ID   X2JKK3_9ACTI            Unreviewed;       414 AA.
AC   X2JKK3;
DT   11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT   11-JUN-2014, sequence version 1.
DT   24-JAN-2024, entry version 20.
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: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., Friedman M.;
RT   "Boom and bust: ancient and recent diversification in bichirs
RT   (polypteridae: actinopterygii), a relictual lineage of ray-finned 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 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; KF792588; AHN66335.1; -; Genomic_DNA.
DR   AlphaFoldDB; X2JKK3; -.
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   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|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:AHN66335.1"
FT   NON_TER         414
FT                   /evidence="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
//