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O28469 (TOP1_ARCFU) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 106. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | 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:AF_1806
OrganismArchaeoglobus fulgidus (strain ATCC 49558 / VC-16 / DSM 4304 / JCM 9628 / NBRC 100126) [Reference proteome] [HAMAP]
Taxonomic identifier224325 [NCBI]
Taxonomic lineageArchaeaEuryarchaeotaArchaeoglobiArchaeoglobalesArchaeoglobaceaeArchaeoglobus

Protein attributes

Sequence length663 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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 663663DNA topoisomerase 1 HAMAP-Rule MF_00952
PRO_0000145177

Regions

Domain4 – 137134Toprim
Zinc finger583 – 61028C4-type 1 HAMAP-Rule MF_00952
Zinc finger629 – 65325C4-type 2; atypical HAMAP-Rule MF_00952
Region193 – 1986Interaction with DNA By similarity

Sites

Active site3061O-(5'-phospho-DNA)-tyrosine intermediate By similarity
Metal binding101Magnesium 1; catalytic By similarity
Metal binding1061Magnesium 1; catalytic By similarity
Metal binding1061Magnesium 2 By similarity
Metal binding1081Magnesium 2 By similarity
Site521Interaction with DNA By similarity
Site1651Interaction with DNA By similarity
Site1691Interaction with DNA By similarity
Site3081Interaction with DNA By similarity
Site4921Interaction with DNA By similarity

Sequences

Sequence LengthMass (Da)Tools
O28469 [UniParc].

Last modified January 1, 1998. Version 1.
Checksum: 0A07E4FD20871BAC

FASTA66376,018
        10         20         30         40         50         60 
MVMSWLIITE KDNTARRIAS ILFKDVKTLK KGRVSYYHSP SNDAYVVGLK GHIVELDFPK 

        70         80         90        100        110        120 
ELNNWTKTPL EKLLQAELVK KVKERTISSI LKEIAKKADR VTVATDYDRE GELIGVEALE 

       130        140        150        160        170        180 
IVKSVNPTVK VDRVRYSAVT EKEIRSAFSK PVKVDFNLAN AALARQKIDL IWGATLTRLI 

       190        200        210        220        230        240 
SVHSGRMGKD FLSVGRVQTP TLRLIVDREL EIQNFKPEKY YEIFAEFEGF IAKHPKRYGS 

       250        260        270        280        290        300 
KEEAEKLFAK IGETAKVEEF TRRRMEENRP TPFNTTEFLR EASKFMSPHK AMNIAETLYM 

       310        320        330        340        350        360 
NGYISYPRTD NTVYPPTINL IEIVSALSSV FPREAQIVLS QDKITPSRGR RETKDHPPIY 

       370        380        390        400        410        420 
PTGVAKRGEL SKDEWTIYEL VVRRFLATLA PKAVWDVRRV VLDSNGVKFV ANGRQLVEAG 

       430        440        450        460        470        480 
WRDIYIYSKA EETELPLLKK GDVLRILKKR LEEKETKPPG RYSASSLIKM MEKLNLGTKS 

       490        500        510        520        530        540 
TRHEIIQKLV SRRYIHGNPF RPSETAFSVI NVLKETAETI TLPDMTAKLE NEMDLIAEGK 

       550        560        570        580        590        600 
KREPEVVDES REMLLQILRA IDYRKLSKDL REGVKKDKIV GKCPECGGEL VVRQSKAGKR 

       610        620        630        640        650        660 
FIGCSNYPDC TFTLPLPQNG TLYITAKQCK EHEIKEVKIR TKKGYWNLGC PYCNYLNWKK 


ENS 

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Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE000782 Genomic DNA. Translation: AAB89443.1.
PIRE69475.
RefSeqNP_070633.1. NC_000917.1.

3D structure databases

ProteinModelPortalO28469.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING224325.AF1806.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAB89443; AAB89443; AF_1806.
GeneID1485029.
KEGGafu:AF1806.

Phylogenomic databases

eggNOGCOG0551.
KOK03168.
OMAYIESDPP.
ProtClustDBCLSK2747048.

Enzyme and pathway databases

BioCycAFUL224325:GJBC-1841-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.
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. 1 hit.
PROSITEPS00396. TOPOISOMERASE_I_PROK. 1 hit.
PS50880. TOPRIM. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameTOP1_ARCFU
AccessionPrimary (citable) accession number: O28469
Entry history
Integrated into UniProtKB/Swiss-Prot: June 20, 2001
Last sequence update: January 1, 1998
Last modified: February 19, 2014
This is version 106 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