ID F0WZT3_9STRA Unreviewed; 273 AA.
AC F0WZT3;
DT 03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 03-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE RecName: Full=HECT-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012485};
DE EC=2.3.2.26 {ECO:0000256|ARBA:ARBA00012485};
GN Name=AlNc14C441G11674 {ECO:0000313|EMBL:CCA27010.1};
GN ORFNames=ALNC14_131540 {ECO:0000313|EMBL:CCA27010.1};
OS Albugo laibachii Nc14.
OC Eukaryota; Sar; Stramenopiles; Oomycota; Albuginales; Albuginaceae; Albugo.
OX NCBI_TaxID=890382 {ECO:0000313|EMBL:CCA27010.1};
RN [1] {ECO:0000313|EMBL:CCA27010.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=21750662; DOI=10.1371/journal.pbio.1001094;
RA Kemen E., Gardiner A., Schultz-Larsen T., Kemen A.C., Balmuth A.L.,
RA Robert-Seilaniantz A., Bailey K., Holub E., Studholme D.J., Maclean D.,
RA Jones J.D.;
RT "Gene gain and loss during evolution of obligate parasitism in the white
RT rust pathogen of Arabidopsis thaliana.";
RL PLoS Biol. 9:e1001094-e1001094(2011).
RN [2] {ECO:0000313|EMBL:CCA27010.1}
RP NUCLEOTIDE SEQUENCE.
RA MacLean D.;
RL Submitted (FEB-2011) 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; FR824484; CCA27010.1; -; Genomic_DNA.
DR AlphaFoldDB; F0WZT3; -.
DR EnsemblProtists; CCA27010; CCA27010; ALNC14_131540.
DR HOGENOM; CLU_1020910_0_0_1; -.
DR GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IEA:InterPro.
DR Gene3D; 3.30.2410.10; Hect, E3 ligase catalytic domain; 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 Ligase {ECO:0000313|EMBL:CCA27010.1};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW ECO:0000256|PROSITE-ProRule:PRU00104}.
FT DOMAIN 135..273
FT /note="HECT"
FT /evidence="ECO:0000259|PROSITE:PS50237"
FT ACT_SITE 240
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00104"
SQ SEQUENCE 273 AA; 31432 MW; 30116FACC3CCE948 CRC64;
MDMCKCIEAT RKPQLHICCS MPILQYPELQ CSRICDSATI FVGRMILLSV SKLPQVSRVA
DIEIVPTKLP SKAMEPIPHH IASSLPSLLL LLQLLLLLLR SNYNIDLRTH VTHVLWRENS
FRYDIIPRTS LAVFDYQLPL CGVPSIDVDN WPSRTYVKYH EIDQPNRREK NTAEWFWEFF
SSFLQEKPAR LLQFATGSSR VSVKRFKALL GSDGRVRRVG IRLVSCGTPF EGLFPQAHTC
FNRIDLPIYE SKEKEETYLN LVINMEIAGF SMQ
//
