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A2QH21

- EGLC_ASPNC

UniProt

A2QH21 - EGLC_ASPNC

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Protein

Probable glucan endo-1,3-beta-glucosidase eglC

Gene

eglC

Organism
Aspergillus niger (strain CBS 513.88 / FGSC A1513)
Status
Reviewed - Annotation score: 4 out of 5- Protein inferred from homologyi

Functioni

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.By similarity

Catalytic activityi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei128 – 1281NucleophileBy similarity
Active sitei239 – 2391Proton donorBy similarity

GO - Molecular functioni

  1. glucan endo-1,3-beta-D-glucosidase activity Source: UniProtKB-EC

GO - Biological processi

  1. cell wall organization Source: UniProtKB-KW
  2. polysaccharide catabolic process Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Carbohydrate metabolism, Cell wall biogenesis/degradation, Polysaccharide degradation

Protein family/group databases

CAZyiGH17. Glycoside Hydrolase Family 17.

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:eglC
ORF Names:An03g05290
OrganismiAspergillus niger (strain CBS 513.88 / FGSC A1513)
Taxonomic identifieri425011 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus
ProteomesiUP000006706: Chromosome 6R

Subcellular locationi

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

GO - Cellular componenti

  1. anchored component of membrane Source: UniProtKB-KW
  2. cell wall Source: UniProtKB-KW
  3. extracellular region Source: UniProtKB-KW
  4. plasma membrane Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cell wall, Membrane, Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1818Sequence AnalysisAdd
BLAST
Chaini19 – 430412Probable glucan endo-1,3-beta-glucosidase eglCPRO_5000219799Add
BLAST
Propeptidei431 – 46030Removed in mature formSequence AnalysisPRO_0000395144Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi183 – 1831N-linked (GlcNAc...)Sequence Analysis
Glycosylationi312 – 3121N-linked (GlcNAc...)Sequence Analysis
Glycosylationi367 – 3671N-linked (GlcNAc...)Sequence Analysis
Glycosylationi373 – 3731N-linked (GlcNAc...)Sequence Analysis
Lipidationi430 – 4301GPI-anchor amidated serineSequence Analysis

Post-translational modificationi

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.By similarity

Keywords - PTMi

Glycoprotein, GPI-anchor, Lipoprotein

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi309 – 445137Ser-richAdd
BLAST

Sequence similaritiesi

Belongs to the glycosyl hydrolase 17 family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiCOG5309.
HOGENOMiHOG000179527.
OrthoDBiEOG7TBCCK.

Family and domain databases

Gene3Di3.20.20.80. 1 hit.
InterProiIPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
SUPFAMiSSF51445. SSF51445. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

A2QH21-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MQLAQLAAFA MTLATSEAAY QGFNYGNKFS DESSKFQADF EAEFKAAKNL
60 70 80 90 100
VGTSGFTSAR LYTMIQAYST SDVIEAIPAA IAQDTSLLLG LWASGGGMDN
110 120 130 140 150
EITALKTAIS QYGEELGKLV VGISVGSEDL YRNSVEGAEA DAGVGVNPDE
160 170 180 190 200
LVEYIKEVRS VIAGTALADV SIGHVDTWDS WTNSSNSAVV EAVDWLGFDG
210 220 230 240 250
YPFFQSSMAN SIDNAKTLFE ESVAKTKAVA GDKEVWITET GWPVSGDSQG
260 270 280 290 300
DAVASIANAK TFWDEVGCPL FGNVNTWWYI LQDASPTTPN PSFGIVGSTL
310 320 330 340 350
STTPLFDLSC KNSTTSSSSA VVSAAASSAA GSKAVGSSQA SSGAAAWATS
360 370 380 390 400
ASGSAKPTFT VGRPGVNGTV FGNGTYPLRP SGSASARPSA GAISSGSGSS
410 420 430 440 450
SSGSGSSGST GTSATSGQSS SSGSSAAAGS SSPAAFSGAS TLSGSLFGAV
460
VAVFMTLAAL
Length:460
Mass (Da):46,347
Last modified:June 15, 2010 - v2
Checksum:iF7B5114CE78833B2
GO

Sequence cautioni

The sequence CAK49181.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AM270057 Genomic DNA. Translation: CAK49181.1. Different initiation.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AM270057 Genomic DNA. Translation: CAK49181.1 . Different initiation.

3D structure databases

ModBasei Search...
MobiDBi Search...

Protein family/group databases

CAZyi GH17. Glycoside Hydrolase Family 17.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Phylogenomic databases

eggNOGi COG5309.
HOGENOMi HOG000179527.
OrthoDBi EOG7TBCCK.

Family and domain databases

Gene3Di 3.20.20.80. 1 hit.
InterProi IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view ]
SUPFAMi SSF51445. SSF51445. 1 hit.
ProtoNeti Search...

Publicationsi

  1. "Genome sequencing and analysis of the versatile cell factory Aspergillus niger CBS 513.88."
    Pel H.J., de Winde J.H., Archer D.B., Dyer P.S., Hofmann G., Schaap P.J., Turner G., de Vries R.P., Albang R., Albermann K., Andersen M.R., Bendtsen J.D., Benen J.A.E., van den Berg M., Breestraat S., Caddick M.X., Contreras R., Cornell M.
    , Coutinho P.M., Danchin E.G.J., Debets A.J.M., Dekker P., van Dijck P.W.M., van Dijk A., Dijkhuizen L., Driessen A.J.M., d'Enfert C., Geysens S., Goosen C., Groot G.S.P., de Groot P.W.J., Guillemette T., Henrissat B., Herweijer M., van den Hombergh J.P.T.W., van den Hondel C.A.M.J.J., van der Heijden R.T.J.M., van der Kaaij R.M., Klis F.M., Kools H.J., Kubicek C.P., van Kuyk P.A., Lauber J., Lu X., van der Maarel M.J.E.C., Meulenberg R., Menke H., Mortimer M.A., Nielsen J., Oliver S.G., Olsthoorn M., Pal K., van Peij N.N.M.E., Ram A.F.J., Rinas U., Roubos J.A., Sagt C.M.J., Schmoll M., Sun J., Ussery D., Varga J., Vervecken W., van de Vondervoort P.J.J., Wedler H., Woesten H.A.B., Zeng A.-P., van Ooyen A.J.J., Visser J., Stam H.
    Nat. Biotechnol. 25:221-231(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: CBS 513.88 / FGSC A1513.

Entry informationi

Entry nameiEGLC_ASPNC
AccessioniPrimary (citable) accession number: A2QH21
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 15, 2010
Last sequence update: June 15, 2010
Last modified: October 29, 2014
This is version 42 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3