A0A803M7S8 · A0A803M7S8_CHEQI
- ProteinPoly [ADP-ribose] polymerase
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids953 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
Function
function
Involved in the base excision repair (BER) pathway, by catalyzing the poly(ADP-ribosyl)ation of a limited number of acceptor proteins involved in chromatin architecture and in DNA metabolism. This modification follows DNA damages and appears as an obligatory step in a detection/signaling pathway leading to the reparation of DNA strand breaks.
Catalytic activity
- L-aspartyl-[protein] + NAD+ = 4-O-(ADP-D-ribosyl)-L-aspartyl-[protein] + nicotinamide
- L-glutamyl-[protein] + NAD+ = 5-O-(ADP-D-ribosyl)-L-glutamyl-[protein] + nicotinamide
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | nucleolus | |
Molecular Function | DNA binding | |
Molecular Function | NAD binding | |
Molecular Function | NAD+-protein poly-ADP-ribosyltransferase activity | |
Molecular Function | nucleotidyltransferase activity | |
Molecular Function | zinc ion binding | |
Biological Process | double-strand break repair | |
Biological Process | protein poly-ADP-ribosylation |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended namePoly [ADP-ribose] polymerase
- EC number
Organism names
- Organism
- Strain
- Taxonomic lineageEukaryota > Viridiplantae > Streptophyta > Embryophyta > Tracheophyta > Spermatophyta > Magnoliopsida > eudicotyledons > Gunneridae > Pentapetalae > Caryophyllales > Chenopodiaceae > Chenopodioideae > Atripliceae > Chenopodium
Accessions
- Primary accessionA0A803M7S8
Proteomes
Genome annotation databases
Subcellular Location
PTM/Processing
Keywords
- PTM
Structure
Family & Domains
Features
Showing features for domain, region, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 8-142 | PARP-type | ||||
Sequence: WKAEYAKSARAACRTCKNNIAKEILRFGKMVQSPHFDGFMPLACLSISELLKIAAVCGATFCASLDFFVDMHVFSDDKDLLPTEMVRISAKIDGQASRGLSWYHATCFLESYPSTFPDKLSGWQSLSSSDQASVQ | ||||||
Region | 146-183 | Disordered | ||||
Sequence: KGKAPSAESGLGSSEKFLKDSKTRDGAKRKNAGGSDQD | ||||||
Compositional bias | 160-183 | Basic and acidic residues | ||||
Sequence: EKFLKDSKTRDGAKRKNAGGSDQD | ||||||
Domain | 361-452 | BRCT | ||||
Sequence: FKDEKLEDLRVAIAGLPKETVEDFRSKIEGAGGQVHAKIKKDTNCLVVGGGLSDQHAELKKARRMKIPIVREEYLVNCIQKQKKLPFNLYKM | ||||||
Domain | 481-581 | WGR | ||||
Sequence: SGHILEEGPSIYNTTLSLSDLSSGINSYYILQIIQDDKGQECHVFRKWGRVGNEKIGSSKIEEISKSDAIEEFKRLFLEKTGNPWEAWVHKKNFRKHPGRF | ||||||
Domain | 603-721 | PARP alpha-helical | ||||
Sequence: NSKLAPALKELIKMLFNVETYRAAMLEFEINLSEMPLGKLSKSNIQQGFEALTQIQNLLENTGLQPSVKESLIVDASNRFFTMIPSIHPHVIRDEDDFKSKVKMLEALQDIEIASRLVG | ||||||
Domain | 728-953 | PARP catalytic | ||||
Sequence: EPLDTKYKKLQCDMVPLSHDSEDYQLIEKYLLTTHAPTHTEWSLELEEVFSLEREGELDKFAPKREKLGNRMLLWHGSRLTNFVGILSQGLRIAPPEAPATGYMFGKGVYFADLVSKSAQYCFTDKKNPVGLMLLSEVALGKVHELKKAQYMDKPPRGKHSTKGLGKKVPDEAGFAKWRDEVVVPCGKPVDSKDKTSDLMYNEYIVYDAAQVKMQYLLKVRFRYKR |
Sequence similarities
Belongs to the ARTD/PARP family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length953
- Mass (Da)106,753
- Last updated2021-06-02 v1
- Checksum63ED86472632C06B
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 160-183 | Basic and acidic residues | ||||
Sequence: EKFLKDSKTRDGAKRKNAGGSDQD |
Keywords
- Technical term