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Database: UniProt
Entry: A9Y411_SCEMA
LinkDB: A9Y411_SCEMA
Original site: A9Y411_SCEMA 
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
//
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