ID F2VLY6_9SAUR Unreviewed; 335 AA.
AC F2VLY6;
DT 31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 31-MAY-2011, sequence version 1.
DT 24-JAN-2024, entry version 47.
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:ADZ14146.1};
OS Woodworthia maculata (Raukawa gecko).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Gekkota; Pygopoidea; Diplodactylidae;
OC Woodworthia.
OX NCBI_TaxID=1165302 {ECO:0000313|EMBL:ADZ14146.1};
RN [1] {ECO:0000313|EMBL:ADZ14146.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=RAH 292 {ECO:0000313|EMBL:ADZ14146.1};
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; GU459449; ADZ14146.1; -; Genomic_DNA.
DR AlphaFoldDB; F2VLY6; -.
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; 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; 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-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..335
FT /note="RAG1-type"
FT /evidence="ECO:0000259|PROSITE:PS51765"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:ADZ14146.1"
FT NON_TER 335
FT /evidence="ECO:0000313|EMBL:ADZ14146.1"
SQ SEQUENCE 335 AA; 38073 MW; DADAE900D21F5B86 CRC64;
KAVPEESHPA NNEKEKVAAS LDQVREEQAD ATALMQEPFQ TGKKLNNGTQ TIDEDAFCVN
QREIEAHEVN LQQLCRICGG SFKNDPYKRS HPVHGPVDDE TQALLKKKER RATSWPDLLV
KVFKTDVRGD IDTIHPTNFC HNCWKVIQRK FSSAPCEVYF PRKGTMEWHP HSVSCDVCGT
SSRGMKRKKQ ALNPQVSKKL RITAERARKI MYTRSQKPKA NSKSLMKKIT NCKKIHLSTN
MLTVDYPADF VKSISCQICE HILADPVETT CKHLFCRLCI LKCLKVMGSY CPSCRYPCFP
TDLMNPVRSF LTVINTLVVR CPVADCHEEI ALGKY
//
