KITH_BHV2H
ID KITH_BHV2H Reviewed; 323 AA.
AC P22649;
DT 01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT 27-MAY-2002, sequence version 2.
DT 03-AUG-2022, entry version 76.
DE RecName: Full=Thymidine kinase {ECO:0000255|HAMAP-Rule:MF_04029};
DE EC=2.7.1.21 {ECO:0000255|HAMAP-Rule:MF_04029};
GN Name=TK {ECO:0000255|HAMAP-Rule:MF_04029};
OS Bovine herpesvirus 2 (strain BHM-1) (BoHV-2) (Bovine mammillitis virus).
OC Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC Herpesvirales; Herpesviridae; Alphaherpesvirinae; Simplexvirus.
OX NCBI_TaxID=10297;
OH NCBI_TaxID=9913; Bos taurus (Bovine).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2555436; DOI=10.1099/0022-1317-70-11-3067;
RA Sheppard M., May J.T.;
RT "Location and characterization of the bovine herpesvirus type 2 thymidine
RT kinase gene.";
RL J. Gen. Virol. 70:3067-3071(1989).
RN [2]
RP SEQUENCE REVISION TO C-TERMINUS.
RA Sheppard M., May J.T.;
RL Submitted (OCT-2001) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the transfer of the gamma-phospho group of ATP to
CC thymidine to generate dTMP in the salvage pathway of pyrimidine
CC synthesis. The dTMP serves as a substrate for DNA polymerase during
CC viral DNA replication. Allows the virus to be reactivated and to grow
CC in non-proliferative cells lacking a high concentration of
CC phosphorylated nucleic acid precursors. {ECO:0000255|HAMAP-
CC Rule:MF_04029}.
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:0000255|HAMAP-Rule:MF_04029};
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_04029}.
CC -!- SIMILARITY: Belongs to the herpesviridae thymidine kinase family.
CC {ECO:0000255|HAMAP-Rule:MF_04029}.
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DR EMBL; D00537; BAA00425.2; -; Genomic_DNA.
DR PIR; JT0532; KIBEB2.
DR SMR; P22649; -.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004797; F:thymidine kinase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0071897; P:DNA biosynthetic process; IEA:UniProtKB-UniRule.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0006230; P:TMP biosynthetic process; IEA:UniProtKB-UniRule.
DR Gene3D; 3.40.50.300; -; 1.
DR HAMAP; MF_04029; HSV_KITH; 1.
DR InterPro; IPR001889; Herpes_TK.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF00693; Herpes_TK; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
PE 3: Inferred from homology;
KW ATP-binding; DNA synthesis; Early protein; Kinase; Nucleotide-binding;
KW Transferase.
FT CHAIN 1..323
FT /note="Thymidine kinase"
FT /id="PRO_0000175063"
FT ACT_SITE 36
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04029"
FT BINDING 11..18
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04029"
FT BINDING 54
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04029"
FT BINDING 78
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04029"
FT BINDING 169
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04029"
FT BINDING 175
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04029"
SQ SEQUENCE 323 AA; 34661 MW; 5AB03D3F17EF1199 CRC64;
MSRLLRVYVD GPHGLGKTTA ASALASERGD AIYLPEPMSY WSGAGEDDLV ARVYTAQHRM
DRGEIDAREA AGVVLGAQLT MSTPYVALNG LIAPHIGEEP SPGNATPPDL ILIFDRHPIA
SLLCYPLARY LTRCLPIESV LSLIALIPPT PPGTNLILGT APAEDHLSRL VARGRPGELP
DARMLRAIRY VYALLANTVK YLQSGGSWRA DLGSEPPRLP LAPPEIGDPN NPGGHNTLLA
LIHGAGATRG CAAMTSWTLD LLADRLRSMN MFTVDYSAPP EACVAQMRNL LPSMQCTVTP
KPESHRAVAD AALAFMREMS NCK
