ID W2YKH8_PHYPR Unreviewed; 759 AA.
AC W2YKH8;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-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=F442_16230 {ECO:0000313|EMBL:ETP35555.1};
OS Phytophthora parasitica P10297.
OC Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC Phytophthora.
OX NCBI_TaxID=1317064 {ECO:0000313|EMBL:ETP35555.1, ECO:0000313|Proteomes:UP000018948};
RN [1] {ECO:0000313|EMBL:ETP35555.1, ECO:0000313|Proteomes:UP000018948}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=P10297 {ECO:0000313|EMBL:ETP35555.1,
RC ECO:0000313|Proteomes:UP000018948};
RG The Broad Institute Genomics Platform;
RA Russ C., Tyler B., Panabieres F., Shan W., Tripathy S., Grunwald N.,
RA Machado M., Johnson C.S., Walker B., Young S.K., Zeng Q., Gargeya S.,
RA Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Phytophthora parasitica P10297.";
RL Submitted (NOV-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};
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:ETP35555.1}.
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DR EMBL; ANIY01003429; ETP35555.1; -; Genomic_DNA.
DR AlphaFoldDB; W2YKH8; -.
DR EnsemblProtists; ETP35555; ETP35555; F442_16230.
DR Proteomes; UP000018948; Unassembled WGS sequence.
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 Reference proteome {ECO:0000313|Proteomes:UP000018948};
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 167..197
FT /note="RanBP2-type"
FT /evidence="ECO:0000259|PROSITE:PS50199"
FT DOMAIN 423..759
FT /note="HECT"
FT /evidence="ECO:0000259|PROSITE:PS50237"
FT ACT_SITE 726
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00104"
SQ SEQUENCE 759 AA; 85368 MW; F781DBB4BE71002F CRC64;
MHRYLRVHAR LNTTRHPRLI RCLQAAKMRI ANVSRASAIR RRNFLSIVAG LLLCTIKSVA
ATVTDTQADQ LEGADKRDVV GLRGLMPIVD GTYSNSSGGY GYYYESSSGY NGYEDSSDGS
SSVKTVVIGV SIGVGLMLIT VCLTWKACVE CCTSTNRRSR HRAFIERPNA GWKCEVCLHT
NEFSQTGCVL CGTTAEELKI IRSRQEDTNT SAVVAPQVED STRSASNYLL MSSPRAAWVR
SLNTFHSGDL TDRQLVARER HQWKRCIGGQ NVRWVHIPFE VLQDNEALCS TIIKERDFQD
WHKRHPPKVS GPSRMSVSSV LFSDSSGQQL SWLTPGTAFV RDDDSRSQSR TARWRLAEEF
SASSRQYSKT VVRASTLVFS EKAQWFYQYS LKLCSSIVDG YHTIRIHRDR VLKQSMNLFM
SAPSGTLHRR LRVDFMDEAG VDGGGILREW LHLVCSQLFA EAPGLFTLTS SSAHQGYWFN
RTSAEKCTKQ LEMYIFFGKL LGKALLEGLL LNVRLSIPLL KHILGVPLKL SDLYLLDETV
YSSMMWILEN DNTNALGLNF TVEGVELIPS GADVTLHDGN KQLYVAKVAQ YYLFDSVRAE
ISSIMEGLRS VISDTVLHVF DFKELDLLLS GLPQIDVNDW RQHTDVRFYE QSTHEFELVG
WFWEVLESFS QDQRGRLLQY VTGSSGVPVE GFKGLTGMDG EIQLFTIQLG KDVSTVYTVL
PHASTCLNRL DLPLYASKAE LERILTMVVE MDVTGFSSR
//
