ID C4MH28_9SAUR Unreviewed; 284 AA.
AC C4MH28;
DT 07-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 07-JUL-2009, sequence version 1.
DT 24-JAN-2024, entry version 39.
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:ACE63168.1};
OS Oligosoma waimatense.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Scinciformata; Scincidae;
OC Eugongylinae; Oligosoma.
OX NCBI_TaxID=421930 {ECO:0000313|EMBL:ACE63168.1};
RN [1] {ECO:0000313|EMBL:ACE63168.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=OWA2 {ECO:0000313|EMBL:ACE63168.1};
RX PubMed=19345273; DOI=10.1016/j.ympev.2009.03.021;
RA Chapple D.G., Ritchie P.A., Daugherty C.H.;
RT "Origin, diversification, and systematics of the New Zealand skink fauna
RT (Reptilia: Scincidae).";
RL Mol. Phylogenet. Evol. 52:470-487(2009).
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; EU568095; ACE63168.1; -; Genomic_DNA.
DR AlphaFoldDB; C4MH28; -.
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: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; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR024627; RAG1.
DR InterPro; IPR035714; RAG1_imp-bd.
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 SMART; SM00184; RING; 1.
DR SUPFAM; SSF57850; RING/U-box; 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 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:PRU00175}.
FT DOMAIN 245..284
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:ACE63168.1"
FT NON_TER 284
FT /evidence="ECO:0000313|EMBL:ACE63168.1"
SQ SEQUENCE 284 AA; 32636 MW; 6EA2385B78D7B3F3 CRC64;
CSHMANHDKG RVEDTVDQVF EEKEDGVDPF QRDKDRNNSV ETDKDVFRMN QREIEAHQAR
LQHLCRICGG SFKADPCKRS HPVHGPVDNV MQALLRKKER RATSWPELLA KVFKIDVRGD
IDTIHPTKFC HNCWNFIQRK FSNVPSEVYF PRNGPMEWHP HSSGCEVCGT SAHGVKRKRQ
ALKPQVSKKL RIVARRASQI RPVRSPQKVH SKNLMKKIVN CNKIHISTKR FAVDYPADFV
KAVSCQICEH VLADPVETTC KHLFCRVCIL KCLKVLGSYC PSCR
//
