ID Q27SA1_PHRPL Unreviewed; 350 AA. AC Q27SA1; DT 04-APR-2006, integrated into UniProtKB/TrEMBL. DT 04-APR-2006, sequence version 1. DT 29-MAY-2024, entry version 72. DE RecName: Full=V(D)J recombination-activating protein 1 {ECO:0000256|ARBA:ARBA00021277}; DE EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483}; DE Flags: Fragment; GN Name=RAG-1 {ECO:0000313|EMBL:ABD49424.1}; OS Phrynosoma platyrhinos (Desert horned lizard). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera; OC Iguania; Phrynosomatidae; Phrynosomatinae; Phrynosoma. OX NCBI_TaxID=52577 {ECO:0000313|EMBL:ABD49424.1}; RN [1] {ECO:0000313|EMBL:ABD49424.1} RP NUCLEOTIDE SEQUENCE. RX PubMed=16488160; DOI=10.1016/j.ympev.2005.12.016; RA Leache A.D., McGuire J.A.; RT "Phylogenetic relationships of horned lizards (Phrynosoma) based on nuclear RT and mitochondrial data: evidence for a misleading mitochondrial gene RT tree."; RL Mol. Phylogenet. Evol. 39:628-644(2006). 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 -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000256|ARBA:ARBA00001946}; CC -!- COFACTOR: CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; CC Evidence={ECO:0000256|ARBA:ARBA00001936}; CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|PROSITE-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, 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}. 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; DQ385419; ABD49424.1; -; Genomic_DNA. DR GO; GO:0097519; C:DNA recombinase complex; IEA:TreeGrafter. DR GO; GO:1905347; C:endodeoxyribonuclease complex; IEA:TreeGrafter. DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell. DR GO; GO:1990238; F:double-stranded DNA endonuclease activity; IEA:TreeGrafter. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. 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:0002250; P:adaptive immune response; IEA:TreeGrafter. DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW. DR GO; GO:0002331; P:pre-B cell allelic exclusion; IEA:TreeGrafter. DR GO; GO:0033151; P:V(D)J recombination; IEA:UniProtKB-UniRule. DR CDD; cd16530; RING-HC_RAG1; 1. DR Gene3D; 3.30.160.60; Classic Zinc Finger; 1. DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 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:SF0; V(D)J RECOMBINATION-ACTIVATING PROTEIN 1; 1. DR PANTHER; PTHR11539; VDJ RECOMBINATION ACTIVATING PROTEIN 1 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; beta-beta-alpha zinc fingers; 1. DR SUPFAM; SSF57850; RING/U-box; 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 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}; Endonuclease {ECO:0000256|ARBA:ARBA00022759}; KW Hydrolase {ECO:0000256|ARBA:ARBA00022801}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723}; KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268}; KW Nuclease {ECO:0000256|ARBA:ARBA00022722}; KW Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|PROSITE- KW ProRule:PRU00820}; Transferase {ECO:0000256|ARBA:ARBA00022679}; KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786}; KW Zinc {ECO:0000256|ARBA:ARBA00022833}; KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE- KW ProRule:PRU01101}. FT DOMAIN 243..282 FT /note="RING-type" FT /evidence="ECO:0000259|PROSITE:PS50089" FT DOMAIN 304..333 FT /note="RAG1-type" FT /evidence="ECO:0000259|PROSITE:PS51765" FT DOMAIN 344..350 FT /note="NBD" FT /evidence="ECO:0000259|PROSITE:PS51487" FT NON_TER 1 FT /evidence="ECO:0000313|EMBL:ABD49424.1" FT NON_TER 350 FT /evidence="ECO:0000313|EMBL:ABD49424.1" SQ SEQUENCE 350 AA; 40020 MW; 2EBCF6641497ECAA CRC64; KGKVAATLDK VIEKEIETVS LISNTPFETD TELNKGMLTT DKSVLYMSQR EVETHQANLQ HLCRFCGGSF KTDPYKRSHP VHGPVDDETQ ALLRKKEKKA TSWPDLLAKV FKIDVKGDID TVHPTKFCHQ CWTVVQKKLN NFPCEMFFPR KSLVEWHPHS PSCDVCGASF HGMKRKRKVL NPQLNKKLRM VTRSARKKRQ IRNPKQVNQK SLVKMIASCK KIHLTTKILA VDYPADFVKS XSCQICEHIL ADPVETTCKH LFCRACILKC LKIMGSYCPA CRYPCFPTDL VGPVKSFLNI LNSLPVRCPV KDCQEEVCLV KYCHHLSSHK EVEDKEGYVY INKGGRPRQH //