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P19570 (GUN3_BACCJ) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 86. 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:
Endoglucanase C

EC=3.2.1.4
Alternative name(s):
Cellulase C
Endo-1,4-beta-glucanase C
Gene names
Name:celC
OrganismBacillus cellulosilyticus (strain ATCC 21833 / DSM 2522 / FERM P-1141 / JCM 9156 / N-4)
Taxonomic identifier649639 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus

Protein attributes

Sequence length825 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceInferred from homology

General annotation (Comments)

Catalytic activity

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

Sequence similarities

Belongs to the glycosyl hydrolase 5 (cellulase A) family.

Ontologies

Keywords
   Biological processCarbohydrate metabolism
Cellulose degradation
Polysaccharide degradation
   DomainSignal
   Molecular functionGlycosidase
Hydrolase
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 – 2828 Potential
Chain29 – 825797Endoglucanase C
PRO_0000007836

Sites

Active site2191Proton donor By similarity
Active site3351Nucleophile By similarity

Sequences

Sequence LengthMass (Da)Tools
P19570 [UniParc].

Last modified February 1, 1991. Version 1.
Checksum: A1727DA3D7632617

FASTA82592,015
        10         20         30         40         50         60 
MRNKLRRLLA IMMAVLLITS LFAPMVSAEE GDNGDDDDLV TPIEIEERPH ESNYEKYPAL 

        70         80         90        100        110        120 
LDGGLDERRP SEAGALQLVE VDGQVTLADQ DGVPIQLRGM STHGLQWFGE IVNENAFAAL 

       130        140        150        160        170        180 
ANDWGSNVIR LALYIGENAY RYNPDLIEKV YAGIELAKEN DMYVIIDWHV HAPGDPNADI 

       190        200        210        220        230        240 
YQGGVNEDGE EYLGAKDFFL HIAEKYPNDP HLIYELANEP SSNSSGGPGI TNDEDGWEAV 

       250        260        270        280        290        300 
REYAQPIVDA LRDSGNAEDN IIIVGSPNWS QRMDLAAADN PIDDHHTMYT LHFYTGTHEG 

       310        320        330        340        350        360 
TNESYPEGIS SEDRSNVMAN AKYALDKGKA IFATEWGVSE ADGNNGPYLN EADVWLNFLN 

       370        380        390        400        410        420 
ENNISWTNWS LTNKNETSGA FTPFILNESD ATDLDPGEDQ VWSMEELSVS GEYVRSRILG 

       430        440        450        460        470        480 
EEYQPIDRTP REEFSEVIWD FNDGTTQGFV QNSDSPLDVT IENVNDALQI TGLDESNAIA 

       490        500        510        520        530        540 
GEEEDYWSNV RISADEWEET FDILGAEELS MDVVVDDPTT VAIAAIPQSS AHEWANASNS 

       550        560        570        580        590        600 
VLITEDDFEE QEDGTYKALL TITGEDAPNL TNIAEDPEGS ELNNIILFVG TENADVISLD 

       610        620        630        640        650        660 
NITVTGDRES VPEPVEHDTK GDSALPSDFE DGTRQGWEWD SESAVRTALT IEEANGSNAL 

       670        680        690        700        710        720 
SWEYAYPEVK PSDDWATAPR LTLYKDDLVR GDYEFVAFDF YIDPIEDRAT EGAIDINLIF 

       730        740        750        760        770        780 
QPPAAGYWAQ ASETFEIDLE ELDSATVTDD GLYHYEVEIN IEDIENDIEL RNLMLIFADD 

       790        800        810        820 
ESDFAGRVFL DNVRMDMSLE TKVEVLERNI NELQEQLVEV EALMR 

« Hide

References

[1]"The third cellulase of alkalophilic Bacillus sp. strain N-4: evolutionary relationships within the cel gene family."
Fukumori F., Kudo T., Sashihara N., Nagata Y., Ito K., Horikoshi K.
Gene 76:289-298(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M25500 Genomic DNA. Translation: AAA22306.1.
PIRJS0174.

3D structure databases

ProteinModelPortalP19570.
SMRP19570. Positions 68-429, 615-796.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

CAZyCBM17. Carbohydrate-Binding Module Family 17.
CBM28. Carbohydrate-Binding Module Family 28.
GH5. Glycoside Hydrolase Family 5.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

Gene3D2.60.120.260. 2 hits.
3.20.20.80. 1 hit.
InterProIPR005086. CBM_fam_17/28.
IPR008979. Galactose-bd-like.
IPR001547. Glyco_hydro_5.
IPR018087. Glyco_hydro_5_CS.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PfamPF03424. CBM_17_28. 2 hits.
PF00150. Cellulase. 1 hit.
[Graphical view]
SUPFAMSSF49785. SSF49785. 2 hits.
SSF51445. SSF51445. 1 hit.
PROSITEPS00659. GLYCOSYL_HYDROL_F5. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameGUN3_BACCJ
AccessionPrimary (citable) accession number: P19570
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1991
Last sequence update: February 1, 1991
Last modified: May 14, 2014
This is version 86 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