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Database: UniProt
Entry: A0A078A1Y1_STYLE
LinkDB: A0A078A1Y1_STYLE
Original site: A0A078A1Y1_STYLE 
ID   A0A078A1Y1_STYLE        Unreviewed;       515 AA.
AC   A0A078A1Y1;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   24-JAN-2024, entry version 27.
DE   RecName: Full=HECT-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012485};
DE            EC=2.3.2.26 {ECO:0000256|ARBA:ARBA00012485};
GN   Name=Contig6502.g6956 {ECO:0000313|EMBL:CDW75488.1};
GN   ORFNames=STYLEM_4478 {ECO:0000313|EMBL:CDW75488.1};
OS   Stylonychia lemnae (Ciliate).
OC   Eukaryota; Sar; Alveolata; Ciliophora; Intramacronucleata; Spirotrichea;
OC   Stichotrichia; Sporadotrichida; Oxytrichidae; Stylonychinae; Stylonychia.
OX   NCBI_TaxID=5949 {ECO:0000313|EMBL:CDW75488.1, ECO:0000313|Proteomes:UP000039865};
RN   [1] {ECO:0000313|EMBL:CDW75488.1, ECO:0000313|Proteomes:UP000039865}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=130c {ECO:0000313|EMBL:CDW75488.1,
RC   ECO:0000313|Proteomes:UP000039865};
RA   Swart Estienne;
RL   Submitted (JUN-2014) to the EMBL/GenBank/DDBJ databases.
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=2.3.2.26; Evidence={ECO:0000256|ARBA:ARBA00000885};
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00104}.
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DR   EMBL; CCKQ01004336; CDW75488.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A078A1Y1; -.
DR   EnsemblProtists; CDW75488; CDW75488; STYLEM_4478.
DR   InParanoid; A0A078A1Y1; -.
DR   OMA; CEQRRIS; -.
DR   OrthoDB; 179728at2759; -.
DR   Proteomes; UP000039865; Unassembled WGS sequence.
DR   GO; GO:0004842; F:ubiquitin-protein transferase activity; IEA:InterPro.
DR   Gene3D; 3.30.2160.10; Hect, E3 ligase catalytic domain; 1.
DR   Gene3D; 3.30.2410.10; Hect, E3 ligase catalytic domain; 1.
DR   Gene3D; 3.90.1750.10; Hect, E3 ligase catalytic domains; 1.
DR   InterPro; IPR000569; HECT_dom.
DR   InterPro; IPR035983; Hect_E3_ubiquitin_ligase.
DR   PANTHER; PTHR11254:SF67; E3 UBIQUITIN-PROTEIN LIGASE HUWE1; 1.
DR   PANTHER; PTHR11254; HECT DOMAIN UBIQUITIN-PROTEIN LIGASE; 1.
DR   Pfam; PF00632; HECT; 1.
DR   SMART; SM00119; HECTc; 1.
DR   SUPFAM; SSF56204; Hect, E3 ligase catalytic domain; 1.
DR   PROSITE; PS50237; HECT; 1.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000039865};
KW   Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW   ECO:0000256|PROSITE-ProRule:PRU00104}.
FT   DOMAIN          201..485
FT                   /note="HECT"
FT                   /evidence="ECO:0000259|PROSITE:PS50237"
SQ   SEQUENCE   515 AA;  60615 MW;  4D9C6B47075AD13D CRC64;
     MRSHTSPSIV QKRNFYGGEF NNELPVILEV NESNIASTVY NRKVSNNQND ALQGTNLRSQ
     VFQSLIISRI SDSDEDVDIS SESEFSEDIV DPAEVGLEIP DESENFITFF LDQEMTWQKN
     ILQNGKVNWV KKKRSQKLQL NPNLKKLSCA KVRNMQLEEK KFWFEYQCEQ RRISFIQDSI
     TLVIQRDNVL RDSFEQFRTT DDFDLHKEIK IHYIDEVAQD AGGITREWVT QLTQQLFSDD
     QQLFKQMKSD HSLNYFPNQN AKFLYENGYK DYFRFAGQVL AKALFDKIPV NVSLNSAILK
     KLVAISPKEQ KITLEDLRDY DQQIYNSIKF ISDDPSINFD EEEFYFTIIQ DDGSEIELIK
     KGKETRVTAQ NRTQYAKKVA KYYLYKQVKT EIDEFVKGFL QVIPNSIISV FDKDELEFIM
     NGSPTIDIDD WIQNSTYRGA FENEGKNHQV ISWFWDILRD LNQEKRRKFL LFCTGNPRLP
     IEGFKIDLPL FNRKEDIENN INGILEQDHY YFDFE
//
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