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Database: UniProt
Entry: Q2RZH4
LinkDB: Q2RZH4
Original site: Q2RZH4 
ID   KITH_SALRD              Reviewed;         227 AA.
AC   Q2RZH4;
DT   27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT   24-JAN-2006, sequence version 1.
DT   16-JAN-2019, entry version 77.
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=SRU_2559;
OS   Salinibacter ruber (strain DSM 13855 / M31).
OC   Bacteria; Bacteroidetes; Bacteroidetes Order II. Incertae sedis;
OC   Rhodothermaceae; Salinibacter.
OX   NCBI_TaxID=309807;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 13855 / M31;
RX   PubMed=16330755; DOI=10.1073/pnas.0509073102;
RA   Mongodin E.F., Nelson K.E., Daugherty S., DeBoy R.T., Wister J.,
RA   Khouri H., Weidman J., Walsh D.A., Papke R.T., Sanchez Perez G.,
RA   Sharma A.K., Nesbo C.L., MacLeod D., Bapteste E., Doolittle W.F.,
RA   Charlebois R.L., Legault B., Rodriguez-Valera F.;
RT   "The genome of Salinibacter ruber: convergence and gene exchange among
RT   hyperhalophilic bacteria and archaea.";
RL   Proc. Natl. Acad. Sci. U.S.A. 102:18147-18152(2005).
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; CP000159; ABC45345.1; -; Genomic_DNA.
DR   RefSeq; WP_011405271.1; NC_007677.1.
DR   RefSeq; YP_446657.1; NC_007677.1.
DR   ProteinModelPortal; Q2RZH4; -.
DR   SMR; Q2RZH4; -.
DR   STRING; 309807.SRU_2559; -.
DR   EnsemblBacteria; ABC45345; ABC45345; SRU_2559.
DR   GeneID; 3851644; -.
DR   KEGG; sru:SRU_2559; -.
DR   PATRIC; fig|309807.25.peg.2666; -.
DR   eggNOG; ENOG4107T8J; Bacteria.
DR   eggNOG; COG1435; LUCA.
DR   HOGENOM; HOG000076390; -.
DR   KO; K00857; -.
DR   OMA; KEQFGWI; -.
DR   BioCyc; SRUB309807:G1G5H-2555-MONOMER; -.
DR   Proteomes; UP000008674; 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; 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    227       Thymidine kinase.
FT                                /FTId=PRO_0000242802.
FT   NP_BIND      15     22       ATP. {ECO:0000255|HAMAP-Rule:MF_00124}.
FT   NP_BIND      87     90       ATP. {ECO:0000255|HAMAP-Rule:MF_00124}.
FT   ACT_SITE     88     88       Proton acceptor. {ECO:0000255|HAMAP-
FT                                Rule:MF_00124}.
FT   METAL       144    144       Zinc. {ECO:0000255|HAMAP-Rule:MF_00124}.
FT   METAL       147    147       Zinc. {ECO:0000255|HAMAP-Rule:MF_00124}.
FT   METAL       176    176       Zinc. {ECO:0000255|HAMAP-Rule:MF_00124}.
FT   METAL       179    179       Zinc. {ECO:0000255|HAMAP-Rule:MF_00124}.
SQ   SEQUENCE   227 AA;  24876 MW;  51934C486650BDDA CRC64;
     MDRDRTTGWM EVICGSMFSG KTEELIRRLR RARIARQHTR VFKPALDERY SEDEVVSHNE
     NSVTTTPVEA PPQIQELVQE ADVVGIDEAQ FFDDDLVPTC QALAEDGHRV IVVGLDTDYR
     AEPFDPMPQL MAVAEHVTKL HAVCVVCGAP ANHSQRIVPG EDRVLVGATE AYEPRCRACF
     EPEPVTVTRP RPHTEALRAV ATDDADASTN EADPEAADAA SADGTAA
//
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