A0A024SH20 · GUN2_HYPJR
- ProteinEndoglucanase EG-II
- Geneegl2
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids418 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score4/5
Function
function
Endoglucanase (EG) that cleaves the internal beta-1,4-glucosidic bonds in cellulose. The degradation of cellulose involves an interplay between different cellulolytic enzymes. Hydrolysis starts with EGs, which cut internal glycosidic linkages to reduce the polymerization degree of the substrate and creates new chain ends for exocellobiohydrolases (CBHs). The CBH release the disaccharide cellobiose from the non-reducing end of the cellulose polymer chain. Finally, beta-1,4-glucosidases hydrolyze the cellobiose and other short cello-oligosaccharides into glucose units.
Catalytic activity
Features
Showing features for active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Active site | 239 | Proton donor/acceptor | ||||
Sequence: E | ||||||
Active site | 350 | Nucleophile | ||||
Sequence: E |
GO annotations
all annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
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Aspect | Term | |
---|---|---|
Cellular Component | extracellular region | |
Molecular Function | cellulase activity | |
Molecular Function | cellulose binding | |
Biological Process | cellulose catabolic process |
Keywords
- Molecular function
- Biological process
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameEndoglucanase EG-II
- EC number
- Short namesEGII
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Fungi > Dikarya > Ascomycota > Pezizomycotina > Sordariomycetes > Hypocreomycetidae > Hypocreales > Hypocreaceae > Trichoderma
Accessions
- Primary accessionA0A024SH20
Proteomes
Subcellular Location
PTM/Processing
Features
Showing features for signal, modified residue, chain, disulfide bond, glycosylation.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-21 | |||||
Sequence: MNKSVAPLLLAASILYGGAAA | ||||||
Modified residue | 22 | Pyrrolidone carboxylic acid | ||||
Sequence: Q | ||||||
Chain | PRO_5001537231 | 22-418 | Endoglucanase EG-II | |||
Sequence: QQTVWGQCGGIGWSGPTNCAPGSACSTLNPYYAQCIPGATTITTSTRPPSGPTTTTRATSTSSSTPPTSSGVRFAGVNIAGFDFGCTTDGTCVTSKVYPPLKNFTGSNNYPDGIGQMQHFVNDDGMTIFRLPVGWQYLVNNNLGGNLDSTSISKYDQLVQGCLSLGAYCIVDIHNYARWNGGIIGQGGPTNAQFTSLWSQLASKYASQSRVWFGIMNEPHDVNINTWAATVQEVVTAIRNAGATSQFISLPGNDWQSAGAFISDGSAAALSQVTNPDGSTTNLIFDVHKYLDSDNSGTHAECTTNNIDGAFSPLATWLRQNNRQAILTETGGGNVQSCIQDMCQQIQYLNQNSDVYLGYVGWGAGSFDSTYVLTETPTGSGNSWTDTSLVSSCLARK | ||||||
Disulfide bond | 107↔113 | |||||
Sequence: CTTDGTC | ||||||
Glycosylation | 124 | N-linked (GlcNAc) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 183↔190 | |||||
Sequence: CLSLGAYC | ||||||
Disulfide bond | 323↔359 | |||||
Sequence: CTTNNIDGAFSPLATWLRQNNRQAILTETGGGNVQSC | ||||||
Disulfide bond | 364↔414 | |||||
Sequence: CQQIQYLNQNSDVYLGYVGWGAGSFDSTYVLTETPTGSGNSWTDTSLVSSC |
Keywords
- PTM
PTM databases
Structure
Family & Domains
Features
Showing features for domain, region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 22-57 | CBM1 | ||||
Sequence: QQTVWGQCGGIGWSGPTNCAPGSACSTLNPYYAQCI | ||||||
Region | 58-91 | Linker | ||||
Sequence: PGATTITTSTRPPSGPTTTTRATSTSSSTPPTSS | ||||||
Region | 63-91 | Disordered | ||||
Sequence: ITTSTRPPSGPTTTTRATSTSSSTPPTSS | ||||||
Region | 92-418 | Catalytic | ||||
Sequence: GVRFAGVNIAGFDFGCTTDGTCVTSKVYPPLKNFTGSNNYPDGIGQMQHFVNDDGMTIFRLPVGWQYLVNNNLGGNLDSTSISKYDQLVQGCLSLGAYCIVDIHNYARWNGGIIGQGGPTNAQFTSLWSQLASKYASQSRVWFGIMNEPHDVNINTWAATVQEVVTAIRNAGATSQFISLPGNDWQSAGAFISDGSAAALSQVTNPDGSTTNLIFDVHKYLDSDNSGTHAECTTNNIDGAFSPLATWLRQNNRQAILTETGGGNVQSCIQDMCQQIQYLNQNSDVYLGYVGWGAGSFDSTYVLTETPTGSGNSWTDTSLVSSCLARK |
Domain
The enzyme consists of two functional domains, a catalytic core joined to a carbohydrate-binding domain (CBM) by a serine-, threonine-, and proline-rich, highly glycosylated linker sequence.
Sequence similarities
Belongs to the glycosyl hydrolase 5 (cellulase A) family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length418
- Mass (Da)44,155
- Last updated2014-07-09 v1
- ChecksumD0F9B9284E062FED
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
KI911141 EMBL· GenBank· DDBJ | ETS04885.1 EMBL· GenBank· DDBJ | Genomic DNA |