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Database: UniProt
Entry: Q18J88
LinkDB: Q18J88
Original site: Q18J88 
ID   KITH_HALWD              Reviewed;         225 AA.
AC   Q18J88;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   25-JUL-2006, sequence version 1.
DT   16-JAN-2019, entry version 81.
DE   RecName: Full=Thymidine kinase {ECO:0000255|HAMAP-Rule:MF_00124};
DE            EC=2.7.1.21 {ECO:0000255|HAMAP-Rule:MF_00124};
GN   Name=tdk {ECO:0000255|HAMAP-Rule:MF_00124};
GN   OrderedLocusNames=HQ_1795A;
OS   Haloquadratum walsbyi (strain DSM 16790 / HBSQ001).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria;
OC   Haloferacales; Haloferacaceae; Haloquadratum.
OX   NCBI_TaxID=362976;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 16790 / HBSQ001;
RX   PubMed=16820047; DOI=10.1186/1471-2164-7-169;
RA   Bolhuis H., Palm P., Wende A., Falb M., Rampp M., Rodriguez-Valera F.,
RA   Pfeiffer F., Oesterhelt D.;
RT   "The genome of the square archaeon Haloquadratum walsbyi: life at the
RT   limits of water activity.";
RL   BMC Genomics 7:169-169(2006).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + thymidine = ADP + dTMP + H(+);
CC         Xref=Rhea:RHEA:19129, ChEBI:CHEBI:15378, ChEBI:CHEBI:17748,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:63528, ChEBI:CHEBI:456216;
CC         EC=2.7.1.21; Evidence={ECO:0000255|HAMAP-Rule:MF_00124};
CC   -!- SUBUNIT: Homotetramer. {ECO:0000255|HAMAP-Rule:MF_00124}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00124}.
CC   -!- SIMILARITY: Belongs to the thymidine kinase family.
CC       {ECO:0000255|HAMAP-Rule:MF_00124}.
DR   EMBL; AM180088; CAJ51923.1; -; Genomic_DNA.
DR   RefSeq; WP_011571070.1; NC_008212.1.
DR   ProteinModelPortal; Q18J88; -.
DR   SMR; Q18J88; -.
DR   STRING; 362976.HQ1795A; -.
DR   EnsemblBacteria; CAJ51923; CAJ51923; HQ_1795A.
DR   GeneID; 4194746; -.
DR   KEGG; hwa:HQ_1795A; -.
DR   eggNOG; arCOG04798; Archaea.
DR   eggNOG; COG1435; LUCA.
DR   HOGENOM; HOG000076390; -.
DR   KO; K00857; -.
DR   OMA; KEQFGWI; -.
DR   BioCyc; HWAL362976:G1G1J-827-MONOMER; -.
DR   Proteomes; UP000001975; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004797; F:thymidine kinase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0071897; P:DNA biosynthetic process; IEA:UniProtKB-KW.
DR   HAMAP; MF_00124; Thymidine_kinase; 1.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR001267; Thymidine_kinase.
DR   InterPro; IPR020633; Thymidine_kinase_CS.
DR   PANTHER; PTHR11441; PTHR11441; 1.
DR   Pfam; PF00265; TK; 2.
DR   PIRSF; PIRSF035805; TK_cell; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   PROSITE; PS00603; TK_CELLULAR_TYPE; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Complete proteome; Cytoplasm; DNA synthesis; Kinase;
KW   Metal-binding; Nucleotide-binding; Reference proteome; Transferase;
KW   Zinc.
FT   CHAIN         1    225       Thymidine kinase.
FT                                /FTId=PRO_1000018156.
FT   NP_BIND      15     22       ATP. {ECO:0000255|HAMAP-Rule:MF_00124}.
FT   NP_BIND     121    124       ATP. {ECO:0000255|HAMAP-Rule:MF_00124}.
FT   ACT_SITE    122    122       Proton acceptor. {ECO:0000255|HAMAP-
FT                                Rule:MF_00124}.
FT   METAL       178    178       Zinc. {ECO:0000255|HAMAP-Rule:MF_00124}.
FT   METAL       181    181       Zinc. {ECO:0000255|HAMAP-Rule:MF_00124}.
FT   METAL       216    216       Zinc. {ECO:0000255|HAMAP-Rule:MF_00124}.
FT   METAL       219    219       Zinc. {ECO:0000255|HAMAP-Rule:MF_00124}.
SQ   SEQUENCE   225 AA;  24833 MW;  9564E79B078512D2 CRC64;
     MRAITNSGWI EVVTGSMFSG KTEELLRRLR RAEIAGQSIA VFKPAVDDRY GETTVGSHVG
     RQWEAAVVPN EGEDIWNIKH ELSKKKQNHR TTTQCRSGDG TNNPGGVIPS NDDSVDVVAI
     DEANFFSTEL VSVCESLAND GYRVVVSGTD QTYRGEPFEP LPQLMAVAEY VDKLQAICTQ
     CGEPATRNQR LVDDSPAHID DPTIVVGADE TYEARCRNCH ILRHE
//
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