_0_2_1; -.
DR   InParanoid; Q4WJ01; -.
DR   OMA; FAPHNIQ; -.
DR   OrthoDB; 1569419at2759; -.
DR   Proteomes; UP000002530; Chromosome 1.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd04275; ZnMc_pappalysin_like; 1.
DR   Gene3D; 3.40.390.10; -; 1.
DR   InterPro; IPR024079; MetalloPept_cat_dom_sf.
DR   InterPro; IPR008754; Peptidase_M43.
DR   Pfam; PF05572; Peptidase_M43; 1.
PE   3: Inferred from homology;
KW   Disulfide bond; Glycoprotein; Hydrolase; Metal-binding; Metalloprotease;
KW   Protease; Reference proteome; Secreted; Signal; Virulence; Zinc.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000255"
FT   CHAIN           23..322
FT                   /note="Extracellular metalloprotease AFUA_1G07730"
FT                   /id="PRO_0000407198"
FT   ACT_SITE        234
FT                   /evidence="ECO:0000250"
FT   BINDING         233
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         237
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        123
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        197
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        272..299
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   322 AA;  35778 MW;  58FBF53C7E93B873 CRC64;
     MLPFNSCVYV LLIISLMSNC RALCRATALQ GRSLCATGGP DAAFRAEHER LSAFESRPSS
     GSYDMRRALE PIEIETWFHI VSGETDADLV TDEMVILQLH YLQKAYEKAS ISYRLKGVTR
     HINETWARNG DDSAMKKALR RGGYSTLNVY FQTNLQPPST TDFARWTSDG DNRHAYNSDL
     APLSVLGFCT LPDPSINSSS PRSSYSKDGC NVLAKTMPGG PMTHYNRGGT AIHEIGHWNG
     LLHTFEGESC SEDNAGDYIA DTPQQSVPTD GCPSQKDSCP DSPGLDDIHN FMDYSSDDCY
     ASFTSNQLKR MRDMWFSMRK GK