ID   A0A1G1A576_9BACT        Unreviewed;       414 AA.
AC   A0A1G1A576;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   27-MAR-2024, entry version 17.
DE   RecName: Full=Peptidase M20 dimerisation domain-containing protein {ECO:0000259|Pfam:PF07687};
GN   ORFNames=A2498_08910 {ECO:0000313|EMBL:OGV65620.1};
OS   Lentisphaerae bacterium RIFOXYC12_FULL_60_16.
OC   Bacteria; Lentisphaerota.
OX   NCBI_TaxID=1798582 {ECO:0000313|EMBL:OGV65620.1, ECO:0000313|Proteomes:UP000178496};
RN   [1] {ECO:0000313|EMBL:OGV65620.1, ECO:0000313|Proteomes:UP000178496}
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   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|ARBA:ARBA00001947};
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:OGV65620.1}.
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DR   EMBL; MHBQ01000065; OGV65620.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1G1A576; -.
DR   STRING; 1798582.A2498_08910; -.
DR   Proteomes; UP000178496; Unassembled WGS sequence.
DR   GO; GO:0016787; F:hydrolase activity; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.70.360; -; 1.
DR   Gene3D; 3.40.630.10; Zn peptidases; 1.
DR   InterPro; IPR036264; Bact_exopeptidase_dim_dom.
DR   InterPro; IPR002933; Peptidase_M20.
DR   InterPro; IPR011650; Peptidase_M20_dimer.
DR   PANTHER; PTHR43808; ACETYLORNITHINE DEACETYLASE; 1.
DR   PANTHER; PTHR43808:SF3; ACETYLORNITHINE DEACETYLASE-RELATED; 1.
DR   Pfam; PF07687; M20_dimer; 1.
DR   Pfam; PF01546; Peptidase_M20; 1.
DR   SUPFAM; SSF55031; Bacterial exopeptidase dimerisation domain; 1.
DR   SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
PE   4: Predicted;
KW   Cobalt {ECO:0000256|ARBA:ARBA00023285};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723}.
FT   DOMAIN          197..308
FT                   /note="Peptidase M20 dimerisation"
FT                   /evidence="ECO:0000259|Pfam:PF07687"
SQ   SEQUENCE   414 AA;  44499 MW;  C58C75A001FD988C CRC64;
     MTPDRIREGI AAVLPEARDF LCDLIRCPST PGCERDAMRL ALGGFKRCAS RATRIPLDDA
     LRNDPDYSTP IPDIRYKGRF NVRAVSKGTG GGPTVLFNTH LDVVPPSEDM AEPWNPRIEG
     TVVHGRGACD AKGQAATIWL VFRALQQLGI RLKGDLVAHI VVEEENGGNG TLAMARRGEK
     ADACIVLEPT EQRILTSIRG AVWFRLVCTG KAGHSGQAGQ TRSALLLARD AMAVLERYHA
     ELLAASRGFP LFDGYPNPMP ITFGSLQAGN WPASAPSKAV LMGVLGLLPN KTHQQVQAEM
     SAALAAGLGA DAMHNVELTF LYRHDSSVLE PSHEVPQALL QSSRKLGAPT EIAGMTASCD
     AWFYNNQLRI PSLVYGPGSL KVAHSRQEQI DLNDVAAAAC VLVDFLTGYS GVTE
//