ID A0A672NXF3_SINGR Unreviewed; 556 AA.
AC A0A672NXF3;
DT 17-JUN-2020, integrated into UniProtKB/TrEMBL.
DT 17-JUN-2020, sequence version 1.
DT 18-JUN-2025, entry version 21.
DE RecName: Full=RBR-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012251};
DE EC=2.3.2.31 {ECO:0000256|ARBA:ARBA00012251};
GN Name=arih1 {ECO:0000313|Ensembl:ENSSGRP00000055643.1};
OS Sinocyclocheilus grahami (Dianchi golden-line fish) (Barbus grahami).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Cyprinidae; Cyprininae; Sinocyclocheilus.
OX NCBI_TaxID=75366 {ECO:0000313|Ensembl:ENSSGRP00000055643.1, ECO:0000313|Proteomes:UP000472262};
RN [1] {ECO:0000313|Ensembl:ENSSGRP00000055643.1}
RP IDENTIFICATION.
RG Ensembl;
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 -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000256|ARBA:ARBA00004906}.
CC -!- SIMILARITY: Belongs to the RBR family. Ariadne subfamily.
CC {ECO:0000256|ARBA:ARBA00005884}.
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DR AlphaFoldDB; A0A672NXF3; -.
DR Ensembl; ENSSGRT00000059421.1; ENSSGRP00000055643.1; ENSSGRG00000029159.1.
DR Proteomes; UP000472262; 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; cd20343; BRcat_RBR_HHARI-like; 1.
DR CDD; cd20356; Rcat_RBR_HHARI-like; 1.
DR CDD; cd16626; RING-HC_RBR_HHARI; 1.
DR FunFam; 1.20.120.1750:FF:000002; RBR-type E3 ubiquitin transferase; 1.
DR FunFam; 3.30.40.10:FF:000019; RBR-type E3 ubiquitin transferase; 1.
DR Gene3D; 1.20.120.1750; -; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR045840; Ariadne.
DR InterPro; IPR048962; ARIH1-like_UBL.
DR InterPro; IPR031127; E3_UB_ligase_RBR.
DR InterPro; IPR002867; IBR_dom.
DR InterPro; IPR044066; TRIAD_supradom.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
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 Pfam; PF21235; UBA_ARI1; 1.
DR SMART; SM00647; IBR; 2.
DR SUPFAM; SSF57850; RING/U-box; 3.
DR PROSITE; PS51873; TRIAD; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 3: Inferred from homology;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000472262};
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 150..379
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS51873"
FT DOMAIN 154..221
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 1..65
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..39
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 556 AA; 64990 MW; 4DE8F8EB271E8D4C CRC64;
MDSDEGYNYE FDDEEEECSE DSGEEETADD TLELGEVELV DPVVAGGERD DCGETGGSGP
GQDEEDYRFE VLTAEQILQH MVECIREVNE VIQNPATITR ILLSHFNWDK EKLMERYFDG
NLDKLFSECH VINPSKKSRT RLMNTRSSAQ DMPCQICYLN YPNSVRSVGV TRYSKLVSLS
LRYFTGLECG HKFCMQCWGD YLTTKIIEEG MGQTISCPAH SCDILVDDNT VMRLITDSKV
KLKYQHLITN SFVECNRLLK WCPAPDCHHV VKVQYPDAKP VRCKCGRQFC FNCGENWHDP
VKCKWLRKWI KKCDDDSETS NWIAANTKEC PKCHVTIEKD GGCNHMVCRN QNCKAEFCWV
CLGPWEPHGS AWYNCNRYNE DDAKAARDAQ EVNYVSPFVL MSEHRSRAAL QRYLFYCNRY
MNHMQSLRFE HKLYAQVKQK MEEMQQHNMS WIEVQFLKKA VDVLCQCRST LMFTYVFAFY
LKKNNQSIIF ENNQADLENA TEVLSGYLER DISQDSLQDI KQKVQDKYRY CESRRRVLLQ
HVHEGYDKDL WEYIED
//