ID A0A4Y5WR26_9MURI Unreviewed; 308 AA. AC A0A4Y5WR26; DT 18-SEP-2019, integrated into UniProtKB/TrEMBL. DT 18-SEP-2019, sequence version 1. DT 16-OCT-2019, entry version 2. DE RecName: Full=V(D)J recombination-activating protein 1 {ECO:0000256|RuleBase:RU366024}; DE EC=2.3.2.27 {ECO:0000256|RuleBase:RU366024}; DE EC=3.1.-.- {ECO:0000256|RuleBase:RU366024}; DE Flags: Fragment; GN Name=Rag1 {ECO:0000313|EMBL:QDE10142.1}; OS Arvicanthis sp. 'Metahara'. OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; OC Muroidea; Muridae; Murinae; Arvicanthis. OX NCBI_TaxID=2590534 {ECO:0000313|EMBL:QDE10142.1}; RN [1] {ECO:0000313|EMBL:QDE10142.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=LAV2092 {ECO:0000313|EMBL:QDE10142.1}; RA Bryja J., Colangelo P., Lavrenchenko L.A., Meheretu Y., Sumbera R., RA Bryjova A., Verheyen E., Leirs H., Castiglia R.; RT "Diversity and evolution of African Grass Rats (Muridae: Arvicanthis) RT - From radiation in East Africa to repeated colonization of RT northwestern and southeastern savannas."; RL J. Zoolog. Syst. Evol. Res. 0:0-0(2019). CC -!- FUNCTION: Catalytic component of the RAG complex, a multiprotein CC complex that mediates the DNA cleavage phase during V(D)J CC recombination. V(D)J recombination assembles a diverse repertoire CC of immunoglobulin and T-cell receptor genes in developing B and T- CC lymphocytes through rearrangement of different V (variable), in CC some cases D (diversity), and J (joining) gene segments. In the CC RAG complex, RAG1 mediates the DNA-binding to the conserved CC recombination signal sequences (RSS) and catalyzes the DNA CC cleavage activities by introducing a double-strand break between CC the RSS and the adjacent coding segment. RAG2 is not a catalytic CC component but is required for all known catalytic activities. DNA CC cleavage occurs in 2 steps: a first nick is introduced in the top CC strand immediately upstream of the heptamer, generating a 3'- CC hydroxyl group that can attack the phosphodiester bond on the CC opposite strand in a direct transesterification reaction, thereby CC creating 4 DNA ends: 2 hairpin coding ends and 2 blunt, 5'- CC phosphorylated ends. {ECO:0000256|RuleBase:RU366024}. CC -!- CATALYTIC ACTIVITY: CC Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L- CC cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin- CC conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor CC protein]-L-lysine.; EC=2.3.2.27; CC Evidence={ECO:0000256|RuleBase:RU366024}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000256|RuleBase:RU366024}; CC -!- COFACTOR: CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; CC Evidence={ECO:0000256|RuleBase:RU366024}; CC Note=Binds 1 divalent metal cation per subunit. Mg(2+) or Mn(2+). CC {ECO:0000256|RuleBase:RU366024}; CC -!- SUBUNIT: Homodimer. {ECO:0000256|RuleBase:RU366024}. CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|RuleBase:RU366024}. CC -!- SIMILARITY: Belongs to the RAG1 family. CC {ECO:0000256|RuleBase:RU366024}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; MK248206; QDE10142.1; -; Genomic_DNA. DR InterPro; IPR024627; RAG1. DR PANTHER; PTHR11539; PTHR11539; 1. DR Pfam; PF12940; RAG1; 1. PE 3: Inferred from homology; KW Chromatin regulator {ECO:0000256|RuleBase:RU366024}; KW DNA recombination {ECO:0000256|RuleBase:RU366024}; KW DNA-binding {ECO:0000256|RuleBase:RU366024}; KW Endonuclease {ECO:0000256|RuleBase:RU366024}; KW Hydrolase {ECO:0000256|RuleBase:RU366024}; KW Metal-binding {ECO:0000256|RuleBase:RU366024}; KW Multifunctional enzyme {ECO:0000256|RuleBase:RU366024}; KW Nuclease {ECO:0000256|RuleBase:RU366024}; KW Nucleus {ECO:0000256|RuleBase:RU366024}; KW Transferase {ECO:0000256|RuleBase:RU366024}; KW Ubl conjugation pathway {ECO:0000256|RuleBase:RU366024}; KW Zinc {ECO:0000256|RuleBase:RU366024}; KW Zinc-finger {ECO:0000256|RuleBase:RU366024}. FT NON_TER 1 1 {ECO:0000313|EMBL:QDE10142.1}. FT NON_TER 308 308 {ECO:0000313|EMBL:QDE10142.1}. SQ SEQUENCE 308 AA; 35137 MW; C57C7C5BD140062E CRC64; DYLNGPFTVV VKESCDGMGD VSEKHGSGPA VPEKAVRFSF TVMRITIEHD SQNVKVFEEP KPNSELCCKP LCLMLADESD HETLTAILSP LIAEREAMKS SELMLEMGGI TRTFKFIFRG TGYDEKLVRE VEGLEASGSV YICTLCDATR LEASQNLVFH SITRSHAENL QRYEVWRSNP YHESVEELRD RVKGVSAKPF IETVPSIDAL HCDIGNAAEF YKIFQLEIGE VYKNPNASKE ERKRWQATLD KHLRKRMNLK PIMRMNGNFA RKLMTQETVD AVCELIPSEE RHEALRELMD LYLKMKPV //