A0A8H8MVE3 · A0A8H8MVE3_9AGAM
- ProteinFanconi-associated nuclease
- GeneCLP1
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids1616 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
Function
function
Nuclease required for the repair of DNA interstrand cross-links (ICL). Acts as a 5'-3' exonuclease that anchors at a cut end of DNA and cleaves DNA successively at every third nucleotide, allowing to excise an ICL from one strand through flanking incisions.
Required for endonucleolytic cleavage during polyadenylation-dependent pre-mRNA 3'-end formation.
Catalytic activity
Cofactor
Mn2+ (UniProtKB | Rhea| CHEBI:29035 )
Features
Showing features for binding site.
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | mRNA cleavage factor complex | |
Molecular Function | 5'-3' exonuclease activity | |
Molecular Function | 5'-flap endonuclease activity | |
Molecular Function | ATP binding | |
Molecular Function | flap-structured DNA binding | |
Molecular Function | metal ion binding | |
Biological Process | interstrand cross-link repair | |
Biological Process | mRNA 3'-end processing |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameFanconi-associated nuclease
- EC number
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageEukaryota > Fungi > Dikarya > Basidiomycota > Agaricomycotina > Agaricomycetes > Cantharellales > Ceratobasidiaceae > Ceratobasidium
Accessions
- Primary accessionA0A8H8MVE3
Proteomes
Subcellular Location
Interaction
Subunit
Component of a pre-mRNA cleavage factor complex. Interacts directly with PCF11.
Structure
Family & Domains
Features
Showing features for region, domain, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 633-660 | Disordered | ||||
Sequence: DDEASDEKPSVADLPQPAPLSTSDSDSS | ||||||
Domain | 1144-1259 | VRR-NUC | ||||
Sequence: EDEGAARRLIEAVDERERPNETWCIGVRWDQFEREALVEIVECLGGRALATICQLLAEYAYRGGGVPDLFIWNYAEKTCKFVEVKGPGDQLSETQKVWIDVLLGAGVDVELCRVYE | ||||||
Region | 1263-1423 | Disordered | ||||
Sequence: TPSAPTKKKKTQGRQVGRGRTSNLQRNSTNPDNGPKPDPESEEEGGSWSSSEDGHGVPQSDGQGADTWEHPNCESRDDHPGTSPPPADTSILGKRDGQMIKLDVHQEVGRTSKRTKANKPIPASTLAQRRSSHRSPKSKIPKDRVRLHTPTPNTTRQRHVP | ||||||
Compositional bias | 1267-1297 | Polar residues | ||||
Sequence: PTKKKKTQGRQVGRGRTSNLQRNSTNPDNGP | ||||||
Compositional bias | 1360-1376 | Basic and acidic residues | ||||
Sequence: QMIKLDVHQEVGRTSKR | ||||||
Compositional bias | 1379-1393 | Polar residues | ||||
Sequence: ANKPIPASTLAQRRS | ||||||
Region | 1475-1616 | Disordered | ||||
Sequence: SQAQSYVRPPPERWLSDPVTPTKRRRETSPASSACVDLEPRSKRKRANSLTDIATCRAPTPSTSSKAAPTDPSPCQADPVEPIITQNRTPRKPAGTLNPKGGVAGSPRDWEKNWPDVFPKWVGDLADQGSDEDYEPSQSQSQ | ||||||
Compositional bias | 1527-1545 | Polar residues | ||||
Sequence: IATCRAPTPSTSSKAAPTD |
Sequence similarities
Belongs to the Clp1 family. Clp1 subfamily.
Belongs to the FAN1 family.
Family and domain databases
Sequence
- Sequence statusComplete
- Length1,616
- Mass (Da)178,960
- Last updated2022-01-19 v1
- ChecksumD58E9A63CC997500
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 1267-1297 | Polar residues | ||||
Sequence: PTKKKKTQGRQVGRGRTSNLQRNSTNPDNGP | ||||||
Compositional bias | 1360-1376 | Basic and acidic residues | ||||
Sequence: QMIKLDVHQEVGRTSKR | ||||||
Compositional bias | 1379-1393 | Polar residues | ||||
Sequence: ANKPIPASTLAQRRS | ||||||
Compositional bias | 1527-1545 | Polar residues | ||||
Sequence: IATCRAPTPSTSSKAAPTD |