ID Q5DWP3_MOGIN Unreviewed; 336 AA.
AC Q5DWP3;
DT 29-MAR-2005, integrated into UniProtKB/TrEMBL.
DT 29-MAR-2005, sequence version 1.
DT 03-JUL-2019, entry version 21.
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:BAD90554.1};
OS Mogera insularis (Insular mole) (Talpa insularis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Laurasiatheria; Eulipotyphla; Talpidae; Mogera.
OX NCBI_TaxID=114413 {ECO:0000313|EMBL:BAD90554.1};
RN [1] {ECO:0000313|EMBL:BAD90554.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=MH6860 {ECO:0000313|EMBL:BAD90554.1};
RX PubMed=15613798; DOI=10.2108/zsj.21.1177;
RA Shinohara A., Suzuki H., Tsuchiya K., Zhang Y.P., Luo J., Jiang X.L.,
RA Wang Y.X., Campbell K.L.;
RT "Evolution and biogeography of talpid moles from continental East Asia
RT and the Japanese islands inferred from mitochondrial and nuclear gene
RT sequences.";
RL Zool. Sci. 21:1177-1185(2004).
RN [2] {ECO:0000313|EMBL:BAP16101.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=SIK0587 {ECO:0000313|EMBL:BAP16101.1};
RA Shinohara A., Kawada S., Son N.T., Koshimoto C., Endo H., Can D.N.,
RA Suzuki H.;
RT "Molecular phylogeny of East and Southeast Asian fossorial moles
RT (Lipotyphla, Talpidae).";
RL J. Mammal. 95:455-466(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; AB176544; BAD90554.1; -; Genomic_DNA.
DR EMBL; AB823158; BAP16101.1; -; 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:BAD90554.1}.
FT NON_TER 336 336 {ECO:0000313|EMBL:BAD90554.1}.
SQ SEQUENCE 336 AA; 38312 MW; 469D0C410646DFB8 CRC64;
SCDGMGDVSE KHGSGPAVPE KAVRFSFTVM KITIAHGSQN VKVFEEAKPN SELCCKPLCL
MLADESDHET LTAILSPLIA EREAMKSSQL MLEMGGILRT FKFIFRGTGY DEKLVREVEG
LEASGSVYIC TLCDATRLEA SQNLVFHSIT RSHTENLERY EVWRSNPYHE SVEELRDRVK
GVSAKPFIET VPSIDALHCD IGNAAEFYKI FQLEIGEVYK NPNASKEERK RWQATLDKHL
RKKMNLKPIM RMNGNFARKL MTKETVEAVC ELIPSEERHA ALQELMDLYL KMKPVWRSSC
PAKECPESLC QYSFNSQRFA ELLSTKFKYR YEGKIT
//