ID   RAG1_GINCI              Reviewed;         106 AA.
AC   Q90523;
DT   15-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 58.
DE   RecName: Full=V(D)J recombination-activating protein 1;
DE            Short=RAG-1;
DE   Includes:
DE     RecName: Full=Endonuclease RAG1;
DE              EC=3.1.-.-;
DE   Includes:
DE     RecName: Full=E3 ubiquitin-protein ligase RAG1;
DE              EC=2.3.2.27;
DE     AltName: Full=RING-type E3 ubiquitin transferase RAG1 {ECO:0000305};
DE   Flags: Fragment;
GN   Name=rag1;
OS   Ginglymostoma cirratum (Nurse shark) (Squalus cirratus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Chondrichthyes;
OC   Elasmobranchii; Galeomorphii; Galeoidea; Orectolobiformes;
OC   Ginglymostomatidae; Ginglymostoma.
OX   NCBI_TaxID=7801;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=7806278; DOI=10.1007/bf00188438;
RA   Greenhalgh P., Steiner L.A.;
RT   "Recombination activating gene 1 (Rag1) in zebrafish and shark.";
RL   Immunogenetics 41:54-55(1995).
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. In addition to its
CC       endonuclease activity, RAG1 also acts as an E3 ubiquitin-protein ligase
CC       that mediates monoubiquitination of histone H3. Histone H3
CC       monoubiquitination is required for the joining step of V(D)J
CC       recombination (By similarity). {ECO:0000250}.
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;
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC       Note=Binds 1 divalent metal cation per subunit. Mg(2+) or Mn(2+).
CC       {ECO:0000250};
CC   -!- SUBUNIT: Homodimer. Component of the RAG complex composed of core
CC       components rag1 and rag2 (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the RAG1 family. {ECO:0000305}.
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DR   EMBL; U13982; AAA62610.1; -; Genomic_DNA.
DR   PIR; I50584; I50584.
DR   AlphaFoldDB; Q90523; -.
DR   SMR; Q90523; -.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0004519; F:endonuclease activity; ISS:UniProtKB.
DR   GO; GO:0042393; F:histone binding; ISS:UniProtKB.
DR   GO; GO:0046872; F:metal ion binding; ISS:UniProtKB.
DR   GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
DR   GO; GO:0043565; F:sequence-specific DNA binding; ISS:UniProtKB.
DR   GO; GO:0061630; F:ubiquitin protein ligase activity; IEA:InterPro.
DR   GO; GO:0004842; F:ubiquitin-protein transferase activity; ISS:UniProtKB.
DR   GO; GO:0008270; F:zinc ion binding; ISS:UniProtKB.
DR   GO; GO:0030183; P:B cell differentiation; ISS:UniProtKB.
DR   GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR   GO; GO:0010390; P:histone monoubiquitination; ISS:UniProtKB.
DR   GO; GO:0033077; P:T cell differentiation in thymus; ISS:UniProtKB.
DR   GO; GO:0033151; P:V(D)J recombination; ISS:UniProtKB.
DR   InterPro; IPR024627; RAG1.
DR   PANTHER; PTHR11539; PTHR11539; 1.
DR   Pfam; PF12940; RAG1; 1.
PE   3: Inferred from homology;
KW   Chromatin regulator; DNA recombination; DNA-binding; Endonuclease;
KW   Hydrolase; Metal-binding; Multifunctional enzyme; Nuclease; Nucleus;
KW   Transferase; Ubl conjugation pathway.
FT   CHAIN           <1..>106
FT                   /note="V(D)J recombination-activating protein 1"
FT                   /id="PRO_0000056010"
FT   BINDING         69
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   NON_TER         1
FT   NON_TER         106
SQ   SEQUENCE   106 AA;  12598 MW;  4393A3F638B910F5 CRC64;
     RSTFPTRECP ELLCQYSCNS QRFAELLRTE FKHRYEGKIT NYLHKTLAHV PEIIERDGSI
     GAWASEGNES GNKLFRRFRK MNARQSKSYE LEGILKHHWL YTSKYL