ID A0A1W6R3G9_CHRAC Unreviewed; 490 AA. AC A0A1W6R3G9; DT 05-JUL-2017, integrated into UniProtKB/TrEMBL. DT 05-JUL-2017, sequence version 1. DT 02-DEC-2020, 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:ARO48906.1}; OS Chrysochir aureus (Reeve's croaker) (Otolithus aureus). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata; OC Eupercaria; Sciaenidae; Chrysochir. OX NCBI_TaxID=443774 {ECO:0000313|EMBL:ARO48906.1}; RN [1] {ECO:0000313|EMBL:ARO48906.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=WJC671 {ECO:0000313|EMBL:ARO48906.1}; RA Seilhamer J.J.; RL Submitted (AUG-2016) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:ARO48906.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=WJC671 {ECO:0000313|EMBL:ARO48906.1}; RX PubMed=28453569; RA Lo P.C., Liu S.H., Nor S.A.M., Chen W.J.; RT "Molecular exploration of hidden diversity in the Indo-West Pacific RT sciaenid clade."; RL PLoS ONE 12:E0176623-E0176623(2017). 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; KX777679; ARO48906.1; -; 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:ARO48906.1" FT NON_TER 490 FT /evidence="ECO:0000313|EMBL:ARO48906.1" SQ SEQUENCE 490 AA; 55774 MW; EF9D025838701512 CRC64; QLFQPLHALR TAEKELLPGF HPFEWQPALK NVSTSCDVGI INGLAGLTSS VDDSPADTIT RRFRYDVALV SALKDLEEDI MEGLKENGME DSACTSGFSV MIKESCDGMG DVSEKHGGGP VIPEKAVRFS FTIMSVSVLA DGEEEEVTIF TEPKPNSELS CKPLCLTFVD ESDHETLTSI LWPIVAERSA MKESRLILPI GGLLRSFRFH FRGTGYDEKM VREMEGLEAS GSTYICTLCD SSRAEASQNM VLHSITRNHE ENLERYEIWR TNPFSESAEE LRERVKGVSA KPFLETHPTL DALHCDIGNA TEFYKIFQDE IGEVYEKVNP SREERRSWRA ALDKQLRNKM KLKPVMRMNG NYARRLMTME AVEVVCELVP SEERREALRE LMRLYLQMKP VWRATCPAKE CPDQLCRYSF NSQRFADLLS SAFKYRYNGK ITNYLHKTLA HVPEIIERDG SIGAWASEGN ECANKLFRRF RKMNARQSKV //