(data stored in SCRATCH zone)

SWISSPROT: A2Q7Q3_ASPNC

ID   A2Q7Q3_ASPNC            Unreviewed;      1072 AA.
AC   A2Q7Q3;
DT   06-MAR-2007, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2007, sequence version 1.
DT   11-DEC-2019, entry version 66.
DE   SubName: Full=Aspergillus niger contig An01c0070, genomic contig {ECO:0000313|EMBL:CAK43526.1};
DE            EC=3.2.1.28 {ECO:0000313|EMBL:CAK43526.1};
GN   ORFNames=An01g01540 {ECO:0000313|EMBL:CAK43526.1};
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:CAK43526.1, 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).
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DR   EMBL; AM269954; CAK43526.1; -; Genomic_DNA.
DR   RefSeq; XP_001388594.1; XM_001388557.2.
DR   CAZy; GH65; Glycoside Hydrolase Family 65.
DR   PaxDb; A2Q7Q3; -.
DR   EnsemblFungi; CAK43526; CAK43526; An01g01540.
DR   GeneID; 4978248; -.
DR   KEGG; ang:ANI_1_2268014; -.
DR   HOGENOM; HOG000178675; -.
DR   Proteomes; UP000006706; Chromosome 2R.
DR   GO; GO:0004555; F:alpha,alpha-trehalase activity; IEA:UniProtKB-EC.
DR   GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   Gene3D; 1.50.10.10; -; 1.
DR   Gene3D; 2.70.98.40; -; 1.
DR   InterPro; IPR008928; 6-hairpin_glycosidase_sf.
DR   InterPro; IPR012341; 6hp_glycosidase-like_sf.
DR   InterPro; IPR011013; Gal_mutarotase_sf_dom.
DR   InterPro; IPR005195; Glyco_hydro_65_M.
DR   InterPro; IPR005196; Glyco_hydro_65_N.
DR   InterPro; IPR037018; Glyco_hydro_65_N_sf.
DR   Pfam; PF03632; Glyco_hydro_65m; 1.
DR   Pfam; PF03636; Glyco_hydro_65N; 1.
DR   SUPFAM; SSF48208; SSF48208; 1.
DR   SUPFAM; SSF74650; SSF74650; 1.
PE   4: Predicted;
DR   PRODOM; A2Q7Q3.
DR   SWISS-2DPAGE; A2Q7Q3.
KW   Glycosidase {ECO:0000313|EMBL:CAK43526.1};
KW   Hydrolase {ECO:0000313|EMBL:CAK43526.1}; Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           23..1072
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5002644574"
FT   DOMAIN          75..339
FT                   /note="Glyco_hydro_65N"
FT                   /evidence="ECO:0000259|Pfam:PF03636"
FT   DOMAIN          435..619
FT                   /note="Glyco_hydro_65m"
FT                   /evidence="ECO:0000259|Pfam:PF03632"
FT   REGION          1053..1072
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1072 AA;  116169 MW;  EDD2A46A363143A0 CRC64;
     MQVKFLATLL PLLLHLPAAV DGLPGKNARI SASLKRHAGR DVPQTALNST NVYQTKFSGV
     TWDEDHWLLT TTTPDQGHYQ SRGSVANGYL GINVANIGPF FELDEPVNGD VINGWPLYSR
     RQSFATISGF WDRQAHTNGS NFPWLSQYGD DSVISGVPHW SGLILDLGDD TYLDATVDNR
     TISNFKSTYD FKSGVLSWSY TWTPQGNKGS YAITYRLFAH KLYVNRAVVD MEITPLTNGN
     ATVVNVLDGY AAVRTDFVAS GQEEGAIFSA VRPWGVNNVT AYVYATLDGS DSVDLSSRRI
     VTDKPYVSTN SSSVAQAVDV MFTANETVRI TKFVGGATTD YFLATQETAK AACLAGLADG
     YVKSLQSHVG EWATIMHDHS VDRFTDPATG KLPEDSHIVD SAIIAVTNTY YLLQNTAGTN
     AIVAAGGIPV NVDSCAPGGL TSDSYGGQIF WDADLWMQPG LVASHPESAQ RFTNYRIALH
     YQAQANIETA FTGSKNQTSF SSSAAIYPWT SGRFGNCTAT GPCWDYQYHL NGDIGLAMIN
     QWVASGDTAW FKNYLFPIYD AAATLYSELV ERNGSSWTLT NMTDPDEYAN SINAGGYTMP
     LIAETLQNAN KLRKQFGLEP NETWDEIAED VLILRENGVT LEYTSMNGSA VVKQADIVLN
     TFPLTYESDN YTATNSLTDL DYYANKQSAD GPAMTYAIFA IVASDVSPSG CSAFTYHQYS
     YAPYARGPWY QLSEQMIDDA SINGGTHPAF PFLTGHGGAN QVALYGYLGL RLHPDDTIYI
     DPNLPPQIPH ITYRTFYWHG WPISAWSNYT HTTIQRDSSL APLASADLLF SNVSIKVQVG
     QSTASADEAT IYYLPLSGAL TVPNRMIGSV NTTPGNQVQC HPVYSPDAYE PGQFPISAVD
     GATSTKWQPS TSDLTSLTVT LSTTAEAGAE EVSGFYFDWS QAPPENLTVI FHDSPIGNPS
     TVFAAAGSNS TGYRVITSMS NIVQSKPYNA ISAEELNVVS IPTANTTTIT LDAPVQKARY
     ATLLIAGNQA NETAGATVAE WVILGQNSTS SSSAQAKRKM SARSKATLAQ LS
//

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