ID P20D1_ASPFN Reviewed; 418 AA.
AC B8NPN0;
DT 27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT 03-MAR-2009, sequence version 1.
DT 27-MAR-2024, entry version 69.
DE RecName: Full=Probable carboxypeptidase AFLA_000940;
DE EC=3.4.17.-;
DE AltName: Full=Peptidase M20 domain-containing protein AFLA_000940;
DE Flags: Precursor;
GN ORFNames=AFLA_000940;
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}.
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DR EMBL; EQ963482; EED47453.1; -; Genomic_DNA.
DR RefSeq; XP_002382295.1; XM_002382254.1.
DR AlphaFoldDB; B8NPN0; -.
DR SMR; B8NPN0; -.
DR STRING; 332952.B8NPN0; -.
DR EnsemblFungi; EED47453; EED47453; AFLA_000940.
DR VEuPathDB; FungiDB:AFLA_011420; -.
DR eggNOG; KOG2275; Eukaryota.
DR HOGENOM; CLU_021802_3_0_1; -.
DR OMA; VHIESDG; -.
DR OrthoDB; 2875217at2759; -.
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 CDD; cd05652; M20_ArgE_DapE-like_fungal; 1.
DR Gene3D; 3.30.70.360; -; 1.
DR Gene3D; 3.40.630.10; Zn peptidases; 1.
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 PANTHER; PTHR43808; ACETYLORNITHINE DEACETYLASE; 1.
DR PANTHER; PTHR43808:SF8; M20_DIMER DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF07687; M20_dimer; 1.
DR Pfam; PF01546; Peptidase_M20; 1.
DR SUPFAM; SSF55031; Bacterial exopeptidase dimerisation domain; 1.
DR SUPFAM; SSF53187; Zn-dependent exopeptidases; 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..18
FT /evidence="ECO:0000255"
FT CHAIN 19..418
FT /note="Probable carboxypeptidase AFLA_000940"
FT /id="PRO_0000411229"
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; 44930 MW; DE0A1B1F094A4BCE CRC64;
MKATDLFHVT VLVAGALALE HQQPLIGDLS QDLNHIIDSS PLLSFHRALV QIPSISEHEK
NVGEYVLDFL SSQNLTVEKQ IVTPESDTEE ERFNIYAYVG KNRQPDVLVT SHIDTVPPFI
PYSLHAPTSD 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
//
