ID Q8JRQ2_9POXV Unreviewed; 164 AA.
AC Q8JRQ2;
DT 01-OCT-2002, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2002, sequence version 1.
DT 03-MAY-2023, entry version 60.
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};
DE Flags: Fragment;
OS Aracatuba virus.
OC Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Pokkesviricetes;
OC Chitovirales; Poxviridae; Chordopoxvirinae; Orthopoxvirus; Vaccinia virus.
OX NCBI_TaxID=201444 {ECO:0000313|EMBL:AAM90949.1};
RN [1] {ECO:0000313|EMBL:AAM90949.1}
RP NUCLEOTIDE SEQUENCE.
RA Trindade G.S., Oliveira J.G., Kroon E.G.;
RL Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:AAM90949.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=12603984;
RA de Souza Trindade G., da Fonseca F.G., Marques J.T., Nogueira M.L.,
RA Mendes L.C., Borges A.S., Peiro J.R., Pituco E.M., Bonjardim C.A.,
RA Ferreira P.C., Kroon E.G.;
RT "Aracatuba virus: a vaccinialike virus associated with infection in humans
RT and cattle.";
RL Emerg. Infect. Dis. 9:155-160(2003).
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; AF503169; AAM90949.1; -; Genomic_DNA.
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 76
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR035805-1"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:AAM90949.1"
FT NON_TER 164
FT /evidence="ECO:0000313|EMBL:AAM90949.1"
SQ SEQUENCE 164 AA; 18653 MW; D03E50564B28696D CRC64;
LIIGPMFSGK STELIRRVRR YQIAQYKCVT IKYSNDNRYG TGLWTHDKNN FEALEATKLC
DVLESITDFS VIGIDEGQFF PDIVEFCERM ANEGKIVIVA ALDGTFQRKP FNNILNLIPL
SEMVVKLTAV CMKCFKEASF SKRLGEETEI EIIGGNDMYQ SVCR
//
