ID F8SXI4_9SCIU Unreviewed; 423 AA. AC F8SXI4; DT 21-SEP-2011, integrated into UniProtKB/TrEMBL. DT 21-SEP-2011, sequence version 1. DT 31-JUL-2019, entry version 41. 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; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciuromorpha; OC Sciuridae; 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 RT and 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 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|PROSITE- CC ProRule:PRU00820, 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, CC with each NBD making contact with both DNA molecules. Each RSS is CC composed of well-conserved heptamer (consensus 5'-CACAGTG-3') and CC nonamer (consensus 5'-ACAAAAACC-3') sequences separated by a CC spacer of either 12 bp or 23 bp. {ECO:0000256|PROSITE- CC 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 CC of 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 RING-type. {ECO:0000259|PROSITE:PS50089}. FT DOMAIN 321 350 RAG1-type. {ECO:0000259|PROSITE:PS51765}. FT DOMAIN 359 423 NBD. {ECO:0000259|PROSITE:PS51487}. FT REGION 1 63 Disordered. {ECO:0000256|SAM:MobiDB- FT lite}. FT COMPBIAS 1 24 Polyampholyte. {ECO:0000256|SAM:MobiDB- FT lite}. FT NON_TER 1 1 {ECO:0000313|EMBL:AEI73032.1}. FT NON_TER 423 423 {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 //