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
//