ID   A0A024U5X2_9STRA        Unreviewed;       591 AA.
AC   A0A024U5X2;
DT   09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT   09-JUL-2014, sequence version 1.
DT   27-MAR-2024, entry version 39.
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_06856 {ECO:0000313|EMBL:ETW01287.1};
OS   Aphanomyces invadans.
OC   Eukaryota; Sar; Stramenopiles; Oomycota; Saprolegniales; Saprolegniaceae;
OC   Aphanomyces.
OX   NCBI_TaxID=157072 {ECO:0000313|EMBL:ETW01287.1};
RN   [1] {ECO:0000313|EMBL:ETW01287.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NJM9701 {ECO:0000313|EMBL:ETW01287.1};
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; KI913963; ETW01287.1; -; Genomic_DNA.
DR   RefSeq; XP_008870285.1; XM_008872063.1.
DR   AlphaFoldDB; A0A024U5X2; -.
DR   STRING; 157072.A0A024U5X2; -.
DR   EnsemblFungi; H310_06856-t26_1; H310_06856-t26_1-p1; H310_06856.
DR   EnsemblProtists; ETW01287; ETW01287; H310_06856.
DR   GeneID; 20083906; -.
DR   VEuPathDB; FungiDB:H310_06856; -.
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   InterPro; IPR000569; HECT_dom.
DR   InterPro; IPR035983; Hect_E3_ubiquitin_ligase.
DR   InterPro; IPR001876; Znf_RanBP2.
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   SUPFAM; SSF56204; Hect, E3 ligase catalytic domain; 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          1..30
FT                   /note="RanBP2-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50199"
FT   DOMAIN          255..591
FT                   /note="HECT"
FT                   /evidence="ECO:0000259|PROSITE:PS50237"
FT   ACT_SITE        558
FT                   /note="Glycyl thioester intermediate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00104"
SQ   SEQUENCE   591 AA;  67393 MW;  D27CBD8FAE3203C0 CRC64;
     MENLWACDVC DFKNYDGHKT CILCGTERDF TLYGKVPSKR TAAVEDGNKA ATAGLSPTNF
     VLMNDSTPRT IKKNRNFAKL RLNNLNIRQK GARRRHDWVR NVDEQSGNIV WGRNRDILDH
     KVLKRIVVKD SLPPLADDGD FDLPMLRDSV SSVSSVGSIA SVGYVSKMVM TPRHPDGRMS
     FETAEGQTAF QTVNPTVFSS AELKDVSQLS FQQKHAWFVQ YTSTMEVPWE YGHMLLEIDR
     ANLLHNSCEQ LLWATHDQLH QSLRIKFLNE PGVDAGGLER EWFTLMTEEI FDERTGLFGA
     CMDNAYMIRA TSSEASEDHL MYFQAIGRFI GRGLFEGMLL DAHLALPLYK HILGTPITFS
     DLEFIDVELY NNLKWLKQNK GVESLCLDFS VNVAQYDKEP LTIDLCPNGR HIAVTDDNKD
     EYIYLRFKWI MMTSISPQLA SLIKGIYSVI PLEMLSVFDH QELELLMCGI PDVNVDDWKA
     HTTYIGNECD PQVIEWFWEV VTGFSTEQRA RLLQFTTGSA RVPVQGFKTL TMNDGRICLF
     AIQGIRKEEC LYPRAHTCFN RLDLPMYSSK KDLETALTMV IKMEVTGFTI E
//