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Protein

Probable endo-beta-1,4-glucanase D

Gene

eglD

Organism
Neosartorya fischeri (strain ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164 / JCM 1740 / NRRL 181 / WB 181) (Aspergillus fischerianus)
Status
Reviewed-Annotation score: Annotation score: 3 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 sitei164Proton donorBy similarity1
Active sitei210NucleophileBy similarity1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Keywords - Biological processi

Carbohydrate 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:NFIA_099510
OrganismiNeosartorya fischeri (strain ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164 / JCM 1740 / NRRL 181 / WB 181) (Aspergillus fischerianus)
Taxonomic identifieri331117 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus
Proteomesi
  • UP000006702 Componenti: Unassembled WGS sequence

Organism-specific databases

EuPathDBiFungiDB:NFIA_099510.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 19Sequence analysisAdd BLAST19
ChainiPRO_000039406820 – 348Probable endo-beta-1,4-glucanase DAdd BLAST329

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi318 ↔ 335By similarity
Glycosylationi322N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi329 ↔ 345By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein

Structurei

3D structure databases

ProteinModelPortaliA1DBS6.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini310 – 346CBM1PROSITE-ProRule annotationAdd BLAST37

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni20 – 234CatalyticAdd BLAST215
Regioni235 – 311Ser/Thr-rich linkerAdd BLAST77

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

HOGENOMiHOG000158937.
KOiK19356.
OMAiMTCNVNG.
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.

A1DBS6-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKSTFGLLAL AAAAKLVSAH ATVHAVWIND VDQGAGNSAD GYIRTPPNNS
60 70 80 90 100
PITDVTSADM TCNVNGKNSV AKTLSVKAGD KVTFEWHHDS RSASDDIIAS
110 120 130 140 150
SHMGPVMVYM APTEKGTAGN GWVKIAEEGY SNGKWAVANL IANKGKHSIT
160 170 180 190 200
VPDVPAGEYL LRPEIIALHE GNRQGGAQFY MECVQVKVTS AGTKTLPAGV
210 220 230 240 250
SIPGAYKATD PGVLFDMYNS FTSYPIPGPA VWDGSSSGSS GSSDSSPATT
260 270 280 290 300
APEASVTSAP TKQGSADTSA SPTTFVTATK PTTTAAPAAP PASTGSNSGS
310 320 330 340
GSSGSGSASG SVKIYQQCGG KNYSGATSCE AGLTCKEWNP YYHQCLKA
Length:348
Mass (Da):35,569
Last modified:January 23, 2007 - v1
Checksum:i3126BF3D4DC88161
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
DS027694 Genomic DNA. Translation: EAW20316.1.
RefSeqiXP_001262213.1. XM_001262212.1.

Genome annotation databases

EnsemblFungiiCADNFIAT00009166; CADNFIAP00008952; CADNFIAG00009166.
GeneIDi4588579.
KEGGinfi:NFIA_099510.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
DS027694 Genomic DNA. Translation: EAW20316.1.
RefSeqiXP_001262213.1. XM_001262212.1.

3D structure databases

ProteinModelPortaliA1DBS6.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiCADNFIAT00009166; CADNFIAP00008952; CADNFIAG00009166.
GeneIDi4588579.
KEGGinfi:NFIA_099510.

Organism-specific databases

EuPathDBiFungiDB:NFIA_099510.

Phylogenomic databases

HOGENOMiHOG000158937.
KOiK19356.
OMAiMTCNVNG.
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_NEOFI
AccessioniPrimary (citable) accession number: A1DBS6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 18, 2010
Last sequence update: January 23, 2007
Last modified: October 5, 2016
This is version 44 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.