SubmitCancel

Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

A2QH21

- EGLC_ASPNC

UniProt

A2QH21 - EGLC_ASPNC

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein
Probable glucan endo-1,3-beta-glucosidase eglC
Gene
eglC, An03g05290
Organism
Aspergillus niger (strain CBS 513.88 / FGSC A1513)
Status
Reviewed - Annotation score: 3 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.

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 – 1281Nucleophile By similarity
Active sitei239 – 2391Proton donor By similarity

GO - Molecular functioni

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

GO - Biological processi

  1. 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; 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-SubCell
  3. extracellular region Source: UniProtKB-KW
  4. plasma membrane Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cell wall, Membrane, Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1818 Reviewed prediction
Add
BLAST
Chaini19 – 430412Probable glucan endo-1,3-beta-glucosidase eglC
PRO_5000219799Add
BLAST
Propeptidei431 – 46030Removed in mature form Reviewed prediction
PRO_0000395144Add
BLAST

Amino acid modifications

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

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.

Keywords - PTMi

Glycoprotein, GPI-anchor, Lipoprotein

Family & Domainsi

Compositional bias

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

Sequence similaritiesi

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

MQLAQLAAFA MTLATSEAAY QGFNYGNKFS DESSKFQADF EAEFKAAKNL    50
VGTSGFTSAR LYTMIQAYST SDVIEAIPAA IAQDTSLLLG LWASGGGMDN 100
EITALKTAIS QYGEELGKLV VGISVGSEDL YRNSVEGAEA DAGVGVNPDE 150
LVEYIKEVRS VIAGTALADV SIGHVDTWDS WTNSSNSAVV EAVDWLGFDG 200
YPFFQSSMAN SIDNAKTLFE ESVAKTKAVA GDKEVWITET GWPVSGDSQG 250
DAVASIANAK TFWDEVGCPL FGNVNTWWYI LQDASPTTPN PSFGIVGSTL 300
STTPLFDLSC KNSTTSSSSA VVSAAASSAA GSKAVGSSQA SSGAAAWATS 350
ASGSAKPTFT VGRPGVNGTV FGNGTYPLRP SGSASARPSA GAISSGSGSS 400
SSGSGSSGST GTSATSGQSS SSGSSAAAGS SSPAAFSGAS TLSGSLFGAV 450
VAVFMTLAAL 460
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: February 19, 2014
This is version 40 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

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

Similar proteinsi