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Database: UniProt
Entry: Q06XB1_STUCI
LinkDB: Q06XB1_STUCI
Original site: Q06XB1_STUCI 
ID   Q06XB1_STUCI            Unreviewed;       957 AA.
AC   Q06XB1;
DT   31-OCT-2006, integrated into UniProtKB/TrEMBL.
DT   31-OCT-2006, sequence version 1.
DT   13-SEP-2023, entry version 80.
DE   RecName: Full=V(D)J recombination-activating protein 1 {ECO:0000256|ARBA:ARBA00021277, ECO:0000256|RuleBase:RU366024};
DE            EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483, ECO:0000256|RuleBase:RU366024};
DE            EC=3.1.-.- {ECO:0000256|RuleBase:RU366024};
DE   Flags: Fragment;
GN   Name=RAG1 {ECO:0000313|EMBL:ABF01036.1};
OS   Sturnus cineraceus (Grey starling).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Passeriformes; Sturnidae; Sturnus.
OX   NCBI_TaxID=36269 {ECO:0000313|EMBL:ABF01036.1};
RN   [1] {ECO:0000313|EMBL:ABF01036.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=16806992; DOI=10.1016/j.ympev.2006.05.007;
RA   Zuccon D., Cibois A., Pasquet E., Ericson P.G.;
RT   "Nuclear and mitochondrial sequence data reveal the major lineages of
RT   starlings, mynas and related taxa.";
RL   Mol. Phylogenet. Evol. 41:333-344(2006).
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|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}.
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DR   EMBL; DQ466808; ABF01036.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q06XB1; -.
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:0006325; P:chromatin organization; IEA:UniProtKB-KW.
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   CDD; cd16530; RING-HC_RAG1; 1.
DR   Gene3D; 6.10.140.510; -; 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; 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; 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   ECO:0000256|RuleBase:RU366024};
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          257..295
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50089"
FT   DOMAIN          318..347
FT                   /note="RAG1-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51765"
FT   DOMAIN          358..425
FT                   /note="NBD"
FT                   /evidence="ECO:0000259|PROSITE:PS51487"
FT   DNA_BIND        358..425
FT                   /note="NBD"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00820"
FT   REGION          1..51
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        11..51
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:ABF01036.1"
FT   NON_TER         957
FT                   /evidence="ECO:0000313|EMBL:ABF01036.1"
SQ   SEQUENCE   957 AA;  109585 MW;  CE0E119DAC0BB189 CRC64;
     KLPSFEKTPS DDSQHINKDQ AEEAVSSNEE FILHKDEAVP RGEKMESTGN RQALEEDAHA
     VKIQDNRAHQ NNLKQLCRIC GVSFKTDCYK KTYPVHGPVD DETLRLLRKK EKTATSWPDL
     IAKVFKIDVR GDVDTIHPTQ FCHNCWSIIH SKFSNTPCEV YFPRNSTMEW KPHSPNCDVC
     HTTRRGVKRK SQPPSVQRGK RAKTTREHAQ LNRGVKNQAQ INNKNLMKEI VNCKDIHLST
     KLLAVDYPLD FIKSISCQIC DHILADPVET TCRHLFCRTC ILKCIRVMGS YCPSCWYPCF
     PTDLVTPVKS FLNILDNLSI RCPVKECDEE ILHGKYGQHL SGHKEMKEGE LHSYINKGGR
     PRQHLLSLTR RAQKHRLREL KRQVKAFAEK EEGGDIKAVC MTLFLLALRA KNEHKQADEL
     EAIMQGRGSG LHPAVCLAIR INTFLSCSQY HKMYRTVKAV TGRQIFQPLH ALRTAEKALL
     PGYHPFEWNP PLKNVSTNTE VGIIDGLSGL PLSIDDYPVD TIAKRFRYDA ALVCALKDME
     EEILEGMKAK NLDDYLNGPF TVVIKESCDG MGDVSEKHGS GPAVPEKAVR FSFTVMNISI
     THENESKRIF EEVKPNSELC CKPLCLMLAD ESDHETLTAI LSPLIAEREA MKNSELLLEM
     GGILRTFRFV FRGTGYDEKL VREVEGLEAS GSTYICTLCD ATRSEASQNL VFHSITRSHA
     ENLERYEIWR SNPYHESVDE LRHRVKGVSA KPFIETVPSI DALHCDIGNA TEFYRIFQME
     IGELYKNPDV SKEERKRWQL TLDKHLRKKM NLKPMLKMSG NFARKLMSKE TVEAVCELIT
     CEERHEALKE LMDLYLKMKP VWRSSCPAKE CPELLCQYSY NSQRFAELLS TKFKYRYEGK
     ITNYFHKTLA HVPEIIERDG SIGAWASEGN ESGNKLFRRF RKMNARQSKV YEMEDVL
//
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