ID A0A0M4VB73_9EUTH Unreviewed; 336 AA. AC A0A0M4VB73; DT 09-DEC-2015, integrated into UniProtKB/TrEMBL. DT 09-DEC-2015, sequence version 1. DT 31-JUL-2019, entry version 8. 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:BAS50177.1}; OS Euroscaptor subanura. OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Laurasiatheria; Eulipotyphla; Talpidae; OC Euroscaptor. OX NCBI_TaxID=1581555 {ECO:0000313|EMBL:BAS50177.1}; RN [1] {ECO:0000313|EMBL:ALN43286.1} RP NUCLEOTIDE SEQUENCE. RA Bannikova A.A., Zemlemerova E.E., Lebedev V.S., Alexandrov D., RA Aleksandrov D.Y., Fang Y., Sheftel B.I.; RT "Phylogenetic Position of the Gansu Mole Scapanulus oweni Thomas, 1912 RT and the Relationships between Strictly Fossorial Tribes of the Family RT Talpidae."; RL Dokl. Biol. Sci. 44:230-234(2015). RN [2] {ECO:0000313|EMBL:BAS50177.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=IEBR-M-1734/SIK0875 {ECO:0000313|EMBL:BAS50165.1}, RC IEBR-M-1735/SIK0876 {ECO:0000313|EMBL:BAS50166.1}, IEBR-M-1798/SIK0882 RC {ECO:0000313|EMBL:BAS50167.1}, IEBR-M-1799/SIK0883 RC {ECO:0000313|EMBL:BAS50168.1}, IEBR-M-3250/SIK0913 RC {ECO:0000313|EMBL:BAS50169.1}, IEBR-M-3251/SIK0914 RC {ECO:0000313|EMBL:BAS50170.1}, IEBR-M-3252/SIK0915 RC {ECO:0000313|EMBL:BAS50171.1}, IEBR-M-3253/SIK0916 RC {ECO:0000313|EMBL:BAS50172.1}, IEBR-M-3254/SIK0917 RC {ECO:0000313|EMBL:BAS50173.1}, IEBR-M-3256/SIK0919 RC {ECO:0000313|EMBL:BAS50175.1}, IEBR-M-3259/SIK0922 RC {ECO:0000313|EMBL:BAS50176.1}, IEBR-M-3261/SIK0924 RC {ECO:0000313|EMBL:BAS50177.1}, SIK0930 {ECO:0000313|EMBL:BAS50178.1}, RC SIK0932 {ECO:0000313|EMBL:BAS50179.1}, SIK0936 RC {ECO:0000313|EMBL:BAS50180.1}, SIK0937 {ECO:0000313|EMBL:BAS50181.1}, RC and SIK0938 {ECO:0000313|EMBL:BAS50182.1}; RA Shinohara A., Kawada S., Son N.T., Can D.N., Sakamoto S.H., RA Koshimoto C.; RT "Molecular phylogenetic relationships and intra-species diversities of RT three Euroscaptor spp. (Talpidae: Lipotyphla: Mammalia) from RT Vietnam."; RL Raffles Bull. Zool. 63:366-375(2015). RN [3] {ECO:0000313|EMBL:ALN43286.1} RP NUCLEOTIDE SEQUENCE. RA Murphy D.; RL Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases. RN [4] {ECO:0000313|EMBL:AQM57842.1} RP NUCLEOTIDE SEQUENCE. RA Zemlemerova E., Bannikova A., Lebedev V., Rozhnov V., Abramov A.; RT "Secrets of the underground Vietnam: an underestimated species RT diversity of Asian moles (Lipotyphla: Talpidae: Euroscaptor)."; RL Tr. Zool. Inst. 320:193-220(2016). 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; KP995375; ALN43286.1; -; Genomic_DNA. DR EMBL; KX164278; AQM57842.1; -; Genomic_DNA. DR EMBL; KX164279; AQM57843.1; -; Genomic_DNA. DR EMBL; KX164280; AQM57844.1; -; Genomic_DNA. DR EMBL; KX164281; AQM57845.1; -; Genomic_DNA. DR EMBL; KX164282; AQM57846.1; -; Genomic_DNA. DR EMBL; KX164283; AQM57847.1; -; Genomic_DNA. DR EMBL; KX164285; AQM57849.1; -; Genomic_DNA. DR EMBL; LC013317; BAS50165.1; -; Genomic_DNA. DR EMBL; LC013318; BAS50166.1; -; Genomic_DNA. DR EMBL; LC013319; BAS50167.1; -; Genomic_DNA. DR EMBL; LC013320; BAS50168.1; -; Genomic_DNA. DR EMBL; LC013321; BAS50169.1; -; Genomic_DNA. DR EMBL; LC013322; BAS50170.1; -; Genomic_DNA. DR EMBL; LC013323; BAS50171.1; -; Genomic_DNA. DR EMBL; LC013324; BAS50172.1; -; Genomic_DNA. DR EMBL; LC013325; BAS50173.1; -; Genomic_DNA. DR EMBL; LC013327; BAS50175.1; -; Genomic_DNA. DR EMBL; LC013328; BAS50176.1; -; Genomic_DNA. DR EMBL; LC013329; BAS50177.1; -; Genomic_DNA. DR EMBL; LC013330; BAS50178.1; -; Genomic_DNA. DR EMBL; LC013331; BAS50179.1; -; Genomic_DNA. DR EMBL; LC013332; BAS50180.1; -; Genomic_DNA. DR EMBL; LC013333; BAS50181.1; -; Genomic_DNA. DR EMBL; LC013334; BAS50182.1; -; 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: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 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:BAS50177.1}. FT NON_TER 336 336 {ECO:0000313|EMBL:BAS50177.1}. SQ SEQUENCE 336 AA; 38340 MW; 76561AAB2EEAF1BC CRC64; SCDGMGDVSE KHGSGPAVPE KAVRFSFTVM KITIAHGSQN VQVFEEAKPN SELCCKPLCL MLADESDHET LTAILSPLIA EREAMKSSQL MLEMGGILRT FKFIFRGTGY DEKLVREVEG LEASGSVYIC TLCDATRLEA SQNLVFHSIT RSHTENLERY EVWRSNPYHE SVEELRDRVK GVSAKPFIET VPSIDALHCD IGNAAEFYKI FQLEIGEVYK NPNASKEERK RWQATLDKHL RKKMNLKPIM RMNGNFARKL MTKETVEAVC ELIPSEERHA ALRELMDLYL KMKPVWRSSC PAKECPESLC QYSFNSQRFA ELLSTKFKYR YEGKIT //