ID Q0Q5S3_APASP Unreviewed; 241 AA.
AC Q0Q5S3;
DT 05-SEP-2006, integrated into UniProtKB/TrEMBL.
DT 05-SEP-2006, sequence version 1.
DT 24-JAN-2024, entry version 61.
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:ABF81739.1};
OS Apalone spinifera hartwegi.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Testudinata; Testudines; Cryptodira; Trionychia;
OC Trionychidae; Apalone.
OX NCBI_TaxID=387429 {ECO:0000313|EMBL:ABF81739.1};
RN [1] {ECO:0000313|EMBL:ABF81739.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=SCan107a {ECO:0000313|EMBL:ABF81739.1}, and SCan107b
RC {ECO:0000313|EMBL:ABF81738.1};
RA McGaugh S.E., Eckerman C.M., Janzen F.J.;
RT "Molecular phylogeography of Apalone spinifera (Reptilia, Trionychidae).";
RL Zool. Scr. 37:289-304(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; DQ529138; ABF81738.1; -; Genomic_DNA.
DR EMBL; DQ529139; ABF81739.1; -; Genomic_DNA.
DR AlphaFoldDB; Q0Q5S3; -.
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 200..239
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:ABF81739.1"
FT NON_TER 241
FT /evidence="ECO:0000313|EMBL:ABF81739.1"
SQ SEQUENCE 241 AA; 27452 MW; 3DD46277D42153F4 CRC64;
ADNLKMKENA AHQANLQQLC RICGVSFKTD CYKRSHPVHG PVDNETQGVL RKKEKKATSW
PDLIAKVFKI DVRADIDTIH PTRFCHNCWS IIHRKFSNAP CEVYFPRNST MEWKSHSPNC
TVCRTAPHGV KRKNQPSNLQ LGKKLKIMAE RARKTKGVKK QSQINNKNLM KKIANCKKIH
LSTKLLAVDY PADFVKSISC QVCEHILADP VETTCSHLFC RTCILKCLKV MGSYCPACRY
P
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