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P68698 (TOP1_VACCW) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 66. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
DNA topoisomerase 1B

Short name=TopIB
EC=5.99.1.2
Alternative name(s):
DNA topoisomerase I
Late protein H6
Gene names
Name:TOP1
Ordered Locus Names:VACWR104
ORF Names:H6R
OrganismVaccinia virus (strain Western Reserve) (VACV) (Vaccinia virus (strain WR)) [Reference proteome]
Taxonomic identifier10254 [NCBI]
Taxonomic lineageVirusesdsDNA viruses, no RNA stagePoxviridaeChordopoxvirinaeOrthopoxvirusVaccinia virus
Virus hostBos taurus (Bovine) [TaxID: 9913]

Protein attributes

Sequence length314 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Releases the supercoiling and torsional tension of DNA introduced during the DNA replication and transcription by transiently cleaving and rejoining one strand of the DNA duplex. Introduces a single-strand break via transesterification at the specific target site 5'-[CT]CCTTp site in duplex DNA. The scissile phosphodiester is attacked by the catalytic tyrosine of the enzyme, resulting in the formation of a DNA-(3'-phosphotyrosyl)-enzyme intermediate and the expulsion of a 5'-OH DNA strand. The free DNA strand then undergoes passage around the unbroken strand thus removing DNA supercoils. Finally, in the religation step, the DNA 5'-OH attacks the covalent intermediate to expel the active-site tyrosine and restore the DNA phosphodiester backbone. Ref.6 Ref.7

Catalytic activity

ATP-independent breakage of single-stranded DNA, followed by passage and rejoining.

Subcellular location

Virion Potential.

Induction

Expressed in the late phase of the viral replicative cycle.

Sequence similarities

Belongs to the type IB topoisomerase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 314314DNA topoisomerase 1B
PRO_0000145216

Sites

Active site2741O-(3'-phospho-DNA)-tyrosine intermediate Ref.5
Site1681Involved in religation By similarity

Experimental info

Mutagenesis2161G → E or K: No change in activity.
Mutagenesis2171I → P: Temperature-sensitive for DNA relaxation in vitro.
Mutagenesis2201K → D: Loss of activity.
Mutagenesis2201K → I or N: Reduced activity.
Mutagenesis2231R → E or G: Loss of activity.
Mutagenesis2231R → K: Reduced activity.
Mutagenesis2241T → G or P: Reduced activity.
Mutagenesis2251Y → H: No change in activity.
Mutagenesis2251Y → R or S: Reduced activity.
Mutagenesis2741Y → F: Complete loss of activity. Ref.5

Secondary structure

.................................................... 314
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P68698 [UniParc].

Last modified August 1, 1988. Version 1.
Checksum: E76FBCFCBF259D27

FASTA31436,666
        10         20         30         40         50         60 
MRALFYKDGK LFTDNNFLNP VSDDNPAYEV LQHVKIPTHL TDVVVYEQTW EEALTRLIFV 

        70         80         90        100        110        120 
GSDSKGRRQY FYGKMHVQNR NAKRDRIFVR VYNVMKRINC FINKNIKKSS TDSNYQLAVF 

       130        140        150        160        170        180 
MLMETMFFIR FGKMKYLKEN ETVGLLTLKN KHIEISPDEI VIKFVGKDKV SHEFVVHKSN 

       190        200        210        220        230        240 
RLYKPLLKLT DDSSPEEFLF NKLSERKVYE CIKQFGIRIK DLRTYGVNYT FLYNFWTNVK 

       250        260        270        280        290        300 
SISPLPSPKK LIALTIKQTA EVVGHTPSIS KRAYMATTIL EMVKDKNFLD VVSKTTFDEF 

       310 
LSIVVDHVKS STDG 

« Hide

References

« Hide 'large scale' references
[1]"Conserved TAAATG sequence at the transcriptional and translational initiation sites of vaccinia virus late genes deduced by structural and functional analysis of the HindIII H genome fragment."
Rosel J.L., Earl P.L., Weir J.P., Moss B.
J. Virol. 60:436-449(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Biochemical analysis of mutant alleles of the vaccinia virus topoisomerase I carrying targeted substitutions in a highly conserved domain."
Klemperer N., Traktman P.
J. Biol. Chem. 268:15887-15899(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE, MUTAGENESIS.
[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]"Identification of a vaccinia virus gene encoding a type I DNA topoisomerase."
Shuman S., Moss B.
Proc. Natl. Acad. Sci. U.S.A. 84:7478-7482(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 1-22, IDENTIFICATION.
[5]"Analogues of vaccinia virus DNA topoisomerase I modified at the active site tyrosine."
Gao R., Zhang Y., Choudhury A.K., Dedkova L.M., Hecht S.M.
J. Am. Chem. Soc. 127:3321-3331(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: ACTIVE SITE, MUTAGENESIS OF TYR-274.
[6]"Major groove interactions of vaccinia Topo I provide specificity by optimally positioning the covalent phosphotyrosine linkage."
Nagarajan R., Stivers J.T.
Biochemistry 45:5775-5782(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[7]"Mechanism and specificity of DNA strand exchange catalyzed by vaccinia DNA topoisomerase type I."
Stahley M.R., Stivers J.T.
Biochemistry 49:2786-2795(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[8]"Crystal structure of the amino-terminal fragment of vaccinia virus DNA topoisomerase I at 1.6-A resolution."
Sharma A., Hanai R., Mondragon A.
Structure 2:767-777(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 1-77.
[9]"Conservation of structure and mechanism between eukaryotic topoisomerase I and site-specific recombinases."
Cheng C., Kussie P., Pavletich N., Shuman S.
Cell 92:841-850(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 81-314.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M13209 Genomic DNA. Translation: AAB59842.1.
L13447 Unassigned DNA. Translation: AAA02841.1.
AY243312 Genomic DNA. Translation: AAO89383.1.
PIRQQVZH7. G24481.
RefSeqYP_232986.1. NC_006998.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1A41X-ray2.30A81-314[»]
1VCCX-ray1.60A1-77[»]
ProteinModelPortalP68698.
SMRP68698. Positions 1-314.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID3707560.

Phylogenomic databases

ProtClustDBPHA3101.

Family and domain databases

Gene3D1.20.120.380. 1 hit.
3.30.66.10. 1 hit.
3.90.15.10. 1 hit.
InterProIPR011010. DNA_brk_join_enz.
IPR001631. TopoI.
IPR018521. TopoI_AS.
IPR014711. TopoI_cat_a-hlx-sub_euk.
IPR027362. TopoI_cat_dom2.
IPR013500. TopoI_cat_euk.
IPR015346. TopoI_N_vir.
[Graphical view]
PfamPF01028. Topoisom_I. 1 hit.
PF09266. VirDNA-topo-I_N. 1 hit.
[Graphical view]
PRINTSPR00416. EUTPISMRASEI.
SUPFAMSSF56349. SSF56349. 1 hit.
PROSITEPS00176. TOPOISOMERASE_I_EUK. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP68698.

Entry information

Entry nameTOP1_VACCW
AccessionPrimary (citable) accession number: P68698
Secondary accession number(s): P08585
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: August 1, 1988
Last modified: April 16, 2014
This is version 66 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references