ID G2IEV0_9CLOT Unreviewed; 194 AA.
AC G2IEV0;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 24-JAN-2024, entry version 48.
DE RecName: Full=Thymidine kinase {ECO:0000256|ARBA:ARBA00012118, ECO:0000256|RuleBase:RU000544};
DE EC=2.7.1.21 {ECO:0000256|ARBA:ARBA00012118, ECO:0000256|RuleBase:RU000544};
GN Name=tdk {ECO:0000313|EMBL:BAK81674.1};
GN ORFNames=RATSFB_1112 {ECO:0000313|EMBL:BAK81674.1};
OS Candidatus Arthromitus sp. SFB-rat-Yit.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Candidatus Arthromitus.
OX NCBI_TaxID=1041504 {ECO:0000313|EMBL:BAK81674.1, ECO:0000313|Proteomes:UP000001273};
RN [1] {ECO:0000313|EMBL:BAK81674.1, ECO:0000313|Proteomes:UP000001273}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SFB-rat-Yit {ECO:0000313|EMBL:BAK81674.1};
RX PubMed=21925114;
RA Prakash T., Oshima K., Morita H., Fukuda S., Imaoka A., Kumar N.,
RA Sharma V.K., Kim S.-W., Takahashi M., Saitou N., Taylor T.D., Ohno H.,
RA Umesaki Y., Hattori M.;
RT "Complete genome sequences of rat and mouse segmented filamentous bacteria,
RT a potent inducer of th17 cell differentiation.";
RL Cell Host Microbe 10:273-284(2011).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + thymidine = ADP + dTMP + H(+); Xref=Rhea:RHEA:19129,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17748, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:63528, ChEBI:CHEBI:456216; EC=2.7.1.21;
CC Evidence={ECO:0000256|RuleBase:RU000544};
CC -!- SIMILARITY: Belongs to the thymidine kinase family.
CC {ECO:0000256|ARBA:ARBA00007587, ECO:0000256|RuleBase:RU004165}.
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DR EMBL; AP012210; BAK81674.1; -; Genomic_DNA.
DR RefSeq; WP_014095134.1; NC_016012.1.
DR AlphaFoldDB; G2IEV0; -.
DR STRING; 1041504.RATSFB_1112; -.
DR KEGG; asb:RATSFB_1112; -.
DR eggNOG; COG1435; Bacteria.
DR HOGENOM; CLU_064400_2_2_9; -.
DR OrthoDB; 9781579at2; -.
DR Proteomes; UP000001273; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004797; F:thymidine kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0071897; P:DNA biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR Gene3D; 3.30.60.20; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR001267; Thymidine_kinase.
DR PANTHER; PTHR11441; THYMIDINE KINASE; 1.
DR PANTHER; PTHR11441:SF0; THYMIDINE KINASE, CYTOSOLIC; 1.
DR Pfam; PF00265; TK; 1.
DR PIRSF; PIRSF035805; TK_cell; 1.
DR SUPFAM; SSF57716; Glucocorticoid receptor-like (DNA-binding domain); 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU000544};
KW DNA synthesis {ECO:0000256|ARBA:ARBA00022634,
KW ECO:0000256|RuleBase:RU000544};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|RuleBase:RU000544};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU000544};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU000544}.
FT ACT_SITE 86
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR035805-1"
SQ SEQUENCE 194 AA; 22181 MW; 165CBD111C83383C CRC64;
MAKLYFRYGA MNSGKTTAML QVAHNYEEKG MKVLLLKPSI DTKGYDRVVS RLGIDRKVDF
LVSNTDSLKV LLEPFRKSVH CIIIDEVQFL KKFQIDELFY ISNIWDIPVI CYGLRTDFLM
NGFEGSERLL LIAHSIEELK TICECGKKAI TNGRKINGKF VFSGEQCVID GEENVSYEPL
CGKCFIKKRE ICDV
//
