Q8NJQ5 · CHI37_TRIHA
- ProteinEndochitinase 37
- Genechit37
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids337 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score4/5
Function
function
Secreted chitinase involved in the degradation of chitin, a component of the cell walls of fungi and exoskeletal elements of some animals (including worms and arthropods). Plays a morphogenetic role during apical growth, cell division and differentiation (cell wall morphogenesis). May be involved in the degradation and further assimilation of phytopathogenic fungi, namely mycoparasitism, the major mechanism accounting for the antagonistic activity against phytopathogenic fungi displayed by Trichoderma.
Catalytic activity
Biotechnology
The antagonistic activity of Trichoderma harzianum is used for the control of several soil borne plant pathogenic fungi.
Kinetics
KM | SUBSTRATE | pH | TEMPERATURE[C] | NOTES | EVIDENCE | |
---|---|---|---|---|---|---|
0.5 mg/ml | colloidal chitin | |||||
0.7 mM | p-nitrophenyl-N-N'-diacetylchitobiose |
Temperature Dependence
Optimum temperature is 45-50 degrees Celsius.
Features
Showing features for active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Active site | 160 | Proton donor | ||||
Sequence: E |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | extracellular region | |
Molecular Function | chitin binding | |
Molecular Function | chitinase activity | |
Biological Process | chitin catabolic process | |
Biological Process | polysaccharide catabolic process |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended nameEndochitinase 37
- EC number
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Fungi > Dikarya > Ascomycota > Pezizomycotina > Sordariomycetes > Hypocreomycetidae > Hypocreales > Hypocreaceae > Trichoderma
Accessions
- Primary accessionQ8NJQ5
Subcellular Location
Phenotypes & Variants
PTM/Processing
Features
Showing features for signal, chain, glycosylation.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-25 | |||||
Sequence: MTRLLDASFLLLPVIASTLFGTASA | ||||||
Chain | PRO_0000429894 | 26-337 | Endochitinase 37 | |||
Sequence: QSTCATKGKPAGKVLQGYWENWDGSANGVHPGFGWTPIENPVIAQNGYNVINAAFPVILSDGTALWEDGMDATVKVATPAEMCQAKAAGATILMSIGGATAGIDLSSSTVADKFISTIVPILKQYNFDGIDIDIETGLVGSGSIGTLSTSQANLIRIIDGVLAQMPANFGLTMAPETAYVTGGSVVYGSIWGSYLPIIKKYVDNGRLWWLNMQYYNGDMYGCSGDSYAAGTVQGFTAQTDCLNNGITIQGTTIKVPYNMQVPGLPAQSGAGGGYMTPALVGQAWDHYNGALKGLMTWSINWDGSKNWTFGDN | ||||||
Glycosylation | 331 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N |
Keywords
- PTM
PTM databases
Expression
Induction
Specifically induced by chitin.
Interaction
Subunit
Monomer.
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 38-337 | GH18 | ||||
Sequence: KVLQGYWENWDGSANGVHPGFGWTPIENPVIAQNGYNVINAAFPVILSDGTALWEDGMDATVKVATPAEMCQAKAAGATILMSIGGATAGIDLSSSTVADKFISTIVPILKQYNFDGIDIDIETGLVGSGSIGTLSTSQANLIRIIDGVLAQMPANFGLTMAPETAYVTGGSVVYGSIWGSYLPIIKKYVDNGRLWWLNMQYYNGDMYGCSGDSYAAGTVQGFTAQTDCLNNGITIQGTTIKVPYNMQVPGLPAQSGAGGGYMTPALVGQAWDHYNGALKGLMTWSINWDGSKNWTFGDN |
Sequence similarities
Belongs to the glycosyl hydrolase 18 family. Chitinase class V subfamily.
Keywords
- Domain
Family and domain databases
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length337
- Mass (Da)35,478
- Last updated2002-10-01 v1
- Checksum0C9B50F416897EF1