ID A0A087DGY1_9BIFI Unreviewed; 415 AA.
AC A0A087DGY1;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=Peptidase M20 domain-containing protein 2 {ECO:0000256|PIRNR:PIRNR037226};
GN ORFNames=BSCA_0836 {ECO:0000313|EMBL:KFI94781.1};
OS Bifidobacterium scardovii.
OC Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC Bifidobacteriaceae; Bifidobacterium.
OX NCBI_TaxID=158787 {ECO:0000313|EMBL:KFI94781.1, ECO:0000313|Proteomes:UP000029033};
RN [1] {ECO:0000313|EMBL:KFI94781.1, ECO:0000313|Proteomes:UP000029033}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LMG 21589 {ECO:0000313|EMBL:KFI94781.1,
RC ECO:0000313|Proteomes:UP000029033};
RA Ventura M., Milani C., Lugli G.A.;
RT "Genomics of Bifidobacteria.";
RL Submitted (MAR-2014) 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:KFI94781.1}.
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DR EMBL; JGZO01000006; KFI94781.1; -; Genomic_DNA.
DR RefSeq; WP_051923177.1; NZ_JGZO01000006.1.
DR AlphaFoldDB; A0A087DGY1; -.
DR STRING; 158787.BSCA_0836; -.
DR GeneID; 85166991; -.
DR eggNOG; COG1473; Bacteria.
DR Proteomes; UP000029033; Unassembled WGS sequence.
DR GO; GO:0016805; F:dipeptidase activity; IEA:InterPro.
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:KFI94781.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000029033}.
FT DOMAIN 170..260
FT /note="Peptidase M20 dimerisation"
FT /evidence="ECO:0000259|Pfam:PF07687"
FT REGION 387..415
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 415 AA; 46045 MW; 09D311C217FEBF31 CRC64;
MGSIYPQLLD AVAALRDDAF TVTQYLTAHP EVGGRERESS RFVTEFLERH GYTVERNYMD
YPYAFRAYRT DDGRPRAALM CEYDALPDIG HGCGHSLSCG ISVLAAMALD RAFPDFPWQI
ELVGTPAEET EGAKCQLVAD GAFDRYDFAA MCHMDHLNAP IMWNLACNDM TITLHGRTAH
ASASPWKGVN AMNAAELIMH GVALMRSRFK PFMQIHGIVE EGGGLPNVVP DKAVLNYYTR
ALNLTELAEL RRWVRQLVRG VALATGVTYE ITQQYPTFAE LYRNPIELKA IEETFDDLGQ
PHGRYETPGA STDAGNVDML IPTIHMEIRA SDPDTSLHTA AFESFMHGER ANRTLLDGAS
AFATVIARLA YEDGLFASIR REHDRYRAEQ HADPHIDTGL VEAGGPDGPT SSREE
//
