ID I6XHI8_9CAUD Unreviewed; 191 AA.
AC I6XHI8;
DT 03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 03-OCT-2012, sequence version 1.
DT 22-FEB-2023, entry version 38.
DE RecName: Full=Thymidine kinase {ECO:0000256|ARBA:ARBA00020079, ECO:0000256|RuleBase:RU000544};
DE EC=2.7.1.21 {ECO:0000256|ARBA:ARBA00012118, ECO:0000256|RuleBase:RU000544};
GN Name=tk {ECO:0000313|EMBL:AFN39566.1};
GN ORFNames=CC2_370 {ECO:0000313|EMBL:AFN39566.1};
OS Aeromonas phage CC2.
OC Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes;
OC Straboviridae; Emmerichvirinae; Ceceduovirus; Ceceduovirus cc2.
OX NCBI_TaxID=1204516 {ECO:0000313|EMBL:AFN39566.1, ECO:0000313|Proteomes:UP000009016};
RN [1] {ECO:0000313|EMBL:AFN39566.1, ECO:0000313|Proteomes:UP000009016}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=22966192; DOI=10.1128/JVI.01882-12;
RA Shen C.J., Liu Y.J., Lu C.P.;
RT "Complete Genome Sequence of Aeromonas hydrophila Phage CC2.";
RL J. Virol. 86:10900-10900(2012).
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|ARBA:ARBA00000506,
CC ECO:0000256|RuleBase:RU000544};
CC -!- SIMILARITY: Belongs to the thymidine kinase family.
CC {ECO:0000256|ARBA:ARBA00007587, ECO:0000256|RuleBase:RU004165}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; JX123262; AFN39566.1; -; Genomic_DNA.
DR RefSeq; YP_007010396.1; NC_019538.1.
DR GeneID; 14016576; -.
DR KEGG; vg:14016576; -.
DR OrthoDB; 9611at10239; -.
DR Proteomes; UP000009016; Genome.
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 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; 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.
DR PROSITE; PS00603; TK_CELLULAR_TYPE; 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 Reference proteome {ECO:0000313|Proteomes:UP000009016};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU000544}.
FT ACT_SITE 87
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR035805-1"
SQ SEQUENCE 191 AA; 21427 MW; 0F662E75D1A14703 CRC64;
MSSLHFHHSA MNAGKSSHLL QVAYNYEERG MGVLVLKPCI DTRDGEMVSS RLGVSRPSIM
FSNRENLTDL YLSYKIGKKI DCILIDEAQF MTVEQVKQLA FIVDNYDVPV MCYGLMSDSN
GEMFDASRQL VVMAEQIVEH KTICWCGSKA TMNLRVDENG KKVIGDQVCI GGNDRYISVC
RKHWVAGMSG K
//
