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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: Annotation score: 3 out of 5-Protein inferred from homologyi

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
Complete GO annotation...

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 Componenti: Unassembled WGS sequence

Organism-specific databases

EuPathDBiFungiDB:ACLA_062560.

Subcellular locationi

  1. Secreted By similarity

GO - Cellular componenti

  1. extracellular region Source: UniProtKB-SubCell
Complete GO annotation...

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.
OMAiGQQAWGD.
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

        10         20         30         40         50
MKNFAPSLAL SLLLPTVQAQ QTMWGQCGGA GWSGATDCVA GGVCSTQNAY
60 70 80 90 100
YAQCLPGATT ATTLSTTSKG TTTTTTSSTT STGGGSSSTT TKTSTSAGPT
110 120 130 140 150
VTGSPSGNPF SGYQQYANPY YSSEVHTLAI PSMTGALAVK ASAVADVPSF
160 170 180 190 200
VWLDVAAKVP TMGTYLENIR AKNKAGANPP VAGIFVVYDL PDRDCAALAS
210 220 230 240 250
NGEYAIADGG IAKYKAYIDA IRAQLLKYPD VHTILVIEPD SLANLITNIN
260 270 280 290 300
VAKCSGAKDA YLECINYALK QLNLPNVAMY IDAGHGGWLG WDANIGPAAE
310 320 330 340 350
MYAKVYKDAD APAALRGLAV NVANYNAWTI DTCPSYTQGN KNCDEKRYIH
360 370 380 390 400
ALYPLLKAAG WDARFIMDTG RNGVQPTKQQ AQGDWCNVIG TGFGIRPSSE
410 420 430 440 450
TGDDLLDAFV WVKPGAESDG TSDTTAARYD AHCGYTDALK PAPEAGQWFQ
460
AYFEQLLTNA NPAF
Length:464
Mass (Da):48,841
Last modified:January 23, 2007 - v1
Checksum:iDDE4E7406F0F96B6
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
Links Updated
DS027050 Genomic DNA. Translation: EAW12291.1.
RefSeqiXP_001273717.1. XM_001273716.1.

3D structure databases

ProteinModelPortaliA1CCN4.
SMRiA1CCN4. Positions 21-55, 102-464.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

EuPathDBiFungiDB:ACLA_062560.

Phylogenomic databases

eggNOGiCOG5297.
HOGENOMiHOG000178851.
OMAiGQQAWGD.
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]
ProtoNetiSearch...

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: April 29, 2015
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, 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.