(data stored in SCRATCH zone)

SWISSPROT: A2Q888_ASPNC

ID   A2Q888_ASPNC            Unreviewed;      1067 AA.
AC   A2Q888;
DT   06-MAR-2007, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2007, sequence version 1.
DT   11-DEC-2019, entry version 76.
DE   SubName: Full=Aspergillus niger contig An01c0110, genomic contig {ECO:0000313|EMBL:CAK36885.1};
GN   ORFNames=An01g03470 {ECO:0000313|EMBL:CAK36885.1};
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:CAK36885.1, 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};
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DR   EMBL; AM269958; CAK36885.1; -; Genomic_DNA.
DR   PaxDb; A2Q888; -.
DR   EnsemblFungi; CAK36885; CAK36885; An01g03470.
DR   HOGENOM; HOG000208451; -.
DR   Proteomes; UP000006706; Chromosome 2R.
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   Pfam; PF00632; HECT; 1.
DR   SMART; SM00119; HECTc; 1.
DR   SUPFAM; SSF56204; SSF56204; 1.
DR   PROSITE; PS50237; HECT; 1.
PE   4: Predicted;
DR   PRODOM; A2Q888.
DR   SWISS-2DPAGE; A2Q888.
KW   Transferase {ECO:0000256|SAAS:SAAS00628615};
KW   Ubl conjugation pathway {ECO:0000256|PROSITE-ProRule:PRU00104,
KW   ECO:0000256|SAAS:SAAS00593691}.
FT   DOMAIN          726..1067
FT                   /note="HECT"
FT                   /evidence="ECO:0000259|PROSITE:PS50237"
FT   REGION          38..61
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          111..206
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          233..267
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          289..315
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          431..470
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        133..161
FT                   /note="Polar"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        168..192
FT                   /note="Polyampholyte"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        233..262
FT                   /note="Polar"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        292..308
FT                   /note="Polyampholyte"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        448..465
FT                   /note="Pro-rich"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        1035
FT                   /note="Glycyl thioester intermediate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00104"
SQ   SEQUENCE   1067 AA;  119865 MW;  A094C4812E523E30 CRC64;
     MTSGKCMVCN STVRWPRNLK VFRCTECLTV NDLEPFVDSG KAGGNGLSGS DGKAPTPAVP
     RKAMPLSIER TKTILDDCLS RYLQQLLAPQ QQNSTPENYS GKYLDVAQDE NLSQSPTQSS
     GYLSEPRPLV DPRGRSSSTS SKPVKTEGVS GVPNYSKPNL TPSYAHGERK GSEMRSRDAQ
     NAPRRDRSPR NAARSNGPEA RGPTSRPYIF RSLEEYIITS FKGCDCLNSS FTTAQPAPRN
     AGNSSPPKQK AEPSSAQAPS QVTFEPDPKL LLLGDIAENS SWWMNEVEQI SSSHRSRSRE
     RREKTSSSSR PVSSRSPRIN WAELAQWHHM IMTAGTSWVE LWSTMKPTEM KKEEDAVIAQ
     KWNATDLAMV DREITESRLH LHRTLLKATE NLLKRPRRPL KRPEDTRFLL MLLTNPLIYS
     SSSSFASYSL APSAARGDRR PSHPKDGTPR PAPRNPKPPP KPRSNGPGHH YGIVKRILGL
     LANLPNDCHH YLVSWFSRFS AGQFEKIVDL VGGFVTHRLM RQHGRKRSES AQHDDDLVPS
     FSSAAGHTPA ELHAAINGRS PNKANEQRDQ PVVYTDDWQV RAAARVMYLL FTANNANVSR
     KPDGVLGQDA GSVARNQASR RGHMIPISSF YNTLLDYSDL VADFEAWESK TTKFSFCQYP
     FFLSIWAKIH ILEHDARRQM EVKAREAFFN SIMSRTAISQ YLVLKVRRDC LVEDSLRGVS
     EVVGSSQEEI KKGLRIEFLG EEGVDAGGLR KEWFLLLVRE VFDPHHGLFI YDDDSRYCYF
     NPYCFESSEQ FFLVGVLLGL AIYNSTILDI ALPPFAFKKL LAAAPLSSIT RPMYKCSLDD
     LAELRPALAK GLRALLDYEG DVAETFCYDF VAQVDRYGET VSVPLCAGGE NRPVTNANRR
     EFVDLYVHFL LDTAVTRQFE PFKRGFFTVC GGNALSLFRP EEIELLVRGS DEPLDVASLR
     AVATYDNWSN ARPETEPVVR WFWDFFEQTQ PQAQRKILSF VTGSDRIPAM GATSLSIRLV
     CLGDETSRFP TARTCFNQLG LYRYETREKL ERMLWDAVLN GEGFGLK
//

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