ID   P20D1_NEOFI             Reviewed;         441 AA.
AC   A1DM79;
DT   27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 1.
DT   03-AUG-2022, entry version 80.
DE   RecName: Full=Probable carboxypeptidase NFIA_052450;
DE            EC=3.4.17.-;
DE   AltName: Full=Peptidase M20 domain-containing protein NFIA_052450;
DE   Flags: Precursor;
GN   ORFNames=NFIA_052450;
OS   Neosartorya fischeri (strain ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164
OS   / JCM 1740 / NRRL 181 / WB 181) (Aspergillus fischerianus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Fumigati.
OX   NCBI_TaxID=331117;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164 / JCM 1740 / NRRL 181
RC   / WB 181;
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; DS027698; EAW15900.1; -; Genomic_DNA.
DR   RefSeq; XP_001257797.1; XM_001257796.1.
DR   AlphaFoldDB; A1DM79; -.
DR   SMR; A1DM79; -.
DR   STRING; 36630.CADNFIAP00004851; -.
DR   EnsemblFungi; EAW15900; EAW15900; NFIA_052450.
DR   GeneID; 4584312; -.
DR   KEGG; nfi:NFIA_052450; -.
DR   VEuPathDB; FungiDB:NFIA_052450; -.
DR   eggNOG; KOG2275; Eukaryota.
DR   HOGENOM; CLU_021802_3_0_1; -.
DR   OMA; VSGHKGM; -.
DR   OrthoDB; 1432382at2759; -.
DR   Proteomes; UP000006702; 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   InterPro; IPR001160; Peptidase_M20C.
DR   Pfam; PF07687; M20_dimer; 1.
DR   Pfam; PF01546; Peptidase_M20; 1.
DR   PRINTS; PR00934; XHISDIPTASE.
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..16
FT                   /evidence="ECO:0000255"
FT   CHAIN           17..441
FT                   /note="Probable carboxypeptidase NFIA_052450"
FT                   /id="PRO_0000411236"
FT   ACT_SITE        198
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   BINDING         166
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         166
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         199
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        88
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        150
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        354
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        373
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   441 AA;  46450 MW;  00E331ED7B65C009 CRC64;
     MKPLSSLLLS AALSAAAPPH PASPQAPLAD IPRIGVETRT EFSQNSLDDV VNASPLLSFH
     RDLVSIESIS GNEGAAGAFV ADFLESHNFT VIKQPVTTES DARFNIFAFP KSQSHSLDES
     HPSHGPQILL TSHIDTVPPF IPYSLHRDAN DTDDRNILIA GRGTVDAKGS VAAQIFAALD
     TLAVQPPAPL GLLFVVGEET GGDGMKAFSQ STHLNPSPSR FHTVIFGEPT ELALVAGHKG
     MLGFEVAAHG HAAHSGYPWL GESAISAILP ALARVDHLGN IPVEEGGLPA SDKYGRTTVN
     IGQMEGGVAA NVVPSEARAG VAVRLAAGTH DEAREIVLKA VRDATGGDDR VVVNFSLEGY
     GPQDLDTDVA GFNVTTVNYG TDVPNLQLHP RPDGKVKRYL YGPGTIHVAH GDNEALTVAQ
     LEEAVRGYKK LIQAALDRST S