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Database: UniProt
Entry: F2VLV3_9SAUR
LinkDB: F2VLV3_9SAUR
Original site: F2VLV3_9SAUR 
ID   F2VLV3_9SAUR            Unreviewed;       349 AA.
AC   F2VLV3;
DT   31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   31-MAY-2011, sequence version 1.
DT   27-MAR-2024, entry version 51.
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:ADZ14113.1};
OS   Mokopirirakau granulatus (Gray's sticky-toed gecko).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Gekkota; Pygopoidea; Diplodactylidae;
OC   Mokopirirakau.
OX   NCBI_TaxID=1165299 {ECO:0000313|EMBL:ADZ14113.1};
RN   [1] {ECO:0000313|EMBL:ADZ14113.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=RAH 340 {ECO:0000313|EMBL:ADZ14113.1};
RX   PubMed=21184833; DOI=10.1016/j.ympev.2010.12.007;
RA   Nielsen S.V., Bauer A.M., Jackman T.R., Hitchmough R.A., Daugherty C.H.;
RT   "New Zealand geckos (Diplodactylidae): Cryptic diversity in a post-
RT   Gondwanan lineage with trans-Tasman affinities.";
RL   Mol. Phylogenet. Evol. 59:1-22(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; GU459408; ADZ14113.1; -; 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          255..294
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50089"
FT   DOMAIN          316..345
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   COMPBIAS        8..23
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:ADZ14113.1"
FT   NON_TER         349
FT                   /evidence="ECO:0000313|EMBL:ADZ14113.1"
SQ   SEQUENCE   349 AA;  39623 MW;  3381871739EFE415 CRC64;
     KAVPEESGPA NNEKEKVTAS LDKVREKEAD ATALMQEPFQ TGKKLNNGIQ TIDKDAFCVN
     QREIEAHQVN LQQLCRICGG SFKNDPYKRS HPVHGPVDDE TQALLKKKER RATSWPDLLV
     KVFKIDVRGD IDTIHPTNFC HNCWKVIQRK FSSAPCEVYF PRKGTMEWHP HSVSCDVCGT
     SSRGMKRKKQ ALNPQVSKKL RITAERARKI MYARSPKPAN SKXLMKKITN CKKIHLSTNM
     LTVDYPADFV KSISCQICEH ILADPVETTC KHLFCRLCIL KCLKVMGSYC PSCRYPCFPT
     DLMNPVRSFL TVINTLVVRC PVKDCHEEIA LGKYSHHLSS HXDNKDKGM
//
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