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Protein

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

Gene

eglC

Organism
Aspergillus terreus (strain NIH 2624 / FGSC A1156)
Status
Reviewed-Annotation score: 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)DescriptionActionsGraphical viewLength
Active sitei128NucleophileBy similarity1
Active sitei239Proton donorBy similarity1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Carbohydrate metabolism, Cell wall biogenesis/degradation, Polysaccharide degradation

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:ATEG_10288
OrganismiAspergillus terreus (strain NIH 2624 / FGSC A1156)
Taxonomic identifieri341663 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus
Proteomesi
  • UP000007963 Componenti: Unassembled WGS sequence

Organism-specific databases

EuPathDBiFungiDB:ATEG_10288.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cell wall, Membrane, Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 18Sequence analysisAdd BLAST18
ChainiPRO_000039514719 – 463Probable glucan endo-1,3-beta-glucosidase eglCAdd BLAST445
PropeptideiPRO_0000395148464 – 486Removed in mature formSequence analysisAdd BLAST23

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi84N-linked (GlcNAc...)Sequence analysis1
Glycosylationi183N-linked (GlcNAc...)Sequence analysis1
Glycosylationi315N-linked (GlcNAc...)Sequence analysis1
Glycosylationi386N-linked (GlcNAc...)Sequence analysis1
Glycosylationi396N-linked (GlcNAc...)Sequence analysis1
Glycosylationi404N-linked (GlcNAc...)Sequence analysis1
Lipidationi463GPI-anchor amidated glycineSequence analysis1

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

Structurei

3D structure databases

ProteinModelPortaliQ0C7P6.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi310 – 457Ser-richAdd BLAST148
Compositional biasi333 – 402Gly-richAdd BLAST70

Sequence similaritiesi

Belongs to the glycosyl hydrolase 17 family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

OMAiTNTWWYI.
OrthoDBiEOG092C3HT4.

Family and domain databases

Gene3Di3.20.20.80. 1 hit.
InterProiIPR000490. Glyco_hydro_17.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PfamiPF00332. Glyco_hydro_17. 1 hit.
[Graphical view]
SUPFAMiSSF51445. SSF51445. 1 hit.

Sequencei

Sequence statusi: Complete.

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

Q0C7P6-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MQLTQLLALA LSLATSEAAY KGFNYGDKKP DGSSKYQADF ASEFETAQNL
60 70 80 90 100
VGAPGFTSAR LYTMIQAGTA NDPISAIPAA IAQNTSLLLG LWASGNNMNN
110 120 130 140 150
ELTALKAAIS QYGEDLSKLV VGISVGSEDL YRNSVLGQKV NAGVGVDPHV
160 170 180 190 200
LASYIEEVRS TISGTPLSGA PLGHVDTWND WVNGSNAAVI DAVDWVGFDG
210 220 230 240 250
YPYFQNTMAN SIDDAKALFN EAVAKTKSAA GNKEVWITET GWPVSGKTEN
260 270 280 290 300
LAVASIPNAK RFWDEVGCPL FDNTNTWWYT LQDAFGASVP NPSFGIVGST
310 320 330 340 350
LTTQPLFDLS CSKSNTTSSS AIASPTSTAA AAGGVAGGST GSASGSSTGT
360 370 380 390 400
GSSSGSGSNS NTGAASGAVG AADRETSGTS GSANTNGTSG SGSGSNSTSG
410 420 430 440 450
HGSNVTVPTR PTSVSNVSPS KSSSALFTGA ATSMGASPSS VGNVGPSKSS
460 470 480
GAASPSSTTM FTGAATSVSA PVVHVVLLAL MMVIAA
Length:486
Mass (Da):48,753
Last modified:October 17, 2006 - v1
Checksum:iF168A8CD88AF0DD4
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CH476610 Genomic DNA. Translation: EAU29285.1.
RefSeqiXP_001218636.1. XM_001218635.1.

Genome annotation databases

EnsemblFungiiCADATEAT00003164; CADATEAP00003164; CADATEAG00003164.
GeneIDi4354731.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CH476610 Genomic DNA. Translation: EAU29285.1.
RefSeqiXP_001218636.1. XM_001218635.1.

3D structure databases

ProteinModelPortaliQ0C7P6.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiCADATEAT00003164; CADATEAP00003164; CADATEAG00003164.
GeneIDi4354731.

Organism-specific databases

EuPathDBiFungiDB:ATEG_10288.

Phylogenomic databases

OMAiTNTWWYI.
OrthoDBiEOG092C3HT4.

Family and domain databases

Gene3Di3.20.20.80. 1 hit.
InterProiIPR000490. Glyco_hydro_17.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PfamiPF00332. Glyco_hydro_17. 1 hit.
[Graphical view]
SUPFAMiSSF51445. SSF51445. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiEGLC_ASPTN
AccessioniPrimary (citable) accession number: Q0C7P6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 15, 2010
Last sequence update: October 17, 2006
Last modified: September 7, 2016
This is version 45 of the entry and version 1 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.