Domains within Aspergillus nidulans FGSC A4 protein EGLD_EMENI (Q5BCX8)

Endo-beta-1,4-glucanase D

Alternative representations: 1 /

Protein length357 aa
Source databaseUniProt
Identifiers C8VN99, Q1HFV0, EGLD_EMENI, Q5BCX8

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_EMENI 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_EMENI 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 227321.Q5BCX8 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: