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A1C4H2

- EGLD_ASPCL

UniProt

A1C4H2 - EGLD_ASPCL

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Protein
Probable endo-beta-1,4-glucanase D
Gene
eglD, ACLA_059790
Organism
Aspergillus clavatus (strain ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1)
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
Complete GO annotation...

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:ACLA_059790
OrganismiAspergillus clavatus (strain ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1)
Taxonomic identifieri344612 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus
ProteomesiUP000006701: 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 – 353334Probable endo-beta-1,4-glucanase D
PRO_0000394060Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi323 ↔ 340 By similarity
Glycosylationi327 – 3271N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi334 ↔ 350 By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein

Structurei

3D structure databases

ProteinModelPortaliA1C4H2.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini315 – 35137CBM1
Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni20 – 234215Catalytic
Add
BLAST
Regioni235 – 31177Ser/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.

A1C4H2-1 [UniParc]FASTAAdd to Basket

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MKSTFGLLAL AAAAKMAHAH ATVQAIWING VDQGAGNSAS GYIRSPPNNS    50
PLVDVTSADM TCNVNGKNPV AKTLPVKAGD KITFEWHHTD RSPSDDIIAS 100
SHRGPIMVYM APTAKGAAGN GWVKIAEEGY SNGKWAVDNL IANRGKHSIV 150
VPDVPAGDYL FRPEIIALHE GNRLGGAQFY MECVQVKVTS NGANALPAGV 200
SIPGAYKATD PGVHFDIYNS FSSYPMPGPA VWNGASAAGS APAPTAAPTQ 250
KPVVTAAPTT LATLVKPTTT TAAAPAETDS CDGDDDDYET ETPAPQASAT 300
QAPAPQRPAP QTPSGSVKEW YQCGGINYTG AKNCESGLVC KEWNPYYHQC 350
IKA 353
Length:353
Mass (Da):36,822
Last modified:January 23, 2007 - v1
Checksum:iCA30252C3CAB5C4C
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
DS026990 Genomic DNA. Translation: EAW15312.1.
RefSeqiXP_001276738.1. XM_001276737.1.

Genome annotation databases

EnsemblFungiiCADACLAT00005694; CADACLAP00005569; CADACLAG00005694.
GeneIDi4708945.
KEGGiact:ACLA_059790.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
DS026990 Genomic DNA. Translation: EAW15312.1 .
RefSeqi XP_001276738.1. XM_001276737.1.

3D structure databases

ProteinModelPortali A1C4H2.
ModBasei Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblFungii CADACLAT00005694 ; CADACLAP00005569 ; CADACLAG00005694 .
GeneIDi 4708945.
KEGGi act:ACLA_059790.

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: ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1.

Entry informationi

Entry nameiEGLD_ASPCL
AccessioniPrimary (citable) accession number: A1C4H2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 18, 2010
Last sequence update: January 23, 2007
Last modified: November 13, 2013
This is version 25 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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