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Q68X45 (TOP1_RICTY) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 74. 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 1

EC=5.99.1.2
Alternative name(s):
DNA topoisomerase I
Omega-protein
Relaxing enzyme
Swivelase
Untwisting enzyme
Gene names
Name:topA
Ordered Locus Names:RT0317
OrganismRickettsia typhi (strain ATCC VR-144 / Wilmington) [Complete proteome] [HAMAP]
Taxonomic identifier257363 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRickettsialesRickettsiaceaeRickettsieaeRickettsiatyphus group

Protein attributes

Sequence length779 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Releases the supercoiling and torsional tension of DNA, which is 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 a target site in duplex DNA. The scissile phosphodiester is attacked by the catalytic tyrosine of the enzyme, resulting in the formation of a DNA-(5'-phosphotyrosyl)-enzyme intermediate and the expulsion of a 3'-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 3'-OH attacks the covalent intermediate to expel the active-site tyrosine and restore the DNA phosphodiester backbone By similarity. HAMAP-Rule MF_00952

Catalytic activity

ATP-independent breakage of single-stranded DNA, followed by passage and rejoining. HAMAP-Rule MF_00952

Cofactor

Magnesium. Binds two Mg2+ per subunit By similarity. HAMAP-Rule MF_00952

Subunit structure

Monomer By similarity. HAMAP-Rule MF_00952

Sequence similarities

Belongs to the type IA topoisomerase family.

Contains 1 Toprim domain.

Ontologies

Keywords
   DomainZinc-finger
   LigandDNA-binding
Magnesium
Metal-binding
Zinc
   Molecular functionIsomerase
Topoisomerase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological_processDNA topological change

Inferred from electronic annotation. Source: UniProtKB-HAMAP

   Cellular_componentchromosome

Inferred from electronic annotation. Source: InterPro

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-HAMAP

DNA binding

Inferred from electronic annotation. Source: UniProtKB-KW

DNA topoisomerase type I activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

magnesium ion binding

Inferred from electronic annotation. Source: UniProtKB-HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 779779DNA topoisomerase 1 HAMAP-Rule MF_00952
PRO_0000273106

Regions

Domain1 – 111111Toprim
Zinc finger600 – 62728C4-type HAMAP-Rule MF_00952
Region166 – 1716Interaction with DNA By similarity

Sites

Active site3041O-(5'-phospho-DNA)-tyrosine intermediate By similarity
Metal binding71Magnesium 1; catalytic By similarity
Metal binding801Magnesium 1; catalytic By similarity
Metal binding801Magnesium 2 By similarity
Metal binding821Magnesium 2 By similarity
Site311Interaction with DNA By similarity
Site1421Interaction with DNA By similarity
Site1431Interaction with DNA By similarity
Site1461Interaction with DNA By similarity
Site1581Interaction with DNA By similarity
Site3061Interaction with DNA By similarity
Site4991Interaction with DNA By similarity

Sequences

Sequence LengthMass (Da)Tools
Q68X45 [UniParc].

Last modified October 11, 2004. Version 1.
Checksum: D300A268969CEA89

FASTA77989,083
        10         20         30         40         50         60 
MKLVIVESPA KAKTINKYLG DEFKVIASFG HIRDLPSKKG SVLPDKNFAM EYDISDKASK 

        70         80         90        100        110        120 
YVDAIVKYAR KAEAVYLATD PDREGESISW HVAEVIKEKN KVESDDFFKR VAFNEITKKA 

       130        140        150        160        170        180 
IIHAVENPRK LDTNLVNAQQ ARRALDYLVG FTLSPLLWRK LPGCKSAGRV QSVALRLICD 

       190        200        210        220        230        240 
REDEIERFKA EEYWDISLKM QNSNNELFTA KLTHVNDQKL KKFSIINEKE AKDLTRKLKL 

       250        260        270        280        290        300 
QKFYVEKIEK KQQKRQPQPP FITSSLQQEA ARKLGFSAKK TMQIAQKLYE GVDIGKETIG 

       310        320        330        340        350        360 
LITYMRTDGV TLSNDAIADI RKLIDKNYGN KYLPINPRIY QSKVKNAQEA HEAIRPTNIT 

       370        380        390        400        410        420 
YTPDNLKQKL EKDYYKLYEL IWQRTIACQM ENVIMDLVIA NLASENKEYL AKANGSIIAF 

       430        440        450        460        470        480 
DGFYKVYRES LDDEDEEDNK MLPPLKAQEH IKTKEVIPNK HFTEPPPRYS EASLVKKLEE 

       490        500        510        520        530        540 
LGIGRPSTYA SILSVLQDRK YVTLEKKRFI PEELGRLVTV FLVGFFKKYV EYDFTAGLEN 

       550        560        570        580        590        600 
ELDEIAAGKL EWKTSLNNFW SGFNNNIESV NEQKITEIIN YLQKALDYHL FGENKESKVC 

       610        620        630        640        650        660 
PSCKTGQLSL KLGKFGAFLA CSNYPECTFK KSIVSGNDNN EDEGNLSTIL NDNKILGTDK 

       670        680        690        700        710        720 
DGVEIYLKTG PYGPYIQLGE QCGKVKPKRT PVPTNLKQSE ITLEVALKLL SLPLKIGIHK 

       730        740        750        760        770 
DSGEEIIIGY SKFGPYIKYM CKFISVPKKY DFLNLNLDDA IKLIENNKAK LEKKHRSMV 

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References

[1]"Complete genome sequence of Rickettsia typhi and comparison with sequences of other Rickettsiae."
McLeod M.P., Qin X., Karpathy S.E., Gioia J., Highlander S.K., Fox G.E., McNeill T.Z., Jiang H., Muzny D., Jacob L.S., Hawes A.C., Sodergren E., Gill R., Hume J., Morgan M., Fan G., Amin A.G., Gibbs R.A. expand/collapse author list , Hong C., Yu X.-J., Walker D.H., Weinstock G.M.
J. Bacteriol. 186:5842-5855(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC VR-144 / Wilmington.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE017197 Genomic DNA. Translation: AAU03797.1.
RefSeqYP_067279.1. NC_006142.1.

3D structure databases

ProteinModelPortalQ68X45.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING257363.RT0317.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAU03797; AAU03797; RT0317.
GeneID2958716.
KEGGrty:RT0317.
PATRIC17909828. VBIRicTyp34752_0329.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1754.
HOGENOMHOG000004020.
KOK03168.
OMACERELEI.
OrthoDBEOG6S7XQ9.

Enzyme and pathway databases

BioCycRTYP257363:GJEQ-332-MONOMER.

Family and domain databases

Gene3D1.10.460.10. 2 hits.
2.70.20.10. 2 hits.
3.40.50.140. 1 hit.
HAMAPMF_00952. Topoisom_1_prok.
InterProIPR000380. Topo_IA.
IPR003601. Topo_IA_2.
IPR023406. Topo_IA_AS.
IPR013497. Topo_IA_cen.
IPR013824. Topo_IA_cen_sub1.
IPR013825. Topo_IA_cen_sub2.
IPR023405. Topo_IA_core_domain.
IPR003602. Topo_IA_DNA-bd.
IPR013498. Topo_IA_Znf.
IPR005733. TopoI_bac-type.
IPR028612. Topoisom_1_IA.
IPR006171. Toprim_domain.
[Graphical view]
PANTHERPTHR11390. PTHR11390. 1 hit.
PfamPF01131. Topoisom_bac. 1 hit.
PF01751. Toprim. 1 hit.
PF01396. zf-C4_Topoisom. 1 hit.
[Graphical view]
PRINTSPR00417. PRTPISMRASEI.
SMARTSM00437. TOP1Ac. 1 hit.
SM00436. TOP1Bc. 1 hit.
SM00493. TOPRIM. 1 hit.
[Graphical view]
SUPFAMSSF56712. SSF56712. 2 hits.
TIGRFAMsTIGR01051. topA_bact. 1 hit.
PROSITEPS00396. TOPOISOMERASE_I_PROK. 1 hit.
PS50880. TOPRIM. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameTOP1_RICTY
AccessionPrimary (citable) accession number: Q68X45
Entry history
Integrated into UniProtKB/Swiss-Prot: January 23, 2007
Last sequence update: October 11, 2004
Last modified: July 9, 2014
This is version 74 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Rickettsia typhi

Rickettsia typhi (strain Wilmington): entries and gene names