ID I6U8P6_ACISI Unreviewed; 505 AA. AC I6U8P6; DT 03-OCT-2012, integrated into UniProtKB/TrEMBL. DT 03-OCT-2012, sequence version 1. DT 03-JUL-2019, entry version 7. 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=RAG-1 {ECO:0000313|EMBL:AFM84470.1}; OS Acipenser sinensis (Chinese sturgeon). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Chondrostei; Acipenseriformes; Acipenseridae; OC Acipenser. OX NCBI_TaxID=61970 {ECO:0000313|EMBL:AFM84470.1}; RN [1] {ECO:0000313|EMBL:AFM84470.1} RP NUCLEOTIDE SEQUENCE. RX PubMed=22720083; DOI=10.1371/journal.pone.0039256; RA Shen X.X., Liang D., Zhang P.; RT "The development of three long universal nuclear protein-coding locus RT markers and their application to osteichthyan phylogenetics with RT nested PCR."; RL PLoS ONE 7:E39256-E39256(2012). 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; JQ929572; AFM84470.1; -; 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:AFM84470.1}. FT NON_TER 505 505 {ECO:0000313|EMBL:AFM84470.1}. SQ SEQUENCE 505 AA; 57644 MW; 34E8691677C7373F CRC64; YRTVKATSGR QIFQPLHALR NAEKVLLPGY HPFEWQPALK NVSSSTEVGI IDGLSGWTVS VEDSQMDTIA RRFRYDAALV SALKDLEEDI LEGINEQGLD DSSTEVFTVV IKESCDGMGD VSEKHGGGPL LPEKAIRFSF TIMSIATKNE DGENINVFQE HKPNSELCCK PLCLMFADES DHETLTAILG PVLAEREAMK ESRLILEIGG LSRSFRFIFR GTGYDEKLVR DVEGLEASGS TYICTLCDAT RGEAAQNMVL HSVTRNHEEN LDRYEIWRSN PYSESVDELR DRVKGVSAKP FMETQPSIDA LHCDIGNATE FYKIFQDEIG EVYQNHNPTH EERKRWQSAL DKQLRKKMNL RPVMRMNGNF ARKLMTKETV EAVCELVPSE ERREALRELV HLYIQMKPVW RANCPAKECP DLPCRYSFNS QRFAELLSTT FKYRYDGKIT NYLHKTLAHV PEIIEREGSI GAWASEGNES GNKLFRRFRK MNARQSKCYE LEDIL //