ID   C8CAS5_9SAUR            Unreviewed;       346 AA.
AC   C8CAS5;
DT   13-OCT-2009, integrated into UniProtKB/TrEMBL.
DT   13-OCT-2009, sequence version 1.
DT   27-MAR-2024, entry version 59.
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:ACU68581.1};
OS   Hemidactylus parvimaculatus.
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Gekkota; Gekkonidae; Gekkoninae;
OC   Hemidactylus.
OX   NCBI_TaxID=666680 {ECO:0000313|EMBL:ACU68581.1};
RN   [1] {ECO:0000313|EMBL:ACU68581.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=ADS36 {ECO:0000313|EMBL:ACU68581.1};
RX   PubMed=20601010; DOI=10.1016/j.ympev.2010.06.014;
RA   Bauer A.M., Jackman T.R., Greenbaum E., Giri V.B., de Silva A.;
RT   "South Asia supports a major endemic radiation of Hemidactylus geckos.";
RL   Mol. Phylogenet. Evol. 57:343-352(2010).
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; GQ375310; ACU68581.1; -; 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: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: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   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:ACU68581.1"
FT   NON_TER         346
FT                   /evidence="ECO:0000313|EMBL:ACU68581.1"
SQ   SEQUENCE   346 AA;  39219 MW;  5713356817AD1BCC CRC64;
     KSLXKESHLA NNDNVEMAAS LDKGNDAMTV MPQEPFHRGQ NLNNSMQSIG KDALSVNQRE
     IEAHQVNLQH LCRICGGSLK NDLYKRSHPV HGPVDDEMQA LLRKKERKAT SWPDLLNKVF
     KVDVRGDMDT IHPTNFCHNC WSVVQRKFSS VPCEVYFPRK GTMEWHPHST CCDVCGTSSQ
     GIKRKKQDPS PQGGKKARII AEHARRIMYA RSQKQVNSXN IMKKITNCKK IHLSTKLLTV
     DYPADFVKSI SCQICEHILA DPVETTCKHL FCRLCILKCL KVIGSYCPSC RYPCFPTDLV
     DPVKSFLNIL NALAVRCPVK NCHEEITLGK YSRHLSSHKE KKEKGT
//