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Database: UniProt
Entry: F2TB36_AJEDA
LinkDB: F2TB36_AJEDA
Original site: F2TB36_AJEDA 
ID   F2TB36_AJEDA            Unreviewed;      1341 AA.
AC   F2TB36;
DT   31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   14-OCT-2015, sequence version 2.
DT   24-JAN-2024, entry version 45.
DE   SubName: Full=HECT domain-containing protein {ECO:0000313|EMBL:EGE80449.2};
GN   ORFNames=BDDG_03390 {ECO:0000313|EMBL:EGE80449.2};
OS   Ajellomyces dermatitidis (strain ATCC 18188 / CBS 674.68) (Blastomyces
OS   dermatitidis).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Ajellomycetaceae; Blastomyces.
OX   NCBI_TaxID=653446 {ECO:0000313|EMBL:EGE80449.2};
RN   [1] {ECO:0000313|EMBL:EGE80449.2}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 18188 {ECO:0000313|EMBL:EGE80449.2};
RG   The Broad Institute Genome Sequencing Platform;
RG   Broad Institute Genome Sequencing Center for Infectious Disease.;
RA   Cuomo C., Klein B., Sullivan T., Heitman J., Young S., Zeng Q., Gargeya S.,
RA   Alvarado L., Berlin A.M., Chapman S.B., Chen Z., Freedman E., Gellesch M.,
RA   Goldberg J., Griggs A., Gujja S., Heilman E., Heiman D., Howarth C.,
RA   Mehta T., Neiman D., Pearson M., Roberts A., Saif S., Shea T., Shenoy N.,
RA   Sisk P., Stolte C., Sykes S., White J., Yandava C., Haas B., Nusbaum C.,
RA   Birren B.;
RT   "Annotation of Blastomyces dermatitidis strain ATCC 18188.";
RL   Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; GG749420; EGE80449.2; -; Genomic_DNA.
DR   HOGENOM; CLU_001858_0_0_1; -.
DR   GO; GO:0004842; F:ubiquitin-protein transferase activity; IEA:InterPro.
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   Gene3D; 6.10.130.10; Ubiquitin-protein ligase E3A, N-terminal zinc-binding domain (AZUL); 1.
DR   InterPro; IPR032353; AZUL.
DR   InterPro; IPR042556; AZUL_sf.
DR   InterPro; IPR000569; HECT_dom.
DR   InterPro; IPR035983; Hect_E3_ubiquitin_ligase.
DR   PANTHER; PTHR45622:SF51; HECT DOMAIN PROTEIN (AFU_ORTHOLOGUE AFUA_2G04450); 1.
DR   PANTHER; PTHR45622; UBIQUITIN-PROTEIN LIGASE E3A-RELATED; 1.
DR   Pfam; PF16558; AZUL; 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          930..1341
FT                   /note="HECT"
FT                   /evidence="ECO:0000259|PROSITE:PS50237"
FT   REGION          1..26
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          123..224
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          250..424
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1110..1145
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        123..137
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        154..172
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        185..212
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        252..314
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        329..358
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        359..380
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        395..422
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1110..1128
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        1309
FT                   /note="Glycyl thioester intermediate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00104"
SQ   SEQUENCE   1341 AA;  152643 MW;  64FF8313AA18C0C9 CRC64;
     MTRLRGGSGS PPDSGRSASV GDRGLYHPSK LPADAPELLA KNTIAVTDPA GVLAWNRDKR
     QRDFNLLVKR YKNQLLYGCQ DPFCATPTCF SYRRRVTDAP LRRFTELSAR TVACYLASQD
     NPERGLCRNT PATNTDFLSG DGIRRHRRRS CEVSQQSVKF SSDAQGHNNA EDNGAQEKPA
     GDTLHQQHRG NNRTTKSTEA NEKPGPPQSE DGKSSQRLKD PKSFTQNLFD TLSLRMVEWL
     PLRRSHEAFD TVSSDPNDYG SSPSKPPGTE TPGRSQEHPS NPKRNSRQKQ VVSHPNIKSR
     PQTITSSNPN PQPTAVEVKI PGQPVKRLSL GEMEHRKQPS KAFAEDRVRS ERKQPRKASS
     HNTPSNQPNR SLQSPPPLKQ RPQKHKNASD VSNTSKPEQK RHRRVSWDGS HGPRKSESAE
     CDSSRVSIDY SIQHSQSPTE SPEIPVSRDA NNGKLFIPQQ IQTLSHLSEQ IVTGLAKLMF
     ENDEDRDKWI EEMSELESRG YSEPWDWQYA TPRQREVFPF VVQSVFYVLS SPRQLVQSFR
     KDSPTSAESD RRENANTLDI EQVENSFRVL HRICPWETTL HSLWTSLAKL FVPPREFSLP
     RPHMLPVRWV ASSSRAVSKH GDAAYISVIT LLALSSFIPQ TDPKTWEIIR HIRSSGTVLP
     DSEMRKHPRS TRRSLVAISE MFEHDLALRL VNRLVRVVSA RMAFHEISKT RTINIHDIER
     QEKHDFTRLI IRTLRDFSKT NEKSSQTSYS FLHDERPTNP HMVAVEWLRS LLLKEWDGKP
     EMAKSGAFGG ALQLLASMYK ERFRLGLEPE DFHTSFLSER LDPTEMPVEW LGILPNNRTV
     HLLSYPFLFP PSALVIYFRA INYSNMSKSY EAAMTTSRHV TQPAFSSIIP IDDDVSLLAR
     LKTSISTYLV LVVRRDNVLT DALNQLWRRE RRELMRPLKV QMGMDEGEEG IDHGGVQQEF
     FRVALGEALD PSYGMFTMDM RTRMSWFQPC SMEPLYKFEL LGLLMSLAVY NGLTLPVNFP
     VALYKKLLGL RVKNLDDIRV GWPELAKGLD DLLSWDDGDV GDIFMRTYEF SFDAFGTFVS
     VDMEKVDRNE PWPAPERSAW ERKKSGSYYR QSWSGKTSHP GSFDDNTSML RESADENSTS
     KRDGVLSGIL KGASSRTYKA TPPSPPQEAA LVTNANRERF VKDYIFWLTD KSVRPQYEAF
     ARGFYTCLDR TALSIFTPEA LKTVIEGIQE IDIEELEHNA RYEGGFEPNH RVISDFWSIV
     KRYPQTRKRQ LLEFVTASDR VPVNGISSIM FVIQRNGTGD NRLPTSLTCF GRLLLPEYSN
     RAILEEKLEK ALENARGFGV A
//
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