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Database: UniProt
Entry: A0A428PF19_9HYPO
LinkDB: A0A428PF19_9HYPO
Original site: A0A428PF19_9HYPO 
ID   A0A428PF19_9HYPO        Unreviewed;      1147 AA.
AC   A0A428PF19;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   27-MAR-2024, entry version 16.
DE   RecName: Full=HECT-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012485};
DE            EC=2.3.2.26 {ECO:0000256|ARBA:ARBA00012485};
GN   ORFNames=CEP53_008362 {ECO:0000313|EMBL:RSL51624.1};
OS   Fusarium sp. AF-6.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC   Fusarium solani species complex.
OX   NCBI_TaxID=1325737 {ECO:0000313|EMBL:RSL51624.1, ECO:0000313|Proteomes:UP000287544};
RN   [1] {ECO:0000313|EMBL:RSL51624.1, ECO:0000313|Proteomes:UP000287544}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NRRL62590 {ECO:0000313|EMBL:RSL51624.1,
RC   ECO:0000313|Proteomes:UP000287544};
RA   Stajich J.E., Carrillo J., Kijimoto T., Eskalen A., O'Donnell K.,
RA   Kasson M.;
RT   "Comparative genomic analysis of Ambrosia Fusariam Clade fungi.";
RL   Submitted (JUN-2017) to the EMBL/GenBank/DDBJ databases.
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:RSL51624.1}.
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DR   EMBL; NKCJ01000195; RSL51624.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A428PF19; -.
DR   STRING; 1325737.A0A428PF19; -.
DR   Proteomes; UP000287544; Unassembled WGS sequence.
DR   GO; GO:0015629; C:actin cytoskeleton; IEA:UniProt.
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   Pfam; PF00612; IQ; 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   Reference proteome {ECO:0000313|Proteomes:UP000287544};
KW   Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW   ECO:0000256|PROSITE-ProRule:PRU00104}.
FT   DOMAIN          775..1147
FT                   /note="HECT"
FT                   /evidence="ECO:0000259|PROSITE:PS50237"
FT   REGION          1..59
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          646..672
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..44
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        45..59
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        1115
FT                   /note="Glycyl thioester intermediate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00104"
SQ   SEQUENCE   1147 AA;  128232 MW;  F2582E52F942DE56 CRC64;
     MFSTFTGNSR RPRNVNLSGS AGNPFANTSW SPSAVSNASK TVSNAQAERE KRQAERQKIK
     SAVKIQRVWR GHRTRASLRE SQRASFDKLY ASDAAGSPED RLPRAFSLLL LVFSPRRDDD
     IRRAIRYARD TESVPLEAIV PSRTHPARLE RLVRLLVEAL DTSVSTGQLS EDAQLLGKLA
     IRIIASSPNL VLPSVDRYYT VIAKLCQAQQ LPGQWPDIVL EALSAPLGVD SASGTSKVYH
     AYAFSFLASS NLSFFEANIA VLTKNISLPD LSRAIIEGQP SVSNAQTSED ALLWQLAHFV
     DLGRSSTNTT TGSAILETLY TQLATLSSAI SVRLPAKSSN EGLSDEDAAE AHLVLDPYIA
     TKLTSLVESN GISQTLRDFS VNLAGSSHHE FQGVSLLAGY ILTLLQCFPA SSDDIRMRLF
     LEEIPTPSGD IPTVKFLWGI MRRTSVFNKL MTGSEQPIDV LRRYLGVTPS TSGASSSSTE
     EQDWRIILLF LELYIFILRL SDDEDFFSGI YPQLLQSNSS TSRIRSCSLS LEDVKPLTMF
     LKNTAFTLHY KAQELSKSRE ALEAAAKSRV NSYLGASISR PVQDATALSS LKGPARLGLD
     SLRSIVTVAM KMLYERDSRK QFLPTNHWLM TDKLDKEDFI SAVIAEEKRQ SEEDSGDSEG
     EEEEDPLRTF STFGGQSLSR RIRLEQLKAQ QTRAMRERRL AEMGPKLEIL KHMPFVVPFE
     TRVMIFRQFI QLDRGHREGN MPRHFNPFNK HHAQIRRKRL FEDAYKQFYE LGEGFKDPIQ
     ITFVDQFGTP EAGIDGGGVT KEFLISVTSE AFGNHEGAGM FASNEKGLLF PDPTAMDVLR
     ESLRESGLSE EDPEFREFVT SQLRRFEFLG RIVGKCMYEG ILVDLAFAGF FLLKWASTGP
     NDENNYKGSV NDLRDMDEDL YNGMLRLKNY SGDISELGID FTIEDQVSQS GQPVKTITKK
     LIANGDQVHV TNDNRLLYIS YVARHRLVVQ PSLQTAAFLR GLRGIIRPSW LSMFNQSELQ
     RLVGGDSSEI DIDDLRRNTV YSGLYEIGDD GQEHDTIKLF WKVMRGFTDS QRRSVLKYVS
     STPRAPLLGF SQLNPKFSIR DGGTDEDRLP STSTCVNLLK LPRYKTEAVL REKLLYAVTS
     GAGFDLS
//
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