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Database: UniProt
Entry: A0A0W8CDK4_PHYNI
LinkDB: A0A0W8CDK4_PHYNI
Original site: A0A0W8CDK4_PHYNI 
ID   A0A0W8CDK4_PHYNI        Unreviewed;       596 AA.
AC   A0A0W8CDK4;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   27-MAR-2024, entry version 29.
DE   RecName: Full=HECT-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012485};
DE            EC=2.3.2.26 {ECO:0000256|ARBA:ARBA00012485};
GN   ORFNames=AM587_10012569 {ECO:0000313|EMBL:KUF82185.1};
OS   Phytophthora nicotianae (Buckeye rot agent).
OC   Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC   Phytophthora.
OX   NCBI_TaxID=4790 {ECO:0000313|EMBL:KUF82185.1, ECO:0000313|Proteomes:UP000052943};
RN   [1] {ECO:0000313|EMBL:KUF82185.1, ECO:0000313|Proteomes:UP000052943}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=race 0 {ECO:0000313|Proteomes:UP000052943};
RA   Liu H., Ma X., Yu H., Fang D., Li Y., Wang X., Wang W., Dong Y., Xiao B.;
RT   "Genomes and virulence difference between two physiological races of
RT   Phytophthora nicotianae.";
RL   Submitted (NOV-2015) 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: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KUF82185.1}.
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DR   EMBL; LNFO01003805; KUF82185.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0W8CDK4; -.
DR   STRING; 4790.A0A0W8CDK4; -.
DR   EnsemblProtists; KUF82185; KUF82185; AM587_10012569.
DR   OMA; CAGVQFE; -.
DR   Proteomes; UP000052943; 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; 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.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000052943};
KW   Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW   ECO:0000256|PROSITE-ProRule:PRU00104}.
FT   DOMAIN          250..595
FT                   /note="HECT"
FT                   /evidence="ECO:0000259|PROSITE:PS50237"
FT   ACT_SITE        557
FT                   /note="Glycyl thioester intermediate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00104"
SQ   SEQUENCE   596 AA;  67771 MW;  A0B4C4B1DCE77C5C CRC64;
     MILTTYVATT NCGNWHRKLT TLHSKHCNSE QMADLRVIAA QREAERGFAT CVSCGFKNFA
     RVLHCALCGN SSTDSKLPAT VLPSVNDPRE DVALPRRWEW TRELDVHDRL VWRRRLAEGG
     DCSPGYVLRF DLPPETEPEA EREVSKHRQR SLSTGYDPCA DVQFELLEPR DVDPTQFPLP
     PPRTDMSDTM EDLKHTAVHV AAQDFPTKYA HFVASATSLI QAGDRSVRSC LSVHRDYILE
     QSVQHINCIR EESIRSVRLQ VNFAGHEDLP SDEKDVSGLH RGWMTLLNEK LVDPDVGLFL
     CTQRSDQTFF INPQSKLVLG EDHLQHFNAA GRLIGRALLE GSVLNFHLCA PLLKMMLGTP
     ITFGDLEFLD AEIYRNLTWL LDNDSAESLE LDFTVTQRHG NLAQTIELIP AGRNIQVNDD
     NKFEFADRKF RFMMFECVAP QLASFLKGFY DVVPQRMLLP FNYEELDYLL CGSDEIDIAD
     WRLHTHLALE SRQEVTWFWD VVKEMSRVYQ KRLLQLATGC SRVPLVGFQG LTSYDGQLCK
     FTLTDAVGVA YFRSHACHNM LELPYFETKD DLRAALYAAL YNESSAADTK ALNTVP
//
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