ID A0A221LE43_9MURI Unreviewed; 783 AA. AC A0A221LE43; DT 25-OCT-2017, integrated into UniProtKB/TrEMBL. DT 25-OCT-2017, sequence version 1. DT 14-DEC-2022, entry version 15. DE RecName: Full=V(D)J recombination-activating protein 1 {ECO:0000256|ARBA:ARBA00021277, ECO:0000256|RuleBase:RU366024}; DE EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483, 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; Mammalia; OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; OC 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., Fabre P.-H.; RT "The generic status of Rattus annandalei (Bonhote, 1903) (Rodentia, RT Murinae) and its evolutionary implications."; RL J. Mammal. 98:1340-1355(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 of CC immunoglobulin and T-cell receptor genes in developing B and T- CC lymphocytes through rearrangement of different V (variable), in some CC cases D (diversity), and J (joining) gene segments. In the RAG complex, CC RAG1 mediates the DNA-binding to the conserved recombination signal CC sequences (RSS) and catalyzes the DNA cleavage activities by CC introducing a double-strand break between the RSS and the adjacent CC coding segment. RAG2 is not a catalytic component but is required for CC all known catalytic activities. DNA cleavage occurs in 2 steps: a first CC nick is introduced in the top strand immediately upstream of the CC heptamer, generating a 3'-hydroxyl group that can attack the CC phosphodiester bond on the opposite strand in a direct CC transesterification reaction, thereby creating 4 DNA ends: 2 hairpin CC coding ends and 2 blunt, 5'-phosphorylated ends. CC {ECO:0000256|RuleBase:RU366024}. CC -!- CATALYTIC ACTIVITY: CC Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + CC [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L- CC cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.; CC EC=2.3.2.27; Evidence={ECO:0000256|ARBA:ARBA00000900, CC ECO:0000256|RuleBase:RU366024}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000256|ARBA:ARBA00001946, CC 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:0005634; C:nucleus; IEA:UniProtKB-SubCell. DR GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-UniRule. DR GO; GO:0042393; F:histone binding; IEA:UniProtKB-UniRule. DR GO; GO:0042803; F:protein homodimerization activity; IEA:UniProtKB-UniRule. DR GO; GO:0043565; F:sequence-specific DNA binding; IEA:UniProtKB-UniRule. DR GO; GO:0061630; F:ubiquitin protein ligase activity; IEA:UniProtKB-UniRule. DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule. DR GO; GO:0030183; P:B cell differentiation; IEA:UniProtKB-UniRule. DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW. DR GO; GO:0010390; P:histone monoubiquitination; IEA:UniProtKB-UniRule. DR GO; GO:0033077; P:T cell differentiation in thymus; IEA:UniProtKB-UniRule. DR GO; GO:0033151; P:V(D)J recombination; IEA:UniProtKB-UniRule. DR InterPro; IPR024627; RAG1. DR InterPro; IPR035714; RAG1_imp-bd. DR PANTHER; PTHR11539; VDJ RECOMBINATION ACTIVATING PROTEIN 1 RAG1; 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|ARBA:ARBA00023125, ECO:0000256|RuleBase:RU366024}; KW Endonuclease {ECO:0000256|RuleBase:RU366024}; KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU366024}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, KW ECO:0000256|RuleBase:RU366024}; KW Multifunctional enzyme {ECO:0000256|RuleBase:RU366024}; KW Nuclease {ECO:0000256|RuleBase:RU366024}; KW Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|RuleBase:RU366024}; KW Transferase {ECO:0000256|ARBA:ARBA00022679, 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 FT /note="RAG1_imp_bd" FT /evidence="ECO:0000259|Pfam:PF12560" FT REGION 1..36 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1..21 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT NON_TER 1 FT /evidence="ECO:0000313|EMBL:ASM93016.1" FT NON_TER 783 FT /evidence="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 //