DNA ligase - Vaccinia virus (strain Western Reserve) (VACV)

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P16272 (DNLI_VACCW) Reviewed, UniProtKB/Swiss-Prot

Last modified October 19, 2011. Version 74. History...

Clusters with 100%, 90%, 50% identity |

Documents (1) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
DNA ligase
EC=6.5.1.1

Alternative name(s):
Polydeoxyribonucleotide synthase [ATP]

Gene names

Name:	LIG
Ordered Locus Names:	VACWR176
ORF Names:	A50R

Organism

Vaccinia virus (strain Western Reserve) (VACV) (Vaccinia virus (strain WR))

Taxonomic identifier

10254 [NCBI]

Taxonomic lineage

Viruses › dsDNA viruses, no RNA stage › Poxviridae › Chordopoxvirinae › Orthopoxvirus › Vaccinia virus

Virus host

Bos taurus (Bovine) [TaxID: 9913]

Protein attributes

Sequence length	552 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	DNA ligase that seals nicks in double-stranded DNA during DNA replication, DNA recombination and DNA repair. Recruits cellular topoisomerase II to sites of viral replication and assembly.
Catalytic activity	ATP + (deoxyribonucleotide)(n) + (deoxyribonucleotide)(m) = AMP + diphosphate + (deoxyribonucleotide)(n+m).
Cofactor	Divalent metal cations By similarity.
Subunit structure	Interacts with host TOP2A and TOP2B. Ref.6
Subcellular location	Host cytoplasm. Note: Found in sites viral of replication and assembly. Ref.6
Sequence similarities	Belongs to the ATP-dependent DNA ligase family.

Ontologies

Keywords
Biological process	Cell cycle Cell division DNA damage DNA recombination DNA repair DNA replication
Cellular component	Host cytoplasm
Ligand	ATP-binding Metal-binding Nucleotide-binding
Molecular function	Ligase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	DNA ligation involved in DNA repair Inferred from electronic annotation. Source: InterPro DNA recombination Inferred from electronic annotation. Source: UniProtKB-KW DNA replication Inferred from electronic annotation. Source: UniProtKB-KW cell cycle Inferred from electronic annotation. Source: UniProtKB-KW cell division Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	host cell cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW DNA binding Inferred from electronic annotation. Source: InterPro DNA ligase (ATP) activity Inferred from electronic annotation. Source: EC metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 552

552

DNA ligase

PRO_0000059589

Sites

Active site

231

N6-AMP-lysine intermediate By similarity

Metal binding

283

Divalent metal cation 1 By similarity

Metal binding

377

Divalent metal cation 2 By similarity

Binding site

229

ATP By similarity

Binding site

236

ATP By similarity

Binding site

251

ATP By similarity

Binding site

283

ATP By similarity

Binding site

317

ATP By similarity

Binding site

393

ATP By similarity

Binding site

397

ATP By similarity

Sequences

Sequence

Length

Mass (Da)

Tools

P16272 [UniParc].

Last modified August 1, 1990. Version 1.
Checksum: 100F5210559F43DA
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FASTA

552

63,360

        10         20         30         40         50         60 
MTSLREFRKL CCDIYHASGY KEKSKLIRDF ITDRDDKYLI IKLLLPGLDD RIYNMNDKQI 

        70         80         90        100        110        120 
IKLYSIIFKQ SQEDMLQDLG YGYIGDTIRT FFKENTEIRP RDKSILTLED VDSFLTTLSS 

       130        140        150        160        170        180 
VTKESHQIKL LTDIASVCTC NDLKCVVMLI DKDLKIKAGP RYVLNAISPN AYDVFRKSNN 

       190        200        210        220        230        240 
LKEIIENASK QNLDSISISV MTPINPMLAE SCDSVNKAFK KFPSGMFAEV KYDGERVQVH 

       250        260        270        280        290        300 
KNNNEFAFFS RNMKPVLSHK VDYLKEYIPK AFKKATSIVL DSEIVLVDEH NVPLPFGSLG 

       310        320        330        340        350        360 
IHKKKEYKNS NMCLFVFDCL YFDGFDMTDI PLYERRSFLK DVMVEIPNRI VFSELTNISN 

       370        380        390        400        410        420 
ESQLTDVLDD ALTRKLEGLV LKDINGVYEP GKRRWLKIKR DYLNEGSMAD SADLVVLGAY 

       430        440        450        460        470        480 
YGKGAKGGIM AVFLMGCYDD ESGKWKTVTK CSGHDDNTLR VLQDQLTMVK INKDPKKIPE 

       490        500        510        520        530        540 
WLVVNKIYIP DFVVEDPKQS QIWEISGAEF TSSKSHTANG ISIRFPRFTR IREDKTWKES 

       550 
THLNDLVNLT KS

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Nucleotide sequence of 42 kbp of vaccinia virus strain WR from near the right inverted terminal repeat." Smith G.L., Chan Y.S., Howard S.T. J. Gen. Virol. 72:1349-1376(1991) [PubMed: 2045793] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Transcriptional mapping and nucleotide sequence of a vaccinia virus gene encoding a polypeptide with extensive homology to DNA ligases." Smith G.L., Chan Y.S., Kerr S.M. Nucleic Acids Res. 17:9051-9062(1989) [PubMed: 2555782] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]	"Sequencing of the coding region of Vaccinia-WR to an average 9-fold redundancy and an error rate of 0.16/10kb." Esposito J.J., Frace A.M., Sammons S.A., Olsen-Rasmussen M., Osborne J., Wohlhueter R. Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]	"Vaccinia virus encodes a polypeptide with DNA ligase activity." Kerr S.M., Smith G.L. Nucleic Acids Res. 17:9039-9050(1989) [PubMed: 2587253] [Abstract] Cited for: CHARACTERIZATION.
[5]	"Domain structure of vaccinia DNA ligase." Sekiguchi J., Shuman S. Nucleic Acids Res. 25:727-734(1997) [PubMed: 9016621] [Abstract] Cited for: DOMAIN STRUCTURE.
[6]	"Vaccinia virus DNA ligase recruits cellular topoisomerase II to sites of viral replication and assembly." Lin Y.C., Li J., Irwin C.R., Jenkins H., DeLange L., Evans D.H. J. Virol. 82:5922-5932(2008) [PubMed: 18417590] [Abstract] Cited for: SUBCELLULAR LOCATION, INTERACTION WITH HOST TOP2A AND TOP2B.

Cross-references

Sequence databases
EMBL GenBank DDBJ	D11079 Genomic DNA. Translation: BAA01824.1. X16512 Genomic DNA. Translation: CAA34519.1. AY243312 Genomic DNA. Translation: AAO89455.1.
PIR	JQ1788.
RefSeq	YP_233058.1. NC_006998.1.
3D structure databases
ProteinModelPortal	P16272.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	3707705.
Phylogenomic databases
ProtClustDB	CLSP2509847.
Family and domain databases
InterPro	IPR000977. DNA_ligase_ATP-dep. IPR012309. DNA_ligase_ATP-dep_C. IPR012310. DNA_ligase_ATP-dep_cent. IPR016059. DNA_ligase_ATP-dep_CS. IPR012308. DNA_ligase_ATP-dep_N. IPR012340. NA-bd_OB-fold. IPR016027. NA-bd_OB-fold-like. [Graphical view]
Gene3D	G3DSA:2.40.50.140. OB_NA_bd_sub. 1 hit.
Pfam	PF04679. DNA_ligase_A_C. 1 hit. PF01068. DNA_ligase_A_M. 1 hit. PF04675. DNA_ligase_A_N. 1 hit. [Graphical view]
SUPFAM	SSF50249. Nucleic_acid_OB. 1 hit.
TIGRFAMs	TIGR00574. Dnl1. 1 hit.
PROSITE	PS00697. DNA_LIGASE_A1. 1 hit. PS00333. DNA_LIGASE_A2. 1 hit. PS50160. DNA_LIGASE_A3. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

DNLI_VACCW

Accession

Primary (citable) accession number: P16272
Secondary accession number(s): Q76ZM8

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1990
Last sequence update:	August 1, 1990
Last modified:	October 19, 2011
This is version 74 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Viral Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Sites

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protocols and materials databases

Genome annotation databases

Phylogenomic databases

Family and domain databases

Entry information

Relevant documents