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Database: UniProt
Entry: A0A1F8KCG1_9CHLR
LinkDB: A0A1F8KCG1_9CHLR
Original site: A0A1F8KCG1_9CHLR 
ID   A0A1F8KCG1_9CHLR        Unreviewed;       390 AA.
AC   A0A1F8KCG1;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   24-JAN-2024, entry version 15.
DE   RecName: Full=Peptidase M20 dimerisation domain-containing protein {ECO:0000259|Pfam:PF07687};
GN   ORFNames=A2X25_12480 {ECO:0000313|EMBL:OGN71962.1};
OS   Chloroflexi bacterium GWB2_49_20.
OC   Bacteria; Chloroflexota.
OX   NCBI_TaxID=1797612 {ECO:0000313|EMBL:OGN71962.1, ECO:0000313|Proteomes:UP000178842};
RN   [1] {ECO:0000313|EMBL:OGN71962.1, ECO:0000313|Proteomes:UP000178842}
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   -!- 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:OGN71962.1}.
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DR   EMBL; MGMF01000026; OGN71962.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1F8KCG1; -.
DR   STRING; 1797612.A2X25_12480; -.
DR   Proteomes; UP000178842; Unassembled WGS sequence.
DR   GO; GO:0016787; F:hydrolase activity; IEA:InterPro.
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;
FT   DOMAIN          192..279
FT                   /note="Peptidase M20 dimerisation"
FT                   /evidence="ECO:0000259|Pfam:PF07687"
SQ   SEQUENCE   390 AA;  41879 MW;  CE2E5DCB21137892 CRC64;
     MNELNTLDKA KAIHENLISW RRDFHMHPEL GFCEHRTAEK VAEILENLGL EIKKGVGRTG
     VVADIGTGSP VIAIRADMDA LPLQEKNDVS YVSQNPGLMH ACGHDAHTAM LLGVATLLAN
     EKFSGTVRLL FQPSEERADE EGISGAPRMV EDGAMQGVDM VIALHVAPMT PTGQIQIESG
     PASGGVDSWF GRIIGKGGHG ASPQKTIDPF YICSHVIMAL NGIVSRRVAP FSPAVVSIGS
     LHGGHTENVI PEHVDLTGTL RYTVEDVQKE LHTEIRRAFE LSRNLGGDYE LKFEIGDPPM
     INAPRAVKLI SAVAADLIGA DNVLPMDKSL GAEDFGVFSK IAPGAMFSLG SLISGDERVG
     HNPYFDIDED ALPIGTAILV ESALRYLKAK
//
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