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Database: UniProt
Entry: P16272
LinkDB: P16272
Original site: P16272 
ID   DNLI_VACCW              Reviewed;         552 AA.
AC   P16272; Q76ZM8;
DT   01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1990, sequence version 1.
DT   25-OCT-2017, entry version 93.
DE   RecName: Full=DNA ligase;
DE            EC=6.5.1.1 {ECO:0000255|PROSITE-ProRule:PRU10135};
DE   AltName: Full=Polydeoxyribonucleotide synthase [ATP];
GN   Name=LIG; OrderedLocusNames=VACWR176; ORFNames=A50R;
OS   Vaccinia virus (strain Western Reserve) (VACV) (Vaccinia virus (strain
OS   WR)).
OC   Viruses; dsDNA viruses, no RNA stage; Poxviridae; Chordopoxvirinae;
OC   Orthopoxvirus; Vaccinia virus.
OX   NCBI_TaxID=10254;
OH   NCBI_TaxID=9913; Bos taurus (Bovine).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2045793; DOI=10.1099/0022-1317-72-6-1349;
RA   Smith G.L., Chan Y.S., Howard S.T.;
RT   "Nucleotide sequence of 42 kbp of vaccinia virus strain WR from near
RT   the right inverted terminal repeat.";
RL   J. Gen. Virol. 72:1349-1376(1991).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2555782; DOI=10.1093/nar/17.22.9051;
RA   Smith G.L., Chan Y.S., Kerr S.M.;
RT   "Transcriptional mapping and nucleotide sequence of a vaccinia virus
RT   gene encoding a polypeptide with extensive homology to DNA ligases.";
RL   Nucleic Acids Res. 17:9051-9062(1989).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Esposito J.J., Frace A.M., Sammons S.A., Olsen-Rasmussen M.,
RA   Osborne J., Wohlhueter R.;
RT   "Sequencing of the coding region of Vaccinia-WR to an average 9-fold
RT   redundancy and an error rate of 0.16/10kb.";
RL   Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   CHARACTERIZATION.
RX   PubMed=2587253; DOI=10.1093/nar/17.22.9039;
RA   Kerr S.M., Smith G.L.;
RT   "Vaccinia virus encodes a polypeptide with DNA ligase activity.";
RL   Nucleic Acids Res. 17:9039-9050(1989).
RN   [5]
RP   DOMAIN STRUCTURE.
RX   PubMed=9016621; DOI=10.1093/nar/25.4.727;
RA   Sekiguchi J., Shuman S.;
RT   "Domain structure of vaccinia DNA ligase.";
RL   Nucleic Acids Res. 25:727-734(1997).
RN   [6]
RP   SUBCELLULAR LOCATION, AND INTERACTION WITH HOST TOP2A AND TOP2B.
RX   PubMed=18417590; DOI=10.1128/JVI.02723-07;
RA   Lin Y.C., Li J., Irwin C.R., Jenkins H., DeLange L., Evans D.H.;
RT   "Vaccinia virus DNA ligase recruits cellular topoisomerase II to sites
RT   of viral replication and assembly.";
RL   J. Virol. 82:5922-5932(2008).
CC   -!- FUNCTION: DNA ligase that seals nicks in double-stranded DNA
CC       during DNA replication, DNA recombination and DNA repair. Recruits
CC       cellular topoisomerase II to sites of viral replication and
CC       assembly.
CC   -!- CATALYTIC ACTIVITY: ATP + (deoxyribonucleotide)(n)-3'-hydroxyl +
CC       5'-phospho-(deoxyribonucleotide)(m) = (deoxyribonucleotide)(n+m) +
CC       AMP + diphosphate. {ECO:0000255|PROSITE-ProRule:PRU10135}.
CC   -!- COFACTOR:
CC       Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC         Evidence={ECO:0000250};
CC   -!- SUBUNIT: Interacts with host TOP2A and TOP2B.
CC       {ECO:0000269|PubMed:18417590}.
CC   -!- SUBCELLULAR LOCATION: Host cytoplasm
CC       {ECO:0000269|PubMed:18417590}. Note=Found in sites viral of
CC       replication and assembly.
CC   -!- SIMILARITY: Belongs to the ATP-dependent DNA ligase family.
CC       {ECO:0000305}.
DR   EMBL; D11079; BAA01824.1; -; Genomic_DNA.
DR   EMBL; X16512; CAA34519.1; -; Genomic_DNA.
DR   EMBL; AY243312; AAO89455.1; -; Genomic_DNA.
DR   PIR; JQ1788; JQ1788.
DR   RefSeq; YP_233058.1; NC_006998.1.
DR   ProteinModelPortal; P16272; -.
DR   SMR; P16272; -.
DR   GeneID; 3707705; -.
DR   KEGG; vg:3707705; -.
DR   KO; K10776; -.
DR   OrthoDB; VOG0900005P; -.
DR   Proteomes; UP000000344; Genome.
DR   GO; GO:0030430; C:host cell cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0003910; F:DNA ligase (ATP) activity; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   GO; GO:0071897; P:DNA biosynthetic process; IEA:InterPro.
DR   GO; GO:0051103; P:DNA ligation involved in DNA repair; IEA:InterPro.
DR   GO; GO:0006310; P:DNA recombination; IEA:UniProtKB-KW.
DR   GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.3260.10; -; 1.
DR   InterPro; IPR000977; DNA_ligase_ATP-dep.
DR   InterPro; IPR012309; DNA_ligase_ATP-dep_C.
DR   InterPro; IPR012310; DNA_ligase_ATP-dep_cent.
DR   InterPro; IPR016059; DNA_ligase_ATP-dep_CS.
DR   InterPro; IPR012308; DNA_ligase_ATP-dep_N.
DR   InterPro; IPR036599; DNA_ligase_N_sf.
DR   InterPro; IPR012340; NA-bd_OB-fold.
DR   Pfam; PF04679; DNA_ligase_A_C; 1.
DR   Pfam; PF01068; DNA_ligase_A_M; 1.
DR   Pfam; PF04675; DNA_ligase_A_N; 1.
DR   SUPFAM; SSF117018; SSF117018; 1.
DR   SUPFAM; SSF50249; SSF50249; 1.
DR   TIGRFAMs; TIGR00574; dnl1; 1.
DR   PROSITE; PS00697; DNA_LIGASE_A1; 1.
DR   PROSITE; PS00333; DNA_LIGASE_A2; 1.
DR   PROSITE; PS50160; DNA_LIGASE_A3; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; Cell cycle; Cell division; Complete proteome; DNA damage;
KW   DNA recombination; DNA repair; DNA replication; Host cytoplasm;
KW   Ligase; Metal-binding; Nucleotide-binding; Reference proteome.
FT   CHAIN         1    552       DNA ligase.
FT                                /FTId=PRO_0000059589.
FT   ACT_SITE    231    231       N6-AMP-lysine intermediate.
FT                                {ECO:0000255|PROSITE-ProRule:PRU10135}.
FT   METAL       283    283       Divalent metal cation 1. {ECO:0000250}.
FT   METAL       377    377       Divalent metal cation 2. {ECO:0000250}.
FT   BINDING     229    229       ATP. {ECO:0000250}.
FT   BINDING     236    236       ATP. {ECO:0000250}.
FT   BINDING     251    251       ATP. {ECO:0000250}.
FT   BINDING     283    283       ATP. {ECO:0000250}.
FT   BINDING     317    317       ATP. {ECO:0000250}.
FT   BINDING     393    393       ATP. {ECO:0000250}.
FT   BINDING     397    397       ATP. {ECO:0000250}.
SQ   SEQUENCE   552 AA;  63360 MW;  100F5210559F43DA CRC64;
     MTSLREFRKL CCDIYHASGY KEKSKLIRDF ITDRDDKYLI IKLLLPGLDD RIYNMNDKQI
     IKLYSIIFKQ SQEDMLQDLG YGYIGDTIRT FFKENTEIRP RDKSILTLED VDSFLTTLSS
     VTKESHQIKL LTDIASVCTC NDLKCVVMLI DKDLKIKAGP RYVLNAISPN AYDVFRKSNN
     LKEIIENASK QNLDSISISV MTPINPMLAE SCDSVNKAFK KFPSGMFAEV KYDGERVQVH
     KNNNEFAFFS RNMKPVLSHK VDYLKEYIPK AFKKATSIVL DSEIVLVDEH NVPLPFGSLG
     IHKKKEYKNS NMCLFVFDCL YFDGFDMTDI PLYERRSFLK DVMVEIPNRI VFSELTNISN
     ESQLTDVLDD ALTRKLEGLV LKDINGVYEP GKRRWLKIKR DYLNEGSMAD SADLVVLGAY
     YGKGAKGGIM AVFLMGCYDD ESGKWKTVTK CSGHDDNTLR VLQDQLTMVK INKDPKKIPE
     WLVVNKIYIP DFVVEDPKQS QIWEISGAEF TSSKSHTANG ISIRFPRFTR IREDKTWKES
     THLNDLVNLT KS
//
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