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Database: UniProt
Entry: P0C8I4
LinkDB: P0C8I4
Original site: P0C8I4 
ID   KITH_ASFM2              Reviewed;         188 AA.
AC   P0C8I4;
DT   25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT   25-NOV-2008, sequence version 1.
DT   16-JAN-2019, entry version 25.
DE   RecName: Full=Thymidine kinase;
DE            Short=TDK;
DE            EC=2.7.1.21;
GN   OrderedLocusNames=Mal-058;
OS   African swine fever virus (isolate Tick/Malawi/Lil 20-1/1983) (ASFV).
OC   Viruses; dsDNA viruses, no RNA stage; Asfarviridae; Asfivirus.
OX   NCBI_TaxID=10500;
OH   NCBI_TaxID=6937; Ornithodoros (relapsing fever ticks).
OH   NCBI_TaxID=85517; Phacochoerus aethiopicus (Warthog).
OH   NCBI_TaxID=41426; Phacochoerus africanus (Warthog).
OH   NCBI_TaxID=273792; Potamochoerus larvatus (Bushpig).
OH   NCBI_TaxID=9823; Sus scrofa (Pig).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Kutish G.F., Rock D.L.;
RT   "African swine fever virus genomes.";
RL   Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   FUNCTION.
RX   PubMed=9811782;
RA   Moore D.M., Zsak L., Neilan J.G., Lu Z., Rock D.L.;
RT   "The African swine fever virus thymidine kinase gene is required for
RT   efficient replication in swine macrophages and for virulence in
RT   swine.";
RL   J. Virol. 72:10310-10315(1998).
CC   -!- FUNCTION: Phosphorylates thymidine. ASFV replicates in the
CC       cytoplasm of infected cells and contains genes encoding a number
CC       of enzymes needed for DNA synthesis, including thymidine kinase.
CC       Important for growth in swine macrophages in vitro and is a virus
CC       virulence factor in swine. {ECO:0000269|PubMed:9811782}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + thymidine = ADP + dTMP + H(+);
CC         Xref=Rhea:RHEA:19129, ChEBI:CHEBI:15378, ChEBI:CHEBI:17748,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:63528, ChEBI:CHEBI:456216;
CC         EC=2.7.1.21;
CC   -!- SIMILARITY: Belongs to the thymidine kinase family. {ECO:0000305}.
DR   EMBL; AY261361; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   ProteinModelPortal; P0C8I4; -.
DR   SMR; P0C8I4; -.
DR   PRIDE; P0C8I4; -.
DR   Proteomes; UP000000860; Genome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion 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:0009405; P:pathogenesis; IEA:UniProtKB-KW.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR001267; Thymidine_kinase.
DR   InterPro; IPR020633; Thymidine_kinase_CS.
DR   PANTHER; PTHR11441; PTHR11441; 1.
DR   Pfam; PF00265; TK; 1.
DR   PIRSF; PIRSF035805; TK_cell; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   PROSITE; PS00603; TK_CELLULAR_TYPE; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Complete proteome; DNA synthesis; Kinase; Metal-binding;
KW   Nucleotide-binding; Transferase; Virulence; Zinc.
FT   CHAIN         1    188       Thymidine kinase.
FT                                /FTId=PRO_0000355223.
FT   NP_BIND      17     24       ATP. {ECO:0000250}.
FT   REGION      166    170       Substrate binding. {ECO:0000250}.
FT   ACT_SITE     92     92       Proton acceptor. {ECO:0000255}.
FT   METAL       146    146       Zinc. {ECO:0000250}.
FT   METAL       149    149       Zinc. {ECO:0000250}.
FT   METAL       179    179       Zinc. {ECO:0000250}.
FT   METAL       182    182       Zinc. {ECO:0000250}.
FT   BINDING     121    121       Substrate; via amide nitrogen.
FT                                {ECO:0000250}.
SQ   SEQUENCE   188 AA;  21483 MW;  0047D0121BE88938 CRC64;
     MNIIRKLKPG TISLVLGPMF AGKTTFLIHC IYMLERLEKK VVFIKSTKNT RDKTIKTHSG
     IQLQSKQCEI IESTQLSDVG SLTDIHAVVI DEAHFFDDLI KCRAWADEEK IIILAGLNAS
     FEQKMFQPIV HIFPYCSWIK YIGRTCMKCN RHNACFNVRK NADKTLILAG GSELYVTCCN
     NCLKKQMY
//
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