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Database: UniProt
Entry: A0A0D0IJ62_9MICO
LinkDB: A0A0D0IJ62_9MICO
Original site: A0A0D0IJ62_9MICO 
ID   A0A0D0IJ62_9MICO        Unreviewed;       399 AA.
AC   A0A0D0IJ62;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   RecName: Full=Peptidase M20 domain-containing protein 2 {ECO:0000256|PIRNR:PIRNR037226};
GN   ORFNames=SD72_13720 {ECO:0000313|EMBL:KIP51699.1};
OS   Leucobacter komagatae.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC   Leucobacter.
OX   NCBI_TaxID=55969 {ECO:0000313|EMBL:KIP51699.1, ECO:0000313|Proteomes:UP000032120};
RN   [1] {ECO:0000313|EMBL:KIP51699.1, ECO:0000313|Proteomes:UP000032120}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VKM ST2845 {ECO:0000313|EMBL:KIP51699.1,
RC   ECO:0000313|Proteomes:UP000032120};
RA   Karlyshev A.V., Kudryashova E.B.;
RT   "Draft genome sequence of Leucobacter komagatae strain VKM ST2845.";
RL   Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the peptidase M20A family.
CC       {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:KIP51699.1}.
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DR   EMBL; JXSQ01000025; KIP51699.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0D0IJ62; -.
DR   Proteomes; UP000032120; Unassembled WGS sequence.
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   Hydrolase {ECO:0000313|EMBL:KIP51699.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000032120}.
FT   DOMAIN          162..262
FT                   /note="Peptidase M20 dimerisation"
FT                   /evidence="ECO:0000259|Pfam:PF07687"
SQ   SEQUENCE   399 AA;  41905 MW;  19246E27A49D931C CRC64;
     MDRVIARIET LRPELEQLAV ELYEDPETAF QEHRSVARIA QLLERHGHEA TVGAFGLPTA
     FVATVGTEGP HFAIVAEYDA LPGVGHACGH NIIAGVAIGA FLALAPEVAE LGGRLSLIGT
     PAEESGGGKE HVLRAGGFDD VDAAGMVHPS VGNQVSPIYG SGTSGVRRVR VRYHGRAAHA
     AGSPYLGLNA LDAVVTAYQS IAQLRQHILP IDRIHGVIVN GGQAANIVPE FTEAEFLVRS
     SNIETLNVLT ERVIEIFEAA ALATGTRAEI EPDFEPPYLP LKQNVSLVKH WAKHLERSGR
     TVPLQPARVT HGGPSTDMGN VSWAIPSVHP ALGLGGGPDV LPHNASFAAS TIEPPAFAAL
     ADAASALAGL AADYLSDAAL REAAAAEFDR AGGRKRWEG
//
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