ID   A0A0F8V1P6_9EURO        Unreviewed;       437 AA.
AC   A0A0F8V1P6;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   RecName: Full=Peptidase M20 domain-containing protein 2 {ECO:0000256|PIRNR:PIRNR037226};
GN   ORFNames=ARAM_003711 {ECO:0000313|EMBL:KKK25669.1};
OS   Aspergillus rambellii.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=308745 {ECO:0000313|EMBL:KKK25669.1, ECO:0000313|Proteomes:UP000034291};
RN   [1] {ECO:0000313|EMBL:KKK25669.1, ECO:0000313|Proteomes:UP000034291}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SRRC1468 {ECO:0000313|EMBL:KKK25669.1,
RC   ECO:0000313|Proteomes:UP000034291};
RA   Moore G.G., Beltz S.B., Mack B.M.;
RT   "Draft Genome Sequences of Two Closely-Related Aflatoxigenic Aspergillus
RT   Species Obtained from the Cote d'Ivoire.";
RL   Submitted (FEB-2015) 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}.
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:KKK25669.1}.
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DR   EMBL; JZBS01000703; KKK25669.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0F8V1P6; -.
DR   STRING; 308745.A0A0F8V1P6; -.
DR   OrthoDB; 1074531at2759; -.
DR   Proteomes; UP000034291; 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:UP000034291};
KW   Secreted {ECO:0000256|ARBA:ARBA00022525}.
FT   DOMAIN          196..285
FT                   /note="Peptidase M20 dimerisation"
FT                   /evidence="ECO:0000259|Pfam:PF07687"
SQ   SEQUENCE   437 AA;  46825 MW;  2D1D25C67154F641 CRC64;
     MGQLSQHDVQ VLQAALQDQT DVVTAITNAI NDVNPKLYDI NKKIHANPEL GYAEFQAHDN
     ITKMFEDLGY QVTKHAYGLE TSFLVEYGTG GRVVAFNAEY DALPGIGHAC GHNLIAMMSI
     GAFLGVAKML KESGIKGRVR LVGTPAEEGG GGKLKLIDAG AYQDVDACLM VHPGPLNGCP
     GFTGDAYMPT IANHKFSIHF TGRSAHAAVA PWEGINALDA VVLAYNGISM LRQQIMPAER
     IHSVISEGGK RPNIIPEHAS LEYYIRSPTL KSADALMSRA LKCFEGAALQ TGCTMKFEKI
     NTYADVRNNK SISSLYAAAM GNMGSPVKCD FAALPLPGST DQGNVSYECP AFHGYVGIQA
     APGATNHTPG FTAAAEKEEA HTLCLESAKG MAIVGWQILA DENIAKQVRQ DFEDDRNARE
     SDVDLRMYDP LPGGGCC
//