ID F8SXI4_9SCIU Unreviewed; 423 AA. AC F8SXI4; DT 21-SEP-2011, integrated into UniProtKB/TrEMBL. DT 21-SEP-2011, sequence version 1. DT 11-DEC-2019, entry version 42. 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:AEI73032.1}; OS Tamiops maritimus (maritime striped squirrel). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Glires; Rodentia; Sciuromorpha; Sciuridae; OC Callosciurinae; Callosciurini; Tamiops. OX NCBI_TaxID=1048687 {ECO:0000313|EMBL:AEI73032.1}; RN [1] {ECO:0000313|EMBL:AEI73032.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=TW3 {ECO:0000313|EMBL:AEI73032.1}; RA Chang S.-W., Oshida T., Endo H., Nguyen S.T., Dang C.N., Nguyen D.X., RA Jiang X., Li Z.-J., Lin L.-K.; RT "Ancient hybridization and underestimated species diversity in Asian RT striped squirrels (genus Tamiops): inference from paternal, maternal and RT biparental markers."; RL J. Zool. (Lond.) 285:128-138(2011). 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|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|PROSITE-ProRule:PRU00820, CC ECO:0000256|RuleBase:RU366024}. CC -!- DOMAIN: The NBD (nonamer binding) DNA-binding domain mediates the CC specific binding to the nonamer RSS motif by forming a tightly CC interwoven homodimer that binds and synapses 2 nonamer elements, with CC each NBD making contact with both DNA molecules. Each RSS is composed CC of well-conserved heptamer (consensus 5'-CACAGTG-3') and nonamer CC (consensus 5'-ACAAAAACC-3') sequences separated by a spacer of either CC 12 bp or 23 bp. {ECO:0000256|PROSITE-ProRule:PRU00820}. CC -!- SIMILARITY: Belongs to the RAG1 family. {ECO:0000256|PROSITE- CC ProRule:PRU00820, ECO:0000256|RuleBase:RU366024}. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00820}. 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; HQ698449; AEI73032.1; -; 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 Gene3D; 3.30.40.10; -; 1. DR InterPro; IPR024627; RAG1. DR InterPro; IPR035714; RAG1_imp-bd. DR InterPro; IPR019485; RAG1_Znf. DR InterPro; IPR023336; RAG_nonamer-bd_dom. DR InterPro; IPR036236; Znf_C2H2_sf. DR InterPro; IPR001841; Znf_RING. DR InterPro; IPR013083; Znf_RING/FYVE/PHD. DR InterPro; IPR017907; Znf_RING_CS. DR PANTHER; PTHR11539; PTHR11539; 1. DR Pfam; PF12940; RAG1; 1. DR Pfam; PF12560; RAG1_imp_bd; 1. DR Pfam; PF10426; zf-RAG1; 1. DR SMART; SM00184; RING; 1. DR SUPFAM; SSF57667; SSF57667; 1. DR PROSITE; PS51487; NBD; 1. DR PROSITE; PS51765; ZF_RAG1; 1. DR PROSITE; PS00518; ZF_RING_1; 1. DR PROSITE; PS50089; ZF_RING_2; 1. PE 3: Inferred from homology; KW Chromatin regulator {ECO:0000256|RuleBase:RU366024}; KW DNA recombination {ECO:0000256|PROSITE-ProRule:PRU00820, KW ECO:0000256|RuleBase:RU366024}; KW DNA-binding {ECO:0000256|PROSITE-ProRule:PRU00820, KW 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|PROSITE-ProRule:PRU00820, KW 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|PROSITE-ProRule:PRU00175, KW ECO:0000256|RuleBase:RU366024}. FT DOMAIN 260..299 FT /note="RING-type" FT /evidence="ECO:0000259|PROSITE:PS50089" FT DOMAIN 321..350 FT /note="RAG1-type" FT /evidence="ECO:0000259|PROSITE:PS51765" FT DOMAIN 359..423 FT /note="NBD" FT /evidence="ECO:0000259|PROSITE:PS51487" FT REGION 1..63 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1..24 FT /note="Polyampholyte" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT NON_TER 1 FT /evidence="ECO:0000313|EMBL:AEI73032.1" FT NON_TER 423 FT /evidence="ECO:0000313|EMBL:AEI73032.1" SQ SEQUENCE 423 AA; 48575 MW; 798329AA2A2360B8 CRC64; RVRSLEKTTE ETQKEKKDSS EEKPPLEQSP AVLDKSGGQK PVLTQPALKG HPKFSKKFHD GGKARDKAIH QANLRHFCRI CGNSFKTDEH NRRYPVHGPV DAKTQVLLRK KEKRVTSWPD LIARVFRIDV RADVDAIHPT EFCHNCWNIM HRKFSSAPCE VYFPRNATME WHPHTPSCDI CHFARRGLKR KRHQPNVQLS KKLKTVLDQA RQARQCKRRA QARISSKEVM KKITNCSKIH LGTNLLAVDF PAXFVKSISC QICEHILADP VETSCKHVFC RICILRCLKV MGSYCPSCRY PCFPTDLESP VKSFLSILNS LVVKCPAKEC NEEVSLEKYN HHVSSHKESK ETFVHINKGG RPRQHLLSLT RRAQKHRLRE LKLQVKAFAD KEEGGDVKSV CLTLFLLALR ARNEHRQANE LEA //