ID A0A221LE43_9MURI Unreviewed; 783 AA. AC A0A221LE43; DT 25-OCT-2017, integrated into UniProtKB/TrEMBL. DT 25-OCT-2017, sequence version 1. DT 03-JUL-2019, entry version 5. 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:ASM93016.1}; OS Sundamys maxi. OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; OC Muroidea; Muridae; Murinae; Sundamys. OX NCBI_TaxID=2021985 {ECO:0000313|EMBL:ASM93016.1}; RN [1] {ECO:0000313|EMBL:ASM93016.1} RP NUCLEOTIDE SEQUENCE. RA Camacho-Sanchez M., Leonard J.A., Fitriana Y., Tilak M.-K., RA Fabre P.-H.; RT "The generic status of Rattus annandalei (Bonhote, 1903) (Rodentia, RT Murinae) and its evolutionary implications."; RL J. Mammal. 0:0-0(2017). 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; KY467070; ASM93016.1; -; Genomic_DNA. DR GO; GO:0004519; F:endonuclease activity; IEA:InterPro. DR GO; GO:0043565; F:sequence-specific DNA binding; IEA:InterPro. DR GO; GO:0061630; F:ubiquitin protein ligase activity; IEA:InterPro. DR GO; GO:0033151; P:V(D)J recombination; IEA:InterPro. DR InterPro; IPR024627; RAG1. DR InterPro; IPR035714; RAG1_imp-bd. DR PANTHER; PTHR11539; PTHR11539; 2. DR Pfam; PF12940; RAG1; 1. DR Pfam; PF12560; RAG1_imp_bd; 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 DOMAIN 1 249 RAG1_imp_bd. {ECO:0000259|Pfam:PF12560}. FT REGION 1 36 Disordered. {ECO:0000256|MobiDB-lite: FT A0A221LE43}. FT COMPBIAS 1 21 Polyampholyte. {ECO:0000256|MobiDB-lite: FT A0A221LE43}. FT NON_TER 1 1 {ECO:0000313|EMBL:ASM93016.1}. FT NON_TER 783 783 {ECO:0000313|EMBL:ASM93016.1}. SQ SEQUENCE 783 AA; 88625 MW; 1C0AED1BDFB93A2A CRC64; VRSFEKAPEE AQKEKDSSEG KPYLEQSPVV LDKPGGQNSV LTQRALKLHP KFXKKFHXDG KSSDKAIHQA RLRHFCRICG NHFKSDRHNR RYPVHGPVDA KTQRLFRKKE KRVTSWPDLI ARVFRIDVKS DVDSIHPTEF CHNCWGIMHR KFSSAHSQVY CPRNVTVEWH PHTPSCDICF TAHQGLKRKR HQPNMQLSKK LKTVLNHARR DRRKRTQARV SSKEVMKKIS NCSKIHLSTK LLAVDFPAHX XXXXXXXXXX XXXXXPVXXX XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX XXXXXXXXDI LEGMRSQDLD DYLNGPFTVV VKESCDGMGD VSEKHGSGPA VPEKAVRFSF TVMRITIKHG SQNVKIFEEP KPNSELCCKP LCLMLADESD HETLTAILSP LIAEREAMKS SELMLEMGGI PRTFKFIFRG TGYDEKLVRE VEGLEASGSV YICTLCDATR LEASQNLVFH SITRSHAENL QRYEVWRSNP YHESVEELRD RVKGVSAKPF IETVPSIDAL HCDIGNAAEF YKIFQLEIGE VYK //