DNLI_VACCC
ID DNLI_VACCC Reviewed; 552 AA.
AC P20492;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1991, sequence version 1.
DT 03-AUG-2022, entry version 99.
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;
OS Vaccinia virus (strain Copenhagen) (VACV).
OC Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Pokkesviricetes;
OC Chitovirales; Poxviridae; Chordopoxvirinae; Orthopoxvirus; Vaccinia virus.
OX NCBI_TaxID=10249;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=2219722; DOI=10.1016/0042-6822(90)90294-2;
RA Goebel S.J., Johnson G.P., Perkus M.E., Davis S.W., Winslow J.P.,
RA Paoletti E.;
RT "The complete DNA sequence of vaccinia virus.";
RL Virology 179:247-266(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Goebel S.J., Johnson G.P., Perkus M.E., Davis S.W., Winslow J.P.,
RA Paoletti E.;
RT "Appendix to 'The complete DNA sequence of vaccinia virus'.";
RL Virology 179:517-563(1990).
RN [3]
RP CHARACTERIZATION.
RX PubMed=2219723; DOI=10.1016/0042-6822(90)90295-3;
RA Colinas R.J., Goebel S.J., Davis S.W., Johnson G.P., Norton E.K.,
RA Paoletti E.;
RT "A DNA ligase gene in the Copenhagen strain of vaccinia virus is
RT nonessential for viral replication and recombination.";
RL Virology 179:267-275(1990).
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; M35027; AAA48182.1; -; Genomic_DNA.
DR PIR; G42522; WMVZ7W.
DR SMR; P20492; -.
DR Proteomes; UP000008269; 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_0000059588"
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; 63390 MW; D97FA799D2E2F7E9 CRC64;
MTSLREFRKL CCDIYHASGY KEKSKLIRDF ITDRDDKYLI IKLLLPGLDD RIYNMNDKQI
IKLYSIIFKQ SQEDMLQDLG YGYIGDTIRT FFKENTEIRP RDKSILTLED VDSFLTTLSS
VTKESHQIKL LTDIASVCTC NDLKCVVMLI DKDLKIKAGP RYVLNAISPN AYDVFRKSNN
LKEIIENSSK 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 VLQDQLTMIK INKDPKKIPE
WLVVNKIYIP DFVVEDPKQS QIWEISGAEF TSSKSHTANG ISIRFPRFTR IREDKTWKES
THLNDLVNLT KS
