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Database: UniProt/TrEMBL
Entry: X2GK07_9BACI
LinkDB: X2GK07_9BACI
Original site: X2GK07_9BACI 
ID   X2GK07_9BACI            Unreviewed;       190 AA.
AC   X2GK07;
DT   11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT   11-JUN-2014, sequence version 1.
DT   27-SEP-2017, entry version 18.
DE   RecName: Full=Thymidine kinase {ECO:0000256|HAMAP-Rule:MF_00124, ECO:0000256|RuleBase:RU000544};
DE            EC=2.7.1.21 {ECO:0000256|HAMAP-Rule:MF_00124, ECO:0000256|RuleBase:RU000544};
GN   Name=tdk {ECO:0000256|HAMAP-Rule:MF_00124};
GN   ORFNames=T479_02730 {ECO:0000313|EMBL:AHN20493.1};
OS   Lysinibacillus varians.
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae;
OC   Lysinibacillus.
OX   NCBI_TaxID=1145276 {ECO:0000313|EMBL:AHN20493.1, ECO:0000313|Proteomes:UP000019675};
RN   [1] {ECO:0000313|EMBL:AHN20493.1, ECO:0000313|Proteomes:UP000019675}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GY32 {ECO:0000313|EMBL:AHN20493.1,
RC   ECO:0000313|Proteomes:UP000019675};
RX   PubMed=25070216;
RA   Zhu C., Sun G., Chen X., Guo J., Xu M.;
RT   "Lysinibacillus varians sp. nov., an endospore-forming bacterium with
RT   a filament-to-rod cell cycle.";
RL   Int. J. Syst. Evol. Microbiol. 0:0-0(2014).
CC   -!- CATALYTIC ACTIVITY: ATP + thymidine = ADP + thymidine 5'-
CC       phosphate. {ECO:0000256|HAMAP-Rule:MF_00124,
CC       ECO:0000256|RuleBase:RU000544}.
CC   -!- SUBUNIT: Homotetramer. {ECO:0000256|HAMAP-Rule:MF_00124}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00124}.
CC   -!- SIMILARITY: Belongs to the thymidine kinase family.
CC       {ECO:0000256|HAMAP-Rule:MF_00124, ECO:0000256|RuleBase:RU004165}.
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DR   EMBL; CP006837; AHN20493.1; -; Genomic_DNA.
DR   RefSeq; WP_024362886.1; NZ_CP006837.1.
DR   EnsemblBacteria; AHN20493; AHN20493; T479_02730.
DR   KEGG; lgy:T479_02730; -.
DR   PATRIC; fig|1145276.3.peg.510; -.
DR   KO; K00857; -.
DR   Proteomes; UP000019675; 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 {ECO:0000256|HAMAP-Rule:MF_00124,
KW   ECO:0000256|RuleBase:RU000544};
KW   Complete proteome {ECO:0000313|Proteomes:UP000019675};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00124};
KW   DNA synthesis {ECO:0000256|HAMAP-Rule:MF_00124,
KW   ECO:0000256|RuleBase:RU000544};
KW   Kinase {ECO:0000256|HAMAP-Rule:MF_00124,
KW   ECO:0000256|RuleBase:RU000544, ECO:0000313|EMBL:AHN20493.1};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_00124};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00124,
KW   ECO:0000256|RuleBase:RU000544};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00124,
KW   ECO:0000256|RuleBase:RU000544};
KW   Zinc {ECO:0000256|HAMAP-Rule:MF_00124}.
FT   NP_BIND       9     16       ATP. {ECO:0000256|HAMAP-Rule:MF_00124}.
FT   NP_BIND      85     88       ATP. {ECO:0000256|HAMAP-Rule:MF_00124}.
FT   ACT_SITE     86     86       Proton acceptor. {ECO:0000256|HAMAP-Rule:
FT                                MF_00124, ECO:0000256|PIRSR:PIRSR035805-
FT                                1}.
FT   METAL       143    143       Zinc. {ECO:0000256|HAMAP-Rule:MF_00124}.
FT   METAL       146    146       Zinc. {ECO:0000256|HAMAP-Rule:MF_00124}.
FT   METAL       181    181       Zinc. {ECO:0000256|HAMAP-Rule:MF_00124}.
FT   METAL       184    184       Zinc. {ECO:0000256|HAMAP-Rule:MF_00124}.
SQ   SEQUENCE   190 AA;  21759 MW;  591BE8B0C055B188 CRC64;
     MAQLYYKHGA MNSGKSIEIL KVAHNYEEQQ KPVMIFTSGL DTRDEVGFVS SRVGLRQEAI
     PIYEDTNIFE LVKNNEVKPY CVLVDEVQFL KKAHVLQLAN IVDELDIPVM GFGLKNDFQN
     ELFEGSQYML TYADKIEEMK TICWFCHKKA TMNLRVDDNG KPVYTGDQIK IGGNDSYYPV
     CRKCHAHPPL
//
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