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Protein

Probable endo-beta-1,4-glucanase D

Gene

eglD

Organism
Aspergillus kawachii (strain NBRC 4308) (White koji mold) (Aspergillus awamori var. kawachi)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-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 sitei167Proton donorBy similarity1
Active sitei213NucleophileSequence analysis1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Keywords - Biological processi

Carbohydrate metabolism, Cellulose degradation, Polysaccharide degradation

Protein family/group databases

CAZyiAA9. Auxiliary Activities 9.
CBM1. Carbohydrate-Binding Module Family 1.

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 61A
Cellulase D
Gene namesi
Name:eglD
Synonyms:cel61A
ORF Names:AKAW_08531
OrganismiAspergillus kawachii (strain NBRC 4308) (White koji mold) (Aspergillus awamori var. kawachi)
Taxonomic identifieri1033177 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus
Proteomesi
  • UP000006812 Componenti: Unassembled WGS sequence

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 20Sequence analysisAdd BLAST20
ChainiPRO_000039406421 – 408Probable endo-beta-1,4-glucanase DAdd BLAST388

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi151N-linked (GlcNAc...)Sequence analysis1
Glycosylationi331N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi377 ↔ 394By similarity
Glycosylationi381N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi388 ↔ 404By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein

Structurei

3D structure databases

ProteinModelPortaliQ96WQ9.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini369 – 405CBM1PROSITE-ProRule annotationAdd BLAST37

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni21 – 237CatalyticAdd BLAST217
Regioni238 – 254Ser/Thr-rich linkerAdd BLAST17

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
Contains 1 CBM1 (fungal-type carbohydrate-binding) domain.PROSITE-ProRule annotation

Keywords - Domaini

Signal

Phylogenomic databases

InParanoidiQ96WQ9.
OrthoDBiEOG092C48ID.

Family and domain databases

InterProiIPR000254. Cellulose-bd_dom_fun.
IPR005103. Glyco_hydro_61.
[Graphical view]
PfamiPF00734. CBM_1. 1 hit.
PF03443. Glyco_hydro_61. 1 hit.
[Graphical view]
ProDomiPD001821. CBD_fun. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTiSM00236. fCBD. 1 hit.
[Graphical view]
SUPFAMiSSF57180. SSF57180. 1 hit.
PROSITEiPS00562. CBM1_1. 1 hit.
PS51164. CBM1_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q96WQ9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKTTTYSLLA LAAASKLASA HTTVQAVWIN GEDQGLGNTD DGYIRSPPSN
60 70 80 90 100
SPVTDVTSTD MTCNVNGDQA ASKTLSVKAG DVVTFEWHHS DRSDSDDIIA
110 120 130 140 150
SSHKGPVQVY MAPTAKGSNG NNWVKIAEDG YHKSSDEWAT DILIANKGKH
160 170 180 190 200
NITVPDVPAG NYLFRPEIIA LHEGNREGGA QFYMECVQFK VTSDGSNELP
210 220 230 240 250
SGVSIPGVYT ATDPGILFDI YNSFDSYPIP GPDVWDGSSS GSSSSGSSSA
260 270 280 290 300
AVSSAAAAAT TSAVAATTPA TQAAVEVSSS AAAATTEAAA PVVSSAAPVQ
310 320 330 340 350
QATSAVTSQA QAAPTTFATS SKKSSKTACK NKTKSNSQVA AATSSVVAPA
360 370 380 390 400
ATSSVVPVVS ASASASAGGV AKQYERCGGI NHTGPTTCES GSVCKKWNPY

YYQCVASQ
Length:408
Mass (Da):41,650
Last modified:December 1, 2001 - v1
Checksum:iB7CA86C9019F0089
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB055432 Genomic DNA. Translation: BAB62318.1.
DF126473 Genomic DNA. Translation: GAA90417.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB055432 Genomic DNA. Translation: BAB62318.1.
DF126473 Genomic DNA. Translation: GAA90417.1.

3D structure databases

ProteinModelPortaliQ96WQ9.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

CAZyiAA9. Auxiliary Activities 9.
CBM1. Carbohydrate-Binding Module Family 1.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

InParanoidiQ96WQ9.
OrthoDBiEOG092C48ID.

Family and domain databases

InterProiIPR000254. Cellulose-bd_dom_fun.
IPR005103. Glyco_hydro_61.
[Graphical view]
PfamiPF00734. CBM_1. 1 hit.
PF03443. Glyco_hydro_61. 1 hit.
[Graphical view]
ProDomiPD001821. CBD_fun. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTiSM00236. fCBD. 1 hit.
[Graphical view]
SUPFAMiSSF57180. SSF57180. 1 hit.
PROSITEiPS00562. CBM1_1. 1 hit.
PS51164. CBM1_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiEGLD_ASPKW
AccessioniPrimary (citable) accession number: Q96WQ9
Secondary accession number(s): G7XU08
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 18, 2010
Last sequence update: December 1, 2001
Last modified: September 7, 2016
This is version 50 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.