ID A0A316UTR3_9BASI Unreviewed; 859 AA.
AC A0A316UTR3;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, 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};
DE Flags: Fragment;
GN ORFNames=BDZ90DRAFT_210026 {ECO:0000313|EMBL:PWN28384.1};
OS Jaminaea rosea.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC Exobasidiomycetes; Microstromatales; Microstromatales incertae sedis;
OC Jaminaea.
OX NCBI_TaxID=1569628 {ECO:0000313|EMBL:PWN28384.1, ECO:0000313|Proteomes:UP000245884};
RN [1] {ECO:0000313|EMBL:PWN28384.1, ECO:0000313|Proteomes:UP000245884}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MCA 5214 {ECO:0000313|EMBL:PWN28384.1,
RC ECO:0000313|Proteomes:UP000245884};
RX PubMed=29771364; DOI=10.1093/molbev/msy072;
RA Kijpornyongpan T., Mondo S.J., Barry K., Sandor L., Lee J., Lipzen A.,
RA Pangilinan J., LaButti K., Hainaut M., Henrissat B., Grigoriev I.V.,
RA Spatafora J.W., Aime M.C.;
RT "Broad genomic sampling reveals a smut pathogenic ancestry of the fungal
RT clade Ustilaginomycotina.";
RL Mol. Biol. Evol. 0:0-0(2018).
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; KZ819665; PWN28384.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A316UTR3; -.
DR STRING; 1569628.A0A316UTR3; -.
DR OrthoDB; 1386at2759; -.
DR Proteomes; UP000245884; 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 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.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000245884};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW ECO:0000256|PROSITE-ProRule:PRU00104}.
FT DOMAIN 521..859
FT /note="HECT"
FT /evidence="ECO:0000259|PROSITE:PS50237"
FT REGION 387..407
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 827
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00104"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:PWN28384.1"
FT NON_TER 859
FT /evidence="ECO:0000313|EMBL:PWN28384.1"
SQ SEQUENCE 859 AA; 94898 MW; 37D2483E389927D4 CRC64;
RRSIVSLFTR SILSIPSLPN RLPVLLFAKL AASFPLEEMA ASLNSQGVAF SDATQPETAF
AAVHTLANFL ALGSQRVPLL KTGKSLNDYL GALTGLQDHV DPAAFAPEAT GEINAETKKR
LAILPSVKHL TAILNLSNRF PSTTRPALYS FLCSILAAWP SDIKTATLNA VLYGTSESTA
APASSNAASA SAAAGQGPIR ELWRGYTRSS PLARRLGSIS ASNADASLFR KPVDGWAPLV
LLAELYSRLL LTLGDDEFFP SRQGGTATPS SATSGGASAS GTAIAARNPL TMDEVSSLIA
LVRNLAFTLY WHQDVAAVGP RSVESSQHVP GLRYSFAALR DLATRLLQQI HARDARHRFT
KEDFWLMTDE MDMESFIESV MLEEEKLAEE QAERESNTQS SSNAALASAD GDDLFDEEMA
PLEATMPRST TARASSRKFI SARKMAFISP RLGILNNLPF VIPFATRIQI FRAFIYRDAV
RLRLDRSSIN SFHHHRRRVT VRRDHVAEDG MAQLNGLGSK LKESVEIVFM DQWGMEEAGI
DGGGVFKEFL TSLVREAFDT DRGLWRATEQ QELYPNPASY ARQTEQLQWY SFLGRVLGKA
LYEGILVDVR FASFFLSKWL GARRGLTHLD DLASLDSFDS ELYRGLIYLK NYAGDVESDL
SLNFTVTDEE FGQRKVTELV PGGGNMAVTN KNRLSYIFLV ANYRLDAQIR AQSSAFFAGL
SELIDPRWLS IFDQQELSRL IRGSEEPIDV DDLKAHTVYS DYHEKDLAIQ YFWQTLESFD
QEERAALLKF VTSCPSPPLL GFGQLNPKFC IRLSGEDEGR LPTSSTCVNL LKLPRYGSFE
LCREKVLTAV RSGAGFDLS
//
