ID   A0A1B3B3X7_VIPBN        Unreviewed;       268 AA.
AC   A0A1B3B3X7;
DT   02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2016, 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:AOE45986.1};
OS   Vipera berus nikolskii (Nikolsky's adder) (Vipera nikolskii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Serpentes; Colubroidea; Viperidae; Viperinae; Vipera.
OX   NCBI_TaxID=1808362 {ECO:0000313|EMBL:AOE45986.1};
RN   [1] {ECO:0000313|EMBL:AOE45986.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=27480810; DOI=10.1016/j.ympev.2016.07.029;
RA   Alencar L.R., Quental T.B., Grazziotin F.G., Alfaro M.L., Martins M.,
RA   Venzon M., Zaher H.;
RT   "Diversification in vipers: Phylogenetic relationships, time of divergence
RT   and shifts in speciation rates.";
RL   Mol. Phylogenet. Evol. 105:50-62(2016).
RN   [2] {ECO:0000313|EMBL:AOE45986.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Seilhamer J.J.;
RL   Submitted (AUG-2016) to the EMBL/GenBank/DDBJ databases.
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}.
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DR   EMBL; KX695120; AOE45986.1; -; 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:AOE45986.1"
FT   NON_TER         268
FT                   /evidence="ECO:0000313|EMBL:AOE45986.1"
SQ   SEQUENCE   268 AA;  30019 MW;  8A31E9F11270303C CRC64;
     LPGYHPFEWE PPLKNVSSNT DVGIIDGLSG IQQSVDDYPV DTIAKRFRYD VALVAALMDL
     EEEILEGLKT HDLDDYLKGP FTVVIKESCD GMGDVSEKHG SGPAVPEKAV RFSFTLMSIT
     VTHDRGSARI FEESKPNSEL CCKPLCLMLA DESDHETLTA ILSPLIVERE AMKNSALILY
     MAGIPRIFKF IFRGTGYDEK LVREVEGLEA SGSTYICTLC DATRLEASQN LILHSVTRNH
     AENLERYEVW RSNPYHEAVD ELRHRVKG
//