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Database: UniProt
Entry: G4Z255_PHYSP
LinkDB: G4Z255_PHYSP
Original site: G4Z255_PHYSP 
ID   G4Z255_PHYSP            Unreviewed;       673 AA.
AC   G4Z255;
DT   14-DEC-2011, integrated into UniProtKB/TrEMBL.
DT   14-DEC-2011, sequence version 1.
DT   27-MAR-2024, entry version 50.
DE   RecName: Full=HECT-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012485};
DE            EC=2.3.2.26 {ECO:0000256|ARBA:ARBA00012485};
GN   ORFNames=PHYSODRAFT_491598 {ECO:0000313|EMBL:EGZ21390.1};
OS   Phytophthora sojae (strain P6497) (Soybean stem and root rot agent)
OS   (Phytophthora megasperma f. sp. glycines).
OC   Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC   Phytophthora.
OX   NCBI_TaxID=1094619 {ECO:0000313|EMBL:EGZ21390.1, ECO:0000313|Proteomes:UP000002640};
RN   [1] {ECO:0000313|EMBL:EGZ21390.1, ECO:0000313|Proteomes:UP000002640}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=P6497 {ECO:0000313|EMBL:EGZ21390.1,
RC   ECO:0000313|Proteomes:UP000002640};
RX   PubMed=16946064; DOI=10.1126/science.1128796;
RA   Tyler B.M., Tripathy S., Zhang X., Dehal P., Jiang R.H., Aerts A.,
RA   Arredondo F.D., Baxter L., Bensasson D., Beynon J.L., Chapman J.,
RA   Damasceno C.M., Dorrance A.E., Dou D., Dickerman A.W., Dubchak I.L.,
RA   Garbelotto M., Gijzen M., Gordon S.G., Govers F., Grunwald N.J., Huang W.,
RA   Ivors K.L., Jones R.W., Kamoun S., Krampis K., Lamour K.H., Lee M.K.,
RA   McDonald W.H., Medina M., Meijer H.J., Nordberg E.K., Maclean D.J.,
RA   Ospina-Giraldo M.D., Morris P.F., Phuntumart V., Putnam N.H., Rash S.,
RA   Rose J.K., Sakihama Y., Salamov A.A., Savidor A., Scheuring C.F.,
RA   Smith B.M., Sobral B.W., Terry A., Torto-Alalibo T.A., Win J., Xu Z.,
RA   Zhang H., Grigoriev I.V., Rokhsar D.S., Boore J.L.;
RT   "Phytophthora genome sequences uncover evolutionary origins and mechanisms
RT   of pathogenesis.";
RL   Science 313:1261-1266(2006).
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; JH159153; EGZ21390.1; -; Genomic_DNA.
DR   RefSeq; XP_009524107.1; XM_009525812.1.
DR   AlphaFoldDB; G4Z255; -.
DR   STRING; 1094619.G4Z255; -.
DR   EnsemblProtists; EGZ21390; EGZ21390; PHYSODRAFT_491598.
DR   GeneID; 20656726; -.
DR   KEGG; psoj:PHYSODRAFT_491598; -.
DR   InParanoid; G4Z255; -.
DR   OMA; MEYINLR; -.
DR   Proteomes; UP000002640; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; 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   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   Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002640};
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}.
FT   TRANSMEM        27..47
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          340..673
FT                   /note="HECT"
FT                   /evidence="ECO:0000259|PROSITE:PS50237"
FT   REGION          146..167
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        640
FT                   /note="Glycyl thioester intermediate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00104"
SQ   SEQUENCE   673 AA;  76256 MW;  119E32BA7B2950E2 CRC64;
     MLLCGQEAAA SEPARRRLAD SSDSYNFMFY FVIGAMMLTC LIYNIFFKHK MEANFLRQQA
     LPETMLRQDV IASDQDMNNL WDCDVCGFKS YDAHTTCMLC GTDRAFKLLD KKDDANSAEL
     GGIAPSSASS SAKYVLYMED KENPLSRSAV NSRATPPRPG RSKSGAKINR EFFKRKLSAL
     NLRQQSARRR HEWSRERNDD GELIWVRKKH YMDRKVLKSL RTLDGLRSQS STSLRDSILS
     TGSVNSVGIV SRIVVSPKNP TGRLSLETAE GALATRCSDS SEFSQDELEQ VGSLPFQQKH
     AWFVQHTAAM EVPWEYGHLL LEIERDNLLH NSCEQLLWAT PDQLHQSLRI KFANEPGVDA
     GGLVREWFTL MTKEVFDDTT GLFYRSGNGD GLMINPASAE ASVDHLMYYQ AIGRFIGRAL
     FEGILIDAHL ALPVCKHILG IPITFSDLEF VDNDLYKNLK WLRDNTGVES LALDFTVNVD
     QTSKVVDLVP NGSNIPVTEE NKMEYINLRF RWIVATSISQ QLGSLMQGLF SIIPKELLSV
     FDHQELELLI CGIPDIDVLD WRTHTIYVGE RDERAITWFW NIVNEFTNEQ KARLLQFTTG
     SARVPVQGFK ALTMNDGRIC PFAIQCVSVD ECLYPRAHTC FNRIDLPRYE AEKDLRIALS
     LVIQMEVTGF TIE
//
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