Protein

UniProt accession
E5G070 [UniProt]
Protein name
Lysozyme
PhaLP type
endolysin

evidence: ML prediction

probability: 99 % (predicted by ML model)

Protein sequence
MATIDLLRVDQQIFNNSYEHVADFKSPSTQRYYFDNKVISSFNKDIVVQPSRISVTCPYQYRYFLDNSINYVRAFDNSRYYYYFITDIIFTAQARTELLLELDVWQTYLWDYSVLDSIVERCHVRRWNDDGTPTKESLYADENIPTGEYIMENGNSDYNIESLSDTVVIASTVPLGILTDSSGGEGTNPPPGEGDCGDWTNGVMSRNGFRFMKGYEGFGAYLYKDSGGVPTIGYGVTKSEPSEFDDLVARQPVSEEYASQVSYKLKQTNYGKPIVNFCKEIGITKQNQFDALCDLAFNAGVGAVVGTPTYTSLPSALRKDPFNESYIRPIWENYIISDAVGNVLNGLKARRKAECDIYFKNIYEFRPIVTINQNGSYGNPITANNGNGWLPECSSKPEGLYVDNEVGKDWLVPVSGTISAMYPSYPSGSPHNGVDIACPVGTPVYASKDGLVRVRKELTTSYGKYLIIAHGDSDVVYAHNSQLLVNEGDNVKQGQMIARSGNSGNSSGPHLHWEIRNPNGEIIQHGVKTVNPMPGYKLNQKV
Physico‐chemical
properties
protein length:542 AA
molecular weight:60465,00000 Da
isoelectric point:5,09916
aromaticity:0,11624
hydropathy:-0,42934

Domains

Domains [InterPro]
IPR033907
208–359
IPR033907 IPR011055
IPR002196
213–354
IPR002196 IPR016047
IPR050570
342–534
IPR050570
IPR023347
204–366
IPR023347 IPR011055
IPR023346
204–370
IPR023346
Protein sequence: E5G070
1 542
Legend: Pfam SMART CDD TIGRFAM HAMAP SUPFAM PRINTS Gene3D PANTHER Other

Taxonomy

  Name Taxonomy ID Lineage
Phage Clostridium phage CpV1
[NCBI] 		926066 Guelinviridae > Capvunavirus > Capvunavirus CpV1
Host No host information

Coding sequence (CDS)

Coding sequence (CDS)
Genbank protein accession
ADR30490.1 [NCBI]
Genbank nucleotide accession
HM640230 [NCBI]
CDS location
range 11814 -> 13442
strand -
CDS
ATGGCTACAATAGATTTACTTAGAGTAGACCAACAAATATTTAATAATAGCTATGAACACGTAGCAGACTTTAAAAGTCCTAGCACTCAAAGGTACTATTTTGATAATAAAGTTATTTCATCATTTAATAAAGATATTGTAGTGCAACCCTCAAGAATAAGCGTTACTTGTCCATATCAATATAGGTACTTTTTAGATAATAGTATCAATTATGTTAGAGCCTTTGACAACTCCCGTTATTACTATTATTTCATAACAGATATAATCTTTACGGCTCAAGCTAGAACAGAGCTATTACTTGAATTAGATGTATGGCAAACTTACCTTTGGGATTATTCCGTATTGGATAGTATTGTCGAAAGATGTCATGTTAGAAGGTGGAACGATGACGGTACACCAACAAAAGAGAGTTTATACGCCGATGAAAATATCCCAACAGGTGAATATATAATGGAAAATGGTAATAGTGATTATAACATTGAATCTCTATCAGATACGGTCGTAATTGCTAGTACCGTACCTTTAGGAATATTAACAGATAGTTCGGGTGGTGAGGGTACTAACCCACCACCTGGTGAAGGTGATTGTGGAGACTGGACAAACGGAGTAATGTCAAGAAATGGTTTTAGGTTTATGAAAGGCTATGAGGGATTTGGTGCATATCTATACAAAGATAGTGGTGGAGTTCCTACCATTGGTTACGGTGTAACTAAGTCAGAGCCTTCGGAATTTGATGATTTAGTGGCAAGACAACCGGTTTCAGAGGAATATGCTTCTCAAGTTAGTTACAAATTAAAACAAACAAATTACGGAAAACCTATCGTAAATTTCTGTAAGGAGATTGGAATAACTAAACAAAATCAATTTGATGCTTTATGTGATTTAGCATTTAATGCCGGTGTGGGTGCGGTAGTTGGTACACCTACTTACACGTCATTACCGAGCGCATTACGTAAAGACCCATTCAATGAAAGTTATATCCGCCCTATATGGGAAAATTATATTATAAGTGACGCCGTGGGGAATGTACTTAATGGATTAAAAGCTAGAAGAAAAGCAGAGTGTGATATATATTTTAAGAATATATACGAATTTAGACCAATAGTAACCATAAATCAAAATGGTTCATATGGTAACCCAATCACGGCTAATAACGGTAATGGTTGGCTTCCTGAATGTTCTAGTAAACCCGAGGGGCTTTACGTGGATAATGAAGTTGGTAAAGATTGGTTAGTGCCTGTTAGTGGAACTATAAGTGCTATGTACCCTTCCTATCCTTCAGGTTCTCCGCATAATGGCGTTGATATTGCTTGTCCCGTAGGTACACCGGTCTACGCTTCAAAAGATGGATTGGTTAGAGTTCGTAAAGAGCTTACAACAAGTTATGGAAAATATTTAATTATAGCTCATGGGGATAGTGATGTAGTTTACGCACATAATAGCCAACTATTGGTAAACGAAGGTGATAACGTAAAACAGGGTCAAATGATAGCACGTTCGGGTAATAGTGGTAACTCATCAGGCCCACATTTACATTGGGAAATACGTAACCCAAACGGTGAAATAATTCAACACGGAGTAAAAACCGTTAACCCTATGCCTGGGTATAAGTTAAACCAAAAAGTGTAA

Gene Ontology

Description Category Evidence (source)
GO:0003796 lysozyme activity Molecular function Inferred from Electronic Annotation (UniProt)
GO:0004222 metalloendopeptidase activity Molecular function Inferred from Electronic Annotation (InterPro)
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:0030430 host cell cytoplasm Cellular component Inferred from Electronic Annotation (UniProt)
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.