ID A0A5Q0V1H2_9PLEU Unreviewed; 500 AA. AC A0A5Q0V1H2; DT 26-FEB-2020, integrated into UniProtKB/TrEMBL. DT 26-FEB-2020, sequence version 1. DT 24-JAN-2024, entry version 14. DE RecName: Full=V(D)J recombination-activating protein 1 {ECO:0000256|ARBA:ARBA00021277, ECO:0000256|RuleBase:RU366024}; DE EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483, ECO:0000256|RuleBase:RU366024}; DE EC=3.1.-.- {ECO:0000256|RuleBase:RU366024}; DE Flags: Fragment; GN Name=RAG1 {ECO:0000313|EMBL:QGA87592.1}; OS Aseraggodes kobensis (milky spotted sole). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata; OC Carangaria; Pleuronectiformes; Pleuronectoidei; Soleidae; Aseraggodes. OX NCBI_TaxID=195596 {ECO:0000313|EMBL:QGA87592.1}; RN [1] {ECO:0000313|EMBL:QGA87592.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=WJC945 {ECO:0000313|EMBL:QGA87592.1}; RA Campbell M.A., Chanet B., Chen J.-N., Lee M.-Y., Chen W.-J.; RT "Origins and relationships of the Pleuronectoidei: Molecular and RT morphological analysis of living and fossil taxa."; RL Zool. Scr. 48:640-656(2019). 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; MK616863; QGA87592.1; -; Genomic_DNA. DR AlphaFoldDB; A0A5Q0V1H2; -. 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:0006325; P:chromatin organization; IEA:UniProtKB-KW. 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:SF0; V(D)J RECOMBINATION-ACTIVATING PROTEIN 1; 1. DR PANTHER; PTHR11539; VDJ RECOMBINATION ACTIVATING PROTEIN 1 RAG1; 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|RuleBase:RU366024}; KW Zinc {ECO:0000256|RuleBase:RU366024}; KW Zinc-finger {ECO:0000256|RuleBase:RU366024}. FT NON_TER 1 FT /evidence="ECO:0000313|EMBL:QGA87592.1" FT NON_TER 500 FT /evidence="ECO:0000313|EMBL:QGA87592.1" SQ SEQUENCE 500 AA; 57200 MW; 8BD5043D8F99A374 CRC64; QIFQPLYTLR AAEKELLPGF HQFEWQPALK NVSPSCNVGI INGLSGWASS VDDSPADTIA RRFRYDVALV SALKDLEEDI MEGLRDSGME DSACTSGFRV MIKECCDGMG DVNEKHGGGP AVPEKAVRFS FTVMSVSVRA DDEEKEVTIF SEPKPNSELS CKPLCLIFVD ESNHETLTAL LGPIVAERNA MKESRLILSM GGLPRFFRFH FRGTGYDEKM VREMEGLEAS GSTYVCTLCD SSRAEASQNL VLHSITRSHE ENLERYEIWR TNPFSESLDE LRDRVKGVTA KPFMETQPTL DALHCDIGNA TEFYKIFQDE IGEVYQKVNP SREERRSWRA ALDKQLRKKM KLKPIMRMNG NYARRLMTME SVEVVCELVP SEERREALRE LMRLYLQMKP VWRATCPAKE CPDQLCRYSF NSQRFADLLS STFKYRYNGK ITNYLHKTLA HVPEIVERDG SIGAWASEGN ESANKLFRRF RKMNARQSKT FELEDVLKHH //