ProRule PRU01257
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PURL: https://purl.expasy.org/prosite/rule/PRU01257
General rule information
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| Accession | PRU01257 |
| Dates | 03-OCT-2019 (Created)
22-NOV-2019 (Last updated, Version ) |
| 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; |
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