ID   P20D1_ASPOR             Reviewed;         418 AA.
AC   Q2U9N9;
DT   27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT   24-JAN-2006, sequence version 1.
DT   03-AUG-2022, entry version 84.
DE   RecName: Full=Probable carboxypeptidase AO090166000075;
DE            EC=3.4.17.-;
DE   AltName: Full=Peptidase M20 domain-containing protein AO090166000075;
DE   Flags: Precursor;
GN   ORFNames=AO090166000075;
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   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC       Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000250};
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the peptidase M20A family. {ECO:0000305}.
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DR   EMBL; AP007163; BAE61726.1; -; Genomic_DNA.
DR   RefSeq; XP_001822859.1; XM_001822807.2.
DR   AlphaFoldDB; Q2U9N9; -.
DR   SMR; Q2U9N9; -.
DR   STRING; 510516.Q2U9N9; -.
DR   EnsemblFungi; BAE61726; BAE61726; AO090166000075.
DR   GeneID; 5994915; -.
DR   KEGG; aor:AO090166000075; -.
DR   VEuPathDB; FungiDB:AO090166000075; -.
DR   HOGENOM; CLU_021802_3_0_1; -.
DR   OMA; DFIRSHN; -.
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:0008233; F:peptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   InterPro; IPR001261; ArgE/DapE_CS.
DR   InterPro; IPR036264; Bact_exopeptidase_dim_dom.
DR   InterPro; IPR002933; Peptidase_M20.
DR   InterPro; IPR011650; Peptidase_M20_dimer.
DR   Pfam; PF07687; M20_dimer; 1.
DR   Pfam; PF01546; Peptidase_M20; 1.
DR   SUPFAM; SSF55031; SSF55031; 1.
DR   PROSITE; PS00758; ARGE_DAPE_CPG2_1; 1.
DR   PROSITE; PS00759; ARGE_DAPE_CPG2_2; 1.
PE   3: Inferred from homology;
KW   Glycoprotein; Hydrolase; Metal-binding; Protease; Reference proteome;
KW   Secreted; Signal; Zinc.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000255"
FT   CHAIN           19..418
FT                   /note="Probable carboxypeptidase AO090166000075"
FT                   /id="PRO_0000411231"
FT   ACT_SITE        179
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   BINDING         147
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         147
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         180
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        74
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        168
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   418 AA;  44844 MW;  395121A75BA4D246 CRC64;
     MKATDLFHVT ALVAGALALE HQQPLIGDLS QDLNHIIDSS PLLSFHRALV QIPSISEHEK
     NVGEYVLDFL SSQNLTVEKQ IVTPESDTEE ERFNIYAYVG KNRQPDVLVT SHIDTVPPFI
     PYSLHAPTSG TSFIRTDLVI AGRGTVDAKA SVAAIVFAAL ETLDENPNAS IGLLFDVGEE
     NSGVGMKHFS NSELNPTPPT YHTVIFGEPT ELSLVAAHKG TLGFKLVAEG KAAHSGYPWL
     GESAISSLIP VLAHLDTLQD LPPEKGGLLR SETLGKSTLN IGRVHGGIAA NVVPAHAEAA
     ISVRLAAGTP EDTRTIIERA VAKVTSGDRS VYPDFGDRKA GAPPQYFDVD VDGFEVITVN
     YGTDAPALKI HDQRTQRVKR YLYGPGSILV AHADNEAITV GELEEAVRGY KRLIAASL