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MEP1_ASPOR
ID   MEP1_ASPOR              Reviewed;         318 AA.
AC   Q2UBF0;
DT   05-APR-2011, integrated into UniProtKB/Swiss-Prot.
DT   24-JAN-2006, sequence version 1.
DT   03-AUG-2022, entry version 66.
DE   RecName: Full=Extracellular metalloprotease AO090012001025;
DE            EC=3.4.24.-;
DE   Flags: Precursor;
GN   ORFNames=AO090012001025;
OS   Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=510516;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 42149 / RIB 40;
RX   PubMed=16372010; DOI=10.1038/nature04300;
RA   Machida M., Asai K., Sano M., Tanaka T., Kumagai T., Terai G., Kusumoto K.,
RA   Arima T., Akita O., Kashiwagi Y., Abe K., Gomi K., Horiuchi H.,
RA   Kitamoto K., Kobayashi T., Takeuchi M., Denning D.W., Galagan J.E.,
RA   Nierman W.C., Yu J., Archer D.B., Bennett J.W., Bhatnagar D.,
RA   Cleveland T.E., Fedorova N.D., Gotoh O., Horikawa H., Hosoyama A.,
RA   Ichinomiya M., Igarashi R., Iwashita K., Juvvadi P.R., Kato M., Kato Y.,
RA   Kin T., Kokubun A., Maeda H., Maeyama N., Maruyama J., Nagasaki H.,
RA   Nakajima T., Oda K., Okada K., Paulsen I., Sakamoto K., Sawano T.,
RA   Takahashi M., Takase K., Terabayashi Y., Wortman J.R., Yamada O.,
RA   Yamagata Y., Anazawa H., Hata Y., Koide Y., Komori T., Koyama Y.,
RA   Minetoki T., Suharnan S., Tanaka A., Isono K., Kuhara S., Ogasawara N.,
RA   Kikuchi H.;
RT   "Genome sequencing and analysis of Aspergillus oryzae.";
RL   Nature 438:1157-1161(2005).
CC   -!- FUNCTION: Secreted metalloproteinase that allows assimilation of
CC       proteinaceous substrates. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the peptidase M43B family. {ECO:0000305}.
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DR   EMBL; AP007161; BAE61115.1; -; Genomic_DNA.
DR   RefSeq; XP_001727954.1; XM_001727902.2.
DR   AlphaFoldDB; Q2UBF0; -.
DR   SMR; Q2UBF0; -.
DR   MEROPS; M43.008; -.
DR   EnsemblFungi; BAE61115; BAE61115; AO090012001025.
DR   GeneID; 5988428; -.
DR   KEGG; aor:AO090012001025; -.
DR   VEuPathDB; FungiDB:AO090012001025; -.
DR   HOGENOM; CLU_048726_0_2_1; -.
DR   OMA; LYFQTDL; -.
DR   Proteomes; UP000006564; Chromosome 4.
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; Zinc.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000255"
FT   CHAIN           24..318
FT                   /note="Extracellular metalloprotease AO090012001025"
FT                   /id="PRO_0000407199"
FT   ACT_SITE        230
FT                   /evidence="ECO:0000250"
FT   BINDING         229
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
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   CARBOHYD        106
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        121
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        193
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        268..295
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   318 AA;  35208 MW;  07B262717EA8E548 CRC64;
     MSHFPTLHIL ILVIANLQIQ CFAFVSQSRG FCATGPPTES LKAEYRRLSA LGSQSYNPVD
     SESRAAITPI VIDTWFHIIT GEAGTELISD EMIADQLSYL QNAYWNATIS YRLQGVTRSA
     NDTWARNEDE MAMKTVLRRG SYRTLNVYFH TDLQASPNAG ARAFDIVRRE LGVSQQQPTS
     MLGFCTLPDP SINASSPPST YIKDGCNVLA ETMPGGSLAH YNRGGTAIHE IGHWNGLLHT
     FEGESCSSDN EGDFIADTPQ QSKPTEGCPA QKDSCPELPG FDAIHNFMDY SSDECYDSFT
     PDQVSRMRSM WFAMRDGK
 
 
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