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