ID   T1KN81_TETUR            Unreviewed;       638 AA.
AC   T1KN81;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2013, sequence version 1.
DT   27-MAR-2024, entry version 50.
DE   RecName: Full=HECT-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012485};
DE            EC=2.3.2.26 {ECO:0000256|ARBA:ARBA00012485};
GN   Name=107365964 {ECO:0000313|EnsemblMetazoa:tetur16g00020.1};
OS   Tetranychus urticae (Two-spotted spider mite).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida; Acari;
OC   Acariformes; Trombidiformes; Prostigmata; Eleutherengona; Raphignathae;
OC   Tetranychoidea; Tetranychidae; Tetranychus.
OX   NCBI_TaxID=32264 {ECO:0000313|EnsemblMetazoa:tetur16g00020.1, ECO:0000313|Proteomes:UP000015104};
RN   [1] {ECO:0000313|Proteomes:UP000015104}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=London {ECO:0000313|Proteomes:UP000015104};
RA   Rombauts S.;
RL   Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EnsemblMetazoa:tetur16g00020.1}
RP   IDENTIFICATION.
RG   EnsemblMetazoa;
RL   Submitted (JUN-2015) to UniProtKB.
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; CAEY01000270; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; XP_015789032.1; XM_015933546.1.
DR   AlphaFoldDB; T1KN81; -.
DR   STRING; 32264.T1KN81; -.
DR   EnsemblMetazoa; tetur16g00020.1; tetur16g00020.1; tetur16g00020.
DR   GeneID; 107365964; -.
DR   KEGG; tut:107365964; -.
DR   eggNOG; KOG0940; Eukaryota.
DR   HOGENOM; CLU_002173_1_1_1; -.
DR   OMA; KENCNNH; -.
DR   OrthoDB; 5480520at2759; -.
DR   UniPathway; UPA00143; -.
DR   Proteomes; UP000015104; Unassembled WGS sequence.
DR   GO; GO:0061630; F:ubiquitin protein ligase activity; IEA:InterPro.
DR   GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR   GO; GO:0009966; P:regulation of signal transduction; IEA:UniProt.
DR   GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:InterPro.
DR   CDD; cd00078; HECTc; 1.
DR   CDD; cd00201; WW; 2.
DR   Gene3D; 2.20.70.10; -; 1.
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; IPR024928; E3_ub_ligase_SMURF1.
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:SF395; E3 UBIQUITIN-PROTEIN LIGASE SMURF1; 1.
DR   PANTHER; PTHR11254; HECT DOMAIN UBIQUITIN-PROTEIN LIGASE; 1.
DR   Pfam; PF00632; HECT; 1.
DR   Pfam; PF00397; WW; 1.
DR   PIRSF; PIRSF001569; E3_ub_ligase_SMURF1; 3.
DR   SMART; SM00119; HECTc; 1.
DR   SMART; SM00456; WW; 2.
DR   SUPFAM; SSF56204; Hect, E3 ligase catalytic domain; 1.
DR   SUPFAM; SSF51045; WW domain; 2.
DR   PROSITE; PS50237; HECT; 1.
DR   PROSITE; PS50020; WW_DOMAIN_2; 2.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000015104};
KW   Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW   ECO:0000256|PROSITE-ProRule:PRU00104}.
FT   DOMAIN          124..157
FT                   /note="WW"
FT                   /evidence="ECO:0000259|PROSITE:PS50020"
FT   DOMAIN          173..209
FT                   /note="WW"
FT                   /evidence="ECO:0000259|PROSITE:PS50020"
FT   DOMAIN          301..638
FT                   /note="HECT"
FT                   /evidence="ECO:0000259|PROSITE:PS50237"
FT   REGION          17..67
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        17..61
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        606
FT                   /note="Glycyl thioester intermediate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001569-1,
FT                   ECO:0000256|PROSITE-ProRule:PRU00104"
SQ   SEQUENCE   638 AA;  72886 MW;  4C86DD7338791618 CRC64;
     MVFSIKMNFS KVLNLVNHSH NNNSNNNQSH SHNQGNSSSS SLSTNNHSSR NENVISGRNY
     QRRSTRHSRY LSRNQLHSAA ANVSISPPPP PPPSSNLHPV NLPPTTHNLT CANNGSLGSS
     TSPIGLPEGY EMRIAPKGQV YFHHVPTSKS TWHDPRVPRE LLNQNFDLDK LVGKLPSGWE
     IRTISSGDHE RVYFVDHNRK TTQFTDPRLV ANPDILKKIL RERPNLCYAN VEKTPKHSGR
     SSNGADPHIF RESCKRKNLV QKMAGLRQEL QEMQPQTGHC RLEVSRKDIF EDSYRAVMKK
     KPKDLMKRLI VTFKGEEGLD YGGLAREWLY LLSHEMLNPQ YGLFQYTRED VYTLQINRDS
     SVNPDHLTYF HFVGRIIGMA IFHGHYIDGG FTLPFYKMLL NKSINLEDIQ VVDPELYRSL
     CWMLENNLSG VLETTFSVEH NSFGHLQVHE LKPNGKNIPV TDENKREYVK LYVNYRFRRG
     IGQQFHALQK GLNELVPTSS LQIFDEKELE LVISGLGNID INDWKSNTRL KHCTPDTPVV
     KWFWQAVESY AEERRARLLQ FVTGSSRVPL QGFKALQGST GASGPRLFTI HLIEASSDNL
     PKAHTCFNRI DLPPYETYEK LYEKLTQAIE ETCGFAVE
//