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Q5B430 (BTGC_EMENI) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. 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:
Glucan endo-1,3-beta-glucosidase btgC

EC=3.2.1.39
Alternative name(s):
Endo-1,3-beta-glucanase btgC
Laminarinase btgC
Gene names
Name:btgC
ORF Names:AN4700
OrganismEmericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans) [Reference proteome]
Taxonomic identifier227321 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus

Protein attributes

Sequence length649 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Glucanases play a role in cell expansion during growth, in cell-cell fusion during mating, and in spore release during sporulation. This enzyme may be involved in beta-glucan degradation. Active on laminarin and lichenan. Ref.1

Catalytic activity

Hydrolysis of (1->3)-beta-D-glucosidic linkages in (1->3)-beta-D-glucans.

Subcellular location

Cell membrane; Single-pass type II membrane protein By similarity.

Sequence similarities

Belongs to the glycosyl hydrolase 17 family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 649649Glucan endo-1,3-beta-glucosidase btgC
PRO_0000395128

Regions

Topological domain1 – 274274Cytoplasmic Potential
Transmembrane275 – 29521Helical; Signal-anchor for type II membrane protein; Potential
Topological domain296 – 649354Extracellular Potential
Compositional bias222 – 30079Gly-rich

Sites

Active site5511Nucleophile By similarity
Active site6191Proton donor By similarity

Amino acid modifications

Glycosylation3691N-linked (GlcNAc...) Potential
Glycosylation3921N-linked (GlcNAc...) Potential
Glycosylation4201N-linked (GlcNAc...) Potential
Glycosylation5961N-linked (GlcNAc...) Potential

Sequences

Sequence LengthMass (Da)Tools
Q5B430 [UniParc].

Last modified April 26, 2005. Version 1.
Checksum: 8476F1DF5B3F1D93

FASTA64968,963
        10         20         30         40         50         60 
MGDRSEQYGD IPPISSQHRM HGYGNNGEPA AMPGDGQQNW GSGPGIAHTH SMRTASTATP 

        70         80         90        100        110        120 
GMDNLGPSAV GGGISGIALG VANTHDRQSG IDAFRDADAT LGYIPAERGY HTTGADNPYV 

       130        140        150        160        170        180 
PSPPSVGPGP DESSEGLRSH ETFGSSAALS AAGAPAGNWT PPSGSRHSFL DGSYQGVASG 

       190        200        210        220        230        240 
PYQRHSAYSS QDYPADINPD DILDDGDDGF AAAPSNKPNA AGGAATGGAA GGLLGEFFGA 

       250        260        270        280        290        300 
KKAADASYDP VPGAGLPSVE KYAKPRPSGA SRKRGWIIGG ILAFIVIGAI VGGAVGGTLG 

       310        320        330        340        350        360 
NRRSETASES SEVSADDDTE TNGDLDKNSD EIKSLMAMEG LHKVFPGMDY TPWGVQHPEC 

       370        380        390        400        410        420 
DKWPPSQNNV TRDMAVLSRL TNTVRLYGTD CNQTEMVLHA IDRLELTDMK LWLGVWIDTN 

       430        440        450        460        470        480 
TTTNERQLSQ LYDILDKRSD HSVFKGAIIG NEALYRAGST KEEARKNIID YMRQVRKHFN 

       490        500        510        520        530        540 
DHNIDIKVAT SDLGDNWDET LADATDVVMS NVHPFFGGVE VSKAAGWTWS FWNSHNAPLT 

       550        560        570        580        590        600 
QGTNKGNIIA EVGWPSGGGN DCGDGANCKD DTSGAVAGVK QMNQFMADWV CPALENGTDY 

       610        620        630        640 
FWFEAFDEPW KVKFNKGDEQ WEDKWGLMDP GRNLKPGIEI PDCGGKTAA 

« Hide

References

« Hide 'large scale' references
[1]"Development and application of a suite of polysaccharide-degrading enzymes for analyzing plant cell walls."
Bauer S., Vasu P., Persson S., Mort A.J., Somerville C.R.
Proc. Natl. Acad. Sci. U.S.A. 103:11417-11422(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION.
Strain: FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139.
[2]"Sequencing of Aspergillus nidulans and comparative analysis with A. fumigatus and A. oryzae."
Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R., Batzoglou S., Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J., Kapitonov V., Jurka J., Scazzocchio C., Farman M.L., Butler J., Purcell S., Harris S., Braus G.H. expand/collapse author list , Draht O., Busch S., D'Enfert C., Bouchier C., Goldman G.H., Bell-Pedersen D., Griffiths-Jones S., Doonan J.H., Yu J., Vienken K., Pain A., Freitag M., Selker E.U., Archer D.B., Penalva M.A., Oakley B.R., Momany M., Tanaka T., Kumagai T., Asai K., Machida M., Nierman W.C., Denning D.W., Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L., Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W.
Nature 438:1105-1115(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139.
[3]"The 2008 update of the Aspergillus nidulans genome annotation: a community effort."
Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J., Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H., Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M., Estrada C.G. expand/collapse author list , Geysens S., Goldman G., de Groot P.W., Hansen K., Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G., Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L., Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M., van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P., Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J., Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A., Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X., Robson G., Seiboth B., van Solingen P., Specht T., Sun J., Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H., van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y., Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J., Oliver S.G., Turner G.
Fungal Genet. Biol. 46:S2-13(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: GENOME REANNOTATION.
Strain: FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
DQ490493 mRNA. Translation: ABF50869.1.
AACD01000080 Genomic DNA. Translation: EAA60742.1.
BN001303 Genomic DNA. Translation: CBF76969.1.
RefSeqXP_662304.1. XM_657212.1.

3D structure databases

ProteinModelPortalQ5B430.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

CAZyGH17. Glycoside Hydrolase Family 17.
mycoCLAPLAM17A_EMENI.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiCADANIAT00005730; CADANIAP00005730; CADANIAG00005730.
GeneID2872500.
KEGGani:AN4700.2.

Phylogenomic databases

eggNOGCOG5309.
HOGENOMHOG000173877.
OMASDNPYVP.
OrthoDBEOG7P8PHC.

Family and domain databases

Gene3D3.20.20.80. 1 hit.
InterProIPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
SUPFAMSSF51445. SSF51445. 1 hit.
ProtoNetSearch...

Entry information

Entry nameBTGC_EMENI
AccessionPrimary (citable) accession number: Q5B430
Secondary accession number(s): C8VAX6, Q1HFT1
Entry history
Integrated into UniProtKB/Swiss-Prot: June 15, 2010
Last sequence update: April 26, 2005
Last modified: February 19, 2014
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