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.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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
//