ID   P20D1_ASPCL             Reviewed;         452 AA.
AC   A1CE70;
DT   27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 1.
DT   03-AUG-2022, entry version 71.
DE   RecName: Full=Probable carboxypeptidase ACLA_088580;
DE            EC=3.4.17.-;
DE   AltName: Full=Peptidase M20 domain-containing protein ACLA_088580;
DE   Flags: Precursor;
GN   ORFNames=ACLA_088580;
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; DS027052; EAW11169.1; -; Genomic_DNA.
DR   RefSeq; XP_001272595.1; XM_001272594.1.
DR   AlphaFoldDB; A1CE70; -.
DR   SMR; A1CE70; -.
DR   STRING; 5057.CADACLAP00008451; -.
DR   EnsemblFungi; EAW11169; EAW11169; ACLA_088580.
DR   GeneID; 4705004; -.
DR   KEGG; act:ACLA_088580; -.
DR   VEuPathDB; FungiDB:ACLA_088580; -.
DR   eggNOG; KOG2275; Eukaryota.
DR   HOGENOM; CLU_021802_3_0_1; -.
DR   OMA; VSGHKGM; -.
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..18
FT                   /evidence="ECO:0000255"
FT   CHAIN           19..452
FT                   /note="Probable carboxypeptidase ACLA_088580"
FT                   /id="PRO_0000411227"
FT   ACT_SITE        207
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   BINDING         175
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         175
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         208
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        107
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        156
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   452 AA;  47419 MW;  8EA0B6E52F42301C CRC64;
     MRSLTLLLSL STALRSVAAP HPASPQGQIP LGGIPSASTS EVGIGIGIGI EEDPFPPAAG
     SGHNDLEDVI NASPLLSFHR DLVSIESISG HEARAAAFVA DFLEAHNFTV VKQPVAGDRV
     NIFASPRAHA HSRPEILLTS HLDTVPPFIP YSLHRNDSRP TDRQLIRIAG RGAVDAKASV
     AAQIFAALDI LHADPSAPLG LLFVVGEEVG GDGMKAFSHD PRLNPAPSRF HTVIFGEPTD
     FALVAGHKGM LGFEVLASGR PAHSGYPWLG RSAVSAILPA LRRVDALGHI PVHHGGLPAS
     HKYGRTTLNI GVLEGGVATN VVPAAARADV AVRLAAGSVD DARAIIAAAV ADATHRDPAV
     VVDFSRHLEA YPPQDLDVDV PGFEITTVNY GTDVPNLHLH PRPDGPVKRY LYGPGSIFVA
     HGENEGLTVG ALEEAVGGYK KLVQAALERT RA