ID A0A672P264_SINGR Unreviewed; 494 AA.
AC A0A672P264;
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=LOC107583871 {ECO:0000313|Ensembl:ENSSGRP00000057352.1};
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:ENSSGRP00000057352.1, ECO:0000313|Proteomes:UP000472262};
RN [1] {ECO:0000313|Ensembl:ENSSGRP00000057352.1}
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; A0A672P264; -.
DR Ensembl; ENSSGRT00000061226.1; ENSSGRP00000057352.1; ENSSGRG00000029910.1.
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; IPR031127; E3_UB_ligase_RBR.
DR InterPro; IPR002867; IBR_dom.
DR InterPro; IPR044066; TRIAD_supradom.
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 SMART; SM00647; IBR; 2.
DR SUPFAM; SSF57850; RING/U-box; 3.
DR PROSITE; PS51873; TRIAD; 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}.
FT DOMAIN 111..323
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS51873"
FT REGION 1..66
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 494 AA; 57678 MW; 9C04E79C0280A03C CRC64;
MDSDEGYNYE FDDEEEECSE DSGEEETADD TLELGEVELV DPVVAGGERD DCGETGGSGL
GPGQDEEDYR FEVLTAEQIL QHMVECIREV NEVIQVSIFR ASPELRSPWI TRYNKRGDFY
IALGNFYFTG LECGHKFCMQ CWGDYLTTKI IEEGMGQTIS CPAHSCDILV DDSTVMRLIT
DSKVKLKYQH LITNSFVECN RLLKWCPAPD CHHVVKVQYP DAKPVRCKCG RQFCFNCGEN
WHDPVKCKWL RKWIKKCDDD SETSNWIAAN TKECPKCHVT IEKDGGCNHM VCRNQNCKAE
FCWVCLGPWE PHGSAWYNCN RYNEDDAKAA RDAQEVNNVS PFRSRAALQR YLFYCNRYMN
HMQSLRFEHK LYAQVKQKME EMQQHNMSWI EVQFLKKAVD VLCQCRSTLM FTYVFAFYLK
KNNQSIIFEN NQADLENATE VLSGYLERDI SQDSLQDIKQ KVQDKYRYCE SRRRVLLQHV
HEGYDKDLWE YIED
//
