ID   KITM_MACFA              Reviewed;         265 AA.
AC   Q9N0C5;
DT   24-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   27-MAR-2024, entry version 90.
DE   RecName: Full=Thymidine kinase 2, mitochondrial {ECO:0000305};
DE            EC=2.7.1.21 {ECO:0000250|UniProtKB:Q9R088};
DE   AltName: Full=2'-deoxyuridine kinase TK2 {ECO:0000305};
DE            EC=2.7.1.74 {ECO:0000250|UniProtKB:Q9R088};
DE   AltName: Full=Deoxycytidine kinase TK2 {ECO:0000305};
DE            EC=2.7.1.- {ECO:0000250|UniProtKB:Q9R088};
DE   Flags: Precursor;
GN   Name=TK2; ORFNames=QccE-13136;
OS   Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9541;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain cortex;
RA   Osada N., Hida M., Kusuda J., Tanuma R., Iseki K., Hirai M., Terao K.,
RA   Suzuki Y., Sugano S., Hashimoto K.;
RT   "Isolation of full-length cDNA clones from macaque brain cDNA libraries.";
RL   Submitted (JUL-2000) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Phosphorylates thymidine, deoxycytidine, and deoxyuridine in
CC       the mitochondrial matrix (By similarity). In non-replicating cells,
CC       where cytosolic dNTP synthesis is down-regulated, mtDNA synthesis
CC       depends solely on TK2 and DGUOK (By similarity).
CC       {ECO:0000250|UniProtKB:O00142, ECO:0000250|UniProtKB:Q9R088}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + thymidine = ADP + dTMP + H(+); Xref=Rhea:RHEA:19129,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:17748, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:63528, ChEBI:CHEBI:456216; EC=2.7.1.21;
CC         Evidence={ECO:0000250|UniProtKB:Q9R088};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19130;
CC         Evidence={ECO:0000250|UniProtKB:Q9R088};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2'-deoxycytidine + ATP = ADP + dCMP + H(+);
CC         Xref=Rhea:RHEA:46040, ChEBI:CHEBI:15378, ChEBI:CHEBI:15698,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:57566, ChEBI:CHEBI:456216;
CC         EC=2.7.1.74; Evidence={ECO:0000250|UniProtKB:Q9R088};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:46041;
CC         Evidence={ECO:0000250|UniProtKB:Q9R088};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2'-deoxyuridine + ATP = ADP + dUMP + H(+);
CC         Xref=Rhea:RHEA:28206, ChEBI:CHEBI:15378, ChEBI:CHEBI:16450,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:246422, ChEBI:CHEBI:456216;
CC         Evidence={ECO:0000250|UniProtKB:Q9R088};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:28207;
CC         Evidence={ECO:0000250|UniProtKB:Q9R088};
CC   -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:Q9R088}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250|UniProtKB:Q9R088}.
CC   -!- SIMILARITY: Belongs to the DCK/DGK family. {ECO:0000305}.
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DR   EMBL; AB046005; BAB01587.1; -; mRNA.
DR   RefSeq; NP_001272031.1; NM_001285102.1.
DR   AlphaFoldDB; Q9N0C5; -.
DR   SMR; Q9N0C5; -.
DR   STRING; 9541.ENSMFAP00000031231; -.
DR   eggNOG; KOG4235; Eukaryota.
DR   OrthoDB; 5393913at2759; -.
DR   Proteomes; UP000233100; Unplaced.
DR   GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004797; F:thymidine kinase activity; IEA:UniProtKB-EC.
DR   GO; GO:1901135; P:carbohydrate derivative metabolic process; IEA:UniProt.
DR   GO; GO:0071897; P:DNA biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
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; DEOXYNUCLEOSIDE KINASE; 1.
DR   PANTHER; PTHR10513:SF35; THYMIDINE KINASE 2, MITOCHONDRIAL; 1.
DR   Pfam; PF01712; dNK; 1.
DR   PIRSF; PIRSF000705; DNK; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
PE   2: Evidence at transcript level;
KW   ATP-binding; DNA synthesis; Kinase; Mitochondrion; Nucleotide-binding;
KW   Reference proteome; Transferase; Transit peptide.
FT   TRANSIT         1..33
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           34..265
FT                   /note="Thymidine kinase 2, mitochondrial"
FT                   /id="PRO_0000016843"
FT   REGION          21..45
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        133
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:O57203"
FT   BINDING         57..65
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:O57203"
SQ   SEQUENCE   265 AA;  30744 MW;  6104E608C0E809A0 CRC64;
     MLLRPLRGWA ALALRCFEPG SPGSPASGPG SRRVQRGAWP SDKEREKEKK SVICVEGNIA
     SGKTTCLEFF SNATDIEVLT EPVSKWRNVR GHNPLGLMYQ DASRWGLTLQ TYVQLTMLDR
     HTCPQVSSVR LMERSIHSAR YIFVENLYRS GKMPEVDYVV LSEWFDWILR NMDVSIDLIV
     YLRTNPETCY QRLKRRCREE EKVIPLEYLE AIHHLHEEWL IKGSLFPVAA PVLVIEADHH
     MERMLQLFEQ NRDRILTPEN RKLGP
//