ID C7AAS2_MUSST Unreviewed; 930 AA. AC C7AAS2; DT 22-SEP-2009, integrated into UniProtKB/TrEMBL. DT 22-SEP-2009, sequence version 1. DT 07-JUN-2017, entry version 36. DE SubName: Full=Recombination activating protein 1 {ECO:0000313|EMBL:ACT37615.1}; 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; OC Parulidae; 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., RA Ericson P.G.P.; RT "Phylogeny of babblers (Aves, Passeriformes): major lineages, family RT limits and classification."; RL Zool. Scr. 38:225-236(2009). CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|PROSITE- CC ProRule:PRU00820}. 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}. 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 ProteinModelPortal; C7AAS2; -. DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell. DR GO; GO:0004519; F:endonuclease activity; IEA:InterPro. 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:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0033151; P:V(D)J recombination; IEA:UniProtKB-UniRule. DR CDD; cd00162; RING; 1. DR Gene3D; 3.30.40.10; -; 2. DR InterPro; IPR024627; RAG1. DR InterPro; IPR019485; RAG1_Znf. DR InterPro; IPR023336; RAG_nonamer-bd_dom. DR InterPro; IPR013087; Znf_C2H2_type. 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; 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 DNA recombination {ECO:0000256|PROSITE-ProRule:PRU00820}; KW DNA-binding {ECO:0000256|PROSITE-ProRule:PRU00820}; KW Metal-binding {ECO:0000256|SAAS:SAAS00547282}; KW Nucleus {ECO:0000256|PROSITE-ProRule:PRU00820}; KW Zinc {ECO:0000256|SAAS:SAAS00547042}; KW Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU01101, KW ECO:0000256|SAAS:SAAS00546951}. FT DOMAIN 256 294 RING-type. {ECO:0000259|PROSITE:PS50089}. FT DOMAIN 317 346 RAG1-type. {ECO:0000259|PROSITE:PS51765}. FT DOMAIN 357 424 NBD (nonamer binding) DNA-binding. FT {ECO:0000259|PROSITE:PS51487}. FT DNA_BIND 357 424 NBD. {ECO:0000256|PROSITE-ProRule: FT PRU00820}. FT NON_TER 1 1 {ECO:0000313|EMBL:ACT37615.1}. FT NON_TER 930 930 {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 //