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Database: UniProt
Entry: Q2SSX9
LinkDB: Q2SSX9
Original site: Q2SSX9 
ID   KITH_MYCCT              Reviewed;         209 AA.
AC   Q2SSX9;
DT   27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT   24-JAN-2006, sequence version 1.
DT   16-JAN-2019, entry version 76.
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=MCAP_0143;
OS   Mycoplasma capricolum subsp. capricolum (strain California kid / ATCC
OS   27343 / NCTC 10154).
OC   Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma.
OX   NCBI_TaxID=340047;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=California kid / ATCC 27343 / NCTC 10154;
RA   Glass J.I., Lartigue C., Pfannkoch C., Baden-Tillson H., Smith H.O.,
RA   Venter J.C., Roske K., Wise K.S., Calcutt M.J., Nelson W.C.,
RA   Nierman W.C.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
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; CP000123; ABC01477.1; -; Genomic_DNA.
DR   RefSeq; WP_011387039.1; NC_007633.1.
DR   ProteinModelPortal; Q2SSX9; -.
DR   SMR; Q2SSX9; -.
DR   EnsemblBacteria; ABC01477; ABC01477; MCAP_0143.
DR   GeneID; 23778904; -.
DR   KEGG; mcp:MCAP_0143; -.
DR   HOGENOM; HOG000076390; -.
DR   KO; K00857; -.
DR   OMA; KEQFGWI; -.
DR   OrthoDB; 1279539at2; -.
DR   BioCyc; MCAP340047:G1G57-141-MONOMER; -.
DR   Proteomes; UP000001928; 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   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; Transferase; Zinc.
FT   CHAIN         1    209       Thymidine kinase.
FT                                /FTId=PRO_0000242795.
FT   NP_BIND      25     32       ATP. {ECO:0000255|HAMAP-Rule:MF_00124}.
FT   NP_BIND     103    106       ATP. {ECO:0000255|HAMAP-Rule:MF_00124}.
FT   ACT_SITE    104    104       Proton acceptor. {ECO:0000255|HAMAP-
FT                                Rule:MF_00124}.
FT   METAL       160    160       Zinc. {ECO:0000255|HAMAP-Rule:MF_00124}.
FT   METAL       163    163       Zinc. {ECO:0000255|HAMAP-Rule:MF_00124}.
FT   METAL       198    198       Zinc. {ECO:0000255|HAMAP-Rule:MF_00124}.
FT   METAL       201    201       Zinc. {ECO:0000255|HAMAP-Rule:MF_00124}.
SQ   SEQUENCE   209 AA;  23820 MW;  3570598B0F5A11E0 CRC64;
     MTELDINEIE AYNSNKMGWI ELITGCMFAG KTEEFIRRLK VLSYAKKRVL AFKPSIDNRY
     SVENIISHSG SKLDSYLVKS SDEIKQIVEK ENQIQQVDVI GIDEVQFFDE NVVDIIEQLA
     DNGIIVIVNG LDKDFRGLPF KNVDKLLVKA EFVTKLRARC HLCGSFANRS QRIVNGQPAL
     WDSPLILVDG KESYEARCRK CFISPKKDV
//
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