A0A075W5Y3 · A0A075W5Y3_9SYLV

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

  • 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+.

Features

Showing features for dna binding.

TypeIDPosition(s)Description
DNA binding43-110NBD

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
      RAG-1

Organism names

  • Taxonomic identifier
  • Strains
    • 12557
    • 12562
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Archelosauria > Archosauria > Dinosauria > Saurischia > Theropoda > Coelurosauria > Aves > Neognathae > Neoaves > Telluraves > Australaves > Passeriformes > Sylvioidea > Sylviidae > Acrocephalinae > Acrocephalus

Accessions

  • Primary accession
    A0A075W5Y3

Subcellular Location

Keywords

  • Cellular component

Interaction

Subunit

Homodimer.

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain3-32RAG1-type
Domain43-110NBD

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
    271
  • Mass (Da)
    30,415
  • Last updated
    2014-10-29 v1
  • Checksum
    D8B85E443B6467D0
DNLSIKCPVKECDEEILHGKYGQHLSSHKEMKDGELYSYINKGGRPRQHLLSLTRRAQKHRLRELKRQVKAFAEKEEGGDIKAVCMTLFLLALRAKNEHKQADELEAIMQGKGSGLHPAVCLAIRINTFLSCSQYHKMYRTVKAVTGRQIFQPLHSLRTAEKALLPGYHPFEWKPPLKNVSTNTEVGIIDGLSGLPLSIDDYPVDTIAKRFRYDAALVCALKDMEEEILEGMKEKNLDDYLNGPFTVVVKESCDGMGDVSEKHGSGPAVPE

Features

Showing features for non-terminal residue.

TypeIDPosition(s)Description
Non-terminal residue1
Non-terminal residue271

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
KJ453486
EMBL· GenBank· DDBJ
AIG95582.1
EMBL· GenBank· DDBJ
Genomic DNA
KJ453487
EMBL· GenBank· DDBJ
AIG95583.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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