ID A0A5Q0V1H2_9PLEU Unreviewed; 500 AA.
AC A0A5Q0V1H2;
DT 26-FEB-2020, integrated into UniProtKB/TrEMBL.
DT 26-FEB-2020, sequence version 1.
DT 29-SEP-2021, entry version 8.
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:QGA87592.1};
OS Aseraggodes kobensis (milky spotted sole).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Carangaria; Pleuronectiformes; Pleuronectoidei; Soleidae; Aseraggodes.
OX NCBI_TaxID=195596 {ECO:0000313|EMBL:QGA87592.1};
RN [1] {ECO:0000313|EMBL:QGA87592.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=WJC945 {ECO:0000313|EMBL:QGA87592.1};
RA Campbell M.A., Chanet B., Chen J.-N., Lee M.-Y., Chen W.-J.;
RT "Origins and relationships of the Pleuronectoidei: Molecular and
RT morphological analysis of living and fossil taxa.";
RL Zool. Scr. 48:640-656(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; MK616863; QGA87592.1; -; Genomic_DNA.
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: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; 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|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:QGA87592.1"
FT NON_TER 500
FT /evidence="ECO:0000313|EMBL:QGA87592.1"
SQ SEQUENCE 500 AA; 57200 MW; 8BD5043D8F99A374 CRC64;
QIFQPLYTLR AAEKELLPGF HQFEWQPALK NVSPSCNVGI INGLSGWASS VDDSPADTIA
RRFRYDVALV SALKDLEEDI MEGLRDSGME DSACTSGFRV MIKECCDGMG DVNEKHGGGP
AVPEKAVRFS FTVMSVSVRA DDEEKEVTIF SEPKPNSELS CKPLCLIFVD ESNHETLTAL
LGPIVAERNA MKESRLILSM GGLPRFFRFH FRGTGYDEKM VREMEGLEAS GSTYVCTLCD
SSRAEASQNL VLHSITRSHE ENLERYEIWR TNPFSESLDE LRDRVKGVTA KPFMETQPTL
DALHCDIGNA TEFYKIFQDE IGEVYQKVNP SREERRSWRA ALDKQLRKKM KLKPIMRMNG
NYARRLMTME SVEVVCELVP SEERREALRE LMRLYLQMKP VWRATCPAKE CPDQLCRYSF
NSQRFADLLS STFKYRYNGK ITNYLHKTLA HVPEIVERDG SIGAWASEGN ESANKLFRRF
RKMNARQSKT FELEDVLKHH
//