ID A0A1F8TND5_9CHLR Unreviewed; 376 AA.
AC A0A1F8TND5;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE RecName: Full=Peptidase M20 domain-containing protein 2 {ECO:0000256|PIRNR:PIRNR037226};
GN ORFNames=A3G84_05725 {ECO:0000313|EMBL:OGO73733.1};
OS Chloroflexi bacterium RIFCSPLOWO2_12_FULL_71_12.
OC Bacteria; Chloroflexota.
OX NCBI_TaxID=1797673 {ECO:0000313|EMBL:OGO73733.1, ECO:0000313|Proteomes:UP000179700};
RN [1] {ECO:0000313|EMBL:OGO73733.1, ECO:0000313|Proteomes:UP000179700}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27774985; DOI=10.1038/ncomms13219;
RA Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA Williams K.H., Hubbard S.S., Banfield J.F.;
RT "Thousands of microbial genomes shed light on interconnected biogeochemical
RT processes in an aquifer system.";
RL Nat. Commun. 7:13219-13219(2016).
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:OGO73733.1}.
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; MGOO01000061; OGO73733.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F8TND5; -.
DR Proteomes; UP000179700; 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;
FT DOMAIN 159..257
FT /note="Peptidase M20 dimerisation"
FT /evidence="ECO:0000259|Pfam:PF07687"
SQ SEQUENCE 376 AA; 39808 MW; 84AC8031AF1DDA05 CRC64;
MSVDGKLRDD LLKLSREIHS DPELAYQERR AADRICALLG KHGHQAERKL GGLETAFRAR
VGPAGPSVAL LAEYDALPDI GHACGHNLIA MTNVGAFLAV AADPKGLEIG VELIGTPAEE
SGGGKIDLLD AGVFKQVEAV LSSHPSGSPE WETTSVSLGI VAKRVAFKGV ASHAAFSPDL
GKNALNAVIR LFVGVDGWRQ HMPRDARVHG VITHGGGPAH NIVPAFAECV FGLRAKTQEE
LDGMVRTFEG IARGAALQTE TEVNITDEMR LYAPTAPNER IGELLREELR ARGAEAVPGV
LVLASTDFGN VSQAVPSDYI GFPVATRRIG GHNIEMRESS VTDLAHENAF IVVEALAAAA
RRIATDKGLR AGLRAG
//
