ID   P20D2_ASPCL             Reviewed;         415 AA.
AC   A1CAX3;
DT   27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 1.
DT   03-AUG-2022, entry version 69.
DE   RecName: Full=Probable carboxypeptidase ACLA_013260;
DE            EC=3.4.17.-;
DE   AltName: Full=Peptidase M20 domain-containing protein ACLA_013260;
DE   Flags: Precursor;
GN   ORFNames=ACLA_013260;
OS   Aspergillus clavatus (strain ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 /
OS   NRRL 1 / QM 1276 / 107).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Fumigati.
OX   NCBI_TaxID=344612;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1;
RX   PubMed=18404212; DOI=10.1371/journal.pgen.1000046;
RA   Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P., Anderson M.J.,
RA   Crabtree J., Silva J.C., Badger J.H., Albarraq A., Angiuoli S., Bussey H.,
RA   Bowyer P., Cotty P.J., Dyer P.S., Egan A., Galens K., Fraser-Liggett C.M.,
RA   Haas B.J., Inman J.M., Kent R., Lemieux S., Malavazi I., Orvis J.,
RA   Roemer T., Ronning C.M., Sundaram J.P., Sutton G., Turner G., Venter J.C.,
RA   White O.R., Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H.,
RA   Wortman J.R., Jiang B., Denning D.W., Nierman W.C.;
RT   "Genomic islands in the pathogenic filamentous fungus Aspergillus
RT   fumigatus.";
RL   PLoS Genet. 4:E1000046-E1000046(2008).
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; DS027049; EAW12891.1; -; Genomic_DNA.
DR   RefSeq; XP_001274317.1; XM_001274316.1.
DR   AlphaFoldDB; A1CAX3; -.
DR   SMR; A1CAX3; -.
DR   STRING; 5057.CADACLAP00000766; -.
DR   EnsemblFungi; EAW12891; EAW12891; ACLA_013260.
DR   GeneID; 4706375; -.
DR   KEGG; act:ACLA_013260; -.
DR   VEuPathDB; FungiDB:ACLA_013260; -.
DR   eggNOG; KOG2275; Eukaryota.
DR   HOGENOM; CLU_021802_3_0_1; -.
DR   OMA; DFIRSHN; -.
DR   OrthoDB; 1432382at2759; -.
DR   Proteomes; UP000006701; 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; Reference proteome;
KW   Secreted; Signal; Zinc.
FT   SIGNAL          1..17
FT                   /evidence="ECO:0000255"
FT   CHAIN           18..415
FT                   /note="Probable carboxypeptidase ACLA_013260"
FT                   /id="PRO_0000411243"
FT   ACT_SITE        177
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   BINDING         145
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         145
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         178
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        97
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        271
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   415 AA;  44188 MW;  79893694272A1413 CRC64;
     MKFPWLLLVK GAASVAAQKP LATSGSGQVL GTFNLEDIIN ASPLLSFHRD IVKIPSTTDN
     EYEVGQFIGD FLEQKHFTVE KQSISDSRFN VYAYQGNNSL PDILVTSHID TVPPFLPYNL
     DYPILGGGHE FDRQSVLIAG RGTVDAKGSV AAQIFAVLEI LEEKPDASIG LLFVVGEEKG
     GIGMETFSKN PSPSSFHTVI FGEPTGLNLV SGHKGVIGFN IKATGRAAHS GYPWLGKNAI
     SALLPVASFT ERLGEIPFQD GGLPSSLKYG NSTVNLGVIQ GGVAVNVVPD SAEAIFSVRV
     AAGTPDESKS IITREVNKFT KNDPNIEVAF YPGGLSPTDL DTDVEGFDII TVNYGTDVPK
     LAIHGGGDRV VKRYLYGPGS ILVAHGEDEA LTVGDLEGAV QGYRVLIEKA LSRDV