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Database: UniProt
Entry: A0A1Y2RIL5_9BACT
LinkDB: A0A1Y2RIL5_9BACT
Original site: A0A1Y2RIL5_9BACT 
ID   A0A1Y2RIL5_9BACT        Unreviewed;       427 AA.
AC   A0A1Y2RIL5;
DT   30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT   30-AUG-2017, sequence version 1.
DT   27-MAR-2024, entry version 14.
DE   SubName: Full=Peptidase M20 {ECO:0000313|EMBL:OSZ81297.1};
GN   ORFNames=CAP36_08695 {ECO:0000313|EMBL:OSZ81297.1};
OS   Chitinophagaceae bacterium IBVUCB2.
OC   Bacteria; Bacteroidota; Chitinophagia; Chitinophagales; Chitinophagaceae.
OX   NCBI_TaxID=1985174 {ECO:0000313|EMBL:OSZ81297.1, ECO:0000313|Proteomes:UP000194400};
RN   [1] {ECO:0000313|EMBL:OSZ81297.1, ECO:0000313|Proteomes:UP000194400}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IBVUCB2 {ECO:0000313|EMBL:OSZ81297.1,
RC   ECO:0000313|Proteomes:UP000194400};
RA   Orr R.J.;
RT   "Draft genome sequences of novel bacteria, isolated from environmental
RT   samples.";
RL   Submitted (MAY-2017) to the EMBL/GenBank/DDBJ databases.
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:OSZ81297.1}.
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DR   EMBL; NFUV01000001; OSZ81297.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Y2RIL5; -.
DR   STRING; 1985174.CAP36_08695; -.
DR   InParanoid; A0A1Y2RIL5; -.
DR   OrthoDB; 9783294at2; -.
DR   Proteomes; UP000194400; 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:SF8; M20_DIMER DOMAIN-CONTAINING PROTEIN; 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   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000194400};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           22..427
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5012305367"
FT   DOMAIN          210..326
FT                   /note="Peptidase M20 dimerisation"
FT                   /evidence="ECO:0000259|Pfam:PF07687"
SQ   SEQUENCE   427 AA;  45937 MW;  BB6B82A8A295C1D7 CRC64;
     MKKLVSVFIF LAIVVAGSSQ ALSKVEQQLI NSVEADMKAT IDLLKESVNI NSGTYNIAGV
     KQVGDLYGKE LAALGFTVEW ISLPDSLKRA GHLVAHRKGK KGKKLFLIGH LDTVFEPDMP
     ANPFTMLTDT TATGQGVQDM KGGDVMVIAA LKAMHKHGLL NDVSITVYFT GDEENAGRPR
     DISRGDFIER AKQHDIALAF EGGSLNQVAT ARRGASEWTL EVEGKQAHSS GIFGTVGYGS
     IFEASRIINE FREKLGNEQY LTFNPGLFIG GSEVNYDHEK QQGDVSGKTN IISPRTVVIG
     DLRFLTEAQK EKARANMREI VAKNLAGAKA SISFKDGIPS MPPTAGNDSL VKILNVVNLA
     LGFGEVKAGN PGARGAGDIS YIAAYVDCLD GLGAEGKGAH APGEVINLKE YPKLIKRTAL
     FLYRLTR
//
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