Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q9YB01 (TOP1_AERPE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 101. 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:APE_1794
OrganismAeropyrum pernix (strain ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1) [Complete proteome] [HAMAP]
Taxonomic identifier272557 [NCBI]
Taxonomic lineageArchaeaCrenarchaeotaThermoproteiDesulfurococcalesDesulfurococcaceaeAeropyrum

Protein attributes

Sequence length673 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 – 673673DNA topoisomerase 1 HAMAP-Rule MF_00952
PRO_0000145176

Regions

Domain1 – 134134Toprim
Zinc finger595 – 61521C4-type HAMAP-Rule MF_00952
Region189 – 1946Interaction with DNA By similarity

Sites

Active site3111O-(5'-phospho-DNA)-tyrosine intermediate By similarity
Metal binding41Magnesium 1; catalytic By similarity
Metal binding1031Magnesium 1; catalytic By similarity
Metal binding1031Magnesium 2 By similarity
Metal binding1051Magnesium 2 By similarity
Site501Interaction with DNA By similarity
Site1591Interaction with DNA By similarity
Site1631Interaction with DNA By similarity
Site3131Interaction with DNA By similarity
Site5011Interaction with DNA By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9YB01 [UniParc].

Last modified November 1, 1999. Version 1.
Checksum: D26799337623C584

FASTA67375,571
        10         20         30         40         50         60 
MVAEKPKAAA KIAYALSDGR GVLRCSEYGV PYWIVRRDGA AIVVAPSAGH LFGPHTDSRG 

        70         80         90        100        110        120 
FPVFDFEWRP IFEFDRGAGY LSKFYRMLSR ILPGASLYVN ACDYDIEGSV IGFKIIEAFG 

       130        140        150        160        170        180 
DVNRARRMKF STLAPQDIRR AYARMERLDV EMIEAGMARS EMDWLWGINV SRALMEAARR 

       190        200        210        220        230        240 
AAGRRVILSA GRVQSPTLVE AYRRWREINL HVPKASVAVK ITAEKGGGVF DARPHGWKPQ 

       250        260        270        280        290        300 
SLETARSIKS ELRKNPWLAV EEVRSERSIL RPPPAFNLGD LQKEANRILG LPPLRTQSIA 

       310        320        330        340        350        360 
EELYLEALIS YPRTNSQKLP PSINYRAILD KLAHGPLGRE ARELLKETGG VLRPVQGSKD 

       370        380        390        400        410        420 
DPAHPAIHPT GEKPSQRLSK EHMAVYELIV RRFLAAFSRE AIVSKSSVLL RDFQGRVWRA 

       430        440        450        460        470        480 
EGLRVEDLGW LKYYHYSTPG EKPMPPLDRG DKARVVRVDV RVEWSQTPVR LDKASLLRWM 

       490        500        510        520        530        540 
ESVNIGTEGT RARIIETLYK RGYLEGSRKS EVTPLGEAVA VIIQTLFPEL SKPDLTRRFE 

       550        560        570        580        590        600 
SMIEDIRSGR RTRQEVIDMS KKTISKLLES FLDRLDTAVR EIGVSLGSVE VEAACHLCGR 

       610        620        630        640        650        660 
KAVSAVSGYR LCSHHMEAFD RLRKALPNLA STISSTPREA LEAIARGRSR AGAWVRDVAA 

       670 
LALRDDGLYK ALL 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BA000002 Genomic DNA. Translation: BAA80797.1.
PIRH72563.
RefSeqNP_148170.1. NC_000854.2.

3D structure databases

ProteinModelPortalQ9YB01.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING272557.APE_1794.

Proteomic databases

PRIDEQ9YB01.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAA80797; BAA80797; APE_1794.
GeneID1446244.
KEGGape:APE_1794.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0550.
HOGENOMHOG000004019.
KOK03168.
OMASNRDFIP.

Enzyme and pathway databases

BioCycAPER272557:GJD6-1209-MONOMER.

Family and domain databases

Gene3D1.10.290.10. 1 hit.
1.10.460.10. 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.
IPR013826. Topo_IA_cen_sub3.
IPR023405. Topo_IA_core_domain.
IPR003602. Topo_IA_DNA-bd.
IPR005739. TopoI_arch.
IPR028612. Topoisom_1_IA.
IPR006171. Toprim_domain.
[Graphical view]
PANTHERPTHR11390. PTHR11390. 1 hit.
PfamPF01131. Topoisom_bac. 1 hit.
PF01751. Toprim. 1 hit.
[Graphical view]
PRINTSPR00417. PRTPISMRASEI.
SMARTSM00437. TOP1Ac. 1 hit.
SM00436. TOP1Bc. 1 hit.
SM00493. TOPRIM. 1 hit.
[Graphical view]
SUPFAMSSF56712. SSF56712. 1 hit.
TIGRFAMsTIGR01057. topA_arch. 1 hit.
PROSITEPS00396. TOPOISOMERASE_I_PROK. 1 hit.
PS50880. TOPRIM. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameTOP1_AERPE
AccessionPrimary (citable) accession number: Q9YB01
Entry history
Integrated into UniProtKB/Swiss-Prot: June 20, 2001
Last sequence update: November 1, 1999
Last modified: July 9, 2014
This is version 101 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