ID S4NFN3_9NEOP Unreviewed; 96 AA. AC S4NFN3; DT 18-SEP-2013, integrated into UniProtKB/TrEMBL. DT 18-SEP-2013, sequence version 1. DT 03-JUL-2019, entry version 13. DE RecName: Full=E3 ubiquitin-protein ligase {ECO:0000256|RuleBase:RU366018}; DE EC=2.3.2.27 {ECO:0000256|RuleBase:RU366018}; DE Flags: Fragment; OS Pararge aegeria (specked wood butterfly). OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; OC Pterygota; Neoptera; Holometabola; Lepidoptera; Glossata; Ditrysia; OC Papilionoidea; Nymphalidae; Satyrinae; Satyrini; Parargina; Pararge. OX NCBI_TaxID=116150 {ECO:0000313|EMBL:JAA77586.1}; RN [1] {ECO:0000313|EMBL:JAA77586.1} RP NUCLEOTIDE SEQUENCE. RC TISSUE=Ovary {ECO:0000313|EMBL:JAA77586.1}; RX PubMed=23622113; DOI=10.1186/1471-2164-14-283; RA Carter J.M., Baker S.C., Pink R., Carter D.R., Collins A., Tomlin J., RA Gibbs M., Breuker C.J.; RT "Unscrambling butterfly oogenesis."; RL BMC Genomics 14:283-283(2013). RN [2] {ECO:0000313|EMBL:JAA77586.1} RP NUCLEOTIDE SEQUENCE. RC TISSUE=Ovary {ECO:0000313|EMBL:JAA77586.1}; RA Carter J.-M., Baker S.C., Pink R., Carter D.R.F., Collins A., RA Tomlin J., Gibbs M., Breuker C.J.; RL Submitted (MAY-2013) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Ubiquitin ligase protein which is a component of the N- CC end rule pathway. Recognizes and binds to proteins bearing CC specific N-terminal residues that are destabilizing according to CC the N-end rule, leading to their ubiquitination and subsequent CC degradation. {ECO:0000256|RuleBase:RU366018}. CC -!- CATALYTIC ACTIVITY: CC Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L- CC cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin- CC conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor CC protein]-L-lysine.; EC=2.3.2.27; CC Evidence={ECO:0000256|RuleBase:RU366018}; CC -!- PATHWAY: Protein modification; protein ubiquitination. CC {ECO:0000256|RuleBase:RU366018}. CC -!- SIMILARITY: Belongs to the UBR1 family. CC {ECO:0000256|RuleBase:RU366018}. 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 EMBL; GAIX01014974; JAA77586.1; -; Transcribed_RNA. DR UniPathway; UPA00143; -. DR GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW. DR GO; GO:0061630; F:ubiquitin protein ligase activity; IEA:InterPro. DR GO; GO:0071596; P:ubiquitin-dependent protein catabolic process via the N-end rule pathway; IEA:InterPro. DR Gene3D; 1.10.10.2670; -; 1. DR InterPro; IPR042065; E3_ELL-like. DR InterPro; IPR039164; UBR1-like. DR InterPro; IPR036390; WH_DNA-bd_sf. DR PANTHER; PTHR21497; PTHR21497; 1. DR SUPFAM; SSF46785; SSF46785; 1. PE 3: Inferred from homology; KW Ligase {ECO:0000313|EMBL:JAA77586.1}; KW Metal-binding {ECO:0000256|RuleBase:RU366018}; KW Transferase {ECO:0000256|RuleBase:RU366018}; KW Ubl conjugation pathway {ECO:0000256|RuleBase:RU366018}; KW Zinc {ECO:0000256|RuleBase:RU366018}; KW Zinc-finger {ECO:0000256|RuleBase:RU366018}. FT NON_TER 96 96 {ECO:0000313|EMBL:JAA77586.1}. SQ SEQUENCE 96 AA; 10822 MW; 5FF65F4EECAC4D99 CRC64; MVEEFLGLLI TVVGSRYVPG VGEVCNEERT KKEIIQMLCV KPMPHSELNR ALPEDQLHET GLEAVIHEVA DFVKPSSGNN RGVYKLKPHL FDDYDT //