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Database: UniProt
Entry: A0A5N5M1P1_PANHP
LinkDB: A0A5N5M1P1_PANHP
Original site: A0A5N5M1P1_PANHP 
ID   A0A5N5M1P1_PANHP        Unreviewed;       263 AA.
AC   A0A5N5M1P1;
DT   26-FEB-2020, integrated into UniProtKB/TrEMBL.
DT   26-FEB-2020, sequence version 1.
DT   27-MAR-2024, entry version 10.
DE   RecName: Full=Deoxynucleoside kinase domain-containing protein {ECO:0000259|Pfam:PF01712};
GN   ORFNames=PHYPO_G00063450 {ECO:0000313|EMBL:KAB5549104.1};
OS   Pangasianodon hypophthalmus (Striped catfish) (Helicophagus hypophthalmus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Siluriformes;
OC   Pangasiidae; Pangasianodon.
OX   NCBI_TaxID=310915 {ECO:0000313|EMBL:KAB5549104.1, ECO:0000313|Proteomes:UP000327468};
RN   [1] {ECO:0000313|EMBL:KAB5549104.1, ECO:0000313|Proteomes:UP000327468}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Indonesia {ECO:0000313|EMBL:KAB5549104.1,
RC   ECO:0000313|Proteomes:UP000327468};
RC   TISSUE=Blood {ECO:0000313|EMBL:KAB5549104.1};
RA   Wen M., Zahm M., Roques C., Cabau C., Klopp C., Donnadieu C., Jouanno E.,
RA   Avarre J.-C., Campet M., Ha T.T.T., Dugue R., Lampietro C., Louis A.,
RA   Herpin A., Echchiki A., Berthelot C., Parey E., Roest-Crollius H.,
RA   Braasch I., Postlethwait J., Bobe J., Montfort J., Bouchez O., Begum T.,
RA   Schartl M., Guiguen Y.;
RT   "A chromosome-scale genome assembly of the striped catfish, Pangasianodon
RT   hypophthalmus.";
RL   Submitted (JUN-2019) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2'-deoxyadenosine + ATP = ADP + dAMP + H(+);
CC         Xref=Rhea:RHEA:23452, ChEBI:CHEBI:15378, ChEBI:CHEBI:17256,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:58245, ChEBI:CHEBI:456216;
CC         EC=2.7.1.76; Evidence={ECO:0000256|ARBA:ARBA00036035};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2'-deoxycytidine + a ribonucleoside 5'-triphosphate = a
CC         ribonucleoside 5'-diphosphate + dCMP + H(+); Xref=Rhea:RHEA:20061,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:15698, ChEBI:CHEBI:57566,
CC         ChEBI:CHEBI:57930, ChEBI:CHEBI:61557; EC=2.7.1.74;
CC         Evidence={ECO:0000256|ARBA:ARBA00036126};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2'-deoxyguanosine + ATP = ADP + dGMP + H(+);
CC         Xref=Rhea:RHEA:19201, ChEBI:CHEBI:15378, ChEBI:CHEBI:17172,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:57673, ChEBI:CHEBI:456216;
CC         EC=2.7.1.113; Evidence={ECO:0000256|ARBA:ARBA00036095};
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC   -!- SIMILARITY: Belongs to the DCK/DGK family.
CC       {ECO:0000256|ARBA:ARBA00007420}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KAB5549104.1}.
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DR   EMBL; VFJC01000016; KAB5549104.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A5N5M1P1; -.
DR   OrthoDB; 315858at2759; -.
DR   Proteomes; UP000327468; Chromosome 15.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0019136; F:deoxynucleoside kinase activity; IEA:InterPro.
DR   GO; GO:1901564; P:organonitrogen compound metabolic process; IEA:UniProt.
DR   CDD; cd01673; dNK; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   InterPro; IPR002624; DCK/DGK.
DR   InterPro; IPR031314; DNK_dom.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   PANTHER; PTHR10513:SF19; DEOXYCYTIDINE KINASE; 1.
DR   PANTHER; PTHR10513; DEOXYNUCLEOSIDE KINASE; 1.
DR   Pfam; PF01712; dNK; 1.
DR   PIRSF; PIRSF000705; DNK; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|PIRSR:PIRSR000705-3};
KW   Nucleotide-binding {ECO:0000256|PIRSR:PIRSR000705-3};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Reference proteome {ECO:0000313|Proteomes:UP000327468}.
FT   DOMAIN          24..260
FT                   /note="Deoxynucleoside kinase"
FT                   /evidence="ECO:0000259|Pfam:PF01712"
FT   ACT_SITE        127
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000705-1"
FT   BINDING         28..36
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000705-3"
FT   BINDING         53
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000705-2"
FT   BINDING         86
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000705-2"
FT   BINDING         97
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000705-2"
FT   BINDING         128
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000705-2"
FT   BINDING         133
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000705-2"
FT   BINDING         188..192
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000705-3"
FT   BINDING         197
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000705-2"
FT   BINDING         240..242
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000705-3"
SQ   SEQUENCE   263 AA;  31163 MW;  F0A9E427CD51D717 CRC64;
     MSRTPKRACS SSLNDSLEKR LKRISVEGNI AAGKSTFVRL LEQHDKEWEV VPEPIARWCN
     VQTQHDEFEE LTTSQKSGGN VLQMMYEKPE RWAYTFQSYA CMSRVRAQIN SASGKLRHAE
     NPVQFFERSV YSDRYIFAAN LYESECLNET EWAIYQDWHT WLHKKFGQHI ELDGIIYLRA
     KPERCLERLH LRGREEEQGI PLEYLEKLHY KHECWLQHRT LRMDFDYLCE VPVLTLDVND
     DFKGDKSKCV DMIEKVKDFL STL
//
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