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Protein

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

Gene

eglC

Organism
Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold)
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

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:AO090009000117
OrganismiAspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold)
Taxonomic identifieri510516 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus
Proteomesi
  • UP000006564 Componenti: Chromosome 1

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_000039514519 – 440Probable glucan endo-1,3-beta-glucosidase eglCAdd BLAST422
PropeptideiPRO_0000395146441 – 463Removed in mature formSequence analysisAdd BLAST23

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi84N-linked (GlcNAc...)Sequence analysis1
Glycosylationi183N-linked (GlcNAc...)Sequence analysis1
Glycosylationi312N-linked (GlcNAc...)Sequence analysis1
Lipidationi440GPI-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

ProteinModelPortaliQ2UUZ1.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi309 – 448Ser-richAdd BLAST140

Sequence similaritiesi

Belongs to the glycosyl hydrolase 17 family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

HOGENOMiHOG000179527.
KOiK01199.
OMAiTNTWWYI.
OrthoDBiEOG092C3HT4.

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.

Q2UUZ1-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MQLTHLLAFA LSLATSEAAY KGFNYGATKS DGSVKSQSDF ESEFSTAKNL
60 70 80 90 100
VGTSGFTSAR LYTMIQGGTT NSPISAIPAA IAENTSLLLG LWASGGGMDN
110 120 130 140 150
ELAALKSAIS QYGDSFAKLV VGISVGSEDL YRASSEGEKV NAGIGIGPDD
160 170 180 190 200
LVSFIKEVRS IISGTALSSV PIGHVDTWTA WTNGSNSAVI DAVDWLGFDG
210 220 230 240 250
YPYFQSSMSN SISDAKSLFD DSVAKTKAVA KGKEVWITET GWPVSGSTQN
260 270 280 290 300
LGVASLANAK TYWDEVGCPL FDETNTWWYI LQDANPTTPN PSFGVVGSTL
310 320 330 340 350
STTPLFDLSC SNSTRPSASA SSSAAGSATP VGSAVPSGSA AVNPSSSGIV
360 370 380 390 400
SSAVPSTTPG FTVGKGFRPS NSSAAAYYSS ASASGSAYPK FTKTASGSSA
410 420 430 440 450
TSTTAGSSSD SSSTNSGKSS SESSSTNSGA SASSSILATG GASSVSGSVF
460
GALVAVFAFV ATL
Length:463
Mass (Da):46,656
Last modified:January 24, 2006 - v1
Checksum:i0D6C9932A360FDA8
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AP007150 Genomic DNA. Translation: BAE54624.1.
RefSeqiXP_001816626.1. XM_001816574.2.

Genome annotation databases

EnsemblFungiiBAE54624; BAE54624; AO090009000117.
GeneIDi5988556.
KEGGiaor:AOR_1_198184.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AP007150 Genomic DNA. Translation: BAE54624.1.
RefSeqiXP_001816626.1. XM_001816574.2.

3D structure databases

ProteinModelPortaliQ2UUZ1.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

CAZyiGH17. Glycoside Hydrolase Family 17.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiBAE54624; BAE54624; AO090009000117.
GeneIDi5988556.
KEGGiaor:AOR_1_198184.

Phylogenomic databases

HOGENOMiHOG000179527.
KOiK01199.
OMAiTNTWWYI.
OrthoDBiEOG092C3HT4.

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.
ProtoNetiSearch...

Entry informationi

Entry nameiEGLC_ASPOR
AccessioniPrimary (citable) accession number: Q2UUZ1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 15, 2010
Last sequence update: January 24, 2006
Last modified: November 30, 2016
This is version 56 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.