ID   A0A4Y5U3Q7_KASSE        Unreviewed;       307 AA.
AC   A0A4Y5U3Q7;
DT   18-SEP-2019, integrated into UniProtKB/TrEMBL.
DT   18-SEP-2019, sequence version 1.
DT   16-OCT-2019, entry version 2.
DE   RecName: Full=V(D)J recombination-activating protein 1 {ECO:0000256|RuleBase:RU366024};
DE            EC=2.3.2.27 {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;
OC   Amphibia; Batrachia; Anura; Neobatrachia; Microhyloidea; Hyperoliidae;
OC   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.,
RA   Harvey J., Hillers A., Hirschfeld M., Jongsma G.F.M., Kielgast J.,
RA   Kouete M.T., Lawson L.P., Leache A.D., Loader S.P., Lotters S.,
RA   Meijden A.V., Menegon M., Muller S., Nagy Z.T., Ofori-Boateng C.,
RA   Ohler A., Papenfuss T.J., Rossler D., Sinsch U., Rodel M.O., Veith M.,
RA   Vindum J., Zassi-Boulou A.G., McGuire J.A.;
RT   "Sexual Dichromatism Drives Diversification within a Major Radiation
RT   of 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
CC       of immunoglobulin and T-cell receptor genes in developing B and T-
CC       lymphocytes through rearrangement of different V (variable), in
CC       some cases D (diversity), and J (joining) gene segments. In the
CC       RAG complex, RAG1 mediates the DNA-binding to the conserved
CC       recombination signal sequences (RSS) and catalyzes the DNA
CC       cleavage activities by introducing a double-strand break between
CC       the RSS and the adjacent coding segment. RAG2 is not a catalytic
CC       component but is required for all known catalytic activities. DNA
CC       cleavage occurs in 2 steps: a first nick is introduced in the top
CC       strand immediately upstream of the heptamer, generating a 3'-
CC       hydroxyl group that can attack the phosphodiester bond on the
CC       opposite strand in a direct transesterification reaction, thereby
CC       creating 4 DNA ends: 2 hairpin coding ends and 2 blunt, 5'-
CC       phosphorylated ends. {ECO:0000256|RuleBase:RU366024}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-
CC         cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-
CC         conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor
CC         protein]-L-lysine.; EC=2.3.2.27;
CC         Evidence={ECO:0000256|RuleBase:RU366024};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={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   InterPro; IPR024627; RAG1.
DR   PANTHER; PTHR11539; PTHR11539; 1.
DR   Pfam; PF12940; RAG1; 1.
PE   3: Inferred from homology;
KW   Chromatin regulator {ECO:0000256|RuleBase:RU366024};
KW   DNA recombination {ECO:0000256|RuleBase:RU366024};
KW   DNA-binding {ECO:0000256|RuleBase:RU366024};
KW   Endonuclease {ECO:0000256|RuleBase:RU366024};
KW   Hydrolase {ECO:0000256|RuleBase:RU366024};
KW   Metal-binding {ECO:0000256|RuleBase:RU366024};
KW   Multifunctional enzyme {ECO:0000256|RuleBase:RU366024};
KW   Nuclease {ECO:0000256|RuleBase:RU366024};
KW   Nucleus {ECO:0000256|RuleBase:RU366024};
KW   Transferase {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      1       {ECO:0000313|EMBL:QDC18297.1}.
FT   NON_TER     307    307       {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
//