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Q0H904

- XYNC_ASPFU

UniProt

Q0H904 - XYNC_ASPFU

Protein

Endo-1,4-beta-xylanase C

Gene

xlnC

Organism
Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) (Aspergillus fumigatus)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 44 (01 Oct 2014)
      Sequence version 2 (23 Mar 2010)
      Previous versions | rss
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    Functioni

    Endo-1,4-beta-xylanase involved in the hydrolysis of xylan, a major structural heterogeneous polysaccharide found in plant biomass representing the second most abundant polysaccharide in the biosphere, after cellulose.By similarity

    Catalytic activityi

    Endohydrolysis of (1->4)-beta-D-xylosidic linkages in xylans.

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei155 – 1551Proton donorBy similarity
    Active sitei261 – 2611NucleophileBy similarity

    GO - Molecular functioni

    1. endo-1,4-beta-xylanase activity Source: UniProtKB

    GO - Biological processi

    1. xylan catabolic process Source: UniProtKB

    Keywords - Molecular functioni

    Glycosidase, Hydrolase

    Keywords - Biological processi

    Carbohydrate metabolism, Polysaccharide degradation, Xylan degradation

    Enzyme and pathway databases

    UniPathwayiUPA00114.

    Protein family/group databases

    CAZyiGH10. Glycoside Hydrolase Family 10.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Endo-1,4-beta-xylanase C (EC:3.2.1.8)
    Short name:
    Xylanase C
    Alternative name(s):
    1,4-beta-D-xylan xylanohydrolase C
    Gene namesi
    Name:xlnC
    Synonyms:xynf10a
    OrganismiNeosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) (Aspergillus fumigatus)
    Taxonomic identifieri330879 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus
    ProteomesiUP000002530: Chromosome 4

    Subcellular locationi

    Secreted By similarity

    GO - Cellular componenti

    1. extracellular region Source: UniProtKB

    Keywords - Cellular componenti

    Secreted

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 1919Sequence AnalysisAdd
    BLAST
    Chaini20 – 325306Endo-1,4-beta-xylanase CPRO_0000393188Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi279 ↔ 285By similarity

    Keywords - PTMi

    Disulfide bond

    Expressioni

    Inductioni

    Expressed in presence of xylan and repressed by glucose.

    Interactioni

    Protein-protein interaction databases

    STRINGi5085.CADAFUAP00008146.

    Structurei

    3D structure databases

    ProteinModelPortaliQ0H904.
    SMRiQ0H904. Positions 27-325.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Keywords - Domaini

    Signal

    Phylogenomic databases

    HOGENOMiHOG000019847.
    KOiK01181.
    OrthoDBiEOG7GJ6PM.

    Family and domain databases

    Gene3Di3.20.20.80. 1 hit.
    InterProiIPR001000. Glyco_hydro_10.
    IPR013781. Glyco_hydro_catalytic_dom.
    IPR017853. Glycoside_hydrolase_SF.
    [Graphical view]
    PfamiPF00331. Glyco_hydro_10. 1 hit.
    [Graphical view]
    PRINTSiPR00134. GLHYDRLASE10.
    SMARTiSM00633. Glyco_10. 1 hit.
    [Graphical view]
    SUPFAMiSSF51445. SSF51445. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    Q0H904-1 [UniParc]FASTAAdd to Basket

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    MVVLSKLVSS ILFVSLVSAG VIEERQAASI NQAFTSHGKK YFGTASDQAL    50
    LQKSQNEAIV RKDFGQLTPE NSMKWDATEP SQGRFNFAGA DFLVNYAKQN 100
    GKKVRGHTLV WHSQLPSWVS AISDKNTLTS VLKNHITTVM TRYKGQIYAW 150
    DVVNEIFNED GSLRDSVFSR VLGEDFVRIA FETARSVDPS AKLYINDYNL 200
    DSASYGKTQG MVRYVKKWLA AGIPIDGIGT QTHLGAGASS SVKGALTALA 250
    SSGVSEVAIT ELDIAGASSQ DYVNVVKACL DVPKCVGITV WGVSDRDSWR 300
    SGSSPLLFDS NYQPKAAYNA IIAAL 325
    Length:325
    Mass (Da):35,221
    Last modified:March 23, 2010 - v2
    Checksum:iBB2D1688371B3F92
    GO

    Sequence cautioni

    The sequence EAL89839.1 differs from that shown. Reason: Erroneous gene model prediction.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti14 – 141V → A in ABA40421. 1 PublicationCurated
    Sequence conflicti40 – 401K → R in ABA40421. 1 PublicationCurated
    Sequence conflicti214 – 2141Y → C in ABA40421. 1 PublicationCurated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    DQ156555 mRNA. Translation: ABA40421.1.
    EF375874 Genomic DNA. Translation: ABN48479.1.
    AAHF01000005 Genomic DNA. Translation: EAL89839.1. Sequence problems.
    RefSeqiXP_751877.1. XM_746784.1.

    Genome annotation databases

    EnsemblFungiiCADAFUAT00008146; CADAFUAP00008146; CADAFUAG00008146.
    GeneIDi3509139.
    KEGGiafm:AFUA_4G09480.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    DQ156555 mRNA. Translation: ABA40421.1 .
    EF375874 Genomic DNA. Translation: ABN48479.1 .
    AAHF01000005 Genomic DNA. Translation: EAL89839.1 . Sequence problems.
    RefSeqi XP_751877.1. XM_746784.1.

    3D structure databases

    ProteinModelPortali Q0H904.
    SMRi Q0H904. Positions 27-325.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 5085.CADAFUAP00008146.

    Protein family/group databases

    CAZyi GH10. Glycoside Hydrolase Family 10.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii CADAFUAT00008146 ; CADAFUAP00008146 ; CADAFUAG00008146 .
    GeneIDi 3509139.
    KEGGi afm:AFUA_4G09480.

    Phylogenomic databases

    HOGENOMi HOG000019847.
    KOi K01181.
    OrthoDBi EOG7GJ6PM.

    Enzyme and pathway databases

    UniPathwayi UPA00114 .

    Family and domain databases

    Gene3Di 3.20.20.80. 1 hit.
    InterProi IPR001000. Glyco_hydro_10.
    IPR013781. Glyco_hydro_catalytic_dom.
    IPR017853. Glycoside_hydrolase_SF.
    [Graphical view ]
    Pfami PF00331. Glyco_hydro_10. 1 hit.
    [Graphical view ]
    PRINTSi PR00134. GLHYDRLASE10.
    SMARTi SM00633. Glyco_10. 1 hit.
    [Graphical view ]
    SUPFAMi SSF51445. SSF51445. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "Characterization of recombinant xylan degrading enzymes from Aspergillus fumigatus isolate SL1."
      Dabrowski S., Ahring B.K.
      Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Strain: SL1.
    2. "Cloning and characterization of xynf10a gene from Aspergillus fumigatus MKU1."
      Thiagarajan S., Jeya M., Gunasekaran P.
      Submitted (JAN-2007) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: MKU1.
    3. "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 nameiXYNC_ASPFU
    AccessioniPrimary (citable) accession number: Q0H904
    Secondary accession number(s): A3FG82, Q4WPJ5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 23, 2010
    Last sequence update: March 23, 2010
    Last modified: October 1, 2014
    This is version 44 of the entry and version 2 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. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3