GenomeNet

Database: UniProt
Entry: A0A1G1CKS8_9BACT
LinkDB: A0A1G1CKS8_9BACT
Original site: A0A1G1CKS8_9BACT 
ID   A0A1G1CKS8_9BACT        Unreviewed;       359 AA.
AC   A0A1G1CKS8;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   24-JAN-2024, entry version 21.
DE   RecName: Full=Peptidase M20 dimerisation domain-containing protein {ECO:0000259|Pfam:PF07687};
GN   ORFNames=A2W24_07070 {ECO:0000313|EMBL:OGV95629.1};
OS   Microgenomates group bacterium RBG_16_45_19.
OC   Bacteria.
OX   NCBI_TaxID=1817747 {ECO:0000313|EMBL:OGV95629.1, ECO:0000313|Proteomes:UP000178440};
RN   [1] {ECO:0000313|EMBL:OGV95629.1, ECO:0000313|Proteomes:UP000178440}
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   -!- COFACTOR:
CC       Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC         Evidence={ECO:0000256|PIRSR:PIRSR001123-2};
CC       Note=Binds 2 divalent metal cations per subunit.
CC       {ECO:0000256|PIRSR:PIRSR001123-2};
CC   -!- SIMILARITY: Belongs to the peptidase M42 family.
CC       {ECO:0000256|PIRNR:PIRNR001123}.
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:OGV95629.1}.
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; MHDC01000045; OGV95629.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1G1CKS8; -.
DR   STRING; 1817747.A2W24_07070; -.
DR   Proteomes; UP000178440; Unassembled WGS sequence.
DR   GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
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   InterPro; IPR008007; Peptidase_M42.
DR   PANTHER; PTHR42994; PEPTIDASE T; 1.
DR   PANTHER; PTHR42994:SF2; T, PUTATIVE-RELATED; 1.
DR   Pfam; PF07687; M20_dimer; 1.
DR   Pfam; PF01546; Peptidase_M20; 1.
DR   PIRSF; PIRSF001123; PepA_GA; 3.
DR   SUPFAM; SSF55031; Bacterial exopeptidase dimerisation domain; 1.
DR   SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|PIRSR:PIRSR001123-2}.
FT   DOMAIN          168..259
FT                   /note="Peptidase M20 dimerisation"
FT                   /evidence="ECO:0000259|Pfam:PF07687"
FT   BINDING         64
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001123-2"
SQ   SEQUENCE   359 AA;  38569 MW;  299DC557F35319C7 CRC64;
     MKEAIERTFR ELAAFNSPSK NEVRVASYLQ EQLTTMGLEV KVDDFGNVIG YLSGRGESIL
     LNAHMDGVPP AKGHIPVKEG DVLRSDGSTN LRADDIAGIT IILEATITII EGKKKHPPLV
     LAFTAQEEIG LWGAKALDVT EYDVNQGIVF DNAFGAGTVV SKGACYVAFD VEIKGKETHP
     GKDLSQGVNA VKVLLDTGIQ VGEADKGQTR VNIGTVSAGK ARNVVPGNAT IQGEIRSFLT
     GDKLSGRLSE VEMAFKNAAS RNGAQVEFTQ KQLAFAYKVD EDEPLVQKYK EVVGARGGEF
     EMAETFVASD ANALREKGLK VFVISTGVES EHSVNETVKL SDMEQLTSDL VALLELLPQ
//
DBGET integrated database retrieval system