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A1DBS6

- EGLD_NEOFI

UniProt

A1DBS6 - EGLD_NEOFI

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Protein
Probable endo-beta-1,4-glucanase D
Gene
eglD, NFIA_099510
Organism
Neosartorya fischeri (strain ATCC 1020 / DSM 3700 / FGSC A1164 / NRRL 181) (Aspergillus fischerianus)
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:NFIA_099510
OrganismiNeosartorya fischeri (strain ATCC 1020 / DSM 3700 / FGSC A1164 / NRRL 181) (Aspergillus fischerianus)
Taxonomic identifieri331117 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeNeosartorya
ProteomesiUP000006702: 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 – 348329Probable endo-beta-1,4-glucanase D
PRO_0000394068Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi318 ↔ 335 By similarity
Glycosylationi322 – 3221N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi329 ↔ 345 By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein

Structurei

3D structure databases

ProteinModelPortaliA1DBS6.
SMRiA1DBS6. Positions 312-346.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini310 – 34637CBM1
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.

A1DBS6-1 [UniParc]FASTAAdd to Basket

« Hide

MKSTFGLLAL AAAAKLVSAH ATVHAVWIND VDQGAGNSAD GYIRTPPNNS    50
PITDVTSADM TCNVNGKNSV AKTLSVKAGD KVTFEWHHDS RSASDDIIAS 100
SHMGPVMVYM APTEKGTAGN GWVKIAEEGY SNGKWAVANL IANKGKHSIT 150
VPDVPAGEYL LRPEIIALHE GNRQGGAQFY MECVQVKVTS AGTKTLPAGV 200
SIPGAYKATD PGVLFDMYNS FTSYPIPGPA VWDGSSSGSS GSSDSSPATT 250
APEASVTSAP TKQGSADTSA SPTTFVTATK PTTTAAPAAP PASTGSNSGS 300
GSSGSGSASG SVKIYQQCGG KNYSGATSCE AGLTCKEWNP YYHQCLKA 348
Length:348
Mass (Da):35,569
Last modified:January 23, 2007 - v1
Checksum:i3126BF3D4DC88161
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
Links Updated
DS027694 Genomic DNA. Translation: EAW20316.1 .
RefSeqi XP_001262213.1. XM_001262212.1.

3D structure databases

ProteinModelPortali A1DBS6.
SMRi A1DBS6. Positions 312-346.
ModBasei Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblFungii CADNFIAT00009166 ; CADNFIAP00008952 ; CADNFIAG00009166 .
GeneIDi 4588579.
KEGGi nfi:NFIA_099510.

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 1020 / DSM 3700 / FGSC A1164 / NRRL 181.

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: November 13, 2013
This is version 29 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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