P30189 · TOP1_DROME
- ProteinDNA topoisomerase 1
- GeneTop1
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids972 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
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 (By similarity).
Introduces a single-strand break via transesterification at a target site in duplex DNA (By similarity).
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 (By similarity).
The free DNA strand then undergoes passage around the unbroken strand thus removing DNA supercoils (By similarity).
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).
Introduces a single-strand break via transesterification at a target site in duplex DNA (By similarity).
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 (By similarity).
The free DNA strand then undergoes passage around the unbroken strand thus removing DNA supercoils (By similarity).
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).
Miscellaneous
Eukaryotic topoisomerase I and II can relax both negative and positive supercoils, whereas prokaryotic enzymes relax only negative supercoils.
Catalytic activity
Features
Showing features for site, active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Site | 539 | Interaction with DNA | ||||
Sequence: R | ||||||
Site | 587 | Interaction with DNA | ||||
Sequence: R | ||||||
Site | 635 | Interaction with DNA | ||||
Sequence: W | ||||||
Site | 666 | Interaction with DNA | ||||
Sequence: K | ||||||
Site | 723 | Interaction with DNA | ||||
Sequence: T | ||||||
Site | 754 | Interaction with DNA | ||||
Sequence: K | ||||||
Site | 796 | Interaction with DNA | ||||
Sequence: N | ||||||
Site | 854 | Interaction with DNA | ||||
Sequence: H | ||||||
Site | 872 | Interaction with DNA | ||||
Sequence: K | ||||||
Active site | 930 | O-(3'-phospho-DNA)-tyrosine intermediate | ||||
Sequence: Y |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Cellular Component | cytosol | |
Cellular Component | euchromatin | |
Cellular Component | nucleolus | |
Cellular Component | nucleus | |
Cellular Component | polytene chromosome | |
Cellular Component | polytene chromosome puff | |
Molecular Function | DNA binding | |
Molecular Function | DNA topoisomerase activity | |
Molecular Function | DNA topoisomerase type I (single strand cut, ATP-independent) activity | |
Biological Process | chromosome condensation | |
Biological Process | chromosome segregation | |
Biological Process | DNA replication | |
Biological Process | DNA topological change | |
Biological Process | instar larval development | |
Biological Process | oogenesis | |
Biological Process | regulation of embryonic development |
Keywords
- Molecular function
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameDNA topoisomerase 1
- EC number
- Alternative names
Gene names
Organism names
- Strains
- Taxonomic lineageEukaryota > Metazoa > Ecdysozoa > Arthropoda > Hexapoda > Insecta > Pterygota > Neoptera > Endopterygota > Diptera > Brachycera > Muscomorpha > Ephydroidea > Drosophilidae > Drosophila > Sophophora
Accessions
- Primary accessionP30189
- Secondary accessions
Proteomes
Organism-specific databases
PTM/Processing
Features
Showing features for chain, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000145205 | 1-972 | DNA topoisomerase 1 | |||
Sequence: MSGDVAAENSIHIQNGGSCEVVQSNGVTTNGHGHHHHHHSSSSSSSKHKSSSKDKHRDREREHKSSNSSSSSKEHKSSSRDKDRHKSSSSSSKHRDKDKERDGSSNSHRSGSSSSHKDKDGSSSSKHKSSSGHHKRSSKDKERRDKDKDRGSSSSSRHKSSSSSRDKERSSSSHKSSSSSSSSKSKHSSSRHSSSSSSKDHPSYDGVFVKPEPVSQQLMHSGSVDAFQMQQLGSYEAAAAGTNFNGNGNVAGANYKNGYEESIVDIKKEEESFNNLSQASSCDYSMSQFRADEPPFVVKHEQSYAEEDSTMNYNDHDDDADEMNDDEEDVPLAMRKRKQEATDRPDGGMDNDDDDDIPLLARKKVKKEKIKKESKEKSKKRVKEEPSDDYGNVKPKKKKMKKEPEPAVSPGKRQKAKAKVEEEEVWRWWEEEKRADGVKWSTLEHKGPVFAPRYERVPRNVRFYYDGKPLELSEETEEAATFYAKMLNHDYCTKEVFNNNFFKDFRKSMTPREREIIKDFRKCNFQEMFNYFQAESEKRKAASKEEKLIKKNENEALMKEFGFCMIDGHKEKIGNFRLEPPGLFRGRGEHPKMGMIKRRIQASDVSINCGKDSKVPSPPPGSRWKEVRHDNTVTWLASWIENVQGQVKYIMLNPSSKLKGEKDHIKYETARRLDKVIDKIRATYRDEWKSKEMRVRQRAVALYFIDKLALRAGNEKDEDQADTVGCCSLRVEHVQLHKELNGKENVVVFDFPGKDSIRYYNEVEVEKRVFKNLELFMEHKKEGDDLFDRLNTQVLNEHLKELMEGLTAKVFRTYNASKTLQSQLDLLTDPSATVPEKLLAYNRANRAVAILCNHQRSVPKSHEKSMENLKEKIKAKREAIEKCESEYHSRDEKKGKQLERLRDQLKKLELQETDRDENKTIALGTSKLNYLDPRISVAWCKKHDVPIEKIFNKTQRTKFLWAVHMADENYRF | ||||||
Modified residue | 303 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 304 | Phosphotyrosine | ||||
Sequence: Y |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Developmental stage
Detected in germline and follicle cells. Expressed in follicle cells throughout oogenesis. In germline cells, expression levels increase as cells develop and move to the posterior region of the germarium, then at stage 5 of egg chamber development levels decrease until it is no longer detected (at protein level).
Gene expression databases
Structure
Family & Domains
Features
Showing features for region, compositional bias, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-210 | Disordered | ||||
Sequence: MSGDVAAENSIHIQNGGSCEVVQSNGVTTNGHGHHHHHHSSSSSSSKHKSSSKDKHRDREREHKSSNSSSSSKEHKSSSRDKDRHKSSSSSSKHRDKDKERDGSSNSHRSGSSSSHKDKDGSSSSKHKSSSGHHKRSSKDKERRDKDKDRGSSSSSRHKSSSSSRDKERSSSSHKSSSSSSSSKSKHSSSRHSSSSSSKDHPSYDGVFVK | ||||||
Compositional bias | 7-30 | Polar residues | ||||
Sequence: AENSIHIQNGGSCEVVQSNGVTTN | ||||||
Compositional bias | 31-47 | Basic residues | ||||
Sequence: GHGHHHHHHSSSSSSSK | ||||||
Compositional bias | 48-127 | Basic and acidic residues | ||||
Sequence: HKSSSKDKHRDREREHKSSNSSSSSKEHKSSSRDKDRHKSSSSSSKHRDKDKERDGSSNSHRSGSSSSHKDKDGSSSSKH | ||||||
Compositional bias | 135-173 | Basic and acidic residues | ||||
Sequence: KRSSKDKERRDKDKDRGSSSSSRHKSSSSSRDKERSSSS | ||||||
Compositional bias | 174-202 | Polar residues | ||||
Sequence: HKSSSSSSSSKSKHSSSRHSSSSSSKDHP | ||||||
Region | 300-416 | Disordered | ||||
Sequence: HEQSYAEEDSTMNYNDHDDDADEMNDDEEDVPLAMRKRKQEATDRPDGGMDNDDDDDIPLLARKKVKKEKIKKESKEKSKKRVKEEPSDDYGNVKPKKKKMKKEPEPAVSPGKRQKA | ||||||
Compositional bias | 312-328 | Acidic residues | ||||
Sequence: NYNDHDDDADEMNDDEE | ||||||
Compositional bias | 329-346 | Basic and acidic residues | ||||
Sequence: DVPLAMRKRKQEATDRPD | ||||||
Compositional bias | 371-416 | Basic and acidic residues | ||||
Sequence: KKESKEKSKKRVKEEPSDDYGNVKPKKKKMKKEPEPAVSPGKRQKA | ||||||
Region | 648-649 | Interaction with DNA | ||||
Sequence: KY | ||||||
Domain | 655-972 | Topo IB-type catalytic | ||||
Sequence: SSKLKGEKDHIKYETARRLDKVIDKIRATYRDEWKSKEMRVRQRAVALYFIDKLALRAGNEKDEDQADTVGCCSLRVEHVQLHKELNGKENVVVFDFPGKDSIRYYNEVEVEKRVFKNLELFMEHKKEGDDLFDRLNTQVLNEHLKELMEGLTAKVFRTYNASKTLQSQLDLLTDPSATVPEKLLAYNRANRAVAILCNHQRSVPKSHEKSMENLKEKIKAKREAIEKCESEYHSRDEKKGKQLERLRDQLKKLELQETDRDENKTIALGTSKLNYLDPRISVAWCKKHDVPIEKIFNKTQRTKFLWAVHMADENYRF | ||||||
Region | 711-716 | Interaction with DNA | ||||
Sequence: RAGNEK | ||||||
Region | 807-809 | Interaction with DNA | ||||
Sequence: TAK |
Sequence similarities
Belongs to the type IB topoisomerase family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length972
- Mass (Da)111,688
- Last updated1993-04-01 v1
- Checksum3764B8BDEEFA30CD
Computationally mapped potential isoform sequences
There are 4 potential isoforms mapped to this entry
Features
Showing features for compositional bias, sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 7-30 | Polar residues | ||||
Sequence: AENSIHIQNGGSCEVVQSNGVTTN | ||||||
Compositional bias | 31-47 | Basic residues | ||||
Sequence: GHGHHHHHHSSSSSSSK | ||||||
Sequence conflict | 40 | in Ref. 3; AAF48440 | ||||
Sequence: S → H | ||||||
Sequence conflict | 46 | in Ref. 3; AAF48440 | ||||
Sequence: S → SSS | ||||||
Compositional bias | 48-127 | Basic and acidic residues | ||||
Sequence: HKSSSKDKHRDREREHKSSNSSSSSKEHKSSSRDKDRHKSSSSSSKHRDKDKERDGSSNSHRSGSSSSHKDKDGSSSSKH | ||||||
Compositional bias | 135-173 | Basic and acidic residues | ||||
Sequence: KRSSKDKERRDKDKDRGSSSSSRHKSSSSSRDKERSSSS | ||||||
Compositional bias | 174-202 | Polar residues | ||||
Sequence: HKSSSSSSSSKSKHSSSRHSSSSSSKDHP | ||||||
Sequence conflict | 201 | in Ref. 3; AAF48440 | ||||
Sequence: H → Q | ||||||
Compositional bias | 312-328 | Acidic residues | ||||
Sequence: NYNDHDDDADEMNDDEE | ||||||
Compositional bias | 329-346 | Basic and acidic residues | ||||
Sequence: DVPLAMRKRKQEATDRPD | ||||||
Compositional bias | 371-416 | Basic and acidic residues | ||||
Sequence: KKESKEKSKKRVKEEPSDDYGNVKPKKKKMKKEPEPAVSPGKRQKA |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
M74557 EMBL· GenBank· DDBJ | AAA28951.1 EMBL· GenBank· DDBJ | mRNA | ||
U80064 EMBL· GenBank· DDBJ | AAC24158.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AE014298 EMBL· GenBank· DDBJ | AAF48440.1 EMBL· GenBank· DDBJ | Genomic DNA |