ID C7AAS2_MUSST Unreviewed; 930 AA. AC C7AAS2; DT 22-SEP-2009, integrated into UniProtKB/TrEMBL. DT 22-SEP-2009, sequence version 1. DT 02-JUN-2021, entry version 55. 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:ACT37615.1}; OS Muscicapa striata (Spotted flycatcher) (Setophaga striata). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda; OC Coelurosauria; Aves; Neognathae; Passeriformes; Passeroidea; Parulidae; OC Setophaga. OX NCBI_TaxID=1212470 {ECO:0000313|EMBL:ACT37615.1}; RN [1] {ECO:0000313|EMBL:ACT37615.1} RP NUCLEOTIDE SEQUENCE. RA Gelang M., Cibois A., Pasquet E., Olsson U., Alstrom P., Ericson P.G.P.; RT "Phylogeny of babblers (Aves, Passeriformes): major lineages, family limits RT and classification."; RL Zool. Scr. 38:225-236(2009). 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|ARBA:ARBA00001936}; 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 --------------------------------------------------------------------------- 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; FJ358149; ACT37615.1; -; 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; IPR018957; Znf_C3HC4_RING-type. 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; PF00097; zf-C3HC4; 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|ARBA:ARBA00022853, KW ECO:0000256|RuleBase:RU366024}; Coiled coil {ECO:0000256|SAM:Coils}; KW DNA recombination {ECO:0000256|ARBA:ARBA00023172, ECO:0000256|PROSITE- KW ProRule:PRU00820}; KW DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|PROSITE- KW ProRule:PRU00820}; KW Endonuclease {ECO:0000256|ARBA:ARBA00022759, KW 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|ARBA:ARBA00023268, KW ECO:0000256|RuleBase:RU366024}; KW Nuclease {ECO:0000256|ARBA:ARBA00022722, ECO:0000256|RuleBase:RU366024}; KW Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|PROSITE- KW ProRule:PRU00820}; KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU366024}; KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786, KW ECO:0000256|RuleBase:RU366024}; KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU366024}; KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE- KW ProRule:PRU01101}. FT DOMAIN 256..294 FT /note="RING-type" FT /evidence="ECO:0000259|PROSITE:PS50089" FT DOMAIN 317..346 FT /note="RAG1-type" FT /evidence="ECO:0000259|PROSITE:PS51765" FT DOMAIN 357..424 FT /note="NBD" FT /evidence="ECO:0000259|PROSITE:PS51487" FT DNA_BIND 357..424 FT /note="NBD" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00820" FT REGION 1..46 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COILED 369..389 FT /evidence="ECO:0000256|SAM:Coils" FT COMPBIAS 1..41 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT NON_TER 1 FT /evidence="ECO:0000313|EMBL:ACT37615.1" FT NON_TER 930 FT /evidence="ECO:0000313|EMBL:ACT37615.1" SQ SEQUENCE 930 AA; 106327 MW; 2814CB19A265CA47 CRC64; KLRSFEKTPS DDSQHXNKDQ AEEASSNKEL ILHKDEAVPS GEKMELMGNR QALEEDAHAM KTQDNRAHQN NLKQLCRICG VSFKTDCHKK TYPVHGPVDD ETLRLLRKKE KTATSWPDLI TKVFKIDVRG DVDTIHPTHF CHNCWSIIHS KYSNTLCEVY FPRNSTMEWQ PHSPNCDVCH XIRRGVKRKS QPPSVQRGKR VKTTGERAQL NRGVKNQAQI NNKNLMKEIV NCKDIHLSTK LLAVDYPPDF IKSISCQVCD HILADPVETT CRHLFCRTCI LKCIRVMGSY CPSCWYPCFP TDLVTPVKSF LNILDNLSIR CPVEECDEEI MHGRYGQHLS GHKEMKDREL PSYINKGGRP RQHLLSLTRR AQKHRLRELK RQVKAFAEKE EGGDIKAVCM TLFLLALRAK NEHKQADELE AIMQGRGSGL HPAVCLAIRI NTFLSCSQYH KMYRTVKAVT GRQIFQPLHA LRTAEKALLP GYHPFEWNPP LKNVSTNTEV GIIDGLSGLP LSIDDYPVDT IAKRFRYDAA LVCALKDMEE EILEGMKAKN LDDYLNGPFT VVIKESCDGM GDVSEKHGSG PAVPEKAVRF SFTVMNISIA HGNESKRIFE EVKPNSELCC KPLCLMLADE SDHETLTAIL SPLIAEREAM KNSELLLEMG GILRTFRFVF RGTGYDEKLV REVEGLEASG STYICTLCDA TRLEASQNLV FHSITRSHAE NLERYEIWRS NPYHESVDEL RDRVKGVSAK PFIETVPSID ALHCDIGNAT EFYRIFQMEI GELYKNPDVS KEERKRWQMT LDKHLRKKMN LKPMLKMSGN FARKLMSKET VEAVCELITC EERHEALKEL MDLYLKMKPV WRSSCPAKEC PELLCQYSYN SQRFAELLST KFKYRYEGKI TNYFHKTLAH VPEIIERDGS IGAWASEGNE //