ID B0Z672_9SAUR Unreviewed; 324 AA.
AC B0Z672;
DT 08-APR-2008, integrated into UniProtKB/TrEMBL.
DT 08-APR-2008, sequence version 1.
DT 24-JAN-2024, entry version 64.
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:ABZ82389.1};
OS Hemidactylus fasciatus (banded leaf-toed gecko).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Gekkota; Gekkonidae; Gekkoninae;
OC Hemidactylus.
OX NCBI_TaxID=401547 {ECO:0000313|EMBL:ABZ82389.1};
RN [1] {ECO:0000313|EMBL:ABZ82389.1}
RP NUCLEOTIDE SEQUENCE.
RA Bauer A.M., Giri V.B., Greenbaum E., Jackman T.R., Dharne M.S.,
RA Shouche Y.S.;
RT "On the systematics of the gekkonid genus Teratolepis Guenther, 1869:
RT Another one bites the dust.";
RL Hamadryad 0:0-0(2008).
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; EU268292; ABZ82389.1; -; 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; 3.30.40.10; 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 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 252..291
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT DOMAIN 313..324
FT /note="RAG1-type"
FT /evidence="ECO:0000259|PROSITE:PS51765"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:ABZ82389.1"
FT NON_TER 324
FT /evidence="ECO:0000313|EMBL:ABZ82389.1"
SQ SEQUENCE 324 AA; 36698 MW; B3F6F7ECBA3C80A7 CRC64;
KSLPKESHLA NSDNVEMAAS LDKGNDAMTV MLQEPFHRGQ NLNNSMQSIG KDTFSVNQRE
IEAHQVNLQH LCRICGGSLK NDLYKRSHPV HGPVDDEMQA XLRKKERKAT SWPDLLNKVF
KVDVKGDIDT IHPTNFCHNC WNVVQRKFSS VPCEVYFPRK GTMEWHPHST CCDVCGTSSR
GIKRKKQDPS PPGGKKARII AEHARRIMYA RSQKQVNSKN IMKKITNCKK IHLSTKLLTV
DYPADFVKSI SCQICEHILA DPVETTCKHL FCRLCILKCL KVVGSYCPSC RYPCFPTDLV
DPVKSFLNIL NALAVRCPVK NCHE
//
