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Database: UniProt
Entry: G9HTT6_9SAUR
LinkDB: G9HTT6_9SAUR
Original site: G9HTT6_9SAUR 
ID   G9HTT6_9SAUR            Unreviewed;       346 AA.
AC   G9HTT6;
DT   22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT   22-FEB-2012, sequence version 1.
DT   24-JAN-2024, entry version 49.
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:AEW27020.1};
OS   Gehyra oceanica (Pacific dtella).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Gekkota; Gekkonidae; Gekkoninae; Gehyra.
OX   NCBI_TaxID=747213 {ECO:0000313|EMBL:AEW27020.1};
RN   [1] {ECO:0000313|EMBL:AEW27020.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Heinicke M.P., Greenbaum E., Jackman T.R., Bauer A.M.;
RT   "Phylogeny of a trans-Wallacean radiation (Squamata, Gekkonidae, Gehyra)
RT   supports a single early colonization of Australia.";
RL   Zool. Scr. 40:584-602(2011).
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; JN393967; AEW27020.1; -; Genomic_DNA.
DR   AlphaFoldDB; G9HTT6; -.
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:0042803; F:protein homodimerization activity; IEA:UniProtKB-UniRule.
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:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR   GO; GO:0033151; P:V(D)J recombination; IEA:InterPro.
DR   CDD; cd16530; RING-HC_RAG1; 1.
DR   Gene3D; 3.30.160.60; Classic Zinc Finger; 1.
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; IPR019485; RAG1_Znf.
DR   InterPro; IPR036236; Znf_C2H2_sf.
DR   InterPro; IPR018957; Znf_C3HC4_RING-type.
DR   InterPro; IPR001841; Znf_RING.
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   Pfam; PF10426; zf-RAG1; 1.
DR   SMART; SM00184; RING; 1.
DR   SUPFAM; SSF57667; beta-beta-alpha zinc fingers; 1.
DR   SUPFAM; SSF57850; RING/U-box; 1.
DR   PROSITE; PS51765; ZF_RAG1; 1.
DR   PROSITE; PS00518; ZF_RING_1; 1.
DR   PROSITE; PS50089; ZF_RING_2; 1.
PE   4: Predicted;
KW   DNA recombination {ECO:0000256|ARBA:ARBA00023172};
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
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, ECO:0000256|PROSITE-
KW   ProRule:PRU01101}.
FT   DOMAIN          252..291
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50089"
FT   DOMAIN          313..342
FT                   /note="RAG1-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51765"
FT   REGION          1..20
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..19
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:AEW27020.1"
FT   NON_TER         346
FT                   /evidence="ECO:0000313|EMBL:AEW27020.1"
SQ   SEQUENCE   346 AA;  39441 MW;  965F2909E44E6FC9 CRC64;
     KSLPEESHLA NNDNGKVAAS SDKVNDAMTL MLQDPFHRGQ NLNNSTQTVD KDVFSVSQRE
     IEAHQVNLQH LCRICGGSFK NDPYKRNHPV HGPVDDEMQA LLRKKERRAT SWPDLLNKVF
     KTDVRGDMDT IHPTNFCHNC RSVIQRKFSN VPCEMYFPRK GTMEWQPHST SCNVCGTSPH
     GIKRKKQAPS PQGRKKLRII AERARKIMYA RSQKQVNSKT IMKKITNCKK IHLSTKMLTV
     DYPVDFVKSI SCQICEHILA DPVETSCKHL FCRLCILKCL KVIGSFCPSC RYPCFPTDLV
     NPVRSFLSIL NTLAVRCPVK DCHEEVTLGK YSHHLVSHKE KKDKGT
//
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