ID B4YHB3_PSETE Unreviewed; 355 AA.
AC B4YHB3;
DT 23-SEP-2008, integrated into UniProtKB/TrEMBL.
DT 23-SEP-2008, sequence version 1.
DT 27-MAR-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=RAG1 {ECO:0000313|EMBL:ACF60761.1};
OS Pseudonaja textilis (Eastern brown snake).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Elapidae; Acanthophiinae; Pseudonaja.
OX NCBI_TaxID=8673 {ECO:0000313|EMBL:ACF60761.1};
RN [1] {ECO:0000313|EMBL:ACF60761.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=18384538; DOI=10.1111/j.1420-9101.2008.01525.x;
RA Sanders K.L., Lee M.S., Leys R., Foster R., Keogh J.S.;
RT "Molecular phylogeny and divergence dates for Australasian elapids and sea
RT snakes (hydrophiinae): evidence from seven genes for rapid evolutionary
RT radiations.";
RL J. Evol. Biol. 21:682-695(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; EU546875; ACF60761.1; -; Genomic_DNA.
DR AlphaFoldDB; B4YHB3; -.
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 258..297
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT DOMAIN 319..348
FT /note="RAG1-type"
FT /evidence="ECO:0000259|PROSITE:PS51765"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:ACF60761.1"
FT NON_TER 355
FT /evidence="ECO:0000313|EMBL:ACF60761.1"
SQ SEQUENCE 355 AA; 40306 MW; E41D034B2002DB69 CRC64;
SLVQPLSEDS HQANSAKENV TGSLGVTDEQ PKAATVMSQV PFETAPELNK NSLAKEKVIF
HMSQSEMEVH QANLQHLCRI CGGSLKTDPY KKCHPVHGPV DEETQALLRK KEKRATSWPD
LFVKVFKIDV RGDIDTIHPT HFCHNCWKAM QRKVSNAPHE AHLLERDPVE WHPHSTSCDV
CVTSFRGIKR KKTMLNSQLS KKLRIIAGHT RKIRCIRKVK QLNNKSLMKK ISNCKQIHLS
TKILAIDYPV DFVKSISCQV CEHILADPVE TTCKHLFCRV CILKCLKIMG SYCPSCRYPC
FPTDLVSPVK SFLSILNNLV LRCPIKGCHE EVFLEKYCQH RSNHKGAEST DSYVN
//
