ID   A0A091FSJ0_9AVES        Unreviewed;       575 AA.
AC   A0A091FSJ0;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   27-MAR-2024, entry version 31.
DE   RecName: Full=HECT-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012485};
DE            EC=2.3.2.26 {ECO:0000256|ARBA:ARBA00012485};
DE   Flags: Fragment;
GN   ORFNames=N303_14320 {ECO:0000313|EMBL:KFO72583.1};
OS   Cuculus canorus (common cuckoo).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Cuculiformes; Cuculidae; Cuculus.
OX   NCBI_TaxID=55661 {ECO:0000313|EMBL:KFO72583.1, ECO:0000313|Proteomes:UP000053760};
RN   [1] {ECO:0000313|EMBL:KFO72583.1, ECO:0000313|Proteomes:UP000053760}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BGI_N303 {ECO:0000313|EMBL:KFO72583.1};
RA   Zhang G., Li C.;
RT   "Genome evolution of avian class.";
RL   Submitted (APR-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   -!- PATHWAY: Protein modification; protein ubiquitination.
CC       {ECO:0000256|ARBA:ARBA00004906}.
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DR   EMBL; KL447356; KFO72583.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A091FSJ0; -.
DR   STRING; 55661.A0A091FSJ0; -.
DR   UniPathway; UPA00143; -.
DR   Proteomes; UP000053760; Unassembled WGS sequence.
DR   GO; GO:0004842; F:ubiquitin-protein transferase activity; IEA:InterPro.
DR   GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR   CDD; cd00078; HECTc; 1.
DR   CDD; cd00201; WW; 4.
DR   Gene3D; 2.20.70.10; -; 3.
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   InterPro; IPR001202; WW_dom.
DR   InterPro; IPR036020; WW_dom_sf.
DR   PANTHER; PTHR11254; HECT DOMAIN UBIQUITIN-PROTEIN LIGASE; 1.
DR   PANTHER; PTHR11254:SF396; NEDD4-LIKE E3 UBIQUITIN-PROTEIN LIGASE WWP2; 1.
DR   Pfam; PF00632; HECT; 1.
DR   Pfam; PF00397; WW; 4.
DR   PRINTS; PR00403; WWDOMAIN.
DR   SMART; SM00119; HECTc; 1.
DR   SMART; SM00456; WW; 4.
DR   SUPFAM; SSF56204; Hect, E3 ligase catalytic domain; 1.
DR   SUPFAM; SSF51045; WW domain; 4.
DR   PROSITE; PS50237; HECT; 1.
DR   PROSITE; PS01159; WW_DOMAIN_1; 3.
DR   PROSITE; PS50020; WW_DOMAIN_2; 4.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000053760};
KW   Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW   ECO:0000256|PROSITE-ProRule:PRU00104}.
FT   DOMAIN          1..28
FT                   /note="WW"
FT                   /evidence="ECO:0000259|PROSITE:PS50020"
FT   DOMAIN          25..58
FT                   /note="WW"
FT                   /evidence="ECO:0000259|PROSITE:PS50020"
FT   DOMAIN          120..141
FT                   /note="WW"
FT                   /evidence="ECO:0000259|PROSITE:PS50020"
FT   DOMAIN          148..181
FT                   /note="WW"
FT                   /evidence="ECO:0000259|PROSITE:PS50020"
FT   DOMAIN          241..575
FT                   /note="HECT"
FT                   /evidence="ECO:0000259|PROSITE:PS50237"
FT   ACT_SITE        543
FT                   /note="Glycyl thioester intermediate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00104"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:KFO72583.1"
FT   NON_TER         575
FT                   /evidence="ECO:0000313|EMBL:KFO72583.1"
SQ   SEQUENCE   575 AA;  68630 MW;  E0317FCC032084DE CRC64;
     WEQRELPNGR IYYVDHNNKT TTWERPLPPG WEKRVDPRGR YYYVDHNTRT TTWQRPTAEY
     VRNYEQWQSQ RNQLQGAMQQ FSQRFLYQGG LFPRLGWQSV LASMLQLTFP LPFLLEKRQD
     NGRVYYVNHN TRTTQWEDPR TQGMIQEPPL PPGWEMKYTN EGVRYFVDHN TRTTTFKDPR
     PGFESGSKQG GSPGAYDRSF RWKYHQFRFL CHSNALPSHV KISVSRQTLF EDSFQQIMNM
     KPYDLRRRLY IIMRGEEGLD YGGIAREWFF LLSHEVLNPM YCLFEYAGKN NYCLQINPAS
     SINPDHLTYF RFIGRFIAMA LYHGKFIDTG FTLPFYKRML NKRPTLKDLE SIDPEFYNSI
     VWTKENSLEE CGLELYFIQD MEILGKVTTH ELKEGGESIR VTEENKEEYI MLLTDWRFTR
     GVEEQTKAFL DGFNEVVPLE WLRYFDEKEL ELMLCGMQEI DMNDWQKNTI YRHYTKNSKQ
     IQWFWQVVKE MDNEKRIRLL QFVTGTCRLP VGGFAELIGS NGPQKFCIDK VGKETWLPRS
     HTCFNRLDLP PYKSYEQLKE KLLYAIEETE GFGQE
//