GenomeNet

Database: UniProt
Entry: X0CXG6_FUSOX
LinkDB: X0CXG6_FUSOX
Original site: X0CXG6_FUSOX 
ID   X0CXG6_FUSOX            Unreviewed;      1146 AA.
AC   X0CXG6;
DT   14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT   14-MAY-2014, 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   ORFNames=FOQG_01611 {ECO:0000313|EMBL:EXK98861.1};
OS   Fusarium oxysporum f. sp. raphani 54005.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC   Fusarium oxysporum species complex.
OX   NCBI_TaxID=1089458 {ECO:0000313|EMBL:EXK98861.1, ECO:0000313|Proteomes:UP000030663};
RN   [1] {ECO:0000313|EMBL:EXK98861.1, ECO:0000313|Proteomes:UP000030663}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=54005 {ECO:0000313|EMBL:EXK98861.1,
RC   ECO:0000313|Proteomes:UP000030663};
RG   The Broad Institute Genome Sequencing Platform;
RA   Ma L.-J., Gale L.R., Schwartz D.C., Zhou S., Corby-Kistler H., Young S.K.,
RA   Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA   Arachchi H.M., Berlin A., Brown A., Chapman S.B., Chen Z., Dunbar C.,
RA   Freedman E., Gearin G., Goldberg J., Griggs A., Gujja S., Heiman D.,
RA   Howarth C., Larson L., Lui A., MacDonald P.J.P., Montmayeur A., Murphy C.,
RA   Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T., Shenoy N.,
RA   Sisk P., Stolte C., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT   "The Genome Sequence of Fusarium oxysporum PHW815.";
RL   Submitted (NOV-2011) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; JH658363; EXK98861.1; -; Genomic_DNA.
DR   AlphaFoldDB; X0CXG6; -.
DR   eggNOG; KOG0942; Eukaryota.
DR   HOGENOM; CLU_002173_2_4_1; -.
DR   Proteomes; UP000030663; Unassembled WGS sequence.
DR   GO; GO:0015629; C:actin cytoskeleton; IEA:UniProt.
DR   GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR   GO; GO:0061630; F:ubiquitin protein ligase activity; IEA:InterPro.
DR   GO; GO:0006996; P:organelle organization; IEA:UniProt.
DR   GO; GO:0000209; P:protein polyubiquitination; 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; IPR044611; E3A/B/C-like.
DR   InterPro; IPR000569; HECT_dom.
DR   InterPro; IPR035983; Hect_E3_ubiquitin_ligase.
DR   InterPro; IPR000048; IQ_motif_EF-hand-BS.
DR   PANTHER; PTHR45700; UBIQUITIN-PROTEIN LIGASE E3C; 1.
DR   PANTHER; PTHR45700:SF2; UBIQUITIN-PROTEIN LIGASE E3C; 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; PS50096; IQ; 1.
PE   4: Predicted;
KW   Ligase {ECO:0000313|EMBL:EXK98861.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000030663};
KW   Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW   ECO:0000256|PROSITE-ProRule:PRU00104}.
FT   DOMAIN          774..1146
FT                   /note="HECT"
FT                   /evidence="ECO:0000259|PROSITE:PS50237"
FT   REGION          1..37
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          646..669
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        1114
FT                   /note="Glycyl thioester intermediate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00104"
SQ   SEQUENCE   1146 AA;  129064 MW;  59A1E5045F11D863 CRC64;
     MFSTFTGNSR RPRNVNLSGT TGNPFTNTSW SPSAVSNTTK TVSNAQAERE KRQADRAKLK
     AAGKIQRIWR GYKTRAELKE SQRNAFDALY KSGPRQNPCE RLPKAFGLLL SFFSLRRDDD
     IQRAICYAHD TESVDLEAIA PSNVHPSRVG CLVQLLLQAL DKSLSIGDLS GDTHLLFKLV
     LRIVTKYPEL VIPAIDSYYT VVAKLCQFQK LSGQWQDVML QAISRPLEAA SHEGTSQVYR
     AYAFSFLAKN NLYFFEENIS TLSNAVRLSD LSKAIVTGLS SPSSEKHFQD AQLWQLAHFI
     DLSRFNANNS SGSGVLETLY TQLSSLSSTI SVRLLAKSTD GDENSSEEPL VPSLDPYITA
     RLMSLVDSNG ISQTLHEFST NLAGSSSQEY QSTSFLAGYI LTLLRCFPAN SDDIRMRLFL
     EEIPTISGDV PTIKFLWHIM SETAVFEKLR TESEAPLNVL RRYLGVTSET SNSLEEEQDW
     RIALLFLELY IFILRLSDDE DFFSGIDPRI MEQNQSISRI RSCSLSLEDV KMLTSFLKNT
     AFTLHYRAQD LSKSADGLEA ASRYRIDTYF GSGQSSAMIS EGPSSPTKSP TRLDIDSLRN
     IVTTAMKMLY ERDSRKQFLP TDHWLMTSKL DQSDFISAVI AEEKRQIDEN SDGSDVEGSE
     HGDGPGLYST IVGQRLSRHA RLEKLKAQQI RSQRERRLAE MKPKLEILKH MPFAVPFETR
     VQIFRHFIQL DRQQRGDNSQ SFFAGPYAKH HAQISRNSLF DDAYKQFYEI GEGLKDPIQI
     TFVDQFGTAE AGIDGGGVTK EFLISVTTEA FGAEGGRGMF TSNEKGLLFP DPTALDVIRE
     ELRHAGMTEA DSTFRDMISD LLKRYEFLGR IVGKCMYEGI LVDLAFAGFF LLKWTSTGPN
     DENTYKGNVN DLRDMDEDLY RGMLRLKNYP GDVSELGIDF TIEDQVSDPK NPVKTVTRKL
     IANGDQIHVT NDNRLLYISY VARHRLVVQP APQTSAFLRG LRSIIRPSWL SMFNQSELQR
     LVGGDSSEID IEDLRNHTIY SGLYQIGDDG EEHETIKLFW KVMRSFTDDQ RRAVLKYVSS
     TPRAPLLGFS QLRPLFSIRD GGTDEERLPS TSTCVNLLKL PRYTSEATLR EKLLYAVQSG
     AGFDLS
//
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