(data stored in ACNUC7421 zone)

SWISSPROT: A2Q849_ASPNC

ID   A2Q849_ASPNC            Unreviewed;      1229 AA.
AC   A2Q849;
DT   06-MAR-2007, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2007, sequence version 1.
DT   11-DEC-2019, entry version 80.
DE   SubName: Full=Aspergillus niger contig An01c0080, genomic contig {ECO:0000313|EMBL:CAK43672.1};
DE            EC=6.3.2.19 {ECO:0000313|EMBL:CAK43672.1};
GN   ORFNames=An01g03060 {ECO:0000313|EMBL:CAK43672.1};
OS   Aspergillus niger (strain CBS 513.88 / FGSC A1513).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=425011 {ECO:0000313|Proteomes:UP000006706};
RN   [1] {ECO:0000313|EMBL:CAK43672.1, ECO:0000313|Proteomes:UP000006706}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 513.88 / FGSC A1513 {ECO:0000313|Proteomes:UP000006706};
RX   PubMed=17259976; DOI=10.1038/nbt1282;
RA   Pel H.J., de Winde J.H., Archer D.B., Dyer P.S., Hofmann G., Schaap P.J.,
RA   Turner G., de Vries R.P., Albang R., Albermann K., Andersen M.R.,
RA   Bendtsen J.D., Benen J.A., van den Berg M., Breestraat S., Caddick M.X.,
RA   Contreras R., Cornell M., Coutinho P.M., Danchin E.G., Debets A.J.,
RA   Dekker P., van Dijck P.W., van Dijk A., Dijkhuizen L., Driessen A.J.,
RA   d'Enfert C., Geysens S., Goosen C., Groot G.S., de Groot P.W.,
RA   Guillemette T., Henrissat B., Herweijer M., van den Hombergh J.P.,
RA   van den Hondel C.A., van der Heijden R.T., van der Kaaij R.M., Klis F.M.,
RA   Kools H.J., Kubicek C.P., van Kuyk P.A., Lauber J., Lu X.,
RA   van der Maarel M.J., Meulenberg R., Menke H., Mortimer M.A., Nielsen J.,
RA   Oliver S.G., Olsthoorn M., Pal K., van Peij N.N., Ram A.F., Rinas U.,
RA   Roubos J.A., Sagt C.M., Schmoll M., Sun J., Ussery D., Varga J.,
RA   Vervecken W., van de Vondervoort P.J., Wedler H., Wosten H.A., Zeng A.P.,
RA   van Ooyen A.J., Visser J., Stam H.;
RT   "Genome sequencing and analysis of the versatile cell factory Aspergillus
RT   niger CBS 513.88.";
RL   Nat. Biotechnol. 25:221-231(2007).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine +
CC         [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-
CC         cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.;
CC         EC=2.3.2.26; Evidence={ECO:0000256|SAAS:SAAS00628607};
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; AM269955; CAK43672.1; -; Genomic_DNA.
DR   RefSeq; XP_001388740.1; XM_001388703.2.
DR   PaxDb; A2Q849; -.
DR   EnsemblFungi; CAK43672; CAK43672; An01g03060.
DR   GeneID; 4977620; -.
DR   KEGG; ang:ANI_1_386014; -.
DR   HOGENOM; HOG000211433; -.
DR   KO; K10589; -.
DR   Proteomes; UP000006706; Chromosome 2R.
DR   GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR   GO; GO:0004842; F:ubiquitin-protein transferase activity; IEA:InterPro.
DR   CDD; cd00078; HECTc; 1.
DR   InterPro; IPR000569; HECT_dom.
DR   InterPro; IPR035983; Hect_E3_ubiquitin_ligase.
DR   InterPro; IPR000048; IQ_motif_EF-hand-BS.
DR   Pfam; PF00632; HECT; 1.
DR   SMART; SM00119; HECTc; 1.
DR   SUPFAM; SSF56204; SSF56204; 1.
DR   PROSITE; PS50237; HECT; 1.
DR   PROSITE; PS50096; IQ; 1.
PE   4: Predicted;
DR   PRODOM; A2Q849.
DR   SWISS-2DPAGE; A2Q849.
KW   Coiled coil {ECO:0000256|SAM:Coils}; Ligase {ECO:0000313|EMBL:CAK43672.1};
KW   Transferase {ECO:0000256|SAAS:SAAS00628615};
KW   Ubl conjugation pathway {ECO:0000256|PROSITE-ProRule:PRU00104,
KW   ECO:0000256|SAAS:SAAS00593691}.
FT   DOMAIN          853..1229
FT                   /note="HECT"
FT                   /evidence="ECO:0000259|PROSITE:PS50237"
FT   REGION          1..41
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          694..714
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          733..753
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   ACT_SITE        1197
FT                   /note="Glycyl thioester intermediate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00104"
SQ   SEQUENCE   1229 AA;  139700 MW;  B097104EEBCAAB7B CRC64;
     MFQSFTGNSR RPRQVNLGGR NTNPFAAYPS GRQNPHGAGP QNTLAIAQQE RLARQQERER
     LTASRLVQRT WRGYRSRKIT RRTWRNEWDT TEKKQGKDHV PSFEILAQQP DVVLQPSLRY
     GTAADCLSQL RLLVQFLEPW DSGDIARLVY FSEAFQRTLH EVPSIATEGE WTTPLKKLAS
     LTLRVLRSVT SPTVPVFAVQ RLLQLLVFLT GLIPKHMARL AKEYYSVMVI LTTDFESIST
     RYKLSRDSLT ESVLALLRPI TSETLTAYEW FAKIYLTIPN LPEYIGSLDG LANNINYKLL
     TSALGPLQTL FGDRPKSAED VDARLWLLAY FIFFHRCALG GQTGRPAPEP GFVKVVSELL
     NSTAVHISRR LESEESNDYD EAPEQTPLHP FIKEQLVSLV NQSNITGLLS QLHTTHLSQG
     ELANAQSDAS KEAKILATYA LTLLRVFPRR GDDIRMWLYL GSATSSDQLT GQEGSRIPAI
     KYFWQASKAS RIFAAISQDS TKVLPLLKPA EESQGTRSPE ISQVERDEEW TIILLFLELY
     TFVLKVMDDE EFFSSESSFT ASSNTRVSWT KESALPLKDI KDMTIFLKNL GFTLYWNSAD
     LSEKEATQDT GGIRSYFSSS AAPPDAIASV RDIEMKNKEK GLPGVTGIPL DYFKGLVTGL
     LRMIHERDSR RKFLPDGHWL MTSRFDMEGF IPAVVAEEEN RHQLQDEDEE EEQDDLMSDA
     YFEPSPGLIG TGRAQLTRRI EALRRRQQQA ARRKQLEAVA PRMEILRNMP FFIPFPTRVQ
     IFREFIYRDQ MRRRQGYIDP DAWRMSVAQA SMGRLIDGRP AVQDILSRHH ANIRRESIFK
     DAFDEFYELG DGLKEPIQIT FIDKFNTTEA GIDGGGVTKE FLTSVTSEAF KSTSDLNLFE
     ENDQHLLYPN PAAVEQRREL LRQLGFVENT AEWNENVRDL LRRYEFLGRI IGKCLYEGIL
     VDVNFAPFFL LKWALTGGTG SAQRETAYRA NLNDLKDLDQ GLYQGLLQLK NYPGDVEDFS
     LNFTVTDTIP LPDGGNRTTT RDLKSHGSDI PVTNQNRLVY ISYIARYRLQ VQPALQTNAF
     LQGLGQIIQP SWLSMFNQTE LQTLVSGDSG DIDVADLRRN TLYGGVYTIG DDKEEHPTVK
     LFWEVMEKMS NEERQKVLRF VTSTPRAPLL GFSHLNPRFS IRDSSEDQER LPSTSTCVNL
     LKLPRYTNAN ILREKLLYAV NSGAGFDLS
//

If you have problems or comments...

PBIL Back to PBIL home page