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Database: UniProt
Entry: A5X9U1_9SAUR
LinkDB: A5X9U1_9SAUR
Original site: A5X9U1_9SAUR 
ID   A5X9U1_9SAUR            Unreviewed;       202 AA.
AC   A5X9U1;
DT   10-JUL-2007, integrated into UniProtKB/TrEMBL.
DT   10-JUL-2007, sequence version 1.
DT   24-JAN-2024, entry version 45.
DE   RecName: Full=V(D)J recombination-activating protein 1 {ECO:0000256|ARBA:ARBA00021277};
DE            EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
DE   Flags: Fragment;
GN   Name=Rag-1 {ECO:0000313|EMBL:ABI78864.1};
OS   Caledoniscincus haplorhinus.
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Scinciformata; Scincidae;
OC   Eugongylinae; Caledoniscincus.
OX   NCBI_TaxID=394121 {ECO:0000313|EMBL:ABI78864.1};
RN   [1] {ECO:0000313|EMBL:ABI78864.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=17400482; DOI=10.1016/j.ympev.2007.02.007;
RA   Smith S.A., Sadlier R.A., Bauer A.M., Austin C.C., Jackman T.;
RT   "Molecular phylogeny of the scincid lizards of New Caledonia and adjacent
RT   areas: evidence for a single origin of the endemic skinks of Tasmantis.";
RL   Mol. Phylogenet. Evol. 43:1151-1166(2007).
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   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946};
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000256|ARBA:ARBA00001936};
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DR   EMBL; DQ675281; ABI78864.1; -; Genomic_DNA.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-KW.
DR   GO; GO:0004519; F:endonuclease activity; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR   InterPro; IPR024627; RAG1.
DR   InterPro; IPR035714; RAG1_imp-bd.
DR   InterPro; IPR018957; Znf_C3HC4_RING-type.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   InterPro; IPR017907; Znf_RING_CS.
DR   PANTHER; PTHR11539:SF0; V(D)J RECOMBINATION-ACTIVATING PROTEIN 1; 1.
DR   PANTHER; PTHR11539; VDJ RECOMBINATION ACTIVATING PROTEIN 1 RAG1; 1.
DR   Pfam; PF12560; RAG1_imp_bd; 1.
DR   Pfam; PF00097; zf-C3HC4; 1.
DR   SUPFAM; SSF57850; RING/U-box; 1.
DR   PROSITE; PS00518; ZF_RING_1; 1.
PE   4: Predicted;
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT   DOMAIN          1..175
FT                   /note="RAG1 importin-binding"
FT                   /evidence="ECO:0000259|Pfam:PF12560"
FT   DOMAIN          177..201
FT                   /note="Zinc finger C3HC4 RING-type"
FT                   /evidence="ECO:0000259|Pfam:PF00097"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:ABI78864.1"
FT   NON_TER         202
FT                   /evidence="ECO:0000313|EMBL:ABI78864.1"
SQ   SEQUENCE   202 AA;  22979 MW;  0D632344E1ACCB44 CRC64;
     GGSFKXDPCK RSHPVHGPVD NVMQAVLRKK ERRATSWPEL LAKVFKIDVR GDIDTIHPXK
     FCHNCWNFIQ RKFSNVPSEV YFPRNGPMEW HPHSSGCEVC GTSTRGVKRK RQALKPQVSK
     KLRIVARCAS QVRPVRSPKK VHSKNLMKKI VNCNKIHVST KSFAVDYPAD FVKAVSCQIC
     EHVLADPVET TCKHLFCRVC IL
//
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