ID A0A091IPS3_EGRGA Unreviewed; 490 AA.
AC A0A091IPS3;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 18-JUN-2025, entry version 52.
DE RecName: Full=E3 ubiquitin-protein ligase ARIH2 {ECO:0000256|ARBA:ARBA00070157};
DE EC=2.3.2.31 {ECO:0000256|ARBA:ARBA00012251};
DE AltName: Full=Triad1 protein {ECO:0000256|ARBA:ARBA00080593};
GN ORFNames=Z169_16150 {ECO:0000313|EMBL:KFP10704.1};
OS Egretta garzetta (Little egret).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Neoaves; Aequornithes; Pelecaniformes;
OC Ardeidae; Egretta.
OX NCBI_TaxID=188379 {ECO:0000313|EMBL:KFP10704.1, ECO:0000313|Proteomes:UP000053119};
RN [1] {ECO:0000313|EMBL:KFP10704.1, ECO:0000313|Proteomes:UP000053119}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_Z169 {ECO:0000313|EMBL:KFP10704.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[E2 ubiquitin-conjugating enzyme]-S-ubiquitinyl-L-cysteine +
CC [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-
CC cysteine + [acceptor protein]-N(6)-ubiquitinyl-L-lysine.;
CC EC=2.3.2.31; Evidence={ECO:0000256|ARBA:ARBA00001798};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000256|ARBA:ARBA00004906}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the RBR family. Ariadne subfamily.
CC {ECO:0000256|ARBA:ARBA00005884}.
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DR EMBL; KK500848; KFP10704.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A091IPS3; -.
DR STRING; 188379.A0A091IPS3; -.
DR KEGG; egz:104134794; -.
DR CTD; 10425; -.
DR OrthoDB; 10009520at2759; -.
DR Proteomes; UP000053119; Unassembled WGS sequence.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016567; P:protein ubiquitination; IEA:InterPro.
DR CDD; cd20344; BRcat_RBR_TRIAD1; 1.
DR CDD; cd20360; Rcat_RBR_TRIAD1; 1.
DR CDD; cd16773; RING-HC_RBR_TRIAD1; 1.
DR FunFam; 1.20.120.1750:FF:000004; RBR-type E3 ubiquitin transferase; 1.
DR FunFam; 2.20.25.20:FF:000005; RBR-type E3 ubiquitin transferase; 1.
DR FunFam; 3.30.40.10:FF:000098; RBR-type E3 ubiquitin transferase; 1.
DR Gene3D; 1.20.120.1750; -; 1.
DR Gene3D; 2.20.25.20; -; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR045840; Ariadne.
DR InterPro; IPR047555; BRcat_RBR_TRIAD1.
DR InterPro; IPR031127; E3_UB_ligase_RBR.
DR InterPro; IPR002867; IBR_dom.
DR InterPro; IPR047556; Rcat_RBR_TRIAD1.
DR InterPro; IPR044066; TRIAD_supradom.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR017907; Znf_RING_CS.
DR PANTHER; PTHR11685; RBR FAMILY RING FINGER AND IBR DOMAIN-CONTAINING; 1.
DR Pfam; PF19422; Ariadne; 1.
DR Pfam; PF01485; IBR; 1.
DR Pfam; PF22191; IBR_1; 1.
DR SMART; SM00647; IBR; 2.
DR SMART; SM00184; RING; 2.
DR SUPFAM; SSF57850; RING/U-box; 3.
DR PROSITE; PS51873; TRIAD; 1.
DR PROSITE; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000053119};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Ubl conjugation {ECO:0000256|ARBA:ARBA00022843};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00175}.
FT DOMAIN 132..341
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS51873"
FT DOMAIN 297..337
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 1..40
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..11
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 12..37
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 490 AA; 57291 MW; D559587CB47625BD CRC64;
MSVDMNSQGS DSNEEDYDPN CEEEEEDEDP GDIEDYYDGV ANDVEQQGAD AFDPEEYQFT
CLTYKESEST LNEHMASLAA TLKVSHAVAK LVLVSFHWQI SEILERHKSN AAQLLVEARV
QPTSSKHAMV HSSHHCAVCM QFVRKENLLS LACQHQFCRS CWEQHCTVLV KDGVGVGVSC
MAQDCLLRTP EDFVFPLLPS EELKDKYRRY LFRDYVESHY QLQLCPGADC PMVIQVQEPK
ARRVQCNRCS EVFCFKCRQM YHAPTDCATI RKWLTKCADD SETANYISAH TKDCPKCNIC
IEKNGGCNHM QCSKCKHDFC WMCLGDWKTH GSEYYECSRY KENPDIVNQS QQAQAREALK
KYLFYFERWE NHNKSLQLEA QTYQRIQEKI QERVMNNLGT WIDWQYLQNA AKLLAKCRYT
LQYTYPYAYY MESGPRKKLF EYQQAQLEAE IENLSWKVER ADSYDRGDLE NQMHIAEQRR
RTLLKDFHDT
//
