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Q4WAJ6 (CELB_ASPFU) Reviewed, UniProtKB/Swiss-Prot

Last modified November 13, 2013. Version 54. 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:
Probable endo-beta-1,4-glucanase celB

Short name=Endoglucanase celB
EC=3.2.1.4
Alternative name(s):
Carboxymethylcellulase celB
Cellulase B
Gene names
Name:celB
ORF Names:AFUA_7G01540
OrganismNeosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) (Aspergillus fumigatus) [Reference proteome]
Taxonomic identifier330879 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus

Protein attributes

Sequence length407 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceInferred from homology

General annotation (Comments)

Function

Has endoglucanase activity on substrates containing beta-1,4 glycosidic bonds, like in carboxymethylcellulose (CMC), hydroxyethylcellulose (HEC) and beta-glucan. Involved in the degradation of complex natural cellulosic substrates By similarity.

Catalytic activity

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

Subcellular location

Secreted By similarity.

Sequence similarities

Belongs to the glycosyl hydrolase 7 (cellulase C) family.

Ontologies

Keywords
   Biological processCarbohydrate metabolism
Cellulose degradation
Polysaccharide degradation
   Cellular componentSecreted
   DomainSignal
   Molecular functionGlycosidase
Hydrolase
   PTMGlycoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcellulose catabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentextracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

   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 – 1818 Potential
Chain19 – 407389Probable endo-beta-1,4-glucanase celB
PRO_0000395156

Sites

Active site2161Nucleophile By similarity
Active site2211Proton donor By similarity

Amino acid modifications

Glycosylation1361N-linked (GlcNAc...) Potential

Sequences

Sequence LengthMass (Da)Tools
Q4WAJ6 [UniParc].

Last modified July 5, 2005. Version 1.
Checksum: 040128FA260BAE75

FASTA40743,418
        10         20         30         40         50         60 
MAQTLAAASL VLVPLVTAQQ IGSIAENHPE LKTYRCGSQA GCVAQSTSVV LDINAHWIHQ 

        70         80         90        100        110        120 
MGAQTSCTTS SGLDPSLCPD KVTCSQNCVV EGITDYSSFG VQNSGDAITL RQYQVQNGQI 

       130        140        150        160        170        180 
KTLRPRVYLL AEDGINYSKL QLLNQEFTFD VDASKLPCGM NGALYLSEMD ASGGRSALNP 

       190        200        210        220        230        240 
AGATYGTGYC DAQCFNPGPW INGEANTLGA GACCQEMDLW EANSRSTIFS PHPCTTAGLY 

       250        260        270        280        290        300 
ACTGAECYSI CDGYGCTYNP YELGAKDYYG YGLTVDTAKP ITVVTQFVTA DNTATGTLAE 

       310        320        330        340        350        360 
IRRLYVQEGM VIGNSAVAMT EAFCSSSRTF EALGGLQRMG EALGRGMVPV FSIWDDPSLW 

       370        380        390        400 
MHWLDSDGAG PCGSTEGDPA FIQANYPNTA VTFSKVRWGD IDSTYSV 

« Hide

References

[1]"Genomic sequence of the pathogenic and allergenic filamentous fungus Aspergillus fumigatus."
Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S., Arroyo J., Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J.W., Bowyer P., Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.L. expand/collapse author list , Fedorova N., Fedorova N.D., Feldblyum T.V., Fischer R., Fosker N., Fraser A., Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K., Griffith-Jones S., Gwilliam R., Haas B.J., Haas H., Harris D.E., Horiuchi H., Huang J., Humphray S., Jimenez J., Keller N., Khouri H., Kitamoto K., Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafton A., Latge J.-P., Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L., Mohamoud Y., Molina M., Monod M., Mouyna I., Mulligan S., Murphy L.D., O'Neil S., Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L., Quail M.A., Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U., Renauld H., Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M., Ronning C.M., Rutter S., Salzberg S.L., Sanchez M., Sanchez-Ferrero J.C., Saunders D., Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F., Turner G., Vazquez de Aldana C.R., Weidman J., White O., Woodward J.R., Yu J.-H., Fraser C.M., Galagan J.E., Asai K., Machida M., Hall N., Barrell B.G., Denning D.W.
Nature 438:1151-1156(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AAHF01000015 Genomic DNA. Translation: EAL84740.1.
RefSeqXP_746778.1. XM_741685.1.

3D structure databases

ProteinModelPortalQ4WAJ6.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING5085.CADAFUAP00001113.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiCADAFUAT00001113; CADAFUAP00001113; CADAFUAG00001113.
GeneID3504201.
KEGGafm:AFUA_7G01540.

Phylogenomic databases

eggNOGNOG138370.
HOGENOMHOG000182210.
KOK01179.
OMAPWINGEA.
OrthoDBEOG7Q8CXJ.

Family and domain databases

Gene3D2.70.100.10. 1 hit.
InterProIPR008985. ConA-like_lec_gl_sf.
IPR001722. Glyco_hydro_7.
[Graphical view]
PfamPF00840. Glyco_hydro_7. 1 hit.
[Graphical view]
PRINTSPR00734. GLHYDRLASE7.
SUPFAMSSF49899. SSF49899. 1 hit.
ProtoNetSearch...

Entry information

Entry nameCELB_ASPFU
AccessionPrimary (citable) accession number: Q4WAJ6
Entry history
Integrated into UniProtKB/Swiss-Prot: June 15, 2010
Last sequence update: July 5, 2005
Last modified: November 13, 2013
This is version 54 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries