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Database: UniProt
Entry: A0A319E6L4_9EURO
LinkDB: A0A319E6L4_9EURO
Original site: A0A319E6L4_9EURO 
ID   A0A319E6L4_9EURO        Unreviewed;      1191 AA.
AC   A0A319E6L4;
DT   10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT   10-OCT-2018, sequence version 1.
DT   27-MAR-2024, entry version 19.
DE   RecName: Full=HECT domain-containing protein {ECO:0000259|PROSITE:PS50237};
GN   ORFNames=BO71DRAFT_178177 {ECO:0000313|EMBL:PYH96348.1};
OS   Aspergillus ellipticus CBS 707.79.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=1448320 {ECO:0000313|EMBL:PYH96348.1, ECO:0000313|Proteomes:UP000247810};
RN   [1] {ECO:0000313|EMBL:PYH96348.1, ECO:0000313|Proteomes:UP000247810}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 707.79 {ECO:0000313|EMBL:PYH96348.1,
RC   ECO:0000313|Proteomes:UP000247810};
RG   DOE Joint Genome Institute;
RA   Vesth T.C., Nybo J., Theobald S., Brandl J., Frisvad J.C., Nielsen K.F.,
RA   Lyhne E.K., Kogle M.E., Kuo A., Riley R., Clum A., Nolan M., Lipzen A.,
RA   Salamov A., Henrissat B., Wiebenga A., De vries R.P., Grigoriev I.V.,
RA   Mortensen U.H., Andersen M.R., Baker S.E.;
RT   "The genomes of Aspergillus section Nigri reveals drivers in fungal
RT   speciation.";
RL   Submitted (FEB-2018) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; KZ825838; PYH96348.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A319E6L4; -.
DR   STRING; 1448320.A0A319E6L4; -.
DR   Proteomes; UP000247810; Unassembled WGS sequence.
DR   GO; GO:0061630; F:ubiquitin protein ligase activity; IEA:InterPro.
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   PANTHER; PTHR45700; 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.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000247810};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW   ECO:0000256|PROSITE-ProRule:PRU00104}.
FT   DOMAIN          850..1191
FT                   /note="HECT"
FT                   /evidence="ECO:0000259|PROSITE:PS50237"
FT   REGION          1..83
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          98..126
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          234..330
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          361..386
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          414..439
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          547..594
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          645..669
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..22
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        234..248
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        255..269
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        417..432
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        559..575
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        1159
FT                   /note="Glycyl thioester intermediate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00104"
SQ   SEQUENCE   1191 AA;  132447 MW;  DE892E1F0A0F63C0 CRC64;
     MPSRSPYNSS HPPTSDSPAS HIASSAIPFP AEGTSPYRNP HDASGLSPMS GNPAASPPHR
     RGHSRSISHP FPSPFGGIAK RRNRSISKKD NFLLDSDDDD VVTYLPDPHS SSPRKGPPRP
     TAGEEMTSGK CMVCNSMVRW PRNLKVFRCT ECLTVNDLEA YVDSGKTSGP GMAGNDGKPP
     TPIVPRKAIP LSVERTKTIV DECLSKYFRQ LLNVSEQPSP EKLGSKRLDV AQDENLSHSP
     SHSSGYLSEP RQPVDPRGRS SSTSNQLGKP EGMGGIPNYS KPSLAPSYAH GEGKGSQMRS
     RDAQNAPRRD RSPRNAVRPN GPEAKNPTSR SYIFRALEEY IITSFKGSDC LNSSFTTVQH
     AAQPAENSSP PKQKAEPSSA QASSQVVFEP DPKLLLLGDI AENSSWWMNE VEQISSTHPS
     RAKERRDKTS SSSRAVSSRS PRINWPELAQ WHQVIMSAGS SWVELWSTMK PCEMRKEEDV
     LVAQKWDTVD LAMVDREITE SRLHLHRTLL KATETLLKRP RRPLKKPEDI RFLLMLLTNP
     LIHPSSPSLA SHLAPSAGRS DRRPSHPKDG NPRPVPRDLK PPPKPRSGGP GHHSGIVKRI
     LGLLANLPND CHHYLVSWFS RFSAGQFEKV VEIVGSFVTY RLTRQHGRKR SDSTQHDDGL
     VPSFSSAAGT TPAELHAAIN GRSPGKAANE NVDKPVVYTD DWQVRAAARV MSLLFTANNA
     SVSRKPDSAF GQDAGSVARH QANRRGHMIP TSSFYNTLLD YSDLVADFEA WESKATKFSF
     CQYPFFLSIW AKIHILEHDA RRQMEVKARE AFFNSIMSRK AISQYLMLKV RRDCLVEDSL
     RGVSEVVGSS QEEIKKGLRI EFVGEEGVDA GGLRKEWFLL LVREVFDPHH GLFIYDEDSQ
     YCYFNPYCFE SSEQFFLVGV LLGLAIYNST ILDIALPPFA FKKLLAAAPL SALSRPAYKC
     SLDDLAEFRP ALAKGLRALL DFDGDVTETF CYDFVAQVDR YGEVVPVPLC AGGESRPVTN
     ANRREFVDLY VHYLLDTAVT RQFEPFKRGF FTVCGGNALS LFRPEEIELL VRGSDEALDV
     ASLRAVATYD NWSNARPETE PVVRWFWDFF EQTQPQAQRK ILSFVTGSDR IPAMGATSLS
     IRLACLGDDT SRFPTARTCF NQLGLYLYET RAKLERVLWD AVLNSEGFGL K
//
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