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DNLI_VACCW
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   03-AUG-2022, entry version 104.
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; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Pokkesviricetes;
OC   Chitovirales; Poxviridae; Chordopoxvirinae; 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 the
RT   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 gene
RT   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., Osborne J.,
RA   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 of
RT   viral replication and assembly.";
RL   J. Virol. 82:5922-5932(2008).
CC   -!- FUNCTION: DNA ligase that seals nicks in double-stranded DNA during DNA
CC       replication, DNA recombination and DNA repair. Recruits cellular
CC       topoisomerase II to sites of viral replication and assembly.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + (deoxyribonucleotide)n-3'-hydroxyl + 5'-phospho-
CC         (deoxyribonucleotide)m = (deoxyribonucleotide)n+m + AMP +
CC         diphosphate.; EC=6.5.1.1; Evidence={ECO:0000255|PROSITE-
CC         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 {ECO:0000269|PubMed:18417590}.
CC       Note=Found in sites viral of replication and assembly.
CC   -!- SIMILARITY: Belongs to the ATP-dependent DNA ligase family.
CC       {ECO:0000305}.
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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   SMR; P16272; -.
DR   GeneID; 3707705; -.
DR   KEGG; vg:3707705; -.
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:0006310; P:DNA recombination; IEA:UniProtKB-KW.
DR   GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR   GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.3260.10; -; 1.
DR   Gene3D; 2.40.50.140; -; 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; DNA damage; DNA recombination;
KW   DNA repair; DNA replication; Host cytoplasm; Ligase; Metal-binding;
KW   Nucleotide-binding; Reference proteome.
FT   CHAIN           1..552
FT                   /note="DNA ligase"
FT                   /id="PRO_0000059589"
FT   ACT_SITE        231
FT                   /note="N6-AMP-lysine intermediate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10135"
FT   BINDING         229
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         236
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         251
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         283
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         283
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         317
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         377
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         393
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         397
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="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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