ID   A0A3G8YFA3_9DEIO        Unreviewed;       296 AA.
AC   A0A3G8YFA3;
DT   13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT   13-FEB-2019, sequence version 1.
DT   24-JAN-2024, entry version 19.
DE   RecName: Full=Putative metal-dependent hydrolase EHF33_08925 {ECO:0000256|HAMAP-Rule:MF_01256};
DE            EC=3.-.-.- {ECO:0000256|HAMAP-Rule:MF_01256};
GN   ORFNames=EHF33_08925 {ECO:0000313|EMBL:AZI42857.1};
OS   Deinococcus psychrotolerans.
OC   Bacteria; Deinococcota; Deinococci; Deinococcales; Deinococcaceae;
OC   Deinococcus.
OX   NCBI_TaxID=2489213 {ECO:0000313|EMBL:AZI42857.1, ECO:0000313|Proteomes:UP000276417};
RN   [1] {ECO:0000313|EMBL:AZI42857.1, ECO:0000313|Proteomes:UP000276417}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=S14-83T {ECO:0000313|EMBL:AZI42857.1,
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   -!- FUNCTION: Possible metal-dependent hydrolase. {ECO:0000256|HAMAP-
CC       Rule:MF_01256}.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_01256};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000256|HAMAP-Rule:MF_01256};
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_01256}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01256}.
CC   -!- SIMILARITY: Belongs to the metal hydrolase YfiT family.
CC       {ECO:0000256|HAMAP-Rule:MF_01256}.
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DR   EMBL; CP034183; AZI42857.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3G8YFA3; -.
DR   KEGG; dph:EHF33_08925; -.
DR   OrthoDB; 9796039at2; -.
DR   Proteomes; UP000276417; Chromosome 1.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR   CDD; cd11531; NTP-PPase_BsYpjD; 1.
DR   Gene3D; 1.20.120.450; dinb family like domain; 1.
DR   Gene3D; 1.10.287.1080; MazG-like; 1.
DR   HAMAP; MF_01256; YfiT_hydrol; 1.
DR   InterPro; IPR024775; DinB-like.
DR   InterPro; IPR034660; DinB/YfiT-like.
DR   InterPro; IPR004518; MazG-like_dom.
DR   InterPro; IPR012359; MazG-related_YpjD.
DR   InterPro; IPR023774; Put_metal_dep_hydrolase_YfiT.
DR   InterPro; IPR047046; YpjD/YvdC.
DR   PANTHER; PTHR42692; NUCLEOTIDE PYROPHOSPHOHYDROLASE; 1.
DR   PANTHER; PTHR42692:SF1; NUCLEOTIDE PYROPHOSPHOHYDROLASE; 1.
DR   Pfam; PF12867; DinB_2; 1.
DR   Pfam; PF03819; MazG; 1.
DR   SUPFAM; SSF101386; all-alpha NTP pyrophosphatases; 1.
DR   SUPFAM; SSF109854; DinB/YfiT-like putative metalloenzymes; 1.
PE   3: Inferred from homology;
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_01256};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_01256};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW   Rule:MF_01256};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|HAMAP-Rule:MF_01256}.
FT   DOMAIN          32..108
FT                   /note="NTP pyrophosphohydrolase MazG-like"
FT                   /evidence="ECO:0000259|Pfam:PF03819"
FT   DOMAIN          148..283
FT                   /note="DinB-like"
FT                   /evidence="ECO:0000259|Pfam:PF12867"
FT   REGION          104..126
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        104..118
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         184
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01256"
FT   BINDING         276
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01256"
FT   BINDING         280
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01256"
SQ   SEQUENCE   296 AA;  33123 MW;  3232D78C278D6911 CRC64;
     MTTPLDTALS FAAASARVDA YVSQFKEGYF PPLLLLARLS EEVGEVARVL SHENGKTPKA
     GEDVGDLELE LADALFVMLC MTNSRGLSLE RGFERMMQKV ETRDAQRWTK KEEASPRTFL
     TDPRYPVGPM PVPGEVSLQA RAEAVEAIRA LPAELRSAAA NLSDAQLDTP YREGGWTLRQ
     VVHHVADSHL NAYARLKWAL TEERPTIKPY QESQWASFAD SALPVEVSLV LLDSLHQRWV
     AVLESLSEAQ WAREFVHPVG GEVLSVGQAA RRYQWHGQHH TAHLLRLRQA QGWPLR
//