ID A9Y411_SCEMA Unreviewed; 320 AA.
AC A9Y411;
DT 05-FEB-2008, integrated into UniProtKB/TrEMBL.
DT 05-FEB-2008, sequence version 1.
DT 24-JAN-2024, entry version 68.
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:ABU44885.1};
OS Sceloporus magister (Desert spiny lizard).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Iguania; Phrynosomatidae; Phrynosomatinae; Sceloporus.
OX NCBI_TaxID=43627 {ECO:0000313|EMBL:ABU44885.1};
RN [1] {ECO:0000313|EMBL:ABU44885.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=17944851; DOI=10.1111/j.1365-294X.2007.03556.x;
RA Leache A.D., Mulcahy D.G.;
RT "Phylogeny, divergence times and species limits of spiny lizards
RT (Sceloporus magister species group) in western North American deserts and
RT Baja California.";
RL Mol. Ecol. 16:5216-5233(2007).
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; EU085649; ABU44885.1; -; 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; 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 240..279
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT DOMAIN 301..320
FT /note="RAG1-type"
FT /evidence="ECO:0000259|PROSITE:PS51765"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:ABU44885.1"
FT NON_TER 320
FT /evidence="ECO:0000313|EMBL:ABU44885.1"
SQ SEQUENCE 320 AA; 35951 MW; CC16362B667FA09D CRC64;
VAAILDXVTE KEIETVALMS HPLFETDSEL NKGIQPIDNS AFSMSQTEAE THQANLQQLC
RLCGGSFKTD PYKRSHPVHG PVDDETQALL RKKEKKATSW PDLLAKVFKI DVKGDIDTIH
PTKFCHQCWT VVQKKLNNSP CEMFFSRKSP VEWNPHSSSC DVCGASLQGV KRKKQVLTPQ
LSKKLRMVSG HARKIRQTRN PKQVSQKSLM KMIASCKKIH LSTKILAVDY PADFVKSVSC
QICEHILADP VETTCKHLFC RACILKYLKI VGSYCPACRY PCFPTDLVSP VKSFLNILNS
LPVICPVKDC QEEICLGKYC
//