ID A0A669QW34_PHACC Unreviewed; 242 AA. AC A0A669QW34; DT 17-JUN-2020, integrated into UniProtKB/TrEMBL. DT 17-JUN-2020, sequence version 1. DT 02-JUN-2021, entry version 7. DE RecName: Full=E3 ubiquitin-protein ligase {ECO:0000256|RuleBase:RU201113}; DE EC=2.3.2.27 {ECO:0000256|RuleBase:RU201113}; OS Phasianus colchicus (Common pheasant). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda; OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae; OC Phasianinae; Phasianus. OX NCBI_TaxID=9054 {ECO:0000313|Ensembl:ENSPCLP00000024882, ECO:0000313|Proteomes:UP000472261}; RN [1] {ECO:0000313|Ensembl:ENSPCLP00000024882} RP IDENTIFICATION. RG Ensembl; RL Submitted (MAR-2020) to UniProtKB. CC -!- FUNCTION: E3 ubiquitin-protein ligase that mediates ubiquitination and CC subsequent proteasomal degradation of target proteins. E3 ubiquitin CC ligases accept ubiquitin from an E2 ubiquitin-conjugating enzyme in the CC form of a thioester and then directly transfers the ubiquitin to CC targeted substrates. {ECO:0000256|RuleBase:RU201113}. 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|RuleBase:RU201113}; CC -!- PATHWAY: Protein modification; protein ubiquitination. CC {ECO:0000256|RuleBase:RU201113}. CC -!- DOMAIN: The RING-type zinc finger domain is essential for ubiquitin CC ligase activity. {ECO:0000256|RuleBase:RU201113}. CC -!- DOMAIN: The SBD domain (substrate-binding domain) mediates the CC interaction with substrate proteins. It is related to the TRAF family. CC {ECO:0000256|RuleBase:RU201113}. CC -!- SIMILARITY: Belongs to the SINA (Seven in absentia) family. CC {ECO:0000256|ARBA:ARBA00009119, ECO:0000256|RuleBase:RU201113}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR Ensembl; ENSPCLT00000034478; ENSPCLP00000024882; ENSPCLG00000021918. DR UniPathway; UPA00143; -. DR Proteomes; UP000472261; Unplaced. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0007275; P:multicellular organism development; IEA:InterPro. DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway. DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:InterPro. DR Gene3D; 2.60.210.10; -; 1. DR InterPro; IPR018121; 7-in-absentia-prot_TRAF-dom. DR InterPro; IPR004162; SINA-like_animal. DR InterPro; IPR008974; TRAF-like. DR PANTHER; PTHR45877; PTHR45877; 2. DR Pfam; PF03145; Sina; 1. DR SUPFAM; SSF49599; SSF49599; 1. PE 3: Inferred from homology; KW Metal-binding {ECO:0000256|RuleBase:RU201113}; KW Reference proteome {ECO:0000313|Proteomes:UP000472261}; KW Ubl conjugation pathway {ECO:0000256|RuleBase:RU201113}; KW Zinc {ECO:0000256|RuleBase:RU201113}; KW Zinc-finger {ECO:0000256|RuleBase:RU201113}. FT DOMAIN 62..227 FT /note="Sina" FT /evidence="ECO:0000259|Pfam:PF03145" SQ SEQUENCE 242 AA; 27180 MW; 6824ECB387DF2AB1 CRC64; MLFFTQCFGA VLDLIHLRFQ HYKAKRVFSA AGQLVCVVNP THSLKYAPTR CAVAQTSTEQ GSLPPCHHHE AVHDPQLVPC TCPLFSCPWE GHLEVVVSHL RQTHRINILQ GAEIVFLATD MHLPAPTDWI IMHSCLGHQF LLVLRKQEKY KGHPQFFATM MLIGTQTQAD NFTYRLELNR NQRRLKWEAT PRSVLECVDS IISDGDCLVL NTSLAQLFAD NGSLAIGIAI TTSKVHNSEA EI //