ID A0A0L1J745_ASPNO Unreviewed; 430 AA.
AC A0A0L1J745;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE SubName: Full=Peptidase {ECO:0000313|EMBL:KNG87243.1};
GN ORFNames=ANOM_003550 {ECO:0000313|EMBL:KNG87243.1};
OS Aspergillus nomiae NRRL 13137.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=1509407 {ECO:0000313|EMBL:KNG87243.1, ECO:0000313|Proteomes:UP000037505};
RN [1] {ECO:0000313|EMBL:KNG87243.1, ECO:0000313|Proteomes:UP000037505}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL 13137 {ECO:0000313|EMBL:KNG87243.1,
RC ECO:0000313|Proteomes:UP000037505};
RA Moore M.G., Shannon B.M., Brian M.M.;
RT "The Genome of the Aflatoxigenic Filamentous Fungus Aspergillus nomius.";
RL Submitted (JUN-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}.
CC -!- SIMILARITY: Belongs to the peptidase M20A family.
CC {ECO:0000256|ARBA:ARBA00006247}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KNG87243.1}.
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DR EMBL; JNOM01000087; KNG87243.1; -; Genomic_DNA.
DR RefSeq; XP_015408166.1; XM_015548807.1.
DR AlphaFoldDB; A0A0L1J745; -.
DR STRING; 1509407.A0A0L1J745; -.
DR GeneID; 26805354; -.
DR OrthoDB; 2875217at2759; -.
DR Proteomes; UP000037505; 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 Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000037505};
KW Secreted {ECO:0000256|ARBA:ARBA00022525}; Signal {ECO:0000256|SAM:SignalP};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT SIGNAL 1..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..430
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5005553487"
FT DOMAIN 226..318
FT /note="Peptidase M20 dimerisation"
FT /evidence="ECO:0000259|Pfam:PF07687"
SQ SEQUENCE 430 AA; 45585 MW; 394D1C2CA12F6F1F CRC64;
MKSIYSLLLS AALTAASPHP AFPQSPLGVP TTSSPSTGTF NSAEEVINAS PFLSFHRDIV
QIESISSNEH NVGEFIADFL RARNFTVIKQ VVISSSQTEN QERFNIFAYP SSNTPEVLIT
SHIDTVPPFI PYSLDTDSTT DNDPSTIRIS GRGSVDAKGS VAAQVFAALD VLEQNPSAPL
GLLFVVGEET GGDGMRAFSE SPLNPAPSSF HTVIFGEPTE LALVSGHKGM LGFEIVANGH
AAHSGYPWLG HSAISAVLPA LSRVDQLGNI PADKGGLPSS PKYGNTTVNI GRVNAGVAAN
VVPATARADV AVRLAAGTPD EARDIVGRAV RDATDGNPDV YADFSTRTEG YPPQDLDTDV
EGFNVTTVNY GTDVPNLQIH EREDGPVRRY LYGPGSIHVA HGDNEAITVG DLQEAVRGYR
KLIEAALQRQ
//
