ID A0A6P7IMI9_9TELE Unreviewed; 511 AA.
AC A0A6P7IMI9;
DT 02-DEC-2020, integrated into UniProtKB/TrEMBL.
DT 02-DEC-2020, sequence version 1.
DT 18-JUN-2025, entry version 22.
DE RecName: Full=RBR-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012251};
DE EC=2.3.2.31 {ECO:0000256|ARBA:ARBA00012251};
GN Name=arih2 {ECO:0000313|RefSeq:XP_028266031.1};
OS Parambassis ranga (Indian glassy fish).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Ambassidae; Parambassis.
OX NCBI_TaxID=210632 {ECO:0000313|Proteomes:UP000515145, ECO:0000313|RefSeq:XP_028266031.1};
RN [1] {ECO:0000313|RefSeq:XP_028266031.1}
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (MAR-2025) to UniProtKB.
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 -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the RBR family. Ariadne subfamily.
CC {ECO:0000256|ARBA:ARBA00005884}.
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DR RefSeq; XP_028266031.1; XM_028410230.1.
DR AlphaFoldDB; A0A6P7IMI9; -.
DR FunCoup; A0A6P7IMI9; 1614.
DR Ensembl; ENSPRNT00000001963; ENSPRNP00000001767; ENSPRNG00000000964.
DR GeneID; 114438707; -.
DR InParanoid; A0A6P7IMI9; -.
DR OrthoDB; 10009520at2759; -.
DR Proteomes; UP000515145; Chromosome 7.
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; 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 Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000515145};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
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 139..348
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS51873"
FT DOMAIN 304..344
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 1..45
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 511 AA; 58932 MW; 4645A4990A1A8160 CRC64;
MSVDMNSQAS DSNEEDFGVN SEEEEDEDDG GEEEDQGDIA SYYEGVASDV EQQGADSFDP
EEYQFTCLTY KESQRLLTEE VNTVAAALKV LPAVAKLILV HFHWQVSQIL DRYKSNSSLL
LSDALVQPSS SCRSVTTPQS LQCGVCLQVV RRDSLLALPC QHSFCKACWE QHCTVLVKDG
MGVGISCMAQ DCSLQMPEDF VLPLLPGEEL KDKYRRYLFR DYVESHFQLQ LCPGADCPIV
IKVQEPRARR VQCSRCSEVF CFKCRQMYHA PTDCATIRKW LTKCADDSET ANYISAHTKD
CPKCNICIEK NGGCNHMQCS KCKHDFCWMC LGDWKTHGSE YYECSRYKEN PDIVNQSQQA
QAREALKKYL FYFERWENHN KSLQLEAQTY QRIQEKIQER VMNNLGTWID WQYLHNAAKL
LAKCRYTLQY TYPYAYYMES GPRKKLFEYQ QAQLEAEIEN LSWKVERADS YERGVVGGEG
ELSASDRGDL ENQMHIAEQR RRTLLKDFHD T
//
