HDDC2_DICDI
ID HDDC2_DICDI Reviewed; 190 AA.
AC Q54FK1;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 84.
DE RecName: Full=5'-deoxynucleotidase HDDC2;
DE EC=3.1.3.89 {ECO:0000250|UniProtKB:P53144};
DE AltName: Full=HD domain-containing protein 2 homolog;
GN Name=hddc2; ORFNames=DDB_G0290795;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
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; AAFI02000171; EAL62031.1; -; Genomic_DNA.
DR RefSeq; XP_635539.1; XM_630447.1.
DR AlphaFoldDB; Q54FK1; -.
DR STRING; 44689.DDB0266402; -.
DR PaxDb; Q54FK1; -.
DR EnsemblProtists; EAL62031; EAL62031; DDB_G0290795.
DR GeneID; 8627837; -.
DR KEGG; ddi:DDB_G0290795; -.
DR dictyBase; DDB_G0290795; hddc2.
DR eggNOG; KOG3197; Eukaryota.
DR HOGENOM; CLU_039453_2_1_1; -.
DR InParanoid; Q54FK1; -.
DR OMA; YEKRDNI; -.
DR PhylomeDB; Q54FK1; -.
DR PRO; PR:Q54FK1; -.
DR Proteomes; UP000002195; Chromosome 5.
DR GO; GO:0002953; F:5'-deoxynucleotidase activity; IBA:GO_Central.
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 3: Inferred from homology;
KW Cobalt; Hydrolase; Magnesium; Manganese; Metal-binding; Reference proteome.
FT CHAIN 1..190
FT /note="5'-deoxynucleotidase HDDC2"
FT /id="PRO_0000327688"
FT DOMAIN 33..143
FT /note="HD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01175"
FT BINDING 36
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q7Z4H3"
FT BINDING 72
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q7Z4H3"
FT BINDING 73
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q7Z4H3"
FT BINDING 76
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q7Z4H3"
FT BINDING 81
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q7Z4H3"
FT BINDING 138
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q7Z4H3"
SQ SEQUENCE 190 AA; 22245 MW; A9B99049DC351150 CRC64;
MSNYLEFFKI CGKLKTLKRT GWVNHGVELP ESVSDHMYRM AMMGMCLDKK ELIGEDGKEI
DKMKIIKMAL VHDLGESLVG DFTPHDKITK EEKYQLEKNA IIEITNTLSG EVGKEIFDLW
QEYEDCKTNE ALLVKDFDKF EMILQAYEYE KQPHQLENKI KLQSFFDSTR GKFHHPLFKS
LALQLESDRK
