ID A0A3G8YI32_9DEIO Unreviewed; 410 AA.
AC A0A3G8YI32;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE SubName: Full=Zn-dependent hydrolase {ECO:0000313|EMBL:AZI44949.1};
GN ORFNames=EHF33_18765 {ECO:0000313|EMBL:AZI44949.1};
OS Deinococcus psychrotolerans.
OG Plasmid unnamed2 {ECO:0000313|EMBL:AZI44949.1,
OG ECO:0000313|Proteomes:UP000276417}.
OC Bacteria; Deinococcota; Deinococci; Deinococcales; Deinococcaceae;
OC Deinococcus.
OX NCBI_TaxID=2489213 {ECO:0000313|EMBL:AZI44949.1, ECO:0000313|Proteomes:UP000276417};
RN [1] {ECO:0000313|EMBL:AZI44949.1, ECO:0000313|Proteomes:UP000276417}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S14-83T {ECO:0000313|EMBL:AZI44949.1,
RC ECO:0000313|Proteomes:UP000276417};
RC PLASMID=unnamed2 {ECO:0000313|EMBL:AZI44949.1,
RC ECO:0000313|Proteomes:UP000276417};
RA Tian J.;
RT "Deinococcus shelandsis sp. nov., isolated from South Shetland Islands soil
RT of Antarctica.";
RL Submitted (NOV-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|PIRSR:PIRSR001235-1};
CC Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000256|PIRSR:PIRSR001235-
CC 1};
CC -!- SIMILARITY: Belongs to the peptidase M20 family.
CC {ECO:0000256|ARBA:ARBA00006153}.
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DR EMBL; CP034186; AZI44949.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3G8YI32; -.
DR KEGG; dph:EHF33_18765; -.
DR OrthoDB; 9808195at2; -.
DR Proteomes; UP000276417; Plasmid unnamed2.
DR GO; GO:0016813; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amidines; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd03884; M20_bAS; 1.
DR Gene3D; 3.30.70.360; -; 1.
DR Gene3D; 3.40.630.10; Zn peptidases; 1.
DR InterPro; IPR010158; Amidase_Cbmase.
DR InterPro; IPR036264; Bact_exopeptidase_dim_dom.
DR InterPro; IPR002933; Peptidase_M20.
DR InterPro; IPR011650; Peptidase_M20_dimer.
DR NCBIfam; TIGR01879; hydantase; 1.
DR PANTHER; PTHR32494:SF5; ALLANTOATE DEIMINASE; 1.
DR PANTHER; PTHR32494; ALLANTOATE DEIMINASE-RELATED; 1.
DR Pfam; PF07687; M20_dimer; 1.
DR Pfam; PF01546; Peptidase_M20; 1.
DR PIRSF; PIRSF001235; Amidase_carbamoylase; 1.
DR SUPFAM; SSF55031; Bacterial exopeptidase dimerisation domain; 1.
DR SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000313|EMBL:AZI44949.1};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR001235-1};
KW Plasmid {ECO:0000313|EMBL:AZI44949.1};
KW Zinc {ECO:0000256|PIRSR:PIRSR001235-1}.
FT DOMAIN 210..301
FT /note="Peptidase M20 dimerisation"
FT /evidence="ECO:0000259|Pfam:PF07687"
FT BINDING 83
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR001235-1"
FT BINDING 94
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR001235-1"
FT BINDING 94
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR001235-1"
FT BINDING 123
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR001235-1"
FT BINDING 188
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR001235-1"
FT BINDING 380
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR001235-1"
SQ SEQUENCE 410 AA; 43671 MW; B10E87AC8321DECD CRC64;
MHDFTAARCE RLERQVKELA AFSDSAVGVT RLTFSERYVD ALKSLTALAT SLGCQVHSDE
AGNFHVTSAA AQHLGWTVAV GSHIDSVPMG GAYDGVAGVL CGFDILQSYP ELPITVVIFA
EEEGASFAGG LVGSRFASGK LTSVDLEQLL DGNGRSFAEG ARWTREAVNV PQLVSTGTPH
WRQYLEIHIE QGRVLQDGSA RLGVVTDIVG LIQAELIFFG RADHAGTTPM TARSDAGVTA
AQFIVDLEEL VRQTGEKAVG TVGVLEFGPG AANVVPGRAR LSLDLRDPDE SNLRSLAERV
KLHGQALAAR RNQQFTYREE LFSAPVPLDL SVVDGLGEAA SQQGIQTQRM ASGAGHDAMM
MAGLVPAGML FVPCLNGVSH SPEEWADVQD LVLAADTVAM YLHNAFDLTQ
//
