Protein
- UniProt accession
- E1A185 [UniProt]
- Protein name
- Lysozyme
- PhaLP type
-
endolysin
evidence: ML prediction
probability: 99 % (predicted by ML model)
- Protein sequence
-
MTLEDMLIYDEGRVLKVYWDHLGYPTVGIGHLIIPQKTTDMALINHTLSKQVGRQVNGVISESECSALFSSDVQTVKSEIKKYPNIKLAYDACDPIRKNAICNLMFQMGGPRLSGFKKSLAFIANKDWSKAYSELLNSSWAKQTPNRAMRVAKVVLTGTMDSYK
- Physico‐chemical
properties -
protein length: 164 AA molecular weight: 18395,00000 Da isoelectric point: 9,21932 aromaticity: 0,08537 hydropathy: -0,21341
Domains
Taxonomy
Name | Taxonomy ID | Lineage | |
---|---|---|---|
Phage |
Aeromonas phage phiAS4 [NCBI] |
879628 | Straboviridae > Tulanevirus > Tulanevirus as4 |
Host |
Aeromonas salmonicida [NCBI] |
645 | Bacteria > Proteobacteria > Gammaproteobacteria > Aeromonadales > Aeromonadaceae > Aeromonas |
Coding sequence (CDS)
Coding sequence (CDS)
Genbank protein accession
ADM79609.1
[NCBI]
Genbank nucleotide accession
HM452125
[NCBI]
CDS location
range 21387 -> 21881
strand -
strand -
CDS
ATGACGTTAGAAGACATGCTCATCTACGATGAGGGAAGAGTTTTGAAAGTGTATTGGGACCATCTAGGGTACCCTACTGTTGGGATAGGTCACCTGATTATACCCCAGAAGACAACCGATATGGCCTTAATAAACCATACATTGAGTAAACAGGTTGGTCGCCAGGTGAACGGGGTTATCTCTGAGAGTGAATGCAGTGCACTGTTTAGCTCTGATGTTCAAACAGTCAAAAGTGAAATCAAGAAATATCCTAATATCAAATTAGCATATGATGCTTGTGACCCTATTAGAAAAAATGCTATTTGTAACTTAATGTTCCAAATGGGAGGTCCTCGTCTATCTGGATTCAAAAAATCACTCGCATTCATAGCCAATAAGGACTGGTCTAAAGCATACTCTGAATTGCTTAATTCATCTTGGGCAAAGCAAACCCCCAACAGGGCAATGCGAGTTGCAAAAGTTGTACTAACTGGCACAATGGATTCTTATAAATGA
Gene Ontology
Description | Category | Evidence (source) | |
---|---|---|---|
GO:0003796 | lysozyme activity | Molecular function | Inferred from Electronic Annotation (UniProt) |
GO:0009253 | peptidoglycan catabolic process | Biological process | Inferred from Electronic Annotation (InterPro) |
GO:0016998 | cell wall macromolecule catabolic process | Biological process | Inferred from Electronic Annotation (InterPro) |
GO:0031640 | killing of cells of another organism | Biological process | Inferred from Electronic Annotation (UniProt) |
GO:0042742 | defense response to bacterium | Biological process | Inferred from Electronic Annotation (UniProt) |
Enzymatic activity
EC Number | Entry Name | Reaction Catalyzed | Classification | Evidence | Source |
---|---|---|---|---|---|
3.2.1.17 |
lysozyme
aka muramidase |
D-glucosamine residues in chitodextrins |
Hydrolases
Glycosylases
Glycosidases, i.e. enzymes hydrolyzing O- and S-glycosyl compounds
|
match to sequence model evidence used in automatic assertion
ECO:0000256 |
RuleBase:RU003788 |
Tertiary structure
No tertiary structures available.