ID F2VM30_9SAUR Unreviewed; 350 AA.
AC F2VM30;
DT 31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 31-MAY-2011, sequence version 1.
DT 27-MAR-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:ADZ14190.1};
OS Hoplodactylus sp. Mt. Arthur Anatoki.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Gekkota; Pygopoidea; Diplodactylidae;
OC Hoplodactylus.
OX NCBI_TaxID=946305 {ECO:0000313|EMBL:ADZ14190.1};
RN [1] {ECO:0000313|EMBL:ADZ14190.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=FT 6301 {ECO:0000313|EMBL:ADZ14190.1};
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};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; GU459501; ADZ14190.1; -; 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 256..295
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT DOMAIN 317..346
FT /note="RAG1-type"
FT /evidence="ECO:0000259|PROSITE:PS51765"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:ADZ14190.1"
FT NON_TER 350
FT /evidence="ECO:0000313|EMBL:ADZ14190.1"
SQ SEQUENCE 350 AA; 39825 MW; CE0BC6C94E5192EF CRC64;
KAVPEERHPA NNEKEKVAAS LDQVREEQXD ATALMQEPFQ TGKKLNNGIQ TIEKDAFCVN
QREIEAHEVN LQQLCRICGG SFKNDPYKRS HPVHGPVDDE TQALLKKKER RATSWPDLLV
KVFKTDVRGD IDTIHPTNFC HNCWKVIQRK FSSAPCEVYF PRKGTMEWHP HSVSCDVCGT
SSRGMKRKKQ ALNPQVSKKL RITAERARKI MYTRSQKPKA NSKSLMKKIT NCKKIHLSTN
MLTVDYPADF VKSISCQICE HILADPVXTT CKHLFCRLCI LKCLKVMGSY CPSCRYPCFP
TDLLNPVRSF LTVINTLVVR CPVAXCQEEI APGKYSHHLS SHXDNKXKGM
//
