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Q4WFK4

- CBHC_ASPFU

UniProt

Q4WFK4 - CBHC_ASPFU

Protein

Probable 1,4-beta-D-glucan cellobiohydrolase C

Gene

cbhC

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

    The biological conversion of cellulose to glucose generally requires three types of hydrolytic enzymes: (1) Endoglucanases which cut internal beta-1,4-glucosidic bonds; (2) Exocellobiohydrolases that cut the dissaccharide cellobiose from the non-reducing end of the cellulose polymer chain; (3) Beta-1,4-glucosidases which hydrolyze the cellobiose and other short cello-oligosaccharides to glucose.By similarity

    Catalytic activityi

    Hydrolysis of (1->4)-beta-D-glucosidic linkages in cellulose and cellotetraose, releasing cellobiose from the non-reducing ends of the chains.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei184 – 1841PROSITE-ProRule annotation
    Active sitei230 – 2301Proton donorPROSITE-ProRule annotation
    Active sitei409 – 4091NucleophilePROSITE-ProRule annotation

    GO - Molecular functioni

    1. cellulose 1,4-beta-cellobiosidase activity Source: UniProtKB-EC
    2. cellulose binding Source: InterPro

    GO - Biological processi

    1. cellulose catabolic process Source: UniProtKB-KW

    Keywords - Molecular functioni

    Glycosidase, Hydrolase

    Keywords - Biological processi

    Carbohydrate metabolism, Cellulose degradation, Polysaccharide degradation

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Probable 1,4-beta-D-glucan cellobiohydrolase C (EC:3.2.1.91)
    Alternative name(s):
    Beta-glucancellobiohydrolase C
    Exocellobiohydrolase C
    Exoglucanase C
    Gene namesi
    Name:cbhC
    ORF Names:AFUA_3G01910
    OrganismiNeosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) (Aspergillus fumigatus)
    Taxonomic identifieri330879 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus
    ProteomesiUP000002530: Chromosome 3

    Subcellular locationi

    Secreted By similarity

    GO - Cellular componenti

    1. extracellular region Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Secreted

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 1919Sequence AnalysisAdd
    BLAST
    Chaini20 – 454435Probable 1,4-beta-D-glucan cellobiohydrolase CPRO_0000394051Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi27 ↔ 44By similarity
    Disulfide bondi38 ↔ 54By similarity
    Disulfide bondi185 ↔ 244By similarity
    Disulfide bondi376 ↔ 423By similarity
    Glycosylationi413 – 4131N-linked (GlcNAc...)Sequence Analysis

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Interactioni

    Protein-protein interaction databases

    STRINGi5085.CADAFUAP00000253.

    Structurei

    3D structure databases

    ProteinModelPortaliQ4WFK4.
    SMRiQ4WFK4. Positions 21-55, 92-454.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini20 – 5536CBM1PROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni59 – 9436Thr-rich linkerAdd
    BLAST
    Regioni95 – 454360CatalyticAdd
    BLAST

    Domaini

    Has a modular structure: a carbohydrate-binding module (CBM) at the N-terminus, a linker rich in threonines, and a C-terminal exocellobiohydrolase catalytic module. The genes for catalytic modules and CBMs seem to have evolved separately and have been linked by gene fusion.

    Sequence similaritiesi

    Contains 1 CBM1 (fungal-type carbohydrate-binding) domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiCOG5297.
    HOGENOMiHOG000178851.
    KOiK01238.
    OMAiKCANAQS.
    OrthoDBiEOG72C594.

    Family and domain databases

    Gene3Di3.20.20.40. 1 hit.
    InterProiIPR016288. Beta_cellobiohydrolase.
    IPR000254. Cellulose-bd_dom_fun.
    IPR001524. Glyco_hydro_6_CS.
    [Graphical view]
    PfamiPF00734. CBM_1. 1 hit.
    PF01341. Glyco_hydro_6. 1 hit.
    [Graphical view]
    PIRSFiPIRSF001100. Beta_cellobiohydrolase. 1 hit.
    PRINTSiPR00733. GLHYDRLASE6.
    ProDomiPD001821. CBD_fun. 1 hit.
    [Graphical view] [Entries sharing at least one domain]
    SMARTiSM00236. fCBD. 1 hit.
    [Graphical view]
    SUPFAMiSSF51989. SSF51989. 1 hit.
    SSF57180. SSF57180. 1 hit.
    PROSITEiPS00562. CBM1_1. 1 hit.
    PS51164. CBM1_2. 1 hit.
    PS00655. GLYCOSYL_HYDROL_F6_1. 1 hit.
    PS00656. GLYCOSYL_HYDROL_F6_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    Q4WFK4-1 [UniParc]FASTAAdd to Basket

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    MKHLASSIAL TLLLPAVQAQ QTVWGQCGGQ GWSGPTSCVA GAACSTLNPY    50
    YAQCIPGATA TSTTLTTTTA ATTTSQTTTK PTTTGPTTSA PTVTASGNPF 100
    SGYQLYANPY YSSEVHTLAM PSLPSSLQPK ASAVAEVPSF VWLDVAAKVP 150
    TMGTYLADIQ AKNKAGANPP IAGIFVVYDL PDRDCAALAS NGEYSIANNG 200
    VANYKAYIDA IRAQLVKYSD VHTILVIEPD SLANLVTNLN VAKCANAQSA 250
    YLECVDYALK QLNLPNVAMY LDAGHAGWLG WPANLGPAAT LFAKVYTDAG 300
    SPAAVRGLAT NVANYNAWSL STCPSYTQGD PNCDEKKYIN AMAPLLKEAG 350
    FDAHFIMDTS RNGVQPTKQN AWGDWCNVIG TGFGVRPSTN TGDPLQDAFV 400
    WIKPGGESDG TSNSTSPRYD AHCGYSDALQ PAPEAGTWFQ AYFEQLLTNA 450
    NPSF 454
    Length:454
    Mass (Da):47,796
    Last modified:July 5, 2005 - v1
    Checksum:i9EFFB0212288A576
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AAHF01000010 Genomic DNA. Translation: EAL86473.1.
    RefSeqiXP_748511.1. XM_743418.1.

    Genome annotation databases

    EnsemblFungiiCADAFUAT00000253; CADAFUAP00000253; CADAFUAG00000253.
    GeneIDi3505986.
    KEGGiafm:AFUA_3G01910.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AAHF01000010 Genomic DNA. Translation: EAL86473.1 .
    RefSeqi XP_748511.1. XM_743418.1.

    3D structure databases

    ProteinModelPortali Q4WFK4.
    SMRi Q4WFK4. Positions 21-55, 92-454.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 5085.CADAFUAP00000253.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii CADAFUAT00000253 ; CADAFUAP00000253 ; CADAFUAG00000253 .
    GeneIDi 3505986.
    KEGGi afm:AFUA_3G01910.

    Phylogenomic databases

    eggNOGi COG5297.
    HOGENOMi HOG000178851.
    KOi K01238.
    OMAi KCANAQS.
    OrthoDBi EOG72C594.

    Family and domain databases

    Gene3Di 3.20.20.40. 1 hit.
    InterProi IPR016288. Beta_cellobiohydrolase.
    IPR000254. Cellulose-bd_dom_fun.
    IPR001524. Glyco_hydro_6_CS.
    [Graphical view ]
    Pfami PF00734. CBM_1. 1 hit.
    PF01341. Glyco_hydro_6. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF001100. Beta_cellobiohydrolase. 1 hit.
    PRINTSi PR00733. GLHYDRLASE6.
    ProDomi PD001821. CBD_fun. 1 hit.
    [Graphical view ] [Entries sharing at least one domain ]
    SMARTi SM00236. fCBD. 1 hit.
    [Graphical view ]
    SUPFAMi SSF51989. SSF51989. 1 hit.
    SSF57180. SSF57180. 1 hit.
    PROSITEi PS00562. CBM1_1. 1 hit.
    PS51164. CBM1_2. 1 hit.
    PS00655. GLYCOSYL_HYDROL_F6_1. 1 hit.
    PS00656. GLYCOSYL_HYDROL_F6_2. 1 hit.
    [Graphical view ]
    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 nameiCBHC_ASPFU
    AccessioniPrimary (citable) accession number: Q4WFK4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 18, 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