ProRule PRU01257
General rule information
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Accession | PRU01257 |
Dates | 3-OCT-2019 (Created)
22-NOV-2019 (Last updated, Version 2) |
Data class | Domain; |
Predictors |
PROSITE; PS51909; LYSOZYME_I |
Name | Invertebrate (I)-type lysozyme domain |
Function | I-type lysozymes have been identified in phylogenetically diverse organisms, including mollusca, nematoda, annelida, arthropoda and echinodermata. I-type lysozymes play an important role in immunity and digestion in invertebrates and are usually regarded as the first barrier against pathogens. I-type lysozymes exert multiple activities, such as muramidase, isopeptidase, chitinase, and non-enzymatic antibacterial activities. |
Scope(s) |
Eukaryota Metazoa |
Example(s) | Q8IU26 (LYS_RUDPH); |
Propagated annotation
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Identifier, protein and gene names
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case <FTGroup:1> | |
Protein name | + RecName: EC=3.2.1.17; |
Comments
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CATALYTIC ACTIVITY | Reaction=Hydrolysis of (1->4)-beta-linkages between N-acetylmuramic acid and N-acetyl-D-glucosamine residues in a peptidoglycan and between N-acetyl-D-glucosamine residues in chitodextrins.; EC=3.2.1.17; |
end case | |
SIMILARITY | Belongs to the glycosyl hydrolase 22 family. Type-I lysozyme subfamily. |
case <FTGroup:1> |
Keywords
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Antimicrobial | |
Bacteriolytic enzyme | |
Glycosidase | |
Hydrolase | |
Antibiotic | |
end case | |
case <FTTag:disulf> | |
Disulfide bond | |
end case |
Gene Ontology
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case <FTGroup:1> | |
GO:0003824; Molecular function:catalytic activity | |
GO:0019835; Biological process:cytolysis | |
GO:0042742; Biological process:defense response to bacterium | |
GO:0016798; Molecular function:hydrolase activity, acting on glycosyl bonds | |
GO:0008152; Biological process:metabolic process | |
GO:0016787; Molecular function:hydrolase activity |
Features
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From: PS51909 | ||||||||||||
Key | From | To | Description | Tag | Condition | FTGroup | ||||||
DOMAIN | from | to | /note="I-type lysozyme #" | |||||||||
ACT_SITE | 16 | 16 | /note="Proton donor" | E | 1 | |||||||
ACT_SITE | 26 | 26 | /note="Nucleophile" | D | 1 | |||||||
DISULFID | 8 | 91 | disulf | C-x*-C | ||||||||
DISULFID | 11 | 123 | disulf | C-x*-C | ||||||||
DISULFID | 13 | 19 | disulf | C-x*-C | ||||||||
DISULFID | 23 | 32 | disulf | C-x*-C | ||||||||
DISULFID | 45 | 73 | disulf | C-x*-C | ||||||||
DISULFID | 63 | 69 | disulf | C-x*-C | ||||||||
DISULFID | 87 | 105 | disulf | C-x*-C |
Additional information
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Size range | 110-130 amino acids |
Related rules |
None |
Fusion | None |
Repeats | 1 |
Topology | Undefined |
PROSITE is copyrighted by the SIB Swiss Institute of Bioinformatics and distributed under the Creative Commons Attribution-NonCommercial-NoDerivatives (CC BY-NC-ND 4.0) License, see prosite_license.html.
UniProtKB rule member sequences
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- UniProtKB/Swiss-Prot sets
Eukaryota [11] All [ 11 ]
- Retrieve set of proteins with 3D structure for this domain