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Protein

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

Gene

cbhA

Organism
Aspergillus terreus (strain NIH 2624 / FGSC A1156)
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 sitei227 – 2271NucleophileBy similarity
Active sitei232 – 2321Proton donorBy similarity

GO - Molecular functioni

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

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 A (EC:3.2.1.91)
Alternative name(s):
Beta-glucancellobiohydrolase A
Cellobiohydrolase D
Exocellobiohydrolase A
Exoglucanase A
Gene namesi
Name:cbhA
Synonyms:celD
ORF Names:ATEG_03727
OrganismiAspergillus terreus (strain NIH 2624 / FGSC A1156)
Taxonomic identifieri341663 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus
ProteomesiUP000007963: Unassembled WGS sequence

Subcellular locationi

Secreted Curated

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 – 1717Sequence AnalysisAdd
BLAST
Chaini18 – 453436Probable 1,4-beta-D-glucan cellobiohydrolase APRO_0000393543Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi62 – 621N-linked (GlcNAc...)Sequence Analysis
Glycosylationi285 – 2851N-linked (GlcNAc...)Sequence Analysis
Glycosylationi388 – 3881N-linked (GlcNAc...)Sequence Analysis
Glycosylationi450 – 4501N-linked (GlcNAc...)Sequence Analysis

Keywords - PTMi

Glycoprotein

Interactioni

Protein-protein interaction databases

STRINGi33178.CADATEAP00005976.

Structurei

3D structure databases

ProteinModelPortaliQ0CRF7.
SMRiQ0CRF7. Positions 18-448.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiNOG85664.
HOGENOMiHOG000182210.
OMAiNWSKCTS.
OrthoDBiEOG7ZGXCF.

Family and domain databases

Gene3Di2.70.100.10. 1 hit.
InterProiIPR013320. ConA-like_dom.
IPR001722. Glyco_hydro_7.
[Graphical view]
PfamiPF00840. Glyco_hydro_7. 1 hit.
[Graphical view]
PRINTSiPR00734. GLHYDRLASE7.
SUPFAMiSSF49899. SSF49899. 1 hit.

Sequencei

Sequence statusi: Complete.

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

Q0CRF7-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MHQRALLFSA LVGAVRAQQA GTLTEEVHPP LTWQKCTADG SCTEQSGSVV
60 70 80 90 100
IDSNWRWLHS TNGSTNCYTG NTWDESLCPD NEACAANCAL DGADYESTYG
110 120 130 140 150
ITTSGDALTL TFVTGENVGS RVYLMAEDDE SYQTFDLVGN EFTFDVDVSN
160 170 180 190 200
LPCGLNGALY FTSMDADGGV SKYPANKAGA KYGTGYCDSQ CPRDLKFING
210 220 230 240 250
MANVEGWTPS DNDKNAGVGG HGSCCPELDI WEANSISSAF TPHPCDDLGQ
260 270 280 290 300
TMCSGDDCGG TYSETRYAGT CDPDGCDFNA YRMGNTSYYG PDKIVDTNSV
310 320 330 340 350
MTVVTQFIGD GGSLSEIKRL YVQNGKVIAN AQSNVDGVTG NSITSDFCTA
360 370 380 390 400
QKTAFGDQDI FSKHGGLSGM GDAMSAMVLI LSIWDDHNSS MMWLDSTYPE
410 420 430 440 450
DADASEPGVA RGTCEHGVGD PETVESQHPG ATVTFSKIKF GPIGSTYSSN

STA
Length:453
Mass (Da):48,073
Last modified:October 17, 2006 - v1
Checksum:i759ABB134EDBBEFA
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CH476598 Genomic DNA. Translation: EAU35529.1.
RefSeqiXP_001212905.1. XM_001212905.1.

Genome annotation databases

EnsemblFungiiCADATEAT00005976; CADATEAP00005976; CADATEAG00005976.
GeneIDi4318706.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CH476598 Genomic DNA. Translation: EAU35529.1.
RefSeqiXP_001212905.1. XM_001212905.1.

3D structure databases

ProteinModelPortaliQ0CRF7.
SMRiQ0CRF7. Positions 18-448.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi33178.CADATEAP00005976.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiCADATEAT00005976; CADATEAP00005976; CADATEAG00005976.
GeneIDi4318706.

Phylogenomic databases

eggNOGiNOG85664.
HOGENOMiHOG000182210.
OMAiNWSKCTS.
OrthoDBiEOG7ZGXCF.

Family and domain databases

Gene3Di2.70.100.10. 1 hit.
InterProiIPR013320. ConA-like_dom.
IPR001722. Glyco_hydro_7.
[Graphical view]
PfamiPF00840. Glyco_hydro_7. 1 hit.
[Graphical view]
PRINTSiPR00734. GLHYDRLASE7.
SUPFAMiSSF49899. SSF49899. 1 hit.
ProtoNetiSearch...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: NIH 2624 / FGSC A1156.

Entry informationi

Entry nameiCBHA_ASPTN
AccessioniPrimary (citable) accession number: Q0CRF7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 20, 2010
Last sequence update: October 17, 2006
Last modified: January 7, 2015
This is version 35 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.