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Database: UniProt/SWISS-PROT
Entry: KITH_JANSC
LinkDB: KITH_JANSC
Original site: KITH_JANSC 
ID   KITH_JANSC              Reviewed;         195 AA.
AC   Q28M21;
DT   27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT   27-JUN-2006, sequence version 2.
DT   16-JAN-2019, entry version 63.
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=Jann_3324;
OS   Jannaschia sp. (strain CCS1).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Rhodobacteraceae; Jannaschia.
OX   NCBI_TaxID=290400;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CCS1;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Pitluck S., Brettin T.,
RA   Bruce D., Han C., Tapia R., Gilna P., Chertkov O., Saunders E.,
RA   Schmutz J., Larimer F., Land M., Kyrpides N., Lykidis A., Moran M.A.,
RA   Belas R., Ye W., Buchan A., Gonzalez J.M., Schell M.A., Richardson P.;
RT   "Complete sequence of chromosome of Jannaschia sp. CCS1.";
RL   Submitted (FEB-2006) 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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=ABD56241.1; Type=Erroneous initiation; Evidence={ECO:0000305};
DR   EMBL; CP000264; ABD56241.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_044006964.1; NC_007802.1.
DR   ProteinModelPortal; Q28M21; -.
DR   SMR; Q28M21; -.
DR   STRING; 290400.Jann_3324; -.
DR   PRIDE; Q28M21; -.
DR   EnsemblBacteria; ABD56241; ABD56241; Jann_3324.
DR   KEGG; jan:Jann_3324; -.
DR   eggNOG; ENOG4107104; Bacteria.
DR   eggNOG; COG1435; LUCA.
DR   HOGENOM; HOG000076391; -.
DR   KO; K00857; -.
DR   OrthoDB; 1279539at2; -.
DR   Proteomes; UP000008326; 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; Reference proteome; Transferase;
KW   Zinc.
FT   CHAIN         1    195       Thymidine kinase.
FT                                /FTId=PRO_0000242793.
FT   NP_BIND       9     16       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       145    145       Zinc. {ECO:0000255|HAMAP-Rule:MF_00124}.
FT   METAL       147    147       Zinc. {ECO:0000255|HAMAP-Rule:MF_00124}.
FT   METAL       182    182       Zinc. {ECO:0000255|HAMAP-Rule:MF_00124}.
FT   METAL       185    185       Zinc. {ECO:0000255|HAMAP-Rule:MF_00124}.
SQ   SEQUENCE   195 AA;  21531 MW;  A612804275E7EAC9 CRC64;
     MAKLYFNYST MNAGKSTLLL QASYNYIERG MQTYLLTANF DDRAGMGRIG SRIGIEAEAD
     TYTQSDDLFA KIDARLKAGP CACVLVDEAQ WMTRDQVWQL ARAVDDLGVP VMCYGLRVDF
     RGELFPGSAA LLALADEMRE VRTICHCGRK ATMVIRVGED GNALAEGAQI EVGGNDRYIS
     LCRKHFREAV GDVPV
//
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