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Database: UniProt
Entry: A7XQ06_9SAUR
LinkDB: A7XQ06_9SAUR
Original site: A7XQ06_9SAUR 
ID   A7XQ06_9SAUR            Unreviewed;       347 AA.
AC   A7XQ06;
DT   23-OCT-2007, integrated into UniProtKB/TrEMBL.
DT   23-OCT-2007, sequence version 1.
DT   24-JAN-2024, entry version 73.
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=RAG1 {ECO:0000313|EMBL:ABU41688.1};
OS   Paroedura masobe.
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Gekkota; Gekkonidae; Gekkoninae;
OC   Paroedura.
OX   NCBI_TaxID=347812 {ECO:0000313|EMBL:ABU41688.1};
RN   [1] {ECO:0000313|EMBL:ABU41688.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=18077188; DOI=10.1016/j.ympev.2007.10.018;
RA   Jackman T.R., Bauer A.M., Greenbaum E., Glaw F., Vences M.;
RT   "Molecular phylogenetic relationships among species of the Malagasy-Comoran
RT   gecko genus Paroedura (Squamata: Gekkonidae).";
RL   Mol. Phylogenet. Evol. 46:74-81(2008).
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; EF536144; ABU41688.1; -; Genomic_DNA.
DR   AlphaFoldDB; A7XQ06; -.
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          253..292
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50089"
FT   DOMAIN          314..343
FT                   /note="RAG1-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51765"
FT   REGION          1..23
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:ABU41688.1"
FT   NON_TER         347
FT                   /evidence="ECO:0000313|EMBL:ABU41688.1"
SQ   SEQUENCE   347 AA;  39364 MW;  BB747E757492C558 CRC64;
     KPLPEESHLA NNDNEKMATS SDKVNDAVTL MPQEAFQKGQ NLNNSMQTRD KDAFPVNQRE
     IEAHRVNLQH LCRICGGSFK NDPYKRSHPV HGPVDDEMQA LLRKKEKKAT SWPDLLNKVF
     KTDVRGDMDT IHPTNFCHNC RSVIQRKFSN VPSEVYFPRK GTMEWQPHST SCDVCGTSSH
     GIKRKMQAPN PPQGGKKLRI VAERARKIMH TRSQKQGNSK SIMKKITNCK KIHLSTKMLT
     VDYPVDFVKS VSCQICEHIL ADPVETTCKH LFCRLCILKC LKVIGSYCPS CRYPCFPTDL
     VNPVRSFQSI LNTLGVRCPV KDCHEEVTPG EYSHHLSSHK EVKDKGA
//
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