ID   X2JKK3_9ACTI            Unreviewed;       414 AA.
AC   X2JKK3;
DT   11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT   11-JUN-2014, sequence version 1.
DT   03-JUL-2019, entry version 7.
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:AHN66335.1};
OS   Polypterus palmas polli.
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Polypteriformes; Polypteridae; Polypterus.
OX   NCBI_TaxID=764553 {ECO:0000313|EMBL:AHN66335.1};
RN   [1] {ECO:0000313|EMBL:AHN66335.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=PpolB {ECO:0000313|EMBL:AHN66335.1};
RX   PubMed=24274466; DOI=10.1111/evo.12323;
RA   Near T.J., Dornburg A., Tokita M., Suzuki D., Brandley M.C.,
RA   Friedman M.;
RT   "Boom and bust: ancient and recent diversification in bichirs
RT   (polypteridae: actinopterygii), a relictual lineage of ray-finned
RT   fishes.";
RL   Evolution 68:1014-1026(2014).
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; KF792588; AHN66335.1; -; Genomic_DNA.
DR   GO; GO:0004519; F:endonuclease activity; IEA:InterPro.
DR   GO; GO:0043565; F:sequence-specific DNA binding; IEA:InterPro.
DR   GO; GO:0061630; F:ubiquitin protein ligase activity; IEA:InterPro.
DR   GO; GO:0033151; P:V(D)J recombination; IEA:InterPro.
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:AHN66335.1}.
FT   NON_TER     414    414       {ECO:0000313|EMBL:AHN66335.1}.
SQ   SEQUENCE   414 AA;  47201 MW;  E638601A3C64198F CRC64;
     YEWQPSLKNV SSNTEVGIID GLSGWKASVD DAQMDTIARR FRYDVAMVAA LKDLEEDILE
     GIKEHELDDS STEIFTVTIK ESCDGMGDVS EKHGGGPALP EKAVRYSFTI MSIATRDEEG
     NNVMIFQESK PNSELCCKPL CLMFADESDH ETLTAILGPV VAEREAMKES RLILDIGGLS
     RCFRFIFRGT GYDEKLVREL EGLEASGSTY ICTLCDSTRV EASRNMILHT ITRSHEENLE
     RYEIWRSNPF SESADDLRDR VKGVSAKPFM ETHPSIDALH CDIGNAAEFY KIFQDEIGEV
     FQNPNPPKEE RKRWQSALDK QLRKKMNLKP IMRMNGNFAR KLITSEAVEA ICELVPSEER
     KEALRELVNL YLQMKPVWRS TCPLKECPDL LCRYSFNSQR FAELLSSTFS YRYD
//