ID D7GU43_9FIRM Unreviewed; 398 AA.
AC D7GU43;
DT 10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT 10-AUG-2010, sequence version 1.
DT 27-MAR-2024, entry version 49.
DE RecName: Full=Peptidase M20 domain-containing protein 2 {ECO:0000256|PIRNR:PIRNR037226};
GN ORFNames=CK3_16680 {ECO:0000313|EMBL:CBL41335.1};
OS butyrate-producing bacterium SS3/4.
OC Bacteria; Bacillota; Clostridia; Eubacteriales.
OX NCBI_TaxID=245014 {ECO:0000313|EMBL:CBL41335.1, ECO:0000313|Proteomes:UP000008961};
RN [1] {ECO:0000313|EMBL:CBL41335.1, ECO:0000313|Proteomes:UP000008961}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SS3/4 {ECO:0000313|EMBL:CBL41335.1,
RC ECO:0000313|Proteomes:UP000008961};
RG metaHIT consortium -- http://www.metahit.eu/;
RA Pajon A., Turner K., Parkhill J., Duncan S., Flint H.;
RT "The genome sequence of Clostridiales sp. SS3/4.";
RL Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:CBL41335.1, ECO:0000313|Proteomes:UP000008961}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SS3/4 {ECO:0000313|EMBL:CBL41335.1,
RC ECO:0000313|Proteomes:UP000008961};
RA Pajon A.;
RL Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the peptidase M20A family.
CC {ECO:0000256|PIRNR:PIRNR037226}.
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; FP929062; CBL41335.1; -; Genomic_DNA.
DR AlphaFoldDB; D7GU43; -.
DR KEGG; bprs:CK3_16680; -.
DR PATRIC; fig|245014.3.peg.79; -.
DR HOGENOM; CLU_031812_1_0_9; -.
DR BioCyc; BBAC245014:G1314-1422-MONOMER; -.
DR Proteomes; UP000008961; Chromosome.
DR GO; GO:0016805; F:dipeptidase activity; IEA:InterPro.
DR CDD; cd03887; M20_Acy1L2; 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:CBL41335.1}.
FT DOMAIN 169..261
FT /note="Peptidase M20 dimerisation"
FT /evidence="ECO:0000259|Pfam:PF07687"
SQ SEQUENCE 398 AA; 43077 MW; 928E088111D36C87 CRC64;
MNQNKLKIIE TIDKMQNELL TLSHQIHDHP ELGFQEHQAV GFIRTFLEGH GFEVETPYCG
LDTSFKAVKK GKHAGPRIAF LAEYDALRGI GHGCGHNIIA TCAVGAFSGL AALMDNYDGE
ISIIGTPAEE GGAGKVILLE RGGFHDTDYA LMMHPSGGGS NLVGRGGRAA TTIRVAFHGK
AAHSSAPSNG INALSAAIHV FNQIDLMRPT FQIQDNINGV ILEGGTAANV IPALVRCEFN
LRAETMIRIE FLIDLVKSSI ERAESLTGAK AEVVVDPIYA ERYPNKPMCE AFKNNMESLG
IHMTWPTPGK LYGSSDIGNV SIKIPAIHDY LSITDDKTIQ SHSKAYADAA ASPQADEICL
KGAKGLAMTA LDILEDSKFR DEINAFHDAQ VPERYHEK
//
