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Q05156 (GUN1_STRRE) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 77. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Cellulase 1

EC=3.2.1.4
Alternative name(s):
Avicelase
Endo-1,4-beta-glucanase
Endoglucanase
Gene names
Name:cel1
OrganismStreptomyces reticuli
Taxonomic identifier1926 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesStreptomycineaeStreptomycetaceaeStreptomyces

Protein attributes

Sequence length746 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

This endoglucanase acts only on crystalline cellulose.

Catalytic activity

Endohydrolysis of (1->4)-beta-D-glucosidic linkages in cellulose, lichenin and cereal beta-D-glucans.

Subcellular location

Note: Exists in both mycelium-associated and extracellular forms.

Sequence similarities

Belongs to the glycosyl hydrolase 9 (cellulase E) family.

Contains 1 CBM-cenC (cenC-type cellulose-binding) domain.

Ontologies

Keywords
   Biological processCarbohydrate metabolism
Cellulose degradation
Polysaccharide degradation
   DomainSignal
   Molecular functionGlycosidase
Hydrolase
   Technical termDirect protein sequencing
Gene Ontology (GO)
   Biological_processcellulose catabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular_functioncellulase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2929 Ref.1
Chain30 – 746717Cellulase 1
PRO_0000007958

Regions

Domain45 – 170126CBM-cenC
Region171 – 21141Linker
Region212 – 746535Catalytic

Sites

Active site6691 By similarity
Active site7171 By similarity
Active site7261 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q05156 [UniParc].

Last modified June 1, 1994. Version 1.
Checksum: FDF1ADB4714A35FD

FASTA74680,000
        10         20         30         40         50         60 
MKRRTTAVLT LTALLGTALT ALPVQQAGAE EVEQVRNGTF DTTTDPWWTS NVTAGLSDGR 

        70         80         90        100        110        120 
LCADVPGGTT NRWDSAIGQN DITLVKGETY RFSFHASGIP EGHVVRAVVG LAVSPYDTWQ 

       130        140        150        160        170        180 
EASPVLTEAD GSYSYTFTAP VDTTQGQVAF QVGGSTDAWR FCVDDVSLLG GVPPEVYEPD 

       190        200        210        220        230        240 
TGPRVRVNQV AYLPAGPKNA TLVTDATARL PWQLRNAQGT TVARGLTVPR GVDASSGQNV 

       250        260        270        280        290        300 
HSIDFGSYRG RGTGYTLVAD GETSHPFDID AAAYRPLRLD SVKYYYTQRS GIAIRDDLRP 

       310        320        330        340        350        360 
GYGRAAGHLN VAPNQGDANV PCQPGVCDYT LDVTGGWYDA GDHGKYVVNG GIATWELLST 

       370        380        390        400        410        420 
YERSLTARTG HPAALGDGTL ALPESGNKVP DVLDEARWEL EFLLKMQVPA GQPLAGMAHH 

       430        440        450        460        470        480 
KLHDEQWTGL PLLPDQDPQK RELHPPTTAA TLNLAATAAQ AARLYRPFDK AFAARALTAA 

       490        500        510        520        530        540 
RTAWQAALAH PDLLADPNDG TGGGAYNDDD VTDEFYWAAA ELYLTTGERQ FADHVLDSPV 

       550        560        570        580        590        600 
HTADIFGPTG FDWGHTAAAG RLDLALVPSR LPGRDQVRRS VIKAADTYLA TLTAHPYGMP 

       610        620        630        640        650        660 
YAPAGNRYDW GSSHQVLNNG VVLASAYDLT GAAKYRDGAL QGMDYVLGRN ALNMSYVTGY 

       670        680        690        700        710        720 
GEVSSHNQHS RWYAHQLDPT LPNPPSGTLA GGPNSSIQDP YAQSKLTGCV GQFCYIDDIQ 

       730        740 
SWSTNETAIN WNAALARMAS FAADQG 

« Hide

References

[1]"The gene encoding the cellulase (Avicelase) Cel1 from Streptomyces reticuli and analysis of protein domains."
Schlochtermeier A., Walter S., Schroeder J., Moorman M., Schrempf H.
Mol. Microbiol. 6:3611-3621(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 30-41 AND 379-391.
Strain: Tu45.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X65616 Genomic DNA. Translation: CAA46570.1.
PIRS27985.

3D structure databases

ProteinModelPortalQ05156.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

CAZyCBM4. Carbohydrate-Binding Module Family 4.
GH9. Glycoside Hydrolase Family 9.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

Gene3D1.50.10.10. 1 hit.
2.60.120.260. 1 hit.
2.60.40.10. 1 hit.
InterProIPR008928. 6-hairpin_glycosidase-like.
IPR012341. 6hp_glycosidase.
IPR003305. CenC_carb-bd.
IPR008979. Galactose-bd-like.
IPR001701. Glyco_hydro_9.
IPR018221. Glyco_hydro_9_AS.
IPR004197. Glyco_hydro_9_Ig-like.
IPR013783. Ig-like_fold.
IPR014756. Ig_E-set.
[Graphical view]
PfamPF02018. CBM_4_9. 1 hit.
PF02927. CelD_N. 1 hit.
PF00759. Glyco_hydro_9. 1 hit.
[Graphical view]
SUPFAMSSF48208. SSF48208. 1 hit.
SSF49785. SSF49785. 1 hit.
SSF81296. SSF81296. 1 hit.
PROSITEPS00698. GLYCOSYL_HYDROL_F9_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameGUN1_STRRE
AccessionPrimary (citable) accession number: Q05156
Entry history
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: June 1, 1994
Last modified: February 19, 2014
This is version 77 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries