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P37698 (GUNF_CLOCE) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 95. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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:
Endoglucanase F

EC=3.2.1.4
Alternative name(s):
Cellulase F
EGCCF
Endo-1,4-beta-glucanase F
Gene names
Name:celCCF
Ordered Locus Names:Ccel_0729
OrganismClostridium cellulolyticum (strain ATCC 35319 / DSM 5812 / JCM 6584 / H10) [Complete proteome] [HAMAP]
Taxonomic identifier394503 [NCBI]
Taxonomic lineageBacteriaFirmicutesClostridiaClostridialesClostridiaceaeClostridium

Protein attributes

Sequence length722 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Probable endoglucanase involved in the degradation of cellulose or related beta-glucans.

Catalytic activity

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

Domain

A 24 residue domain is repeated twice in this enzyme as well as in other C.thermocellum cellulosome enzymes. This domain may function as the binding ligand for the SL component.

Sequence similarities

Belongs to the glycosyl hydrolase 48 (cellulase L) family.

Ontologies

Keywords
   Biological processCarbohydrate metabolism
Cellulose degradation
Polysaccharide degradation
   DomainRepeat
Signal
   Molecular functionGlycosidase
Hydrolase
   Technical term3D-structure
Complete proteome
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 Potential
Chain30 – 722693Endoglucanase F
PRO_0000008026

Regions

Repeat667 – 690241
Repeat699 – 722242
Region667 – 722562 X 24 AA approximate repeats

Secondary structure

........................................................................................................ 722
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P37698 [UniParc].

Last modified October 1, 1996. Version 2.
Checksum: 5E48F85319D70AE5

FASTA72280,544
        10         20         30         40         50         60 
MSKNFKRVGA VAVAAAMSLS IMATTSINAA SSPANKVYQD RFESMYSKIK DPANGYFSEQ 

        70         80         90        100        110        120 
GIPYHSIETL MVEAPDYGHV TTSEAMSYYM WLEAMHGRFS GDFTGFDKSW SVTEQYLIPT 

       130        140        150        160        170        180 
EKDQPNTSMS RYDANKPATY APEFQDPSKY PSPLDTSQPV GRDPINSQLT SAYGTSMLYG 

       190        200        210        220        230        240 
MHWILDVDNW YGFGARADGT SKPSYINTFQ RGEQESTWET IPQPCWDEHK FGGQYGFLDL 

       250        260        270        280        290        300 
FTKDTGTPAK QFKYTNAPDA DARAVQATYW ADQWAKEQGK SVSTSVGKAT KMGDYLRYSF 

       310        320        330        340        350        360 
FDKYFRKIGQ PSQAGTGYDA AHYLLSWYYA WGGGIDSTWS WIIGSSHNHF GYQNPFAAWV 

       370        380        390        400        410        420 
LSTDANFKPK SSNGASDWAK SLDRQLEFYQ WLQSAEGAIA GGATNSWNGR YEAVPSGTST 

       430        440        450        460        470        480 
FYGMGYVENP VYADPGSNTW FGMQVWSMQR VAELYYKTGD ARAKKLLDKW AKWINGEIKF 

       490        500        510        520        530        540 
NADGTFQIPS TIDWEGQPDT WNPTQGYTGN ANLHVKVVNY GTDLGCASSL ANTLTYYAAK 

       550        560        570        580        590        600 
SGDETSRQNA QKLLDAMWNN YSDSKGISTV EQRGDYHRFL DQEVFVPAGW TGKMPNGDVI 

       610        620        630        640        650        660 
KSGVKFIDIR SKYKQDPEWQ TMVAALQAGQ VPTQRLHRFW AQSEFAVANG VYAILFPDQG 

       670        680        690        700        710        720 
PEKLLGDVNG DETVDAIDLA ILKKYLLNSS TTINTANADM NSDNAIDAID YALLKKALLS 


IQ 

« Hide

References

« Hide 'large scale' references
[1]"Molecular study and overexpression of the Clostridium cellulolyticum celF cellulase gene in Escherichia coli."
Reverbel-Leroy C., Belaich A., Bernadac A., Gaudin C., Belaich J.-P., Tardif C.
Microbiology 142:1013-1023(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Complete sequence of Clostridium cellulolyticum H10."
US DOE Joint Genome Institute
Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H., Bruce D., Goodwin L., Pitluck S., Chertkov O., Saunders E., Brettin T., Detter J.C., Han C., Larimer F., Land M., Hauser L., Kyrpides N. expand/collapse author list , Ivanova N., Zhou J., Richardson P.
Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 35319 / DSM 5812 / JCM 6584 / H10.
[3]"Sequence analysis of a gene cluster encoding cellulases from Clostridium cellulolyticum."
Bagnara-Tardif C., Gaudin C., Belaich A., Hoest P., Citard T., Belaich J.-P.
Gene 119:17-28(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 387-722.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U30321 Genomic DNA. Translation: AAB41452.1.
CP001348 Genomic DNA. Translation: ACL75108.1.
M87018 Genomic DNA. Translation: AAA73866.1.
PIRPC1139.
RefSeqYP_002505088.1. NC_011898.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1F9DX-ray2.30A30-658[»]
1F9OX-ray2.50A30-658[»]
1FAEX-ray2.00A30-658[»]
1FBOX-ray2.30A30-658[»]
1FBWX-ray2.00A30-658[»]
1FCEX-ray2.00A30-658[»]
1G9GX-ray1.90A30-658[»]
1G9JX-ray1.90A30-658[»]
2QNOX-ray2.00A30-658[»]
ProteinModelPortalP37698.
SMRP37698. Positions 30-658.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING394503.Ccel_0729.

Protein family/group databases

CAZyGH48. Glycoside Hydrolase Family 48.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACL75108; ACL75108; Ccel_0729.
GeneID7309583.
KEGGcce:Ccel_0729.
PATRIC19432255. VBICloCel57783_0754.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGNOG10655.
HOGENOMHOG000020369.
OMAGMHWLLD.
OrthoDBEOG64V28H.
ProtClustDBCLSK801496.

Enzyme and pathway databases

BioCycCCEL394503:GJET-750-MONOMER.

Family and domain databases

Gene3D1.10.1330.10. 1 hit.
1.50.10.10. 4 hits.
4.10.870.10. 1 hit.
InterProIPR008928. 6-hairpin_glycosidase-like.
IPR012341. 6hp_glycosidase.
IPR016134. Cellulos_enz_dockerin_1.
IPR002105. Cellulos_enz_dockerin_1_Ca-bd.
IPR018242. Dockerin_1.
IPR027390. Endoglucanase_F_dom3.
IPR000556. Glyco_hydro_48F.
[Graphical view]
PfamPF00404. Dockerin_1. 2 hits.
PF02011. Glyco_hydro_48. 1 hit.
[Graphical view]
PRINTSPR00844. GLHYDRLASE48.
SUPFAMSSF48208. SSF48208. 1 hit.
SSF63446. SSF63446. 1 hit.
PROSITEPS00448. CLOS_CELLULOSOME_RPT. 2 hits.
PS00018. EF_HAND_1. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP37698.

Entry information

Entry nameGUNF_CLOCE
AccessionPrimary (citable) accession number: P37698
Secondary accession number(s): B8I7V1
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1994
Last sequence update: October 1, 1996
Last modified: February 19, 2014
This is version 95 of the entry and version 2 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries