ID   TAT3A_XENLA             Reviewed;         270 AA.
AC   Q05AV0;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   14-NOV-2006, sequence version 1.
DT   03-AUG-2022, entry version 55.
DE   RecName: Full=Putative deoxyribonuclease tatdn3-A;
DE            EC=3.1.21.-;
GN   Name=tatdn3-a;
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Ovary;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Putative deoxyribonuclease. {ECO:0000250}.
CC   -!- COFACTOR:
CC       Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC         Evidence={ECO:0000250};
CC       Note=Binds 2 divalent metal cations per subunit. {ECO:0000250};
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily.
CC       TatD-type hydrolase family. {ECO:0000305}.
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DR   EMBL; BC123334; AAI23335.1; -; mRNA.
DR   RefSeq; NP_001090394.1; NM_001096925.1.
DR   AlphaFoldDB; Q05AV0; -.
DR   SMR; Q05AV0; -.
DR   DNASU; 779305; -.
DR   GeneID; 779305; -.
DR   KEGG; xla:779305; -.
DR   CTD; 779305; -.
DR   Xenbase; XB-GENE-5839537; tatdn3.L.
DR   OrthoDB; 988732at2759; -.
DR   Proteomes; UP000186698; Chromosome 5L.
DR   Bgee; 779305; Expressed in testis and 18 other tissues.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004518; F:nuclease activity; IEA:UniProtKB-KW.
DR   CDD; cd01310; TatD_DNAse; 1.
DR   InterPro; IPR032466; Metal_Hydrolase.
DR   InterPro; IPR001130; TatD-like.
DR   Pfam; PF01026; TatD_DNase; 1.
DR   PIRSF; PIRSF005902; DNase_TatD; 1.
DR   SUPFAM; SSF51556; SSF51556; 1.
PE   2: Evidence at transcript level;
KW   Hydrolase; Metal-binding; Nuclease; Nucleus; Reference proteome.
FT   CHAIN           1..270
FT                   /note="Putative deoxyribonuclease tatdn3-A"
FT                   /id="PRO_0000313598"
FT   BINDING         9
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         11
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         103
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         103
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         143
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         166
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         214
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   270 AA;  30482 MW;  D3D5FF6D68BDE8AD CRC64;
     MAVGYVDCHC HMTAEEFSQD TEEVIEESKE NGIQALISVT EHGGEFEKLI YLSDRYPDYI
     MPCFGIHPIQ SNGDGQRSVT IKDLEPVLAQ FDKYKDSLVA IGEIGLDFTP WLAPTSEQRE
     EQMKVFQMQL EMAKRMDLPV NVHSRSAGRQ TVSFLKEQGA EKVLLHNFAG RPSAAQEGVQ
     AGYFFSFPPA VIRNEQRKKL IKMIPLENIC LETDSPSLGP KKEDRNVPSN IRLSCEYIAS
     VKGLMPERVR EVTTLNALRL FPKVSCKLQK