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Q4WMP0

- EXGD_ASPFU

UniProt

Q4WMP0 - EXGD_ASPFU

Protein

Probable glucan 1,3-beta-glucosidase D

Gene

exgD

Organism
Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) (Aspergillus fumigatus)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 53 (01 Oct 2014)
      Sequence version 1 (05 Jul 2005)
      Previous versions | rss
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    Functioni

    Glucosidase involved in the degradation of cellulosic biomass. Active on lichenan By similarity.By similarity

    Catalytic activityi

    Successive hydrolysis of beta-D-glucose units from the non-reducing ends of (1->3)-beta-D-glucans, releasing alpha-glucose.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei599 – 5991Proton donorBy similarity
    Active sitei704 – 7041NucleophileBy similarity

    GO - Molecular functioni

    1. glucan exo-1,3-beta-glucosidase activity Source: UniProtKB-EC

    GO - Biological processi

    1. polysaccharide catabolic process Source: UniProtKB-KW

    Keywords - Molecular functioni

    Glycosidase, Hydrolase

    Keywords - Biological processi

    Carbohydrate metabolism, Cell wall biogenesis/degradation, Polysaccharide degradation

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Probable glucan 1,3-beta-glucosidase D (EC:3.2.1.58)
    Alternative name(s):
    Exo-1,3-beta-glucanase D
    Gene namesi
    Name:exgD
    ORF Names:AFUA_6G09250
    OrganismiNeosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) (Aspergillus fumigatus)
    Taxonomic identifieri330879 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus
    ProteomesiUP000002530: Chromosome 6

    Subcellular locationi

    GO - Cellular componenti

    1. integral component of membrane Source: UniProtKB-KW
    2. plasma membrane Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cell membrane, Membrane

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 833833Probable glucan 1,3-beta-glucosidase DPRO_0000395164Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi332 – 3321N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi378 – 3781N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi383 – 3831N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi395 – 3951N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi548 – 5481N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi560 – 5601N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi569 – 5691N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi638 – 6381N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi671 – 6711N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi691 – 6911N-linked (GlcNAc...)Sequence Analysis

    Keywords - PTMi

    Glycoprotein

    Interactioni

    Protein-protein interaction databases

    STRINGi5085.CADAFUAP00002365.

    Structurei

    3D structure databases

    ProteinModelPortaliQ4WMP0.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 305305CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini327 – 833507ExtracellularSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei306 – 32621Helical; Signal-anchor for type II membrane proteinSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi6 – 176171Arg-richAdd
    BLAST

    Sequence similaritiesi

    Keywords - Domaini

    Signal-anchor, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiCOG2730.
    HOGENOMiHOG000114462.
    KOiK01210.
    OMAiNIITHYG.
    OrthoDBiEOG7ZPNTV.

    Family and domain databases

    Gene3Di3.20.20.80. 1 hit.
    InterProiIPR001547. Glyco_hydro_5.
    IPR013781. Glyco_hydro_catalytic_dom.
    IPR017853. Glycoside_hydrolase_SF.
    [Graphical view]
    PfamiPF00150. Cellulase. 1 hit.
    [Graphical view]
    SUPFAMiSSF51445. SSF51445. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    Q4WMP0-1 [UniParc]FASTAAdd to Basket

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    MPTHSRSRDR YGGRDSDREA RYDYDYARRR YATDDDDDYD DDELEHDLTE    50
    RRYRRDGYRP PRESRARGYY ERDAEGAADE ELLGNERDPG PRASRSYGDD 100
    YDARRREHSR AREAPRRSER HRDRDREGRS RRRAYEDDGR HRTRDGRRDR 150
    GRESDGEARR SRRREAGRET AARKHRSSDS TNSASHLLSA DALAKLGAQY 200
    EKEERRKREI AKDAAKAERK RQKKLAVVGE ETRALRDPPG ESHRDRTKAR 250
    VASGAYLEEG RSPEMRVRHR GGGGPAMEAR WRKEGSWGGT MDDSGGGRPF 300
    WKRKRWIGLG ALIIILVIVI PVAVVVSKKH DNKSDPADSQ GTSPGKSNLD 350
    GLSHDSIPAY AQGTYLDPWT WYDTTDFNVT FTNETVGGLS IMGLNSTWDD 400
    SARPNDNVPP LNEPFPYGSQ PIRGVNLGGW LSIEPFIVPS LFDSYSSVSG 450
    IIDEWTLSKR LGSSAASTLE KHYATFITEQ DFADIRDAGL DHVRIQYSYW 500
    AVATYDDDPY VAKISWRYLL RAIEYCRKYG LRVNLDPHGI PGSQNGWNHS 550
    GREGVIGWLN GTDGELNRNR SLAVHDSVSK FFAQDRYKNI VTIYGLVNEP 600
    LMLSLSIEDV LDWTTEATKL VQKNGITAYV ALHDGFLNLS KWKSMLKNRP 650
    DKMLLDTHQY TIFNTGQIGL NHTAKVNLIC NDWYNMIKEI NSTSTGWGPT 700
    ICGEWSQADT DCAKYLNNVG RGTRWEGTFS LTDSTQYCPT ADTGPPCSCA 750
    NANADVSKYS ADYKKFLQTY AEAQMSAFET GQGWFYWTWR TESAAQWSYR 800
    TAWKNGFMPA KAYAPSFRCG DAVPDFGDLP EYY 833
    Length:833
    Mass (Da):94,775
    Last modified:July 5, 2005 - v1
    Checksum:i6A08231B6A8A1855
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AAHF01000006 Genomic DNA. Translation: EAL88774.1.
    RefSeqiXP_750812.1. XM_745719.1.

    Genome annotation databases

    EnsemblFungiiCADAFUAT00002365; CADAFUAP00002365; CADAFUAG00002365.
    GeneIDi3508103.
    KEGGiafm:AFUA_6G09250.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AAHF01000006 Genomic DNA. Translation: EAL88774.1 .
    RefSeqi XP_750812.1. XM_745719.1.

    3D structure databases

    ProteinModelPortali Q4WMP0.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 5085.CADAFUAP00002365.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii CADAFUAT00002365 ; CADAFUAP00002365 ; CADAFUAG00002365 .
    GeneIDi 3508103.
    KEGGi afm:AFUA_6G09250.

    Phylogenomic databases

    eggNOGi COG2730.
    HOGENOMi HOG000114462.
    KOi K01210.
    OMAi NIITHYG.
    OrthoDBi EOG7ZPNTV.

    Family and domain databases

    Gene3Di 3.20.20.80. 1 hit.
    InterProi IPR001547. Glyco_hydro_5.
    IPR013781. Glyco_hydro_catalytic_dom.
    IPR017853. Glycoside_hydrolase_SF.
    [Graphical view ]
    Pfami PF00150. Cellulase. 1 hit.
    [Graphical view ]
    SUPFAMi SSF51445. SSF51445. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "Genomic sequence of the pathogenic and allergenic filamentous fungus Aspergillus fumigatus."
      Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S., Arroyo J., Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J.W., Bowyer P., Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.L.
      , Fedorova N., Fedorova N.D., Feldblyum T.V., Fischer R., Fosker N., Fraser A., Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K., Griffith-Jones S., Gwilliam R., Haas B.J., Haas H., Harris D.E., Horiuchi H., Huang J., Humphray S., Jimenez J., Keller N., Khouri H., Kitamoto K., Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafton A., Latge J.-P., Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L., Mohamoud Y., Molina M., Monod M., Mouyna I., Mulligan S., Murphy L.D., O'Neil S., Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L., Quail M.A., Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U., Renauld H., Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M., Ronning C.M., Rutter S., Salzberg S.L., Sanchez M., Sanchez-Ferrero J.C., Saunders D., Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F., Turner G., Vazquez de Aldana C.R., Weidman J., White O., Woodward J.R., Yu J.-H., Fraser C.M., Galagan J.E., Asai K., Machida M., Hall N., Barrell B.G., Denning D.W.
      Nature 438:1151-1156(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100.

    Entry informationi

    Entry nameiEXGD_ASPFU
    AccessioniPrimary (citable) accession number: Q4WMP0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 15, 2010
    Last sequence update: July 5, 2005
    Last modified: October 1, 2014
    This is version 53 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Glycosyl hydrolases
      Classification of glycosyl hydrolase families and list of entries
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3