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Database: UniProt
Entry: Q0CR96_ASPTN
LinkDB: Q0CR96_ASPTN
Original site: Q0CR96_ASPTN 
ID   Q0CR96_ASPTN            Unreviewed;      1228 AA.
AC   Q0CR96;
DT   17-OCT-2006, integrated into UniProtKB/TrEMBL.
DT   17-OCT-2006, sequence version 1.
DT   27-MAR-2024, entry version 94.
DE   RecName: Full=HECT-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012485};
DE            EC=2.3.2.26 {ECO:0000256|ARBA:ARBA00012485};
GN   ORFNames=ATEG_03788 {ECO:0000313|EMBL:EAU35590.1};
OS   Aspergillus terreus (strain NIH 2624 / FGSC A1156).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=341663 {ECO:0000313|EMBL:EAU35590.1, ECO:0000313|Proteomes:UP000007963};
RN   [1] {ECO:0000313|Proteomes:UP000007963}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NIH 2624 / FGSC A1156 {ECO:0000313|Proteomes:UP000007963};
RA   Birren B.W., Lander E.S., Galagan J.E., Nusbaum C., Devon K., Henn M.,
RA   Ma L.-J., Jaffe D.B., Butler J., Alvarez P., Gnerre S., Grabherr M.,
RA   Kleber M., Mauceli E.W., Brockman W., Rounsley S., Young S.K., LaButti K.,
RA   Pushparaj V., DeCaprio D., Crawford M., Koehrsen M., Engels R.,
RA   Montgomery P., Pearson M., Howarth C., Larson L., Luoma S., White J.,
RA   Alvarado L., Kodira C.D., Zeng Q., Oleary S., Yandava C., Denning D.W.,
RA   Nierman W.C., Milne T., Madden K.;
RT   "Annotation of the Aspergillus terreus NIH2624 genome.";
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; CH476598; EAU35590.1; -; Genomic_DNA.
DR   RefSeq; XP_001212966.1; XM_001212966.1.
DR   AlphaFoldDB; Q0CR96; -.
DR   STRING; 341663.Q0CR96; -.
DR   EnsemblFungi; EAU35590; EAU35590; ATEG_03788.
DR   GeneID; 4318614; -.
DR   VEuPathDB; FungiDB:ATEG_03788; -.
DR   eggNOG; KOG0942; Eukaryota.
DR   HOGENOM; CLU_002173_2_4_1; -.
DR   OMA; HWLMTNR; -.
DR   OrthoDB; 1386at2759; -.
DR   Proteomes; UP000007963; Unassembled WGS sequence.
DR   GO; GO:0015629; C:actin cytoskeleton; IEA:UniProt.
DR   GO; GO:0061630; F:ubiquitin protein ligase activity; IEA:InterPro.
DR   GO; GO:0006996; P:organelle organization; IEA:UniProt.
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   InterPro; IPR000048; IQ_motif_EF-hand-BS.
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.
DR   PROSITE; PS50096; IQ; 1.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000007963};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW   ECO:0000256|PROSITE-ProRule:PRU00104}.
FT   DOMAIN          852..1228
FT                   /note="HECT"
FT                   /evidence="ECO:0000259|PROSITE:PS50237"
FT   REGION          1..42
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..21
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        1196
FT                   /note="Glycyl thioester intermediate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00104"
SQ   SEQUENCE   1228 AA;  139289 MW;  FC767634A83582E7 CRC64;
     MFQSFTGNSR RPRQVNLGGR TTNPFAAYPA GRQNPHGSGP QNTLAIAQQE RLARQQERER
     LNASRIIQRT WRGYRCRRTV RQTFRTEWDA REQQRSGQLP QFEELAKRSD VTLDSLTPYG
     TAAECLSQLR LLVQFMEPRE NGDIVRLVWF SRAFQQTLQE VPTIATEGEW TTPLRRLARL
     TLRVLQLATS PSTPAFATVP LLKLLVFLTG LIPKQVARLA QVYYSVMASL TKNIGSLADR
     SHLSGDHLAH SVLALLRPIT SETLTAYEWF AKSYLTVPDL RSYLGTLDTL ANNINYKLLT
     SVLGSLQSQA LDPNQTSQDV EARLWLLAYF IYFHRYALGG QAGQQAPEPE FVKVISELLN
     STAVHISRRL ESEDAADEDS VERTPLHPFV KEQLVSLVNQ RSITGLLSQL QSTTLSQGEL
     ADAQSDASRE AKILATYALT LLRVFPRRGD DIRMWLYLGS ATSSDQTTGG PGSRIPAIKY
     FWQASRASRI FATISQDSTK VLSLLKPAND SKDARGSSMS QTERDEEWMI ILLFLELYTF
     VLKVMDDEEF FSSDSSFTAS SNTQISWTKE SALPLKDIKD MTVFLKNLAF TLYWNSADLN
     ENEPTTHDTG GIRSYFGSLP PPSESITSVK DLELKNKEKG LPGVTGIPLD YFKGLVTGLL
     RMIHERDSRR KFLPEGHWLM TNRFDMEGFI PAVVAEEENR HQLQDDEDEE DPDSLMDDAY
     YEPSLGLIGT GRAQQTRRIE ALRRRQQQAA RRKQLEAVAP RLEILRNMPF FIPFPTRVQI
     FREFIYRDQM RRRQGFIDPD AWRMSVAHAS MGRLLEGRSA AQDILSRHHA NIRRESVFED
     AFDQFYELGE GLKEPIQITF IDKFNTAEAG IDGGGVTKEF LTSVTNEAFR STNDSNLFEE
     NDQHLLYPNP AAVERQRHLL RQLGFTEGSP EWNDGIRELL RRYEFLGRVI GKCLYEGILV
     DVNFAPFFLL KWALTGGTGS AQRETAYRAN LNDLKDLDQG LYQGLLQLKN YPGDVEDFAL
     NFTVTDTIPL AESESRTVTR DLKPHGSEIP VTNQNRLVYI SYIARYRLQV QPALQTNAFL
     QGLGQIIQPS WLSMFNQSEL QTLVRGESGD VDVADLRRNT LYGGVYSIGD DGKEHPTVQL
     FWEVMEKMTN EERQKVLRFV TSTPRAPLLG FSHLNPRFSI RDSSDDQERL PSTSTCVNLL
     KLPRYTDANT LREKLLYAVN SGAGFDLS
//
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