F8SXH6 · F8SXH6_DREPE

  • Protein
    V(D)J recombination-activating protein 1
  • Gene
    RAG1
  • Status
    UniProtKB unreviewed (TrEMBL)
  • Amino acids
  • Protein existence
    Inferred from homology
  • Annotation score
    4/5

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.

Caution

Lacks conserved residue(s) required for the propagation of feature annotation.

Catalytic activity

  • S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N6-ubiquitinyl-[acceptor protein]-L-lysine.
    EC:2.3.2.27 (UniProtKB | ENZYME | Rhea)

Cofactor

Protein has several cofactor binding sites:
Mg2+ (UniProtKB | Rhea| CHEBI:18420 )

Mn2+ (UniProtKB | Rhea| CHEBI:29035 )

Note: Binds 1 divalent metal cation per subunit. Mg2+ or Mn2+.

GO annotations

AspectTerm
Cellular ComponentDNA recombinase complex
Cellular Componentendodeoxyribonuclease complex
Cellular Componentnucleus
Molecular Functiondouble-stranded DNA endonuclease activity
Molecular Functionhistone binding
Molecular Functionprotein homodimerization activity
Molecular Functionsequence-specific DNA binding
Molecular Functionubiquitin protein ligase activity
Molecular Functionzinc ion binding
Biological Processadaptive immune response
Biological Processchromatin organization
Biological Processpre-B cell allelic exclusion
Biological ProcessT cell differentiation in thymus
Biological ProcessV(D)J recombination

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    V(D)J recombination-activating protein 1
  • EC number

Gene names

    • Name
      RAG1

Organism names

  • Taxonomic identifier
  • Organism
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Sciuromorpha > Sciuridae > Callosciurinae > Callosciurini > Dremomys

Accessions

  • Primary accession
    F8SXH6

Subcellular Location

Keywords

  • Cellular component

Interaction

Subunit

Homodimer.

Family & Domains

Features

Showing features for compositional bias, region, coiled coil, domain.

TypeIDPosition(s)Description
Compositional bias1-24Basic and acidic residues
Region1-64Disordered
Coiled coil203-230
Domain260-299RING-type
Domain321-350RAG1-type
Domain359-423NBD

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

Family and domain databases

Sequence

  • Sequence status
    Fragment
  • Length
    423
  • Mass (Da)
    48,632
  • Last updated
    2011-09-21 v1
  • Checksum
    0890F5EBA2F81296
RVRSLEKTTEETQKEKKDSSEEKPPLEQSPAVLDKSGGQKPVLTQPALKGHPKFSKKFHDGGKARDKAIHQANLRHFCRICGNSFKTDEHNRRYPVHGPVDAKTQILLRKKEKRVTSWPDLIARVFRIDVKADVDAIHPTEFCHNCWNIMHRKFSSAPCEVYFPRNATMEWHPHTPSCDICHSARRGLKRKRHQPNVQLSKKLKTVFDQARQARQRKRRAQARISSKEVMKKITNCSKIHLGTNLLAVDFPAHFVKSISCQICEHILADPVETSCKHVFCRICILRCLKVMGSYCPSCRYPCFPTDLESPVKSFLSILNSLVVKCPAKECNEEVSLEKYNHHVSSHKESKETFVHINKGGRPRQHLLSLTRRAQKHRLRELKMQVKAFADKEEGGDVKSVCLTLFLLALRARNEHRQANELEA

Features

Showing features for non-terminal residue, compositional bias.

TypeIDPosition(s)Description
Non-terminal residue1
Compositional bias1-24Basic and acidic residues
Non-terminal residue423

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
HQ698441
EMBL· GenBank· DDBJ
AEI73024.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. Our staff consists of biologists and biochemists that are not trained to give medical advice.
We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.
FeedbackHelp