ID   HDDC2_XENLA             Reviewed;         201 AA.
AC   Q66L17;
DT   13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 1.
DT   03-AUG-2022, entry version 61.
DE   RecName: Full=5'-deoxynucleotidase HDDC2;
DE            EC=3.1.3.89 {ECO:0000250|UniProtKB:P53144};
DE   AltName: Full=HD domain-containing protein 2;
GN   Name=hddc2;
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=Tadpole;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (SEP-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the dephosphorylation of the nucleoside 5'-
CC       monophosphates deoxyadenosine monophosphate (dAMP), deoxycytidine
CC       monophosphate (dCMP), deoxyguanosine monophosphate (dGMP) and
CC       deoxythymidine monophosphate (dTMP). {ECO:0000250|UniProtKB:P53144}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 2'-deoxyribonucleoside 5'-phosphate + H2O = a 2'-
CC         deoxyribonucleoside + phosphate; Xref=Rhea:RHEA:36167,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:18274, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:65317; EC=3.1.3.89;
CC         Evidence={ECO:0000250|UniProtKB:P53144};
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000250|UniProtKB:P53144};
CC       Name=Co(2+); Xref=ChEBI:CHEBI:48828;
CC         Evidence={ECO:0000250|UniProtKB:P53144};
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000250|UniProtKB:P53144};
CC       Note=Binds 2 divalent metal cations (By similarity). Shows activity
CC       with Mn(2+), Co(2+) and Mg(2+) but shows no activity with Zn(2+) (By
CC       similarity). {ECO:0000250|UniProtKB:P53144,
CC       ECO:0000250|UniProtKB:Q7Z4H3};
CC   -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P53144}.
CC   -!- SIMILARITY: Belongs to the HDDC2 family. {ECO:0000305}.
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DR   EMBL; BC078480; AAH78480.1; -; mRNA.
DR   RefSeq; NP_001087264.1; NM_001093795.2.
DR   AlphaFoldDB; Q66L17; -.
DR   MaxQB; Q66L17; -.
DR   DNASU; 447085; -.
DR   GeneID; 447085; -.
DR   KEGG; xla:447085; -.
DR   CTD; 447085; -.
DR   Xenbase; XB-GENE-953495; hddc2.L.
DR   OMA; YEKRDNI; -.
DR   OrthoDB; 1363142at2759; -.
DR   Proteomes; UP000186698; Chromosome 5L.
DR   Bgee; 447085; Expressed in testis and 20 other tissues.
DR   GO; GO:0002953; F:5'-deoxynucleotidase activity; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   InterPro; IPR003607; HD/PDEase_dom.
DR   InterPro; IPR006674; HD_domain.
DR   InterPro; IPR039356; YfbR/HDDC2.
DR   PANTHER; PTHR11845; PTHR11845; 1.
DR   Pfam; PF13023; HD_3; 1.
DR   SMART; SM00471; HDc; 1.
DR   PROSITE; PS51831; HD; 1.
PE   2: Evidence at transcript level;
KW   Cobalt; Hydrolase; Magnesium; Manganese; Metal-binding; Reference proteome.
FT   CHAIN           1..201
FT                   /note="5'-deoxynucleotidase HDDC2"
FT                   /id="PRO_0000311392"
FT   DOMAIN          43..145
FT                   /note="HD"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01175"
FT   BINDING         46
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:Q7Z4H3"
FT   BINDING         74
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:Q7Z4H3"
FT   BINDING         75
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:Q7Z4H3"
FT   BINDING         78
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:Q7Z4H3"
FT   BINDING         83
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:Q7Z4H3"
FT   BINDING         84
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:Q7Z4H3"
FT   BINDING         140
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:Q7Z4H3"
SQ   SEQUENCE   201 AA;  23109 MW;  3B51D57859C85F4C CRC64;
     MAAAGSCSSA GKSLLQFMKL VGQLKRVPRT GWIYRQVEKP ESVSDHMYRM AVMAMLTEDR
     KLNKDRCIRL ALVHDMAECI VGDIAPADNI AKEEKHRKEK AAMEHLTQLL PDNLKTEVYD
     LWEEYEHQFT AEAKFVKELD QCEMILQALE YEELEKRPGR LQDFYNSTAG KFKHPEIVQL
     VSAIYEERNS AIAENARTSQ T