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Database: UniProt
Entry: Q9ZIG2
LinkDB: Q9ZIG2
Original site: Q9ZIG2 
ID   KITH_RHOSI              Reviewed;         213 AA.
AC   Q9ZIG2;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   05-DEC-2018, entry version 62.
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};
OS   Rhodothermus sp. (strain ITI 518).
OC   Bacteria; Bacteroidetes; Bacteroidetes Order II. Incertae sedis;
OC   Rhodothermaceae; Rhodothermus.
OX   NCBI_TaxID=71277;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Blondal T., Thorbjarnardottir S.H., Kielezawa J., Eggertsson G.;
RT   "Nucleotide sequence and deduced amino acid sequence of thymidine
RT   kinase gene (tdk) from Rhodothermus sp. ITI 518.";
RL   Submitted (OCT-1997) 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; AF028720; AAC98909.1; -; Genomic_DNA.
DR   PIR; T47123; T47123.
DR   ProteinModelPortal; Q9ZIG2; -.
DR   SMR; Q9ZIG2; -.
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; Cytoplasm; DNA synthesis; Kinase; Metal-binding;
KW   Nucleotide-binding; Transferase; Zinc.
FT   CHAIN         1    213       Thymidine kinase.
FT                                /FTId=PRO_0000175010.
FT   NP_BIND      22     29       ATP. {ECO:0000255|HAMAP-Rule:MF_00124}.
FT   NP_BIND      94     97       ATP. {ECO:0000255|HAMAP-Rule:MF_00124}.
FT   ACT_SITE     95     95       Proton acceptor. {ECO:0000255|HAMAP-
FT                                Rule:MF_00124}.
FT   METAL       151    151       Zinc. {ECO:0000255|HAMAP-Rule:MF_00124}.
FT   METAL       154    154       Zinc. {ECO:0000255|HAMAP-Rule:MF_00124}.
FT   METAL       183    183       Zinc. {ECO:0000255|HAMAP-Rule:MF_00124}.
FT   METAL       186    186       Zinc. {ECO:0000255|HAMAP-Rule:MF_00124}.
SQ   SEQUENCE   213 AA;  23644 MW;  A086F049ED6BD786 CRC64;
     MPMEPLILRH GGSVGWIEVI CGSMFSGKTE ELIRRLRRAQ IARQRVEVFK PRMDRRYSET
     DVVSHDENAL RSTPVDSAEQ ILLLADSADV VGIDEAQFFD MTLVDVCQQL ANDGKRVIVA
     GLDQEYMGRP LEPMPQFMAV AEYVTKLHAI CAVCGAPANH SQRLTDEEGR VVLGAADRYE
     PRCRRCFQPP RPTSTSSLKA PAPAATAPRP ELP
//
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