ID   A0A3F3Q2A7_9EURO        Unreviewed;       414 AA.
AC   A0A3F3Q2A7;
DT   16-JAN-2019, integrated into UniProtKB/TrEMBL.
DT   16-JAN-2019, sequence version 1.
DT   27-MAR-2024, entry version 17.
DE   RecName: Full=Peptidase M20 domain-containing protein 2 {ECO:0000256|PIRNR:PIRNR037226};
GN   ORFNames=BDQ94DRAFT_170461 {ECO:0000313|EMBL:RDH33298.1};
OS   Aspergillus welwitschiae.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=1341132 {ECO:0000313|EMBL:RDH33298.1, ECO:0000313|Proteomes:UP000253729};
RN   [1] {ECO:0000313|EMBL:RDH33298.1, ECO:0000313|Proteomes:UP000253729}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 139.54b {ECO:0000313|EMBL:RDH33298.1,
RC   ECO:0000313|Proteomes:UP000253729};
RG   DOE Joint Genome Institute;
RA   Vesth T.C., Nybo J., Theobald S., Brandl J., Frisvad J.C., Nielsen K.F.,
RA   Lyhne E.K., Kogle M.E., Kuo A., Riley R., Clum A., Nolan M., Lipzen A.,
RA   Salamov A., Henrissat B., Wiebenga A., De vries R.P., Grigoriev I.V.,
RA   Mortensen U.H., Andersen M.R., Baker S.E.;
RT   "The genomes of Aspergillus section Nigri reveals drivers in fungal
RT   speciation.";
RL   Submitted (JUL-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}.
CC   -!- SIMILARITY: Belongs to the peptidase M20A family.
CC       {ECO:0000256|ARBA:ARBA00006247, ECO:0000256|PIRNR:PIRNR037226}.
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DR   EMBL; KZ852047; RDH33298.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3F3Q2A7; -.
DR   STRING; 1341132.A0A3F3Q2A7; -.
DR   OrthoDB; 1074531at2759; -.
DR   Proteomes; UP000253729; Unassembled WGS sequence.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0016805; F:dipeptidase activity; IEA:InterPro.
DR   CDD; cd05672; M20_ACY1L2-like; 1.
DR   Gene3D; 3.30.70.360; -; 1.
DR   Gene3D; 3.40.630.10; Zn peptidases; 1.
DR   InterPro; IPR017439; Amidohydrolase.
DR   InterPro; IPR036264; Bact_exopeptidase_dim_dom.
DR   InterPro; IPR002933; Peptidase_M20.
DR   InterPro; IPR011650; Peptidase_M20_dimer.
DR   InterPro; IPR017144; Xaa-Arg_dipeptidase.
DR   NCBIfam; TIGR01891; amidohydrolases; 1.
DR   PANTHER; PTHR30575; PEPTIDASE M20; 1.
DR   PANTHER; PTHR30575:SF8; PEPTIDASE M20 DOMAIN-CONTAINING PROTEIN 2; 1.
DR   Pfam; PF07687; M20_dimer; 1.
DR   Pfam; PF01546; Peptidase_M20; 1.
DR   PIRSF; PIRSF037226; Amidohydrolase_ACY1L2_prd; 1.
DR   SUPFAM; SSF55031; Bacterial exopeptidase dimerisation domain; 1.
DR   SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000313|EMBL:RDH33298.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000253729};
KW   Secreted {ECO:0000256|ARBA:ARBA00022525}.
FT   DOMAIN          192..284
FT                   /note="Peptidase M20 dimerisation"
FT                   /evidence="ECO:0000259|Pfam:PF07687"
SQ   SEQUENCE   414 AA;  45126 MW;  BD2132E3BA071C24 CRC64;
     MTATQTITQS VPTIDEVKVA VDAALESAQT SLRELNREIW CNPETAYQEH RAHDTICDFL
     EKQGFTVTRH AYGLDTSFEA ISGSGGRLIN FNAEYDALPD IGHACGHNLI TTSSVAAFLA
     LSTVLKQYGI PGRTQLLGTP AEENGGGKAK LIDLGAYKGV DVSLMAHAGP KELFPGVVTD
     SVGGVRMNAR KELHCEFTGR SAHAGGNPWE GINALDALVT SYNNVAVLRQ QLRPDERIHC
     AFLDTPTVAN IIPSYTKAYW QVRSPTLKGL NQLMVKVRNC IEAGALATGC EVKIIENELY
     TDIKINDTLC DRYKEHMSKY DRNVIARLEQ VMTGSSDIGN VSYIVPTLHT MFGITDEPGS
     FPHHPKFAAA AGTDYAHQEA VIVGKSLALI GWEMVTSDEL FGIAQKQLKE CLEE
//