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Database: UniProt
Entry: E0YIP8_9CAUD
LinkDB: E0YIP8_9CAUD
Original site: E0YIP8_9CAUD 
ID   E0YIP8_9CAUD            Unreviewed;       198 AA.
AC   E0YIP8;
DT   02-NOV-2010, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2010, sequence version 1.
DT   22-FEB-2023, entry version 40.
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};
OS   Lactococcus phage 949.
OC   Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes;
OC   Audreyjarvisvirus; Audreyjarvisvirus av949.
OX   NCBI_TaxID=881953 {ECO:0000313|EMBL:ADM73569.1, ECO:0000313|Proteomes:UP000002234};
RN   [1] {ECO:0000313|EMBL:ADM73569.1, ECO:0000313|Proteomes:UP000002234}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=20802084; DOI=10.1128/AEM.00796-10;
RA   Samson J.E., Moineau S.;
RT   "Characterization of Lactococcus lactis phage 949 and comparison with other
RT   lactococcal phages.";
RL   Appl. Environ. Microbiol. 76:6843-6852(2010).
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}.
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DR   EMBL; HM029250; ADM73569.1; -; Genomic_DNA.
DR   RefSeq; YP_004306171.1; NC_015263.1.
DR   GeneID; 10358836; -.
DR   KEGG; vg:10358836; -.
DR   OrthoDB; 9611at10239; -.
DR   Proteomes; UP000002234; 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:UP000002234};
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   198 AA;  22657 MW;  0B68362380E2C9E5 CRC64;
     MAKLFFKYGT MKSGKSTHLL MTKHNYTSQN KRVLVYTSNK DTRWGSEKVI SRIGINSFAL
     PVTDEIFNEI KEEHFKKHIA CVLVDEAQFL SAEQIVALCS VVDNLGIPVI CYGLKNDFRN
     ALFEGSKTLL ELADEIELIK TVCEHHTCGK KATMNLRLVD GKPIYKGEQF QLGDEDYVPV
     CRKHYYNYEE NEDGRYSG
//
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