ID   A0A4Y5U3Q7_KASSE        Unreviewed;       307 AA.
AC   A0A4Y5U3Q7;
DT   18-SEP-2019, integrated into UniProtKB/TrEMBL.
DT   18-SEP-2019, sequence version 1.
DT   03-MAY-2023, entry version 13.
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:QDC18297.1};
OS   Kassina senegalensis (Senegal running frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Neobatrachia; Microhyloidea; Hyperoliidae; Kassina.
OX   NCBI_TaxID=8415 {ECO:0000313|EMBL:QDC18297.1};
RN   [1] {ECO:0000313|EMBL:QDC18297.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=31140573;
RA   Portik D.M., Bell R.C., Blackburn D.C., Bauer A.M., Barratt C.D.,
RA   Branch W.R., Burger M., Channing A., Colston T.J., Conradie W.,
RA   Dehling J.M., Drewes R.C., Ernst R., Greenbaum E., Gvozdik V., Harvey J.,
RA   Hillers A., Hirschfeld M., Jongsma G.F.M., Kielgast J., Kouete M.T.,
RA   Lawson L.P., Leache A.D., Loader S.P., Lotters S., Meijden A.V.,
RA   Menegon M., Muller S., Nagy Z.T., Ofori-Boateng C., Ohler A.,
RA   Papenfuss T.J., Rossler D., Sinsch U., Rodel M.O., Veith M., Vindum J.,
RA   Zassi-Boulou A.G., McGuire J.A.;
RT   "Sexual Dichromatism Drives Diversification within a Major Radiation of
RT   African Amphibians.";
RL   Syst. Biol. 0:0-0(2019).
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|RuleBase:RU366024}.
CC   -!- SIMILARITY: Belongs to the RAG1 family.
CC       {ECO:0000256|RuleBase:RU366024}.
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DR   EMBL; MK498179; QDC18297.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A4Y5U3Q7; -.
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: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   InterPro; IPR024627; RAG1.
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.
PE   3: Inferred from homology;
KW   Chromatin regulator {ECO:0000256|RuleBase:RU366024};
KW   DNA recombination {ECO:0000256|ARBA:ARBA00023172,
KW   ECO:0000256|RuleBase:RU366024};
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|RuleBase:RU366024};
KW   Endonuclease {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|RuleBase:RU366024};
KW   Nuclease {ECO:0000256|RuleBase:RU366024};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|RuleBase:RU366024};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU366024};
KW   Ubl conjugation pathway {ECO:0000256|RuleBase:RU366024};
KW   Zinc {ECO:0000256|RuleBase:RU366024};
KW   Zinc-finger {ECO:0000256|RuleBase:RU366024}.
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:QDC18297.1"
FT   NON_TER         307
FT                   /evidence="ECO:0000313|EMBL:QDC18297.1"
SQ   SEQUENCE   307 AA;  35692 MW;  E988EB3E65CEAFDE CRC64;
     LIAEREAMKS SELMLEIGGI LRNFKFIFRG TGYDEKLVRE VEGLEASGSI YICTLCDATR
     LEASQNLVFH SITRSHSENL QRYETWRANP YNESADELRD RVKGVSAKPF IETLPSIDAL
     HCDIGNAAEF YRIFQLEIGE VYKNPNATKE ERKKWQTILD KHLRKKMNLK PIMRMNGNFA
     RKLMTKETAE AVCELLHSEE RQVAVKELMD LYLNMKPVWR SSCPAKECPE LLCQYSYHSQ
     RFAELLSTKF KYRYQGKITN YFHKTLAHVP EIIERDGSIG AWASEGNESG NKLFRRFRKM
     NARQSKI
//