ID   S4NFN3_9NEOP            Unreviewed;        96 AA.
AC   S4NFN3;
DT   18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT   18-SEP-2013, sequence version 1.
DT   27-NOV-2024, entry version 22.
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 (speckled wood butterfly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Papilionoidea;
OC   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., Tomlin J.,
RA   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-end
CC       rule pathway. Recognizes and binds to proteins bearing specific N-
CC       terminal residues that are destabilizing according to the N-end rule,
CC       leading to their ubiquitination and subsequent degradation.
CC       {ECO:0000256|RuleBase:RU366018}.
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:RU366018};
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC       {ECO:0000256|RuleBase:RU366018}.
CC   -!- SIMILARITY: Belongs to the E3 ubiquitin-protein ligase UBR1-like
CC       family. {ECO:0000256|RuleBase:RU366018}.
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DR   EMBL; GAIX01014974; JAA77586.1; -; Transcribed_RNA.
DR   AlphaFoldDB; S4NFN3; -.
DR   UniPathway; UPA00143; -.
DR   GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR   GO; GO:0061630; F:ubiquitin protein ligase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniRule.
DR   GO; GO:0071596; P:ubiquitin-dependent protein catabolic process via the N-end rule pathway; IEA:UniProtKB-UniRule.
DR   Gene3D; 1.10.10.2670; E3 ubiquitin-protein ligase; 1.
DR   InterPro; IPR042065; E3_ELL-like.
DR   InterPro; IPR039164; UBR1-like.
DR   InterPro; IPR055194; UBR1-like_winged-helix.
DR   InterPro; IPR036390; WH_DNA-bd_sf.
DR   PANTHER; PTHR21497:SF24; E3 UBIQUITIN-PROTEIN LIGASE UBR1; 1.
DR   PANTHER; PTHR21497; UBIQUITIN LIGASE E3 ALPHA-RELATED; 1.
DR   Pfam; PF22960; UBR1-like_wing; 1.
DR   SUPFAM; SSF46785; Winged helix' DNA-binding domain; 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   DOMAIN          30..95
FT                   /note="E3 ubiquitin-protein ligase UBR1-like winged-helix"
FT                   /evidence="ECO:0000259|Pfam:PF22960"
FT   NON_TER         96
FT                   /evidence="ECO:0000313|EMBL:JAA77586.1"
SQ   SEQUENCE   96 AA;  10822 MW;  5FF65F4EECAC4D99 CRC64;
     MVEEFLGLLI TVVGSRYVPG VGEVCNEERT KKEIIQMLCV KPMPHSELNR ALPEDQLHET
     GLEAVIHEVA DFVKPSSGNN RGVYKLKPHL FDDYDT
//