Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

A1CCN4

- CBHC_ASPCL

UniProt

A1CCN4 - CBHC_ASPCL

Protein

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

Gene

cbhC

Organism
Aspergillus clavatus (strain ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 33 (01 Oct 2014)
      Sequence version 1 (23 Jan 2007)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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 sitei194 – 1941PROSITE-ProRule annotation
    Active sitei240 – 2401Proton donorPROSITE-ProRule annotation
    Active sitei419 – 4191NucleophilePROSITE-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:ACLA_062560
    OrganismiAspergillus clavatus (strain ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1)
    Taxonomic identifieri344612 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus
    ProteomesiUP000006701: 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 – 464445Probable 1,4-beta-D-glucan cellobiohydrolase CPRO_0000394049Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi27 ↔ 44By similarity
    Disulfide bondi38 ↔ 54By similarity
    Disulfide bondi195 ↔ 254By similarity
    Disulfide bondi386 ↔ 433By similarity

    Keywords - PTMi

    Disulfide bond

    Structurei

    3D structure databases

    ProteinModelPortaliA1CCN4.
    SMRiA1CCN4. Positions 21-55, 102-464.
    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 – 10244Thr-rich linkerAdd
    BLAST
    Regioni103 – 464362CatalyticAdd
    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.
    OMAiANLMGTF.
    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.

    A1CCN4-1 [UniParc]FASTAAdd to Basket

    « Hide

    MKNFAPSLAL SLLLPTVQAQ QTMWGQCGGA GWSGATDCVA GGVCSTQNAY    50
    YAQCLPGATT ATTLSTTSKG TTTTTTSSTT STGGGSSSTT TKTSTSAGPT 100
    VTGSPSGNPF SGYQQYANPY YSSEVHTLAI PSMTGALAVK ASAVADVPSF 150
    VWLDVAAKVP TMGTYLENIR AKNKAGANPP VAGIFVVYDL PDRDCAALAS 200
    NGEYAIADGG IAKYKAYIDA IRAQLLKYPD VHTILVIEPD SLANLITNIN 250
    VAKCSGAKDA YLECINYALK QLNLPNVAMY IDAGHGGWLG WDANIGPAAE 300
    MYAKVYKDAD APAALRGLAV NVANYNAWTI DTCPSYTQGN KNCDEKRYIH 350
    ALYPLLKAAG WDARFIMDTG RNGVQPTKQQ AQGDWCNVIG TGFGIRPSSE 400
    TGDDLLDAFV WVKPGAESDG TSDTTAARYD AHCGYTDALK PAPEAGQWFQ 450
    AYFEQLLTNA NPAF 464
    Length:464
    Mass (Da):48,841
    Last modified:January 23, 2007 - v1
    Checksum:iDDE4E7406F0F96B6
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    DS027050 Genomic DNA. Translation: EAW12291.1.
    RefSeqiXP_001273717.1. XM_001273716.1.

    Genome annotation databases

    EnsemblFungiiCADACLAT00005938; CADACLAP00005801; CADACLAG00005938.
    GeneIDi4706008.
    KEGGiact:ACLA_062560.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    DS027050 Genomic DNA. Translation: EAW12291.1 .
    RefSeqi XP_001273717.1. XM_001273716.1.

    3D structure databases

    ProteinModelPortali A1CCN4.
    SMRi A1CCN4. Positions 21-55, 102-464.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii CADACLAT00005938 ; CADACLAP00005801 ; CADACLAG00005938 .
    GeneIDi 4706008.
    KEGGi act:ACLA_062560.

    Phylogenomic databases

    eggNOGi COG5297.
    HOGENOMi HOG000178851.
    OMAi ANLMGTF.
    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 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1.

    Entry informationi

    Entry nameiCBHC_ASPCL
    AccessioniPrimary (citable) accession number: A1CCN4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 18, 2010
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 33 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