C7AAS2 · C7AAS2_MUSST
- ProteinV(D)J recombination-activating protein 1
- GeneRAG-1
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids930 (go to sequence)
- Protein existenceInferred from homology
- Annotation score4/5
Function
function
Catalytic component of the RAG complex, a multiprotein complex that mediates the DNA cleavage phase during V(D)J recombination. V(D)J recombination assembles a diverse repertoire of immunoglobulin and T-cell receptor genes in developing B and T-lymphocytes through rearrangement of different V (variable), in some cases D (diversity), and J (joining) gene segments. In the RAG complex, RAG1 mediates the DNA-binding to the conserved recombination signal sequences (RSS) and catalyzes the DNA cleavage activities by introducing a double-strand break between the RSS and the adjacent coding segment. RAG2 is not a catalytic component but is required for all known catalytic activities. DNA cleavage occurs in 2 steps: a first nick is introduced in the top strand immediately upstream of the heptamer, generating a 3'-hydroxyl group that can attack the phosphodiester bond on the opposite strand in a direct transesterification reaction, thereby creating 4 DNA ends: 2 hairpin coding ends and 2 blunt, 5'-phosphorylated ends.
Catalytic activity
Cofactor
Protein has several cofactor binding sites:
Note: Binds 1 divalent metal cation per subunit. Mg2+ or Mn2+.
Features
Showing features for dna binding.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
DNA binding | 357-424 | NBD | |||
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | DNA recombinase complex | |
Cellular Component | endodeoxyribonuclease complex | |
Cellular Component | nucleus | |
Molecular Function | double-stranded DNA endonuclease activity | |
Molecular Function | histone binding | |
Molecular Function | protein homodimerization activity | |
Molecular Function | sequence-specific DNA binding | |
Molecular Function | ubiquitin protein ligase activity | |
Molecular Function | zinc ion binding | |
Biological Process | adaptive immune response | |
Biological Process | chromatin organization | |
Biological Process | pre-B cell allelic exclusion | |
Biological Process | T cell differentiation in thymus | |
Biological Process | V(D)J recombination |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameV(D)J recombination-activating protein 1
- EC number
Gene names
Organism names
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Archelosauria > Archosauria > Dinosauria > Saurischia > Theropoda > Coelurosauria > Aves > Neognathae > Neoaves > Telluraves > Australaves > Passeriformes > Passeroidea > Parulidae > Setophaga
Accessions
- Primary accessionC7AAS2
Subcellular Location
Interaction
Subunit
Homodimer.
Structure
Family & Domains
Features
Showing features for compositional bias, region, domain.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Compositional bias | 1-41 | Basic and acidic residues | |||
Region | 1-46 | Disordered | |||
Domain | 256-294 | RING-type | |||
Domain | 317-346 | RAG1-type | |||
Domain | 357-424 | NBD | |||
Domain
The NBD (nonamer binding) DNA-binding domain mediates the specific binding to the nonamer RSS motif by forming a tightly interwoven homodimer that binds and synapses 2 nonamer elements, with each NBD making contact with both DNA molecules. Each RSS is composed of well-conserved heptamer (consensus 5'-CACAGTG-3') and nonamer (consensus 5'-ACAAAAACC-3') sequences separated by a spacer of either 12 bp or 23 bp.
Sequence similarities
Belongs to the RAG1 family.
Keywords
- Domain
Family and domain databases
Sequence
- Sequence statusFragment
- Length930
- Mass (Da)106,327
- Last updated2009-09-22 v1
- Checksum2814CB19A265CA47
Features
Showing features for non-terminal residue, compositional bias.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Non-terminal residue | 1 | ||||
Compositional bias | 1-41 | Basic and acidic residues | |||
Non-terminal residue | 930 | ||||
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
FJ358149 EMBL· GenBank· DDBJ | ACT37615.1 EMBL· GenBank· DDBJ | Genomic DNA |