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Protein

Probable endo-beta-1,4-glucanase D

Gene

eglD

Organism
Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) (Aspergillus fumigatus)
Status
Reviewed-Annotation score: -Protein inferred from homologyi

Functioni

Has endoglucanase activity on substrates containing beta-1,4 glycosidic bonds, like in carboxymethylcellulose (CMC), hydroxyethylcellulose (HEC) and beta-glucan. Involved in the degradation of complex natural cellulosic substrates (By similarity).By similarity

Catalytic activityi

Endohydrolysis of (1->4)-beta-D-glucosidic linkages in cellulose, lichenin and cereal beta-D-glucans.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei164Proton donorBy similarity1
Active sitei210NucleophileBy similarity1

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionGlycosidase, Hydrolase
Biological processCarbohydrate metabolism, Cellulose degradation, Polysaccharide degradation

Names & Taxonomyi

Protein namesi
Recommended name:
Probable endo-beta-1,4-glucanase D (EC:3.2.1.4)
Short name:
Endoglucanase D
Alternative name(s):
Carboxymethylcellulase D
Cellulase D
Gene namesi
Name:eglD
ORF Names:AFUA_8G06830
OrganismiNeosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) (Aspergillus fumigatus)
Taxonomic identifieri330879 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus
Proteomesi
  • UP000002530 Componentsi: Chromosome 8, Unassembled WGS sequence

Organism-specific databases

EuPathDBiFungiDB:Afu8g06830

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cell wall Cytoskeleton Vacuole Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 19Sequence analysisAdd BLAST19
ChainiPRO_000039406320 – 349Probable endo-beta-1,4-glucanase DAdd BLAST330

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi319 ↔ 336By similarity
Glycosylationi323N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi330 ↔ 346By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein

Interactioni

Protein-protein interaction databases

STRINGi5085.CADAFUBP00007883

Structurei

3D structure databases

ProteinModelPortaliQ4WBU0
SMRiQ4WBU0
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini311 – 347CBM1PROSITE-ProRule annotationAdd BLAST37

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni20 – 235CatalyticAdd BLAST216
Regioni236 – 307Ser/Thr-rich linkerAdd BLAST72

Domaini

Has a modular structure: an endo-beta-1,4-glucanase catalytic module at the N-terminus, a linker rich in serines and threonines, and a C-terminal carbohydrate-binding module (CBM). The genes for catalytic modules and CBMs seem to have evolved separately and have been linked by gene fusion.

Sequence similaritiesi

Belongs to the glycosyl hydrolase 61 family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

HOGENOMiHOG000158937
InParanoidiQ4WBU0
KOiK19356
OMAiLTFEWYH
OrthoDBiEOG092C48ID

Family and domain databases

InterProiView protein in InterPro
IPR035971 CBD_sf
IPR000254 Cellulose-bd_dom_fun
IPR005103 Glyco_hydro_61
PfamiView protein in Pfam
PF00734 CBM_1, 1 hit
PF03443 Glyco_hydro_61, 1 hit
ProDomiView protein in ProDom or Entries sharing at least one domain
PD001821 CBD_fun, 1 hit
SMARTiView protein in SMART
SM00236 fCBD, 1 hit
SUPFAMiSSF57180 SSF57180, 1 hit
PROSITEiView protein in PROSITE
PS00562 CBM1_1, 1 hit
PS51164 CBM1_2, 1 hit

Sequencei

Sequence statusi: Complete.

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

Q4WBU0-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKSTFGLLAL AAAAKLVSAH ATVHAVWIND VDQGAGNSAD GYIRSPPNNS
60 70 80 90 100
PITDVTSTDM TCNVNGKNPV AKTLSVKAGD KVTFEWHHDT RSDSDDIIAS
110 120 130 140 150
SHMGPVMVYM APTEKGTAGN GWVKIAEEGY SNGKWAVANL IANRGKHSIT
160 170 180 190 200
VPDVPAGEYL LRPEIIALHE GNRQGGAQFY MECVQVKVTS AGTKTLPAGV
210 220 230 240 250
SIPGAYKATD PGVLFDMYNS FTSYPIPGPA VWDGSSSGSS GSSGSSPATT
260 270 280 290 300
TAPAVSVTAA PTKEAPVDTS ATPTTFVTAT KPATTAAPAA PSASSGSNSG
310 320 330 340
SDSCNSGSAS GSVKIYGQCG GQNYSGPTSC EAGLICKEWN PYYHQCVSA
Length:349
Mass (Da):35,735
Last modified:July 5, 2005 - v1
Checksum:i19776990098D76C9
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AAHF01000013 Genomic DNA Translation: EAL85444.1
RefSeqiXP_747482.1, XM_742389.1

Genome annotation databases

EnsemblFungiiCADAFUAT00002969; CADAFUAP00002969; CADAFUAG00002969
GeneIDi3504710
KEGGiafm:AFUA_8G06830

Entry informationi

Entry nameiEGLD_ASPFU
AccessioniPrimary (citable) accession number: Q4WBU0
Entry historyiIntegrated into UniProtKB/Swiss-Prot: May 18, 2010
Last sequence update: July 5, 2005
Last modified: April 25, 2018
This is version 63 of the entry and version 1 of the sequence. See 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

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