ID   A0A024UDW6_9STRA        Unreviewed;       611 AA.
AC   A0A024UDW6;
DT   09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT   09-JUL-2014, sequence version 1.
DT   27-MAR-2024, entry version 42.
DE   RecName: Full=HECT-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012485};
DE            EC=2.3.2.26 {ECO:0000256|ARBA:ARBA00012485};
GN   ORFNames=H310_05184 {ECO:0000313|EMBL:ETW03823.1};
OS   Aphanomyces invadans.
OC   Eukaryota; Sar; Stramenopiles; Oomycota; Saprolegniales; Saprolegniaceae;
OC   Aphanomyces.
OX   NCBI_TaxID=157072 {ECO:0000313|EMBL:ETW03823.1};
RN   [1] {ECO:0000313|EMBL:ETW03823.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NJM9701 {ECO:0000313|EMBL:ETW03823.1};
RG   The Broad Institute Genomics Platform;
RA   Russ C., Tyler B., van West P., Dieguez-Uribeondo J., Young S.K., Zeng Q.,
RA   Gargeya S., Fitzgerald M., Abouelleil A., Alvarado L., Chapman S.B.,
RA   Gainer-Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M., Howarth C.,
RA   Imamovic A., Ireland A., Larimer J., McCowan C., Murphy C., Pearson M.,
RA   Poon T.W., Priest M., Roberts A., Saif S., Shea T., Sykes S., Wortman J.,
RA   Nusbaum C., Birren B.;
RT   "The Genome Sequence of Aphanomyces invadans NJM9701.";
RL   Submitted (DEC-2013) 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};
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DR   EMBL; KI913959; ETW03823.1; -; Genomic_DNA.
DR   RefSeq; XP_008868052.1; XM_008869830.1.
DR   AlphaFoldDB; A0A024UDW6; -.
DR   EnsemblFungi; H310_05184-t26_5; H310_05184-t26_5-p1; H310_05184.
DR   EnsemblProtists; ETW03823; ETW03823; H310_05184.
DR   GeneID; 20082234; -.
DR   VEuPathDB; FungiDB:H310_05184; -.
DR   OrthoDB; 5478214at2759; -.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004842; F:ubiquitin-protein transferase activity; IEA:InterPro.
DR   CDD; cd00078; HECTc; 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   Gene3D; 2.30.30.380; Zn-finger domain of Sec23/24; 1.
DR   InterPro; IPR000569; HECT_dom.
DR   InterPro; IPR035983; Hect_E3_ubiquitin_ligase.
DR   InterPro; IPR001876; Znf_RanBP2.
DR   InterPro; IPR036443; Znf_RanBP2_sf.
DR   PANTHER; PTHR11254; HECT DOMAIN UBIQUITIN-PROTEIN LIGASE; 1.
DR   PANTHER; PTHR11254:SF446; HECT-TYPE E3 UBIQUITIN TRANSFERASE; 1.
DR   Pfam; PF00632; HECT; 1.
DR   SMART; SM00119; HECTc; 1.
DR   SMART; SM00547; ZnF_RBZ; 1.
DR   SUPFAM; SSF56204; Hect, E3 ligase catalytic domain; 1.
DR   SUPFAM; SSF90209; Ran binding protein zinc finger-like; 1.
DR   PROSITE; PS50237; HECT; 1.
DR   PROSITE; PS01358; ZF_RANBP2_1; 1.
DR   PROSITE; PS50199; ZF_RANBP2_2; 1.
PE   4: Predicted;
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW   ECO:0000256|PROSITE-ProRule:PRU00104};
KW   Zinc {ECO:0000256|PROSITE-ProRule:PRU00322};
KW   Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00322}.
FT   DOMAIN          32..68
FT                   /note="RanBP2-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50199"
FT   DOMAIN          260..611
FT                   /note="HECT"
FT                   /evidence="ECO:0000259|PROSITE:PS50237"
FT   REGION          140..161
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        144..161
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        578
FT                   /note="Glycyl thioester intermediate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00104"
SQ   SEQUENCE   611 AA;  69012 MW;  060EF2DC1506FC6A CRC64;
     MPTYSAKTCL TGISHHVELI SSIYVDSLTS LRSGSSFMEQ QLWKCSVCSF SNVPDKTNCD
     LCQTTREAKK SKIPSLWRPL FQAAAKTDQA SAKLRGRTKS EEQQLNKVQL AAARRNLWRR
     EALPTGEVRW VRLPGRPHTQ DNHTAILGDD SSSPSPDMCS SRGSSCMSVG YVRVRDSTGR
     LVLNESDQVG GAHRLAPRRF GLASAALVVE VSKMPFLNKL KWYSMEIHRL WVPWELGHVE
     FVVRRDHLVE DSLLHVMRLS PEQLRQRWRV SFMGEPALDA GGVLREWISL LVVELFDPSF
     GLFVSTASSN HCAWVNSMSG AHQVRHLEYF SLIGRVVGKA LFEEQLVPVH FTVPLLKHVL
     GVPISFSDLQ FLDDELYQSL VWLKQCSNPD DVDALMLDFS VTRTTQRQDG KPITTETVPL
     APGGESIAVT VVNKAAYLDL LFQYHILDSV SYQLLMFLAA IYSVVPEELL KVFDYKELEL
     LLCGVPTVDV DDWKRHAQVA YLVENTPTRL ELQNVSWFWA VLDTFTNEQR AKLLQFVTGS
     SRVPAQGFKA LISTDGRVQP FKLSFCPMEH LYPRAHTCFN RLDLPLYESK SEMHTYLIAV
     LSQDATGFSM E
//