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Database: UniProt
Entry: A0A0W7WB08_9MICO
LinkDB: A0A0W7WB08_9MICO
Original site: A0A0W7WB08_9MICO 
ID   A0A0W7WB08_9MICO        Unreviewed;       413 AA.
AC   A0A0W7WB08;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   24-JAN-2024, entry version 22.
DE   SubName: Full=Amidohydrolase {ECO:0000313|EMBL:KUF07754.1};
GN   ORFNames=AUL38_07945 {ECO:0000313|EMBL:KUF07754.1};
OS   Leucobacter sp. G161.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC   Leucobacter.
OX   NCBI_TaxID=663704 {ECO:0000313|EMBL:KUF07754.1, ECO:0000313|Proteomes:UP000053012};
RN   [1] {ECO:0000313|EMBL:KUF07754.1, ECO:0000313|Proteomes:UP000053012}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=G161 {ECO:0000313|EMBL:KUF07754.1,
RC   ECO:0000313|Proteomes:UP000053012};
RA   Ge S., Dong X.;
RT   "High quality draft genome sequence of Leucobacter sp. G161, a distinct and
RT   effective chromium reducer.";
RL   Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases.
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:KUF07754.1}.
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DR   EMBL; LOHP01000047; KUF07754.1; -; Genomic_DNA.
DR   RefSeq; WP_059059717.1; NZ_LOHP01000047.1.
DR   AlphaFoldDB; A0A0W7WB08; -.
DR   STRING; 663704.AUL38_07945; -.
DR   OrthoDB; 9777385at2; -.
DR   Proteomes; UP000053012; Unassembled WGS sequence.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   CDD; cd03886; M20_Acy1; 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   NCBIfam; TIGR01891; amidohydrolases; 1.
DR   PANTHER; PTHR11014:SF63; METALLOPEPTIDASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_6G09600)-RELATED; 1.
DR   PANTHER; PTHR11014; PEPTIDASE M20 FAMILY MEMBER; 1.
DR   Pfam; PF07687; M20_dimer; 1.
DR   Pfam; PF01546; Peptidase_M20; 1.
DR   PIRSF; PIRSF005962; Pept_M20D_amidohydro; 1.
DR   SUPFAM; SSF55031; Bacterial exopeptidase dimerisation domain; 1.
DR   SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
PE   4: Predicted;
KW   Hydrolase {ECO:0000313|EMBL:KUF07754.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053012}.
FT   DOMAIN          204..292
FT                   /note="Peptidase M20 dimerisation"
FT                   /evidence="ECO:0000259|Pfam:PF07687"
SQ   SEQUENCE   413 AA;  42953 MW;  83D558A0D904E27E CRC64;
     MTELSLIDRV ATACSGQGFK LRELRRELHQ RPEIGLSLPT TQQTILDFLA PLDGLEITTG
     RGLSSVTAVL RGGREPASGE KPTILLRGDM DGLPVQEATD LPYASRNTGA MHACGHDLHI
     SAVCGAAAAL CALRDELAID VVFMFQPGEE GYGGAKLMID EGVLTAADRP VDAAYGLHVF
     ATELQAGEFA LKPGVLMAAS DLVSITVHGR GGHGSTPHAA QDPIPAASEI VLALQTLVTR
     GFSVFDPVVI TVGAIHGGTA SNVIPDEVEL ALSVRSFSES ARSTVLRRIH EVTSGVTAAH
     GLTATVVVSE HSYPVTVNDP AAIDRAYEVL TPLFGADRLR AMPDPLPGSE DFSYVLNEVP
     GAFLFLGAAP VGTDPTTAPS NHSSLAQFDD SVLADAATAL AGLAVSHHAP AAK
//
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