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P30181 (TOP1_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 107. 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·Alt products·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
Gene names
Name:TOP1
Ordered Locus Names:At5g55300
ORF Names:MTE17.1
OrganismArabidopsis thaliana (Mouse-ear cress) [Reference proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis

Protein attributes

Sequence length916 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 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-(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 By similarity.

Catalytic activity

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

Subcellular location

Nucleus Ref.5.

Miscellaneous

Eukaryotic topoisomerase I and II can relax both negative and positive supercoils, whereas prokaryotic enzymes relax only negative supercoils.

Sequence similarities

Belongs to the type IB topoisomerase family.

Ontologies

Keywords
   Cellular componentNucleus
   Coding sequence diversityAlternative splicing
   LigandDNA-binding
   Molecular functionIsomerase
Topoisomerase
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processDNA topological change

Inferred from electronic annotation. Source: InterPro

   Cellular_componentchromosome

Inferred from electronic annotation. Source: InterPro

nucleus

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

DNA binding

Inferred from electronic annotation. Source: UniProtKB-KW

DNA topoisomerase type I activity

Inferred from electronic annotation. Source: UniProtKB-EC

DNA topoisomerase type II (ATP-hydrolyzing) activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Alternative products

This entry describes 1 isoform produced by alternative splicing. [Select]

Note: A number of isoforms are produced. According to EST sequences.
Isoform 1 (identifier: P30181-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 916916DNA topoisomerase 1
PRO_0000145206

Regions

Region577 – 5782Interaction with DNA By similarity
Region640 – 6456Interaction with DNA By similarity
Region731 – 7333Interaction with DNA By similarity

Sites

Active site8721O-(3'-phospho-DNA)-tyrosine intermediate By similarity
Site5141Interaction with DNA By similarity
Site5631Interaction with DNA By similarity
Site5951Interaction with DNA By similarity
Site6521Interaction with DNA By similarity
Site6781Interaction with DNA By similarity
Site7201Interaction with DNA By similarity
Site7771Interaction with DNA By similarity

Amino acid modifications

Modified residue1701Phosphoserine Ref.4 Ref.5
Modified residue2861Phosphothreonine Ref.6

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified April 1, 1993. Version 1.
Checksum: 84BF47913F14454F

FASTA916102,799
        10         20         30         40         50         60 
MGTETVSKPV MDNGSGDSDD DKPLAFKRNN TVASNSNQSK SNSQRSKAVP TTKVSPMRSP 

        70         80         90        100        110        120 
VTSPNGTTPS NKTSIVKSSM PSSSSKASPA KSPLRNDMPS TVKDRSQLQK DQSECKIEHE 

       130        140        150        160        170        180 
DSEDDRPLSS ILSGNKGPTS SRQVSSPQPE KKNNGDRPLD RASRIIKDES DDETPISSMF 

       190        200        210        220        230        240 
RKKIDSGMSG GNQLSNDEKK PLVQKLHQNG STVKNEVPNG KVLGKRPLEK NSSADQSSLK 

       250        260        270        280        290        300 
KAKISASPTS VKMKQDSVKK EIDDKGRVLV SPKMKAKQLS TREDGTDDDD DDDVPISKRF 

       310        320        330        340        350        360 
KSDSSNSNTS SAKPKAVKLN STSSAAKPKA RNVVSPRSRA MTKNTKKVTK DSKYSTSSKS 

       370        380        390        400        410        420 
SPSSGDGQKK WTTLVHNGVI FPPPYKPHGI KILYKGKPVD LTIEQEEVAT MFAVMRETDY 

       430        440        450        460        470        480 
YTKPQFRENF WNDWRRLLGK KHVIQKLDDC DFTPIYEWHL EEKEKKKQMS TEEKKALKEE 

       490        500        510        520        530        540 
KMKQEEKYMW AVVDGVKEKI GNFRVEPPGL FRGRGEHPKM GKLKKRIHPC EITLNIGKGA 

       550        560        570        580        590        600 
PIPECPIAGE RWKEVKHDNT VTWLAFWADP INPKEFKYVF LGAGSSLKGL SDKEKYEKAR 

       610        620        630        640        650        660 
NLTDHIDNIR TTYTKNFTAK DVKMRQIAVA TYLIDKLALR AGNEKDDDEA DTVGCCTLKV 

       670        680        690        700        710        720 
GNVECIPPNK IKFDFLGKDS IQYVNTVEVE PLVYKAIGQF QAGKSKTDDL FDELDTSKLN 

       730        740        750        760        770        780 
AHLKELVPGL TAKVFRTYNA SITLDEMLSQ ETKDGDVTQK IVVYQKANKE VAIICNHQRT 

       790        800        810        820        830        840 
VSKTHGAQIE KLTARIEELK EVLKELKTNL DRAKKGKPPL EGSDGKKIRS LEPNAWEKKI 

       850        860        870        880        890        900 
AQQSAKIEKM ERDMHTKEDL KTVALGTSKI NYLDPRITVA WCKRHEVPIE KIFTKSLLEK 

       910 
FAWAMDVEPE YRFSRR 

« Hide

References

« Hide 'large scale' references
[1]Kieber J.K., Signer E.R.
Submitted (SEP-1990) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: cv. Columbia.
[2]"Structural analysis of Arabidopsis thaliana chromosome 5. VII. Sequence features of the regions of 1,013,767 bp covered by sixteen physically assigned P1 and TAC clones."
Nakamura Y., Sato S., Asamizu E., Kaneko T., Kotani H., Miyajima N., Tabata S.
DNA Res. 5:297-308(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: cv. Columbia.
[3]The Arabidopsis Information Resource (TAIR)
Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: cv. Columbia.
[4]"Site-specific phosphorylation profiling of Arabidopsis proteins by mass spectrometry and peptide chip analysis."
de la Fuente van Bentem S., Anrather D., Dohnal I., Roitinger E., Csaszar E., Joore J., Buijnink J., Carreri A., Forzani C., Lorkovic Z.J., Barta A., Lecourieux D., Verhounig A., Jonak C., Hirt H.
J. Proteome Res. 7:2458-2470(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-170, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Root.
[5]"Phosphoproteomic analysis of nuclei-enriched fractions from Arabidopsis thaliana."
Jones A.M.E., MacLean D., Studholme D.J., Serna-Sanz A., Andreasson E., Rathjen J.P., Peck S.C.
J. Proteomics 72:439-451(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-170, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Strain: cv. Columbia.
[6]"Large-scale Arabidopsis phosphoproteome profiling reveals novel chloroplast kinase substrates and phosphorylation networks."
Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A., Grossmann J., Gruissem W., Baginsky S.
Plant Physiol. 150:889-903(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-286, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X57544 mRNA. Translation: CAA40763.1.
AB015479 Genomic DNA. Translation: BAB08547.1.
CP002688 Genomic DNA. Translation: AED96612.1.
PIRS22864.
RefSeqNP_200341.1. NM_124912.4. [P30181-1]
UniGeneAt.197.

3D structure databases

ProteinModelPortalP30181.
SMRP30181. Positions 367-913.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid20867. 1 interaction.
IntActP30181. 1 interaction.

Proteomic databases

PaxDbP30181.
PRIDEP30181.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT5G55300.1; AT5G55300.1; AT5G55300. [P30181-1]
GeneID835623.
KEGGath:AT5G55300.

Organism-specific databases

TAIRAT5G55300.

Phylogenomic databases

eggNOGCOG3569.
HOGENOMHOG000105469.
InParanoidP30181.
KOK03163.
PhylomeDBP30181.

Enzyme and pathway databases

BioCycARA:AT5G55300-MONOMER.
ARA:GQT-376-MONOMER.

Gene expression databases

GenevestigatorP30181.

Family and domain databases

Gene3D1.10.10.41. 1 hit.
1.10.132.10. 1 hit.
2.170.11.10. 2 hits.
3.90.15.10. 1 hit.
InterProIPR011010. DNA_brk_join_enz.
IPR013034. DNA_topo_domain1.
IPR001631. TopoI.
IPR018521. TopoI_AS.
IPR025834. TopoI_C_dom.
IPR014711. TopoI_cat_a-hlx-sub_euk.
IPR014727. TopoI_cat_a/b-sub_euk.
IPR013500. TopoI_cat_euk.
IPR008336. TopoI_DNA-bd_euk.
IPR013030. TopoI_DNA-bd_mixed-a/b_euk.
IPR013499. TopoI_euk.
[Graphical view]
PfamPF14370. Topo_C_assoc. 1 hit.
PF01028. Topoisom_I. 1 hit.
PF02919. Topoisom_I_N. 1 hit.
[Graphical view]
PRINTSPR00416. EUTPISMRASEI.
SMARTSM00435. TOPEUc. 1 hit.
[Graphical view]
SUPFAMSSF56349. SSF56349. 2 hits.
SSF56741. SSF56741. 1 hit.
PROSITEPS00176. TOPOISOMERASE_I_EUK. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameTOP1_ARATH
AccessionPrimary (citable) accession number: P30181
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: April 1, 1993
Last modified: July 9, 2014
This is version 107 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names