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Database: UniProt
Entry: W2FX52_PHYPR
LinkDB: W2FX52_PHYPR
Original site: W2FX52_PHYPR 
ID   W2FX52_PHYPR            Unreviewed;       672 AA.
AC   W2FX52;
DT   19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT   19-MAR-2014, sequence version 1.
DT   27-MAR-2024, entry version 52.
DE   RecName: Full=HECT-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012485};
DE            EC=2.3.2.26 {ECO:0000256|ARBA:ARBA00012485};
GN   ORFNames=L915_18643 {ECO:0000313|EMBL:ETK74615.1}, L916_18547
GN   {ECO:0000313|EMBL:ETL28037.1}, L917_18370
GN   {ECO:0000313|EMBL:ETL81293.1};
OS   Phytophthora parasitica (Potato buckeye rot agent).
OC   Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC   Phytophthora.
OX   NCBI_TaxID=4792 {ECO:0000313|EMBL:ETK74615.1};
RN   [1] {ECO:0000313|EMBL:ETL81293.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CHvinca01 {ECO:0000313|EMBL:ETL81293.1};
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., Arredondo F., Hong C., Coffey M., Young S.K.,
RA   Zeng Q., Gargeya S., Fitzgerald M., Abouelleil A., Alvarado L.,
RA   Chapman S.B., Gainer-Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M.,
RA   Howarth C., Imamovic A., Ireland A., Larimer J., McCowan C., Murphy C.,
RA   Pearson M., Poon T.W., Priest M., Roberts A., Saif S., Shea T., Sykes S.,
RA   Wortman J., Nusbaum C., Birren B.;
RT   "The Genome Sequence of Phytophthora parasitica CHvinca01.";
RL   Submitted (NOV-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ETK74615.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CJ02B3 {ECO:0000313|EMBL:ETK74615.1};
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., Arredondo F., Hong C., Coffey M., Young S.K.,
RA   Zeng Q., Gargeya S., Fitzgerald M., Abouelleil A., Alvarado L.,
RA   Chapman S.B., Gainer-Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M.,
RA   Howarth C., Imamovic A., Ireland A., Larimer J., McCowan C., Murphy C.,
RA   Pearson M., Poon T.W., Priest M., Roberts A., Saif S., Shea T., Sykes S.,
RA   Wortman J., Nusbaum C., Birren B.;
RT   "The Genome Sequence of Phytophthora parasitica CJ02B3.";
RL   Submitted (NOV-2013) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EMBL:ETL28037.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CJ05E6 {ECO:0000313|EMBL:ETL28037.1};
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., Arredondo F., Hong C., Coffey M., Young S.K.,
RA   Zeng Q., Gargeya S., Fitzgerald M., Abouelleil A., Alvarado L.,
RA   Chapman S.B., Gainer-Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M.,
RA   Howarth C., Imamovic A., Ireland A., Larimer J., McCowan C., Murphy C.,
RA   Pearson M., Poon T.W., Priest M., Roberts A., Saif S., Shea T., Sykes S.,
RA   Wortman J., Nusbaum C., Birren B.;
RT   "The Genome Sequence of Phytophthora parasitica CJ05E6.";
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};
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DR   EMBL; KI689027; ETK74615.1; -; Genomic_DNA.
DR   EMBL; KI675830; ETL28037.1; -; Genomic_DNA.
DR   EMBL; KI682535; ETL81293.1; -; Genomic_DNA.
DR   EnsemblProtists; ETK74615; ETK74615; L915_18643.
DR   EnsemblProtists; ETL28037; ETL28037; L916_18547.
DR   EnsemblProtists; ETL81293; ETL81293; L917_18370.
DR   VEuPathDB; FungiDB:PPTG_05324; -.
DR   OMA; WRAHTHV; -.
DR   Proteomes; UP000053236; Unassembled WGS sequence.
DR   Proteomes; UP000053864; Unassembled WGS sequence.
DR   Proteomes; UP000054423; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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   SMART; SM00547; ZnF_RBZ; 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   Membrane {ECO:0000256|SAM:Phobius};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius};
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   TRANSMEM        17..38
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          66..92
FT                   /note="RanBP2-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50199"
FT   DOMAIN          323..672
FT                   /note="HECT"
FT                   /evidence="ECO:0000259|PROSITE:PS50237"
FT   ACT_SITE        639
FT                   /note="Glycyl thioester intermediate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00104"
SQ   SEQUENCE   672 AA;  76094 MW;  2C8202B29C47DCE5 CRC64;
     MSSQAGDVDS VVSAVKWIGI MLGVAAVVAV AIIVYMCCYR KNSTAQSELM DGLLRRDQLE
     ETELEDEGKG WQCVVCGLAN SAKRKTCLMC GTSIGFLMTG ELGRRKSSRM LLRNNSRSIM
     GADMAGGAGE EEDIEALRSR QRALFKRRMN MMAARKNLSQ RQRGAFRRRL WQRKQMSDGK
     FHWVRQNSTD VVDPVPELQD GDAAQPTLQS TEAKSLAGPN GESVTDYHNL RSQGFVSMYD
     ASGRLTWTKA DEVSIDMESF DKMRNGLEKM DFEGVMALSF RMKKQWFLVQ LSRIATPVTE
     AVAKLTVTRE RIIQQSLQLA EAAPDALHAY LKITFEGEPG IDAGGLLREW FGIVCKEIFS
     EKMGLFVPTK GEDMSYWIDP LSGEKNESHL KLFRLAGILI GKALFEGLVL DVHLALPLLK
     HVLGIPISFS DLEFLDEELH RNCKWLRSNN HVEALCLTFS VMLENGTEVD LKENGRNIDV
     TDENKEEYLR LILEHRMLDS IADQLQEFLM GIYDVVPKAL LSVFDYQELE LILCGIPTID
     TADWRTHTHV RYIKPEENRK GKITVEEQNG VLEWFWIVVE GLAPEERAKL LQFVTGTSRV
     PVEGFRGLMS SSGIIHEFTI QFVSRGKEKS DLFPKAHTCF NRLDLPMYRD MEELETYLTM
     VSQMEVFGFG LE
//
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