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Database: UniProt
Entry: A0A0F7S512_9BASI
LinkDB: A0A0F7S512_9BASI
Original site: A0A0F7S512_9BASI 
ID   A0A0F7S512_9BASI        Unreviewed;      1133 AA.
AC   A0A0F7S512;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   27-MAR-2024, entry version 29.
DE   RecName: Full=HECT-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012485};
DE            EC=2.3.2.26 {ECO:0000256|ARBA:ARBA00012485};
GN   Name=SSCI07640.1 {ECO:0000313|EMBL:CDW95491.1};
OS   Sporisorium scitamineum.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC   Ustilaginomycetes; Ustilaginales; Ustilaginaceae; Sporisorium.
OX   NCBI_TaxID=49012 {ECO:0000313|EMBL:CDW95491.1, ECO:0000313|Proteomes:UP000242770};
RN   [1] {ECO:0000313|Proteomes:UP000242770}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Berkman P.J.;
RL   Submitted (JUN-2014) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; CCFA01000394; CDW95491.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0F7S512; -.
DR   STRING; 49012.A0A0F7S512; -.
DR   OrthoDB; 1386at2759; -.
DR   Proteomes; UP000242770; 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   Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW   ECO:0000256|PROSITE-ProRule:PRU00104}.
FT   DOMAIN          795..1133
FT                   /note="HECT"
FT                   /evidence="ECO:0000259|PROSITE:PS50237"
FT   REGION          429..452
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        429..444
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        1101
FT                   /note="Glycyl thioester intermediate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00104"
SQ   SEQUENCE   1133 AA;  126030 MW;  B3D96A4C7FBC9CC6 CRC64;
     MSFHFTGAGR TRAPVSLGGI STLLADPVQT AREQRLEREQ QRRKQSASIR IQSQARRILE
     SRQTRYQWQL QSRQLLEHLE ADLLSRACLG SAEGLSRLVV ATRILLVSLG PESRALDQSD
     AELFLRWIRL VLQSIDGIRL VFLPFKQPSQ NAFDDSWLSL LRLACKHSLR FLAKAAVSRT
     QDASATPTTP TLDLEILAFL GLITGVDATS PANSISLGKH HQTLVTSLLS LLLKLGLHRT
     LRSHILSFTV QQKATATSLS SAVSLALAPI FTFKVSSPFL SKSAKAPLGA SLKDAIALAD
     EPEQKHSSAL HRKAVHSFAV DIMTIPALRK RLPLNLITEL AKHLPFSDLV DWLSSFYPDH
     IGTPYPQAHP ALAASSQPTE AAQALSQPYL LANLLAFGSQ RVSFFHDGPS LAKYLQALTN
     AQDWLPRSAF EPPTSSSTNK VNGTARKAPP PDAAETYERL RILVSDKHLA AILAISNRFP
     TSTRESLFAF ICSAVSAWPL DMRDHVLNRL LYSGAESQGA QNSEQPRSLG PAGTGLIRDF
     WRGYVRGSPL ARSLASAHDN TRAREILSSL SDPNTSKEWP ALILVLEMLS KVLLTLGDDE
     FLPSGDDSFG VSDGGGARSN ARWLSRDEIL SISALLRNVA FAMYWYEGKA PLINLDGGDV
     DDPKGRARTP RVPGMRMTLL SLRTLMTTLL KQLHSRDSRH RFAPADHWLM LRAQQGARSR
     HLSALNLAFL SPRLGILNNV PFMIPFDVRV QIFRQFVQID AVENGIYEGR YQRRRAVQIR
     RGHVAQDGFA RLAPLGANLK KPLEIVFIDQ FGRPEAGIDG GGLFKEFLTS LVREAFDTNR
     GLWKATDAQE LYPNPHTYAT SGEQLEWYEF LGRVIGKALY EGILVDAKFA GFFLSKMLGK
     QSFLDDLGSI DTLDKELYKG LISLKNYQGN VEDLSLNFTV TDEEFGVSMT CELIPGGANI
     PVTNLNRMEY IYRISHYRLS TQIQHQCNAF FNGLADMINP RWLRNFNREE LSVLISGTDD
     PVDLEDLRKH TVLGGYHEQD LTVQHFWKVL EGFDQPMRKA FLKFVTSSPN PPLLGFGQLN
     PLFAIRKAGD DKSRLPTAST CVNLLKLPDY EDEQTCRDKL KYAIQSEAGF HLS
//
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