ID A0A2S6CIH3_9PEZI Unreviewed; 1264 AA.
AC A0A2S6CIH3;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE RecName: Full=HECT domain-containing protein {ECO:0000259|PROSITE:PS50237};
GN ORFNames=CBER1_08885 {ECO:0000313|EMBL:PPJ59530.1};
OS Cercospora berteroae.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Cercospora.
OX NCBI_TaxID=357750 {ECO:0000313|EMBL:PPJ59530.1, ECO:0000313|Proteomes:UP000237631};
RN [1] {ECO:0000313|Proteomes:UP000237631}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS538.71 {ECO:0000313|Proteomes:UP000237631};
RA de Jonge R., Ebert M.K., Huitt-Roehl C.R., Pal P., Suttle J.C.,
RA Spanner R.E., Neubauer J.D., Jurick W.M.II., Stott K.A., Secor G.A.,
RA Thomma B.P.H.J., Van de Peer Y., Townsend C.A., Bolton M.D.;
RT "Conservation of a gene cluster reveals novel cercosporin biosynthetic
RT mechanisms and extends production to the genus Colletotrichum.";
RL bioRxiv 0:0-0(2017).
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:PPJ59530.1}.
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DR EMBL; PNEN01000385; PPJ59530.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2S6CIH3; -.
DR STRING; 357750.A0A2S6CIH3; -.
DR OrthoDB; 5471864at2759; -.
DR Proteomes; UP000237631; 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:SF8; HECT DOMAIN-CONTAINING PROTEIN; 1.
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:UP000237631};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW ECO:0000256|PROSITE-ProRule:PRU00104}.
FT DOMAIN 894..1264
FT /note="HECT"
FT /evidence="ECO:0000259|PROSITE:PS50237"
FT REGION 1..105
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 150..173
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 240..364
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 463..482
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 584..629
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..23
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 150..166
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 250..268
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 269..284
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 305..325
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 329..343
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 584..599
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 1232
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00104"
SQ SEQUENCE 1264 AA; 140954 MW; D3EAFD409BFA4295 CRC64;
MSSTWSRLLP NHGPSSNHNR TKPRPPNECL DPPTLNPERA VQSRAPAARQ HAHSRSVSHP
LPKIFGRKKS TGNFHETDVP LDDDLVPVLD EPAPKKPTRV ISGKRSQVVD EDGKATRVCM
CCDSKCKVPQ ELSRFRCLCC LTINDLKPVE EQGEDDKSRP HPHRAATDPV PAHPAGAALP
ISLAKTRAII DRCVVTYLQG RWQRSGPTQQ RPANVQSDVF GPDQLPAALA VHQLKAEDNA
GGLADTPLSA SPSDGPTASL AIPASGRTTK ERNDSERFAD SRRDLPSDSA MPPPSRGGSS
SVTPRKPVPA PPNRKPPPPP VQMPNRRPSH NLLPPTNGQL TPRARAHSPR AHQSPQLTAQ
EVEQRREYDR IKSIFRPLED YLVASFGDFR CLNSSFSTAR PAMNGRTRSE SEIKTPFKEP
VANSWNPSPM DGLSELDAKT LLLGDIGENG TWWTGRLASK ETEKATRRKK VGEGPRRPVS
SKSPNIDWSE VALWYDMIHS AGDDWRTKQD QLLSDDEGSK TAVLRYDIDS EEIDDDMADA
REHAIRTLLK LTENILKRPS KPLREPEDLR WLLIILANPS LYPSTNPQRT QSGGDRYLSR
STSDKLAGKM PASPLKRTPG KSSSRGGSQH NGLLKRIFGL LAHANENCQR YLIGWYSRFD
EVLFIKHVDL VASFVTYRID RRSSRARGKG GAADNGLIPN LSGGSMNTSA QLHSAMGLSG
SINRGRSENV DEPDWSGDWQ LKAAARVMAM MFHANNIWQG KRLKLEDGHT LSADLSNGLL
TPAAKAKRSG QLLHTSSFYN TLLDYLDMIE DFKEWEKRRD KFTFCQYPLF ISIGTKIKIL
EFDAQRQMSL KAREAYFDQI FRSTRSDGYF HLRVRRECIV DDSLRQISEA VGAGQEDLKK
GMRVHFAGEE GVDAGGPRKE WFLMLVREIF DPDHGMFVYD EESNMCFFNP NSFETSDQYH
LVGVLLGLAI YNSTILDVPL PPFTFRKLLA AAPASITGSS NSNVSSLTGT KGQMTYTLQD
LTEFRPSLAA GLQKLLDFDG DVQETFALDF VASVERYGIV QDVPLTPNGQ NTPVTNANRH
EFVDAYVRYL LDTAVARQFE PFKRGFFTVC AGNALSLFRA EEIELLIRGS DEALDVDSLR
AVAQYENWRH FQPPHQLIAN PAEQVPVIGW FWELFSEASP EKQRKLLTFV TGSDRIPAVG
ATSLILRIQA GGDGWGGGGP DERTRFPVAR TCFNMLVLWR YDYREQLEEK LWRAVDESEG
FGLK
//
