A0AAD5VFI6 · A0AAD5VFI6_9AGAR
- ProteinATP-dependent DNA helicase CHL1
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids1028 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
Function
Catalytic activity
- ATP + H2O = ADP + H+ + phosphate
- Couples ATP hydrolysis with the unwinding of duplex DNA at the replication fork by translocating in the 5'-3' direction. This creates two antiparallel DNA single strands (ssDNA). The leading ssDNA polymer is the template for DNA polymerase III holoenzyme which synthesizes a continuous strand.
Cofactor
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | nucleus | |
Molecular Function | ATP binding | |
Molecular Function | DNA binding | |
Molecular Function | DNA helicase activity | |
Molecular Function | hydrolase activity, acting on acid anhydrides, in phosphorus-containing anhydrides | |
Biological Process | establishment of sister chromatid cohesion | |
Biological Process | nucleobase-containing compound metabolic process | |
Biological Process | phosphorelay signal transduction system |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameATP-dependent DNA helicase CHL1
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageEukaryota > Fungi > Dikarya > Basidiomycota > Agaricomycotina > Agaricomycetes > Agaricomycetidae > Agaricales > Agaricineae > Agaricaceae > Leucocoprinus
Accessions
- Primary accessionA0AAD5VFI6
Proteomes
Subcellular Location
PTM/Processing
Features
Showing features for modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Modified residue | 33 | Phosphohistidine | ||||
Sequence: H |
Keywords
- PTM
Structure
Family & Domains
Features
Showing features for domain, region, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 1-94 | HPt | ||||
Sequence: MVEGFYDQAEETFQSMDGYLESKNLSELSEKGHFLKGSSAAIGITKVQRSCEEIQNYGKLQGNDEKPISTAEALERLQKVLARVKGEYEEAKDW | ||||||
Domain | 187-588 | Helicase ATP-binding | ||||
Sequence: DGFPAFPYDLPYPIQTDLMRHLYENIENRAITIVESPTGTNSSLIFDQGKEWVIEQTRERIRRQLEADELAYQERLVSAGRREEAMRRAARARVLKKPKWGGKGLQEQARRKEEHQDEDDDIFLPDDDRGTQEDEVFISPALQALINRVDKPSRPGSDDAEEVTCTKVYYASRTHSQLAQVLPELRRLKLFRLSSITSDQLPHQQRSSVPHKRGLGNLEEGEETEIMTRTVPLGSRRQLCINEKLRSKAQDLDEACRELLSEKGDKRCPYLPPLDEDIKMIDFRDQILAVPKDIEDLAEAGRLAETCPYFGSRRAIPQAELVTLPYNLLLQKSAREALGIDLKDQIVVIDEAHNLIPTLLSLSTIRLPFNTLDTSLQQVCTYVSKFRTRLSATNMVHLKRLV | ||||||
Region | 284-316 | Disordered | ||||
Sequence: PKWGGKGLQEQARRKEEHQDEDDDIFLPDDDRG | ||||||
Compositional bias | 289-304 | Basic and acidic residues | ||||
Sequence: KGLQEQARRKEEHQDE | ||||||
Region | 387-407 | Disordered | ||||
Sequence: LPHQQRSSVPHKRGLGNLEEG |
Sequence similarities
Family and domain databases
Sequence
- Sequence statusComplete
- Length1,028
- Mass (Da)115,672
- Last updated2024-05-29 v1
- Checksum8F8E040B0BF70A9E
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 289-304 | Basic and acidic residues | ||||
Sequence: KGLQEQARRKEEHQDE |
Keywords
- Technical term