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Protein

DNA topoisomerase 1

Gene

TOP1

Organism
Candida albicans (Yeast)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

Functioni

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 rotates around the intact phosphodiester bond on the opposing 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).By similarity

Catalytic activityi

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

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei736O-(3'-phospho-DNA)-tyrosine intermediate1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Isomerase, Topoisomerase

Keywords - Ligandi

DNA-binding

Names & Taxonomyi

Protein namesi
Recommended name:
DNA topoisomerase 1 (EC:5.99.1.2)
Alternative name(s):
DNA topoisomerase I
Gene namesi
Name:TOP1
OrganismiCandida albicans (Yeast)
Taxonomic identifieri5476 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesDebaryomycetaceaeCandida/Lodderomyces cladeCandida

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001452081 – 778DNA topoisomerase 1Add BLAST778

Interactioni

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei306Interaction with DNABy similarity1
Sitei354Interaction with DNABy similarity1
Sitei385Interaction with DNABy similarity1
Sitei442Interaction with DNABy similarity1
Sitei468Interaction with DNABy similarity1
Sitei511Interaction with DNABy similarity1
Sitei568Interaction with DNABy similarity1
Sitei586Interaction with DNABy similarity1

Structurei

3D structure databases

ProteinModelPortaliQ00313.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni367 – 368Interaction with DNABy similarity2
Regioni430 – 435Interaction with DNABy similarity6
Regioni522 – 524Interaction with DNABy similarity3

Sequence similaritiesi

Belongs to the type IB topoisomerase family.Curated

Family and domain databases

CDDicd00659. Topo_IB_C. 1 hit.
Gene3Di1.10.10.41. 1 hit.
1.10.132.10. 2 hits.
2.170.11.10. 2 hits.
3.90.15.10. 1 hit.
InterProiIPR011010. 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]
PfamiPF14370. Topo_C_assoc. 1 hit.
PF01028. Topoisom_I. 1 hit.
PF02919. Topoisom_I_N. 1 hit.
[Graphical view]
PRINTSiPR00416. EUTPISMRASEI.
SMARTiSM00435. TOPEUc. 1 hit.
[Graphical view]
SUPFAMiSSF56349. SSF56349. 2 hits.
SSF56741. SSF56741. 1 hit.
PROSITEiPS00176. TOPOISOMERASE_I_EUK. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q00313-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNSSDEEDIA LSRLAKKSSS ITSASTYEDD EDDDIPLAKK SRKKRVESDY
60 70 80 90 100
EEDEDEVPLK KLSNGRAKKQ VKTETKVKKE PKSANKSKST SKKDTKVKKE
110 120 130 140 150
KTTVKKESKA TSTKVKEESK TQSDSQASVK SETPEEDQGY KWWEVNQEEE
160 170 180 190 200
GDGYIKWQTL EHNGVMFPPP YEPLPSHVKL YYNNKPVNLP PEAEEVAGFY
210 220 230 240 250
GAMLETDHAK NPVFQKNFFN DFLEVLKECG GCGVEIKKFE KLDFSKMYAH
260 270 280 290 300
FEKLREEKKA MSREEKKRIK EEKEKEEEPY RTCYLNGRKE LVGNFRIEPP
310 320 330 340 350
GLFRGRGAHP KTGKLKRRVV SEQVTLNLGK DAKIPEPPAG HQWGEIRHDN
360 370 380 390 400
EVTWLAMWKE NISDSLKYVR FANNSSVKGQ SDFKKFETAR KLRDHVDSIR
410 420 430 440 450
KDYTKMLKSE KMQDRQMATA MYLIDVFALR AGGEKGEDEA DTVGCCSLRY
460 470 480 490 500
EHVTLKPPNK VIFDLLGKDS IRFYQEVEVD KQVFKNLRIF KKSPKQPGDD
510 520 530 540 550
LFDRINPSLV NRQLQNYMKG LTAKVFRTYN ASKTMQDQID IIENEGTVAE
560 570 580 590 600
KVAKFNAANR TVAILCNHQR TVSKTHGDSV QRINDKLKKF MWQKIRLKKM
610 620 630 640 650
ILQLEPKLKK KDSKYFEEID DLIKEDIEHI HHTIIKRQRE QAKKKLERDN
660 670 680 690 700
EKLKLEGKPL LTESDIKDKL DKIDELEKEY QKELKTGKPI VTKNATVEKL
710 720 730 740 750
KQQIETLENR ILNVSIQLKD KEDNSEVSLG TSKMNYIDPR LIVMFSKKFD
760 770
VPIEKLFTKT LREKFIWAIE SADENWRF
Length:778
Mass (Da):90,484
Last modified:November 1, 1997 - v1
Checksum:iBFABE6B22EA2E5D3
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti2N → S in AAB39507 (PubMed:9043115).Curated1
Sequence conflicti61K → KRK (PubMed:9043115).Curated1
Sequence conflicti465L → F in AAB39507 (PubMed:9043115).Curated1
Sequence conflicti623I → L in AAB39507 (PubMed:9043115).Curated1
Sequence conflicti710R → K in AAB39507 (PubMed:9043115).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U40454 Genomic DNA. Translation: AAC49381.1.
U41342 Genomic DNA. Translation: AAB39507.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U40454 Genomic DNA. Translation: AAC49381.1.
U41342 Genomic DNA. Translation: AAB39507.1.

3D structure databases

ProteinModelPortaliQ00313.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Family and domain databases

CDDicd00659. Topo_IB_C. 1 hit.
Gene3Di1.10.10.41. 1 hit.
1.10.132.10. 2 hits.
2.170.11.10. 2 hits.
3.90.15.10. 1 hit.
InterProiIPR011010. 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]
PfamiPF14370. Topo_C_assoc. 1 hit.
PF01028. Topoisom_I. 1 hit.
PF02919. Topoisom_I_N. 1 hit.
[Graphical view]
PRINTSiPR00416. EUTPISMRASEI.
SMARTiSM00435. TOPEUc. 1 hit.
[Graphical view]
SUPFAMiSSF56349. SSF56349. 2 hits.
SSF56741. SSF56741. 1 hit.
PROSITEiPS00176. TOPOISOMERASE_I_EUK. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiTOP1_CANAX
AccessioniPrimary (citable) accession number: Q00313
Secondary accession number(s): P78593
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1997
Last modified: November 30, 2016
This is version 82 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

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

Documents

  1. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.