Q0CEU4 (EGLD_ASPTN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Probable endo-beta-1,4-glucanase D
Short name=Endoglucanase D
EC=3.2.1.4

Alternative name(s):
Carboxymethylcellulase D
Cellulase D

Gene names

Name:	eglD
ORF Names:	ATEG_07790

Organism

Aspergillus terreus (strain NIH 2624 / FGSC A1156) [Complete proteome]

Taxonomic identifier

341663 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Fungi › Dikarya › Ascomycota › saccharomyceta › Pezizomycotina › leotiomyceta › Eurotiomycetes › Eurotiomycetidae › Eurotiales › Trichocomaceae › mitosporic Trichocomaceae › Aspergillus › Aspergillus terreus

Protein attributes

Sequence length	360 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Inferred from homology

General annotation (Comments)

Function	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 activity	Endohydrolysis of (1->4)-beta-D-glucosidic linkages in cellulose, lichenin and cereal beta-D-glucans.
Subcellular location	Secreted By similarity.
Domain	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 similarities	Belongs to the glycosyl hydrolase 61 family. Contains 1 CBM1 (fungal-type carbohydrate-binding) domain.

Ontologies

Keywords
Biological process	Carbohydrate metabolism Cellulose degradation Polysaccharide degradation
Cellular component	Secreted
Domain	Signal
Molecular function	Glycosidase Hydrolase
PTM	Disulfide bond Glycoprotein
Technical term	Complete proteome
Gene Ontology (GO)
Biological_process	cellulose catabolic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	cellulase activity Inferred from electronic annotation. Source: EC cellulose binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 19	19	Potential
	Chain	20 – 360	341	Probable endo-beta-1,4-glucanase D		PRO_0000394066
Regions
	Domain	322 – 358	37	CBM1
	Region	20 – 234	215	Catalytic
	Region	235 – 303	69	Ser/Thr-rich linker
Sites
	Active site	164	1	Proton donor By similarity
	Active site	210	1	Nucleophile By similarity
Amino acid modifications
	Glycosylation	334	1	N-linked (GlcNAc...) Potential
	Disulfide bond	330 ↔ 347		By similarity
	Disulfide bond	341 ↔ 357		By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q0CEU4 [UniParc]. Last modified October 17, 2006. Version 1. Checksum: 0BABA36D957D8F7D	FASTA	360	36,795
	10 20 30 40 50 60 MKTSFGLLAL AAAAKLVNAH ATVFAVWIND EDQGLGNTAD GYIRSPPNNS PVTDVTSKDM 70 80 90 100 110 120 TCNVNGATAA AKTLDVKAGD KITFEWHHNS RDASDDIIAS SHLGPVMVYM APTEKGSAGS 130 140 150 160 170 180 GWVKIAEDGY SNGKWAVDTL IANRGKHSIT VPDVPAGEYL FRPEIIALHE GNREGGAQLY 190 200 210 220 230 240 MECVQVKVTS DGSKTLPEGV SIPGTYTATD PGILFDIYNS FDSYPIPGPA VWDGSSSGSS 250 260 270 280 290 300 SGSSKTTAAA PAATSAASAS STKAPATTAA PVQTESAKPA TSTTQAAAPT TLVTSAKPTA 310 320 330 340 350 360 TATAGAGDSG SGSCSATAPA TGVVKMYAQC GGMNYSGSTT CESGLTCKQW NPYYHQCVKA

References

[1]

"Annotation of the Aspergillus terreus NIH2624 genome." Birren B.W., Lander E.S., Galagan J.E., Nusbaum C., Devon K., Henn M., Ma L.-J., Jaffe D.B., Butler J., Alvarez P., Gnerre S., Grabherr M., Kleber M., Mauceli E.W., Brockman W., Rounsley S., Young S.K., LaButti K. , Pushparaj V., DeCaprio D., Crawford M., Koehrsen M., Engels R., Montgomery P., Pearson M., Howarth C., Larson L., Luoma S., White J., Alvarado L., Kodira C.D., Zeng Q., Oleary S., Yandava C., Denning D.W., Nierman W.C., Milne T., Madden K. Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: NIH 2624 / FGSC A1156.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CH476604 Genomic DNA. Translation: EAU32052.1.
RefSeq	XP_001216411.1. XM_001216411.1.
3D structure databases
ProteinModelPortal	Q0CEU4.
SMR	Q0CEU4. Positions 324-358.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	CADATEAT00003463; CADATEAP00003463; CADATEAG00003463.
GeneID	4322940.
Phylogenomic databases
eggNOG	NOG120437.
HOGENOM	HOG000158937.
OrthoDB	EOG40W000.
Family and domain databases
InterPro	IPR000254. Cellulose-bd_dom_fun. IPR005103. Glyco_hydro_61. [Graphical view]
Pfam	PF00734. CBM_1. 1 hit. PF03443. Glyco_hydro_61. 1 hit. [Graphical view]
ProDom	PD001821. CBD_fun. 1 hit. [Graphical view] [Entries sharing at least one domain]
SMART	SM00236. fCBD. 1 hit. [Graphical view]
SUPFAM	SSF57180. CBD_fun. 1 hit.
PROSITE	PS00562. CBM1_1. 1 hit. PS51164. CBM1_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

EGLD_ASPTN

Accession

Primary (citable) accession number: Q0CEU4

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 18, 2010
Last sequence update:	October 17, 2006
Last modified:	May 16, 2012
This is version 22 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program