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Q00313

- TOP1_CANAX

UniProt

Q00313 - TOP1_CANAX

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Protein

DNA topoisomerase 1

Gene

TOP1

Organism
Candida albicans (Yeast)
Status
Reviewed - 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 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).By similarity

Catalytic activityi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei306 – 3061Interaction with DNABy similarity
Sitei354 – 3541Interaction with DNABy similarity
Sitei385 – 3851Interaction with DNABy similarity
Sitei442 – 4421Interaction with DNABy similarity
Sitei468 – 4681Interaction with DNABy similarity
Sitei511 – 5111Interaction with DNABy similarity
Sitei568 – 5681Interaction with DNABy similarity
Sitei586 – 5861Interaction with DNABy similarity
Active sitei736 – 7361O-(3'-phospho-DNA)-tyrosine intermediate

GO - Molecular functioni

  1. DNA binding Source: UniProtKB-KW
  2. DNA topoisomerase type I activity Source: UniProtKB-EC
  3. DNA topoisomerase type II (ATP-hydrolyzing) activity Source: InterPro

GO - Biological processi

  1. DNA topological change Source: InterPro
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

  1. chromosome Source: InterPro
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 778778DNA topoisomerase 1PRO_0000145208Add
BLAST

Structurei

3D structure databases

ProteinModelPortaliQ00313.
SMRiQ00313. Positions 155-372.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni367 – 3682Interaction with DNABy similarity
Regioni430 – 4356Interaction with DNABy similarity
Regioni522 – 5243Interaction with DNABy similarity

Sequence similaritiesi

Belongs to the type IB topoisomerase family.Curated

Phylogenomic databases

eggNOGiCOG3569.

Family and domain databases

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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti2 – 21N → S in AAB39507. (PubMed:9043115)Curated
Sequence conflicti61 – 611K → KRK(PubMed:9043115)Curated
Sequence conflicti465 – 4651L → F in AAB39507. (PubMed:9043115)Curated
Sequence conflicti623 – 6231I → L in AAB39507. (PubMed:9043115)Curated
Sequence conflicti710 – 7101R → K in AAB39507. (PubMed:9043115)Curated

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U40454 Genomic DNA. Translation: AAC49381.1.
U41342 Genomic DNA. Translation: AAB39507.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U40454 Genomic DNA. Translation: AAC49381.1 .
U41342 Genomic DNA. Translation: AAB39507.1 .

3D structure databases

ProteinModelPortali Q00313.
SMRi Q00313. Positions 155-372.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Phylogenomic databases

eggNOGi COG3569.

Family and domain databases

Gene3Di 1.10.10.41. 1 hit.
1.10.132.10. 2 hits.
2.170.11.10. 2 hits.
3.90.15.10. 1 hit.
InterProi IPR011010. 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 ]
Pfami PF14370. Topo_C_assoc. 1 hit.
PF01028. Topoisom_I. 1 hit.
PF02919. Topoisom_I_N. 1 hit.
[Graphical view ]
PRINTSi PR00416. EUTPISMRASEI.
SMARTi SM00435. TOPEUc. 1 hit.
[Graphical view ]
SUPFAMi SSF56349. SSF56349. 2 hits.
SSF56741. SSF56741. 1 hit.
PROSITEi PS00176. TOPOISOMERASE_I_EUK. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "Identification of the gene encoding DNA topoisomerase I from Candida albicans."
    Taylor A., Giles K., Sarthy A.V., McGonigal T., Fostel J.
    FEMS Microbiol. Lett. 138:113-121(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 10321 / CCM 8215.
  2. "The topoisomerase I gene from Candida albicans."
    Jiang W., Gerhold D., Kmiec E.B., Hauser M., Becker J.M., Koltin Y.
    Microbiology 143:377-386(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

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: October 29, 2014
This is version 75 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

External Data

Dasty 3