ID   A0A3F3QHP7_9EURO        Unreviewed;       417 AA.
AC   A0A3F3QHP7;
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_165618 {ECO:0000313|EMBL:RDH38479.1};
OS   Aspergillus welwitschiae.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=1341132 {ECO:0000313|EMBL:RDH38479.1, ECO:0000313|Proteomes:UP000253729};
RN   [1] {ECO:0000313|EMBL:RDH38479.1, ECO:0000313|Proteomes:UP000253729}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 139.54b {ECO:0000313|EMBL:RDH38479.1,
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; KZ852033; RDH38479.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3F3QHP7; -.
DR   STRING; 1341132.A0A3F3QHP7; -.
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:SF0; XAA-ARG DIPEPTIDASE; 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   Reference proteome {ECO:0000313|Proteomes:UP000253729};
KW   Secreted {ECO:0000256|ARBA:ARBA00022525}.
FT   DOMAIN          191..283
FT                   /note="Peptidase M20 dimerisation"
FT                   /evidence="ECO:0000259|Pfam:PF07687"
SQ   SEQUENCE   417 AA;  44935 MW;  BBFB1E248B968369 CRC64;
     MSKVLRLLLT RQSLTLEAVP SGARKGRVLT AQVDAHIHDN PELCFKEHKA HNAICDYLEA
     AGVAVIRQAY GQETSFVAEY GDKDGETVDF CAEYDALPEI GHGCGHNLIA VSSIASFLGV
     VDVMKRIKVP GKVRLLGTPA EEGGGGKIKL IEAGALKNTT ASLMSHPTPQ FPHMPAGSAG
     VAFGSCLAAT GFLADFKGKP AHAAQMPWAG VNALDAASLA YQAVGLLRQH IRPTDRINII
     IPEGGTAHNV IPDKAQIRVN VRSETLKEMN ALRERVENCM KGAALATGCE VDIVSAMDPY
     ADIRPNEGLC KEFTRYMGSK GMKYYCDLQK KDIGAFSTDM GNISYEVPSF HGHYFIPTPP
     GTAMHTEAFR DSAKTEEAHN ITMSVGKGMA VAGLKVLTDE SFAAQVKDYF EKDKKLR
//