ID   KITH_PSHV1              Reviewed;         339 AA.
AC   Q6UDK9;
DT   05-APR-2011, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 51.
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}; OrderedLocusNames=UL23;
OS   Psittacid herpesvirus 1 (isolate Amazon parrot/-/97-0001/1997) (PsHV-1)
OS   (Pacheco's disease virus).
OC   Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC   Herpesvirales; Herpesviridae; Alphaherpesvirinae; Iltovirus.
OX   NCBI_TaxID=670426;
OH   NCBI_TaxID=152276; Amazona oratrix (yellow-headed parrot).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16873243; DOI=10.1128/jvi.00134-06;
RA   Thureen D.R., Keeler C.L. Jr.;
RT   "Psittacid herpesvirus 1 and infectious laryngotracheitis virus:
RT   Comparative genome sequence analysis of two avian alphaherpesviruses.";
RL   J. Virol. 80:7863-7872(2006).
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; AY372243; AAQ73701.1; -; Genomic_DNA.
DR   RefSeq; NP_944395.1; NC_005264.1.
DR   SMR; Q6UDK9; -.
DR   GeneID; 2656999; -.
DR   KEGG; vg:2656999; -.
DR   Proteomes; UP000006840; Genome.
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   Reference proteome; Transferase.
FT   CHAIN           1..339
FT                   /note="Thymidine kinase"
FT                   /id="PRO_0000406816"
FT   ACT_SITE        39
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         59
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04029"
FT   BINDING         83
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04029"
FT   BINDING         176
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04029"
FT   BINDING         182
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04029"
SQ   SEQUENCE   339 AA;  38059 MW;  77788121FEACB803 CRC64;
     MGRIVVLYVD GAFGIGKTTV LRQIQKSAAY RFRRIYLEEP MRAWRSWFVD DHDAIREIYT
     TQELKDAGEI DLREASRRVC YAQVSLSAPF HIMNAVIYGI ISGESEATSA HLGEGDYFVG
     VDRHPLASCL CFPVARFVTG YLEYTDLIAL VATLPDYPRG ASIAILDLSV EEQARRITER
     SRSGEHVNKT FLRILRNVFI IMYNTVAYLR NVSIDKACAD REALEDFRGS QLESDMHKID
     IQPRDDPNAS ETLFAVMASD ATWRKNRKQS ALFVYTMAKL DALLRSLNMH IVDINGLSQE
     QCAEKVVAIS SKVPAVTARG NAPDLLFDAV EAYNADMGV