ID A0A0D0G9T4_9BACI Unreviewed; 373 AA. AC A0A0D0G9T4; DT 29-APR-2015, integrated into UniProtKB/TrEMBL. DT 29-APR-2015, sequence version 1. DT 03-MAY-2023, entry version 27. DE RecName: Full=Peptidase M20 dimerisation domain-containing protein {ECO:0000259|Pfam:PF07687}; GN ORFNames=B4166_1322 {ECO:0000313|EMBL:KIO71367.1}, B4167_1706 GN {ECO:0000313|EMBL:KIO73982.1}; OS Caldibacillus thermoamylovorans. OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Caldibacillus. OX NCBI_TaxID=35841 {ECO:0000313|EMBL:KIO73982.1, ECO:0000313|Proteomes:UP000032076}; RN [1] {ECO:0000313|Proteomes:UP000032076, ECO:0000313|Proteomes:UP000032097} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=B4166 {ECO:0000313|EMBL:KIO71367.1, RC ECO:0000313|Proteomes:UP000032097}, and B4167 RC {ECO:0000313|EMBL:KIO73982.1, ECO:0000313|Proteomes:UP000032076}; RA Krawcyk A.O., Berendsen E.M., Eijlander R.T., de Jong A., Wells-Bennik M., RA Kuipers O.P.; RT "Draft Genome Sequences of Four Bacillus thermoamylovorans Strains, RT Isolated From Food Products."; RL Submitted (JAN-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:KIO73982.1}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; JXLT01000001; KIO71367.1; -; Genomic_DNA. DR EMBL; JXLU01000018; KIO73982.1; -; Genomic_DNA. DR RefSeq; WP_041902021.1; NZ_JXLU01000018.1. DR AlphaFoldDB; A0A0D0G9T4; -. DR EnsemblBacteria; KIO71367; KIO71367; B4166_1322. DR EnsemblBacteria; KIO73982; KIO73982; B4167_1706. DR PATRIC; fig|35841.7.peg.67; -. DR OrthoDB; 9776731at2; -. DR Proteomes; UP000032076; Unassembled WGS sequence. DR Proteomes; UP000032097; Unassembled WGS sequence. DR GO; GO:0016787; F:hydrolase activity; IEA:InterPro. DR CDD; cd08018; M20_Acy1_amhX-like; 1. DR Gene3D; 3.30.70.360; -; 1. DR Gene3D; 3.40.630.10; Zn peptidases; 1. DR InterPro; IPR037484; AmhX-like. DR InterPro; IPR017439; Amidohydrolase. DR InterPro; IPR036264; Bact_exopeptidase_dim_dom. DR InterPro; IPR002933; Peptidase_M20. DR InterPro; IPR011650; Peptidase_M20_dimer. DR PANTHER; PTHR11014:SF122; AMIDOHYDROLASE AMHX; 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. DR TIGRFAMs; TIGR01891; amidohydrolases; 1. PE 4: Predicted; FT DOMAIN 176..266 FT /note="Peptidase M20 dimerisation" FT /evidence="ECO:0000259|Pfam:PF07687" SQ SEQUENCE 373 AA; 41463 MW; F9E0A84A620A7F7C CRC64; MRAIEQEVIN TYRYLHNHPE ISWHEFKTTA YIKEKLKEYC SKVITFKNHT GVIGEFGNFD GKRPVVGLRA DIDALWQEVE GKFKPNHSCG HDAHTAIILG VLWKLAEEKL LHDKVAIKFI FQPAEETGDG ALMMVQNHVI DNLDYLYGIH VRPYHETPMG VAAPVIIHGA AKNYEGVIKG EDAHGARPHL NLNAIEVGAQ IVNLFNQIHL DPTVPHSVKM TKFLAGGKSL NIIPGNASFG LDLRAQNNEL MTTLDKKVRE ILSTIANLYG ITIELTHEDY VPAAVMNDTA ISIMKKAIIE TIGESNMKPS ILTPGGDDFH FYSIKKPTLK ATMLGLGCDL RPGLHHPLMT LNEEALLIGV NILFQAIIKT YGL //