ID M5AVM8_CYNPY Unreviewed; 403 AA. AC M5AVM8; DT 29-MAY-2013, integrated into UniProtKB/TrEMBL. DT 29-MAY-2013, sequence version 1. DT 03-JUL-2019, entry version 9. 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=Rag-1 {ECO:0000313|EMBL:BAN05100.1}; OS Cynops pyrrhogaster (Japanese fire-bellied newt). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Amphibia; Batrachia; Caudata; Salamandroidea; Salamandridae; OC Pleurodelinae; Cynops. OX NCBI_TaxID=8330 {ECO:0000313|EMBL:BAN05100.1}; RN [1] {ECO:0000313|EMBL:BAN05100.1} RP NUCLEOTIDE SEQUENCE. RC TISSUE=Liver {ECO:0000313|EMBL:BAN05100.1}; RA Tominaga A., Matsui M., Yoshikawa N., Nishikawa K., Hayashi T., RA Misawa Y., Tanabe S., Ota H.; RT "Phylogeny and historical demography of Cynops pyrrhogaster (Amphibia: RT Urodela): Taxonomic relationships and distributional changes RT associated with climatic oscillations."; RL Mol. Phylogenet. Evol. 66:654-667(2013). 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; AB754784; BAN05100.1; -; Genomic_DNA. DR EMBL; AB754785; BAN05101.1; -; Genomic_DNA. DR EMBL; AB754786; BAN05102.1; -; Genomic_DNA. DR EMBL; AB754787; BAN05103.1; -; Genomic_DNA. DR EMBL; AB754788; BAN05104.1; -; Genomic_DNA. DR EMBL; AB754789; BAN05105.1; -; Genomic_DNA. DR EMBL; AB754792; BAN05108.1; -; Genomic_DNA. DR EMBL; AB754794; BAN05110.1; -; Genomic_DNA. DR EMBL; AB754795; BAN05111.1; -; Genomic_DNA. DR EMBL; AB754797; BAN05113.1; -; Genomic_DNA. DR EMBL; AB754798; BAN05114.1; -; Genomic_DNA. DR EMBL; AB754799; BAN05115.1; -; Genomic_DNA. DR EMBL; AB754800; BAN05116.1; -; Genomic_DNA. DR EMBL; AB754801; BAN05117.1; -; Genomic_DNA. DR EMBL; AB754802; BAN05118.1; -; Genomic_DNA. DR EMBL; AB754803; BAN05119.1; -; Genomic_DNA. DR EMBL; AB754805; BAN05121.1; -; 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 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:BAN05100.1}. FT NON_TER 403 403 {ECO:0000313|EMBL:BAN05100.1}. SQ SEQUENCE 403 AA; 46143 MW; 96922B6190F2C7CF CRC64; RYDVALVSTL KDMEEDILEG LKAHELDDYL SGPFTVVVKE SCDGMGDVSE KHGCGPVVPE KAVRFSFTIM TIAVDHNKDN VRIFEENKPN SELCCKPLCL MLADESDHET LTAILSPLIA ERESMKGSEL MLELGGILRT FKFVFRGTGY DEKLVREVEG LEASGSVYIC TLCDSTRLEA SQNIVLHSIT RSHKENLERY EIWRSNRHHE SVDELRDRVK GVSAKPFIET LPSIDALHCD IGNAAEFYKI FQLEIGEVFK NPNASKEERK RWQSTLDKHL RKKMNLKPIM RMNGNFARKL MSQETVEAVC ELVHSEERRA ALRELMDLYL KMKPVWRSSC PSKECPELLC QYSYNSQRFA ELLSTKFKYR YEGKITNYFH KTLAHVPEII ERDGSIGAWA SEG //