ID Q5DWP3_MOGIN Unreviewed; 336 AA. AC Q5DWP3; DT 29-MAR-2005, integrated into UniProtKB/TrEMBL. DT 29-MAR-2005, sequence version 1. DT 03-JUL-2019, entry version 21. 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:BAD90554.1}; OS Mogera insularis (Insular mole) (Talpa insularis). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Laurasiatheria; Eulipotyphla; Talpidae; Mogera. OX NCBI_TaxID=114413 {ECO:0000313|EMBL:BAD90554.1}; RN [1] {ECO:0000313|EMBL:BAD90554.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=MH6860 {ECO:0000313|EMBL:BAD90554.1}; RX PubMed=15613798; DOI=10.2108/zsj.21.1177; RA Shinohara A., Suzuki H., Tsuchiya K., Zhang Y.P., Luo J., Jiang X.L., RA Wang Y.X., Campbell K.L.; RT "Evolution and biogeography of talpid moles from continental East Asia RT and the Japanese islands inferred from mitochondrial and nuclear gene RT sequences."; RL Zool. Sci. 21:1177-1185(2004). RN [2] {ECO:0000313|EMBL:BAP16101.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=SIK0587 {ECO:0000313|EMBL:BAP16101.1}; RA Shinohara A., Kawada S., Son N.T., Koshimoto C., Endo H., Can D.N., RA Suzuki H.; RT "Molecular phylogeny of East and Southeast Asian fossorial moles RT (Lipotyphla, Talpidae)."; RL J. Mammal. 95:455-466(2014). 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; AB176544; BAD90554.1; -; Genomic_DNA. DR EMBL; AB823158; BAP16101.1; -; 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:BAD90554.1}. FT NON_TER 336 336 {ECO:0000313|EMBL:BAD90554.1}. SQ SEQUENCE 336 AA; 38312 MW; 469D0C410646DFB8 CRC64; SCDGMGDVSE KHGSGPAVPE KAVRFSFTVM KITIAHGSQN VKVFEEAKPN SELCCKPLCL MLADESDHET LTAILSPLIA EREAMKSSQL MLEMGGILRT FKFIFRGTGY DEKLVREVEG LEASGSVYIC TLCDATRLEA SQNLVFHSIT RSHTENLERY EVWRSNPYHE SVEELRDRVK GVSAKPFIET VPSIDALHCD IGNAAEFYKI FQLEIGEVYK NPNASKEERK RWQATLDKHL RKKMNLKPIM RMNGNFARKL MTKETVEAVC ELIPSEERHA ALQELMDLYL KMKPVWRSSC PAKECPESLC QYSFNSQRFA ELLSTKFKYR YEGKIT //