ID A0A0M4VB73_9EUTH Unreviewed; 336 AA. AC A0A0M4VB73; DT 09-DEC-2015, integrated into UniProtKB/TrEMBL. DT 09-DEC-2015, sequence version 1. DT 02-DEC-2020, entry version 11. 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; Mammalia; OC Eutheria; Laurasiatheria; Eulipotyphla; Talpidae; 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 and RT 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., Koshimoto C.; RT "Molecular phylogenetic relationships and intra-species diversities of RT three Euroscaptor spp. (Talpidae: Lipotyphla: Mammalia) from 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 diversity of RT 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 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; 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|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|ARBA:ARBA00022786, KW ECO:0000256|RuleBase:RU366024}; Zinc {ECO:0000256|RuleBase:RU366024}; KW Zinc-finger {ECO:0000256|RuleBase:RU366024}. FT NON_TER 1 FT /evidence="ECO:0000313|EMBL:BAS50177.1" FT NON_TER 336 FT /evidence="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 //