UniProt ID: F1QD74
SUBCELLULAR LOCATION: Nucleus {ECO:0000256|PROSITE- ProRule:PRU00820}.
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. {ECO:0000256|PROSITE- ProRule:PRU00820}.
SIMILARITY: Belongs to the RAG1 family. {ECO:0000256|PROSITE- ProRule:PRU00820}.
UniProt ID: O13033
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. In addition to its endonuclease activity, RAG1 also acts as an E3 ubiquitin-protein ligase that mediates monoubiquitination of histone H3. Histone H3 monoubiquitination is required for the joining step of V(D)J recombination (By similarity). {ECO:0000250}.
CATALYTIC ACTIVITY: Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L- cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin- conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.; EC=2.3.2.27;
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250}; Note=Binds 1 divalent metal cation per subunit. Mg(2+) or Mn(2+). {ECO:0000250};
SUBUNIT: Homodimer. Component of the RAG complex composed of core components rag1 and rag2 (By similarity). {ECO:0000250}.
SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE- ProRule:PRU00820}.
TISSUE SPECIFICITY: In the adult, predominantly expressed in the thymus with lower levels in the pronephros, mesonephros and ovary. {ECO:0000269|PubMed:9089097}.
DEVELOPMENTAL STAGE: First detected in the thymus during day 4 of development. Expression then increases in the thymus for at least three weeks. {ECO:0000269|PubMed:9070331, ECO:0000269|PubMed:9089097}.
DOMAIN: The RING-type zinc finger mediates the E3 ubiquitin- protein ligase activity. {ECO:0000250}.
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. {ECO:0000255|PROSITE- ProRule:PRU00820}.
SIMILARITY: Belongs to the RAG1 family. {ECO:0000255|PROSITE- ProRule:PRU00820}.
UniProt ID: A0A2R8PY29
SUBCELLULAR LOCATION: Nucleus {ECO:0000256|PROSITE- ProRule:PRU00820}.
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. {ECO:0000256|PROSITE- ProRule:PRU00820}.
SIMILARITY: Belongs to the RAG1 family. {ECO:0000256|PROSITE- ProRule:PRU00820}.
UniProt ID: I2BJN1
SUBCELLULAR LOCATION: Nucleus {ECO:0000256|PROSITE- ProRule:PRU00820}.
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. {ECO:0000256|PROSITE- ProRule:PRU00820}.
SIMILARITY: Belongs to the RAG1 family. {ECO:0000256|PROSITE- ProRule:PRU00820}.
CAUTION: Lacks conserved residue(s) required for the propagation of feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00820}.
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