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A1DJQ7

- CBHC_NEOFI

UniProt

A1DJQ7 - CBHC_NEOFI

Protein

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

Gene

cbhC

Organism
Neosartorya fischeri (strain ATCC 1020 / DSM 3700 / FGSC A1164 / NRRL 181) (Aspergillus fischerianus)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 36 (01 Oct 2014)
      Sequence version 1 (23 Jan 2007)
      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 sitei180 – 1801PROSITE-ProRule annotation
    Active sitei226 – 2261Proton donorPROSITE-ProRule annotation
    Active sitei405 – 4051NucleophilePROSITE-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:NFIA_002990
    OrganismiNeosartorya fischeri (strain ATCC 1020 / DSM 3700 / FGSC A1164 / NRRL 181) (Aspergillus fischerianus)
    Taxonomic identifieri331117 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeNeosartorya
    ProteomesiUP000006702: Unassembled WGS sequence

    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 – 450431Probable 1,4-beta-D-glucan cellobiohydrolase CPRO_0000394054Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi27 ↔ 44By similarity
    Disulfide bondi38 ↔ 54By similarity
    Disulfide bondi181 ↔ 240By similarity
    Disulfide bondi372 ↔ 419By similarity
    Glycosylationi409 – 4091N-linked (GlcNAc...)Sequence Analysis

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Structurei

    3D structure databases

    ProteinModelPortaliA1DJQ7.
    SMRiA1DJQ7. Positions 21-55, 88-450.
    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 – 9032Thr-rich linkerAdd
    BLAST
    Regioni91 – 450360CatalyticAdd
    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.
    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.

    A1DJQ7-1 [UniParc]FASTAAdd to Basket

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    MKHLASSIAL TLLLPAVQAQ QTVWGQCGGQ GWSGPTNCVA GAACSTLNPY    50
    YAQCIPGATA TSTTLSTTTT TQTTTKPTTT GPTTSAPTVT ASGNPFSGYQ 100
    LYANPYYSSE VHTLAMPSLP SSLQPKASAV AEVPSFVWLD VAAKVPTMGT 150
    YLADIQAKNK AGASPPIAGI FVVYDLPDRD CAALASNGEY SIANNGVANY 200
    KAYIDAIRAQ LVKYSDVHTI LVIEPDSLAN LVTNLNVAKC ANAQSAYLEC 250
    VDYALKQLNL PNVAMYLDAG HAGWLGWPAN LGPAATLFAK VYTDAGSPAA 300
    LRGLATNVAN YNAWSLSTCP SYTQGDPNCD EKKYINAMAP LLKNAGFDAH 350
    FIMDTSRNGV QPTKQSAWGD WCNVIGTGFG VRPSTNTGDP LQDAFVWIKP 400
    GGESDGTSNS SSARYDAHCG YSDALQPAPE AGTWFQAYFE QLLTNANPSF 450
    Length:450
    Mass (Da):47,383
    Last modified:January 23, 2007 - v1
    Checksum:i591EB3C96C03AB8A
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    DS027697 Genomic DNA. Translation: EAW16946.1.
    RefSeqiXP_001258843.1. XM_001258842.1.

    Genome annotation databases

    EnsemblFungiiCADNFIAT00000050; CADNFIAP00000041; CADNFIAG00000050.
    GeneIDi4585216.
    KEGGinfi:NFIA_002990.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    DS027697 Genomic DNA. Translation: EAW16946.1 .
    RefSeqi XP_001258843.1. XM_001258842.1.

    3D structure databases

    ProteinModelPortali A1DJQ7.
    SMRi A1DJQ7. Positions 21-55, 88-450.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii CADNFIAT00000050 ; CADNFIAP00000041 ; CADNFIAG00000050 .
    GeneIDi 4585216.
    KEGGi nfi:NFIA_002990.

    Phylogenomic databases

    eggNOGi COG5297.
    HOGENOMi HOG000178851.
    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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 1020 / DSM 3700 / FGSC A1164 / NRRL 181.

    Entry informationi

    Entry nameiCBHC_NEOFI
    AccessioniPrimary (citable) accession number: A1DJQ7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 18, 2010
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 36 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

    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