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Q0CEU4

- EGLD_ASPTN

UniProt

Q0CEU4 - EGLD_ASPTN

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Protein
Probable endo-beta-1,4-glucanase D
Gene
eglD, ATEG_07790
Organism
Aspergillus terreus (strain NIH 2624 / FGSC A1156)
Status
Reviewed - 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.

Catalytic activityi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei164 – 1641Proton donor By similarity
Active sitei210 – 2101Nucleophile By similarity

GO - Molecular functioni

  1. cellulase activity Source: UniProtKB-EC
  2. cellulose binding Source: InterPro

GO - Biological processi

  1. cellulose catabolic process Source: UniProtKB-KW
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:ATEG_07790
OrganismiAspergillus terreus (strain NIH 2624 / FGSC A1156)
Taxonomic identifieri341663 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus
ProteomesiUP000007963: Unassembled WGS sequence

Subcellular locationi

Secreted By similarity

GO - Cellular componenti

  1. extracellular region Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1919 Reviewed prediction
Add
BLAST
Chaini20 – 360341Probable endo-beta-1,4-glucanase D
PRO_0000394066Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi330 ↔ 347 By similarity
Glycosylationi334 – 3341N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi341 ↔ 357 By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein

Structurei

3D structure databases

ProteinModelPortaliQ0CEU4.
SMRiQ0CEU4. Positions 324-358.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini322 – 35837CBM1
Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni20 – 234215Catalytic
Add
BLAST
Regioni235 – 30369Ser/Thr-rich linker
Add
BLAST

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

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiNOG120437.
HOGENOMiHOG000158937.
OMAiGYIDSPP.
OrthoDBiEOG7KM64H.

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.

Q0CEU4-1 [UniParc]FASTAAdd to Basket

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MKTSFGLLAL AAAAKLVNAH ATVFAVWIND EDQGLGNTAD GYIRSPPNNS    50
PVTDVTSKDM TCNVNGATAA AKTLDVKAGD KITFEWHHNS RDASDDIIAS 100
SHLGPVMVYM APTEKGSAGS GWVKIAEDGY SNGKWAVDTL IANRGKHSIT 150
VPDVPAGEYL FRPEIIALHE GNREGGAQLY MECVQVKVTS DGSKTLPEGV 200
SIPGTYTATD PGILFDIYNS FDSYPIPGPA VWDGSSSGSS SGSSKTTAAA 250
PAATSAASAS STKAPATTAA PVQTESAKPA TSTTQAAAPT TLVTSAKPTA 300
TATAGAGDSG SGSCSATAPA TGVVKMYAQC GGMNYSGSTT CESGLTCKQW 350
NPYYHQCVKA 360
Length:360
Mass (Da):36,795
Last modified:October 17, 2006 - v1
Checksum:i0BABA36D957D8F7D
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CH476604 Genomic DNA. Translation: EAU32052.1.
RefSeqiXP_001216411.1. XM_001216411.1.

Genome annotation databases

EnsemblFungiiCADATEAT00003463; CADATEAP00003463; CADATEAG00003463.
GeneIDi4322940.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CH476604 Genomic DNA. Translation: EAU32052.1 .
RefSeqi XP_001216411.1. XM_001216411.1.

3D structure databases

ProteinModelPortali Q0CEU4.
SMRi Q0CEU4. Positions 324-358.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblFungii CADATEAT00003463 ; CADATEAP00003463 ; CADATEAG00003463 .
GeneIDi 4322940.

Phylogenomic databases

eggNOGi NOG120437.
HOGENOMi HOG000158937.
OMAi GYIDSPP.
OrthoDBi EOG7KM64H.

Family and domain databases

InterProi IPR000254. Cellulose-bd_dom_fun.
IPR005103. Glyco_hydro_61.
[Graphical view ]
Pfami PF00734. CBM_1. 1 hit.
PF03443. Glyco_hydro_61. 1 hit.
[Graphical view ]
ProDomi PD001821. CBD_fun. 1 hit.
[Graphical view ] [Entries sharing at least one domain ]
SMARTi SM00236. fCBD. 1 hit.
[Graphical view ]
SUPFAMi SSF57180. SSF57180. 1 hit.
PROSITEi PS00562. CBM1_1. 1 hit.
PS51164. CBM1_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: NIH 2624 / FGSC A1156.

Entry informationi

Entry nameiEGLD_ASPTN
AccessioniPrimary (citable) accession number: Q0CEU4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 18, 2010
Last sequence update: October 17, 2006
Last modified: November 13, 2013
This is version 24 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

Documents

  1. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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