Domains within Aspergillus fumigatus Af293 protein EGLD_ASPFU (Q4WBU0)

Probable endo-beta-1,4-glucanase D

Alternative representations: 1 /

Protein length349 aa
Source databaseUniProt
Identifiers EGLD_ASPFU, Q4WBU0

Domain architecture analysis

Display all proteins with similar:

Domain organisationProteins having all the domains as the query in the same order. Additional domains are allowed.
Domain compositionProteins with the same domain composition have at least one copy of each of the domains of the query.

This domain architecture was probably invented with the emergence of Fungi

Predicted functional partners

EGLD_ASPFU is shown as eglD in the network

Click and drag to pan the network, and zoom by using your mouse wheel. Click the protein nodes for additional options.

The network on the left comes from STRING, a database of known and predicted protein interactions. Displayed here is the evidence view, where different line colors represent the types of evidence for the association.

Open the STRING annotation page for eglD

Protein EGLD_ASPFU is possibly involved in these pathways, based on its similarity to the listed KEGG orthologous groups:

KEGG pathways

PathwayDescription
map04514Cell adhesion molecules

KEGG orthologous groups

KONameDescription
K25874KIRREL, NEPHKirrel/Neph family protein

Orthologous groups

Orthology information is taken from eggNOG, a database of orthologous groups of genes. Orthologous groups containing this protein are listed below. This protein is named 330879.Q4WBU0 in eggNOG.

OGTaxonomic classDescription
LKOG3510All organisms (root)Kirrel/Neph family protein,neural cell adhesion molecule,neurotrimin
FS36XDikarya (subkingdom)lytic cellulose monooxygenase (C1-hydroxylating) [EC:1.14.99.54]
KOG3510Eukaryota (superkingdom)Kirrel/Neph family protein,neural cell adhesion molecule,neurotrimin
BPEX8Fungi (kingdom)lytic cellulose monooxygenase (C1-hydroxylating) [EC:1.14.99.54]
9S843Ascomycota (phylum)lytic cellulose monooxygenase (C1-hydroxylating) [EC:1.14.99.54]
C4AWKPezizomycotina (subphylum)lytic cellulose monooxygenase (C1-hydroxylating) [EC:1.14.99.54]
CH1MJEurotiomycetes (class)lytic cellulose monooxygenase (C1-hydroxylating) [EC:1.14.99.54]
7AEMIEurotiomycetidae (subclass)lytic cellulose monooxygenase (C1-hydroxylating) [EC:1.14.99.54]
CJSD1Eurotiales (order)lytic cellulose monooxygenase (C1-hydroxylating) [EC:1.14.99.54]
7HF20Opisthokonta (clade)lytic cellulose monooxygenase (C1-hydroxylating) [EC:1.14.99.54]
CWFSSAspergillaceae (family)lytic cellulose monooxygenase (C1-hydroxylating) [EC:1.14.99.54]
AQJ2SAspergillus (genus)lytic cellulose monooxygenase (C1-hydroxylating) [EC:1.14.99.54]

The SMART diagram above represents a summary of the results shown below. Domains with scores less significant than established cutoffs are not shown in the diagram. Features are also not shown when two or more occupy the same piece of sequence; the priority for display is given by SMART > PFAM > PROSPERO repeats > Signal peptide > Transmembrane > Coiled coil > Low complexity. In either case, features not shown in the above diagram are listed in the right side table below, and the reason for their omission is shown in the 'Reason' column.

Confidently predicted domains, repeats, motifs and features:

Outlier homologues and homologues of known structure:

Features NOT shown in the diagram: