ID E9LFD1_9SAUR Unreviewed; 346 AA.
AC E9LFD1;
DT 05-APR-2011, integrated into UniProtKB/TrEMBL.
DT 05-APR-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:ADV76278.1};
OS Nactus pelagicus.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Gekkota; Gekkonidae; Gekkoninae; Nactus.
OX NCBI_TaxID=221565 {ECO:0000313|EMBL:ADV76278.1};
RN [1] {ECO:0000313|EMBL:ADV76278.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=B11 {ECO:0000313|EMBL:ADV76278.1};
RA Heinicke M.P., Greenbaum E., Jackman T.R., Bauer A.M.;
RT "Molecular Phylogenetics of Pacific Nactus (Squamata: Gekkota: Gekkonidae)
RT and the Diphyly of Australian Species.";
RL Proc. Calif. Acad. Sci. 61:633-636(2010).
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; HM997174; ADV76278.1; -; Genomic_DNA.
DR AlphaFoldDB; E9LFD1; -.
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 252..291
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT DOMAIN 313..342
FT /note="RAG1-type"
FT /evidence="ECO:0000259|PROSITE:PS51765"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:ADV76278.1"
FT NON_TER 346
FT /evidence="ECO:0000313|EMBL:ADV76278.1"
SQ SEQUENCE 346 AA; 39381 MW; D7A3521BE03B0387 CRC64;
KPLPEESHLA NSNNGKMAAS LDTVSDAMTL MPQEPFHKGQ NLNNVMPTTE KDAVSVNQRE
IEAHQMNLQQ LCRICGCSFK NDLYKRSHPV HGPVDDEMQT LLRKKERKAT SWPDLLNKVF
KIDVRGDMDT IHPTNFCHNC WSVIQRKFSS VPSEVYFPRK GTMEWNPHSN SCDVCGTSSR
GIKRKKQAPS PQGGKKLRIT AEHARRIIYA RNQKPANSKS IMKKITNCKK IHLSTKMLTI
DYPAEFVKSI SCQICEHILA DPVETTCKHL FCRHCILKCL KVIGSYCPSC RYPCFPTDLV
NPVRSFLSIL NTLNVRCPVK DCHEEVTLGK YSQHLSSHKE KKYKGI
//
