DNLI_VAR67
ID DNLI_VAR67 Reviewed; 552 AA.
AC P0DOO3; P33798; Q90028;
DT 16-OCT-2019, integrated into UniProtKB/Swiss-Prot.
DT 16-OCT-2019, sequence version 1.
DT 03-AUG-2022, entry version 10.
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; ORFNames=A50R, J4R;
OS Variola virus (isolate Human/India/Ind3/1967) (VARV) (Smallpox virus).
OC Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Pokkesviricetes;
OC Chitovirales; Poxviridae; Chordopoxvirinae; Orthopoxvirus.
OX NCBI_TaxID=587200;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1666548;
RA Shchelkunov S.N., Marennikova S.S., Totmenin A.V., Blinov V.M.,
RA Chizhikov V.E., Gutorov V.V., Safronov P.F., Pozdnyakov S.G.,
RA Shelukhina E.M., Gashnikov P.V., Anjaparidze O.G., Sandakhchiev L.S.;
RT "Creation of a clone library of fragments from the natural variola virus
RT and study of the structural and functional organization of viral genes from
RT a circle of hosts.";
RL Dokl. Akad. Nauk SSSR 321:402-406(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=8384129; DOI=10.1016/0014-5793(93)80041-r;
RA Shchelkunov S.N., Blinov V.M., Sandakhchiev L.S.;
RT "Genes of variola and vaccinia viruses necessary to overcome the host
RT protective mechanisms.";
RL FEBS Lett. 319:80-83(1993).
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 {ECO:0000250}.
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. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Host cytoplasm. Note=Found in sites viral of
CC replication and assembly. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the ATP-dependent DNA ligase family.
CC {ECO:0000305}.
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DR EMBL; X69198; CAA49103.1; -; Genomic_DNA.
DR EMBL; X67118; CAA47545.1; -; Genomic_DNA.
DR PIR; C36854; JQ1857.
DR RefSeq; NP_042206.1; NC_001611.1.
DR SMR; P0DOO3; -.
DR GeneID; 1486450; -.
DR KEGG; vg:1486450; -.
DR Proteomes; UP000002060; 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 3: Inferred from homology;
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_0000059590"
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; 63382 MW; 618EDFB5B92FCE7D CRC64;
MTSLREFRKL CCAIYHASGY KEKSKLIRDF ITDRDDKYLI IKLLLPGLDD RIYNMNDKQI
IKIYSIIFKQ SQKDMLQDLG YGYIGDTIST FFKENTEIRP RNKSILTLED VDSFLTTLSS
ITKESHQIKL LTDIASVCTC NDLKCVVMLI DKDLKIKAGP RYVLNAISPH AYDVFRKSNN
LKEIIENESK QNLDSISVSV MTPINPMLAE SCDSVNKAFK KFPSGMFAEV KYDGERVQVH
KNNNEFAFFS RNMKPVLSYK VDYLKEYIPK AFKKATSIVL DSEIVLVDEH NVQLPFGSLG
IHKKKEYKNS NMCLFVFDCL YFDGFDMTDI PLYKRRSFLK DVMVEIPNRI VFSELTNISN
ESQLTDVLDD ALTRKLEGLV LKDINGVYEP GKRRWLKIKR DYLNEGSMAD SADLVVLGAY
YGKGAKGGIM AVFLMGCYDD ESGKWKTVTK CSGHDDNTLR VLQDQLTMVK INKDPKKIPE
WLVVNKIYIP DFVVEDPKQS QIWEISGAEF TSSKSHTANG ISIRFPRFTR IREDKTWKES
THLNDLVNLT KS
