ID   P20D2_ASPFN             Reviewed;         430 AA.
AC   B8N4P0;
DT   27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT   03-MAR-2009, sequence version 1.
DT   03-AUG-2022, entry version 63.
DE   RecName: Full=Probable carboxypeptidase AFLA_037450;
DE            EC=3.4.17.-;
DE   AltName: Full=Peptidase M20 domain-containing protein AFLA_037450;
DE   Flags: Precursor;
GN   ORFNames=AFLA_037450;
OS   Aspergillus flavus (strain ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357
OS   / JCM 12722 / SRRC 167).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=332952;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357 / JCM 12722 / SRRC
RC   167;
RX   PubMed=25883274; DOI=10.1128/genomea.00168-15;
RA   Nierman W.C., Yu J., Fedorova-Abrams N.D., Losada L., Cleveland T.E.,
RA   Bhatnagar D., Bennett J.W., Dean R., Payne G.A.;
RT   "Genome sequence of Aspergillus flavus NRRL 3357, a strain that causes
RT   aflatoxin contamination of food and feed.";
RL   Genome Announc. 3:E0016815-E0016815(2015).
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; EQ963473; EED56471.1; -; Genomic_DNA.
DR   RefSeq; XP_002375253.1; XM_002375212.1.
DR   AlphaFoldDB; B8N4P0; -.
DR   SMR; B8N4P0; -.
DR   STRING; 5059.CADAFLAP00003118; -.
DR   EnsemblFungi; EED56471; EED56471; AFLA_037450.
DR   VEuPathDB; FungiDB:AFLA_037450; -.
DR   eggNOG; KOG2275; Eukaryota.
DR   HOGENOM; CLU_021802_3_0_1; -.
DR   OMA; VSGHKGM; -.
DR   Proteomes; UP000001875; Unassembled WGS sequence.
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; Secreted; Signal; Zinc.
FT   SIGNAL          1..16
FT                   /evidence="ECO:0000255"
FT   CHAIN           17..430
FT                   /note="Probable carboxypeptidase AFLA_037450"
FT                   /id="PRO_0000411244"
FT   ACT_SITE        188
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   BINDING         156
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         156
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         189
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        84
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        285
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   430 AA;  45810 MW;  905C9C23FBBF76FD CRC64;
     MKSIYSLVLC TALTAASPHP AFPQSPLGVP TTSSPSTGTF NSAEEVINAS PFLSFHRDIV
     QIESISSNEH NVGEFIADFL RARNFTVIEQ AVTSSSQREN QERFNVFAYP SSNTPEILIT
     SHIDTVPPFI PYSLDTDSTT DNDPSTIRIS GRGSVDAKGS VAAQIFAALD VLEQNPSAPL
     GLLFVVGEET GGDGMRAFSE SSLNPAPSAF HTVIFGEPTE LALVSGHKGM LGFEIVAKGH
     AAHSGYPWLG RSAISAVLPA LSRVDQLGNI PADKGGLPSS PKYGNTTVNI GRVDAGVAAN
     VVPATARADV AVRLAAGTPD EARDIVRRAV RDATDGNPDV YAEFNTRSEG YPPQDLDTDV
     DGFDITTVNY GTDVPNLQIH EREDGPVRRY LYGPGSIHVA HGDNEAITVG DLQEAVRGYR
     KLIEAALQRR