Protein

UniProt accession
A1YTR6 [UniProt]
Protein name
N-acetylmuramoyl-L-alanine amidase
PhaLP type
endolysin

evidence: GO annotation

probability: 99 % (predicted by ML model)

Protein sequence
MAKTQAEINKRLDAYAKGTVDSPYRVKKATSYDPSFGVMEAGAIDADGYYHAQCQDLITDYVLWLTDNKVRTWGNAKDQIKQSYGTGFKIHENKPSTVPKKGWIAVFTSGSYEQWGHIGIVYDGGNTSTFTILEQNWNGYANKKPTKRVDNYYGLTHFIEIPVKAGTTVKKETAKKSASTPATRPVTGSWKKNQYGTWYKPENATFVNGNQPIVTRIGSPFLNAPVGGNLPAGATIVYDEVCIQAGHIWIGYNAYNGNRVYCPVRTCQGVPPNQIPGVAWGVFK
Physico‐chemical
properties
protein length:284 AA
molecular weight:31379,00000 Da
isoelectric point:9,32169
aromaticity:0,12324
hydropathy:-0,50563

Domains

Domains [InterPro]
IPR003646
198–264
IPR003646 IPR038765
IPR003646
201–270
IPR003646 IPR007921
IPR007921
29–160
IPR007921
Protein sequence: A1YTR6
1 284
Legend: Pfam SMART CDD TIGRFAM HAMAP SUPFAM PRINTS Gene3D PANTHER Other

Taxonomy

  Name Taxonomy ID Lineage
Phage Staphylococcus phage 812
[NCBI] 		307898 Herelleviridae > Kayvirus >
Host No host information

Coding sequence (CDS)

Coding sequence (CDS)
Genbank protein accession
AHY26472.1 [NCBI]
Genbank nucleotide accession
KJ206563 [NCBI]
CDS location
range ->
strand
CDS

  




        

        
          

        
      
        

          
Genbank protein accession

          

            AHY26256.1 
            [NCBI]
          


          
Genbank nucleotide accession

          

            KJ206562
            [NCBI]
          


          
CDS location

          

            range 34341 -> 35195

            strand -
          



CDS



  

    
ATGGCTAAGACTCAAGCAGAAATAAATAAACGTTTAGATGCTTATGCAAAAGGAACAGTAGATAGCCCTTACAGAGTTAAAAAAGCTACAAGTTATGACCCATCATTTGGTGTAATGGAAGCAGGAGCCATTGATGCAGATGGTTACTATCACGCTCAGTGTCAAGACCTTATTACAGACTATGTTTTATGGTTAACAGATAATAAAGTTAGAACTTGGGGTAATGCTAAAGACCAAATTAAACAGAGTTATGGTACTGGATTTAAAATACATGAAAATAAACCTTCTACTGTACCTAAAAAAGGTTGGATTGCGGTATTTACATCCGGTAGTTATGAACAGTGGGGTCACATAGGTATTGTATATGATGGAGGTAATACTTCTACATTTACTATTTTAGAGCAAAACTGGAATGGTTATGCTAATAAAAAACCTACAAAACGTGTAGATAATTATTACGGATTAACTCACTTCATTGAAATACCTGTAAAAGCAGGAACTACTGTTAAAAAAGAAACAGCTAAGAAAAGCGCAAGTACACCGGCAACTAGACCAGTTACAGGTTCTTGGAAAAAGAACCAGTACGGAACTTGGTATAAACCGGAAAATGCAACATTTGTCAATGGTAACCAACCTATAGTAACTAGAATAGGTTCTCCATTCTTAAATGCTCCAGTAGGCGGTAACTTACCGGCAGGGGCTACAATTGTATATGACGAAGTTTGTATCCAAGCAGGTCACATTTGGATAGGTTATAATGCTTACAACGGTAACAGAGTATATTGCCCTGTTAGAACTTGTCAAGGTGTTCCACCTAATCAAATACCTGGCGTTGCCTGGGGAGTATTCAAATAG

  




        

        
          

        
      
        

          
Genbank protein accession

          

            ABL87142.1 
            [NCBI]
          


          
Genbank nucleotide accession

          

            EF136588
            [NCBI]
          


          
CDS location

          

            range 654 -> 1508

            strand +
          



CDS



  

    
ATGGCTAAGACTCAAGCAGAAATAAATAAACGTTTAGATGCTTATGCAAAAGGAACAGTAGATAGCCCTTACAGAGTTAAAAAAGCTACAAGTTATGACCCATCATTTGGTGTAATGGAAGCAGGAGCCATTGATGCAGATGGTTACTATCACGCTCAGTGTCAAGACCTTATTACAGACTATGTTTTATGGTTAACAGATAATAAAGTTAGAACTTGGGGTAATGCTAAAGACCAAATTAAACAGAGTTATGGTACTGGATTTAAAATACATGAAAATAAACCTTCTACTGTACCTAAAAAAGGTTGGATTGCGGTATTTACATCCGGTAGTTATGAACAGTGGGGTCACATAGGTATTGTATATGATGGAGGTAATACTTCTACATTTACTATTTTAGAGCAAAACTGGAATGGTTATGCTAATAAAAAACCTACAAAACGTGTAGATAATTATTACGGATTAACTCACTTCATTGAAATACCTGTAAAAGCAGGAACTACTGTTAAAAAAGAAACAGCTAAGAAAAGCGCAAGTACACCGGCAACTAGACCAGTTACAGGTTCTTGGAAAAAGAACCAGTACGGAACTTGGTATAAACCGGAAAATGCAACATTTGTCAATGGTAACCAACCTATAGTAACTAGAATAGGTTCTCCATTCTTAAATGCTCCAGTAGGCGGTAACTTACCGGCAGGGGCTACAATTGTATATGACGAAGTTTGTATCCAAGCAGGTCACATTTGGATAGGTTATAATGCTTACAACGGTAACAGAGTATATTGCCCTGTTAGAACTTGTCAAGGTGTTCCACCTAATCAAATACCTGGCGTTGCCTGGGGAGTATTCAAATAG

  




        

        
      
    
  






  

  
  

    
Gene Ontology


  





  


    
    

      

        
          

            
            Description
            Category
            Evidence (source)
          

        
        
          
          

            
              
                GO:0001897
              
            
            symbiont-mediated cytolysis of host cell
            Biological process
            Inferred from Electronic Annotation (InterPro)
          

          
          

            
              
                GO:0003824
              
            
            catalytic activity
            Molecular function
            Inferred from Electronic Annotation (InterPro)
          

          
        
      

    

    

  





  

  
  

    
Enzymatic activity


  





  

    
      

        

          
            

              EC Number
              Entry Name
              Reaction Catalyzed
              Classification
              Evidence
              Source
            

          
          
            
              

                
                  
                    3.5.1.28
                  
                
                
                  N-acetylmuramoyl-L-alanine amidase
                  
                
                residues in certain cell-wall glycopeptides
                
                  
Hydrolases

                  
Acting on carbon-nitrogen bonds, other than peptide bonds

                  
In linear amides

                		
                
                  match to sequence model evidence used in automatic assertion
                  
ECO:0000256
                		
                

  
    ARBA:ARBA00001561
  


                
              

            
          
        

      

    
  




  

  
  

    
Tertiary structure


  





  

    
      
No tertiary structures available.