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Q4WG16 (EGLC_ASPFU) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 55. 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 glucan endo-1,3-beta-glucosidase eglC

EC=3.2.1.39
Alternative name(s):
Endo-1,3-beta-glucanase eglC
Laminarinase eglC
Gene names
Name:eglC
ORF Names:AFUA_3G00270
OrganismNeosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) (Aspergillus fumigatus) [Reference proteome]
Taxonomic identifier330879 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus

Protein attributes

Sequence length446 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceInferred from homology

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 and also function biosynthetically as a transglycosylase By similarity.

Catalytic activity

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

Subcellular location

Cell membrane; Lipid-anchorGPI-anchor By similarity. Secretedcell wall By similarity. Note: Covalently-linked GPI-modified cell wall protein By similarity.

Post-translational modification

The GPI-anchor is attached to the protein in the endoplasmic reticulum and serves to target the protein to the cell surface. There, the glucosamine-inositol phospholipid moiety is cleaved off and the GPI-modified mannoprotein is covalently attached via its lipidless GPI glycan remnant to the 1,6-beta-glucan of the outer cell wall layer By similarity.

Sequence similarities

Belongs to the glycosyl hydrolase 17 family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1818 Potential
Chain19 – 423405Probable glucan endo-1,3-beta-glucosidase eglC
PRO_0000395142
Propeptide424 – 44623Removed in mature form Potential
PRO_0000395143

Regions

Compositional bias309 – 431123Ser-rich

Sites

Active site1281Nucleophile By similarity
Active site2391Proton donor By similarity

Amino acid modifications

Lipidation4231GPI-anchor amidated asparagine Potential
Glycosylation1831N-linked (GlcNAc...) Potential
Glycosylation3641N-linked (GlcNAc...) Potential
Glycosylation3701N-linked (GlcNAc...) Potential

Sequences

Sequence LengthMass (Da)Tools
Q4WG16 [UniParc].

Last modified July 5, 2005. Version 1.
Checksum: BC92A444453E63B3

FASTA44644,651
        10         20         30         40         50         60 
MQFTHLVALA LALATSEAAH QGFNYGNTKS DGSAKSQADF QAEFSTAKNL VGTSGFTSAR 

        70         80         90        100        110        120 
LYTMIQGGTA NTPISAIPAA ITEQTSLLLG LWASGGNFAN EIAALKAAIA QYGDDLAKLV 

       130        140        150        160        170        180 
VGISVGSEDL YRNSVDGVKA NAGIGTNPDE IVSYINEVRS TIAGTKLSGA PIGHVDTWTA 

       190        200        210        220        230        240 
WVNGSNSAVI DACDWLGFDG YPYFQNTMAN SISDAKALFD ESVAKTQAVA KGKEVWITET 

       250        260        270        280        290        300 
GWPVSGKTEN LAVANLANAK TYWDEVGCPL FGKTNTWWYI LQDADPVTPN PSFGIVGSTL 

       310        320        330        340        350        360 
STTPLFDLSC SASSSSSAAA AASSTAGPSA SSVIGGKASG FTTAAANSAK PTFTVGKGPG 

       370        380        390        400        410        420 
GSYNGTGFWN STSSARPSSS AISGSSSGSA AGSSGAGASG ASGQSSSSTG SSSAPSTSNI 

       430        440 
LSNAASGLSG SIFGAVVAVC LALAAL 

« 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
AAHF01000010 Genomic DNA. Translation: EAL86311.1.
RefSeqXP_748349.1. XM_743256.1.

3D structure databases

ProteinModelPortalQ4WG16.
ModBaseSearch...
MobiDBSearch...

Proteomic databases

PRIDEQ4WG16.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiCADAFUAT00000272; CADAFUAP00000272; CADAFUAG00000272.
GeneID3506119.
KEGGafm:AFUA_3G00270.

Phylogenomic databases

eggNOGCOG5309.
HOGENOMHOG000179527.
KOK01238.
OMATNTWWYI.
OrthoDBEOG7TBCCK.

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 nameEGLC_ASPFU
AccessionPrimary (citable) accession number: Q4WG16
Entry history
Integrated into UniProtKB/Swiss-Prot: June 15, 2010
Last sequence update: July 5, 2005
Last modified: February 19, 2014
This is version 55 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