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Conserved domains on  [gi|662242620|dbj|BAP15847|]
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putative lysozyme [Ralstonia phage RSJ2]

Protein Classification

lysozyme( domain architecture ID 10007970)

lysozyme, also called endolysin or muramidase, hydrolyzes (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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
RrrD COG3772
Phage-related lysozyme (muramidase), GH24 family [Cell wall/membrane/envelope biogenesis];
22-160 1.94e-64

Phage-related lysozyme (muramidase), GH24 family [Cell wall/membrane/envelope biogenesis];


:

Pssm-ID: 442986 [Multi-domain]  Cd Length: 146  Bit Score: 193.90  E-value: 1.94e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 662242620  22 FIATHEGTVQQSYADPAlgwKVPTICTGHTGPDVYRGQVATKEMCRAWLQQDSASAAKAVHRCVSYRLNQPQFDALVSFT 101
Cdd:COG3772   11 LIKEFEGFRLKAYRDPA---GVWTIGYGHTGKDVKPGDTITEEEAEALLAADLAKAEAAVRRLVKVPLTQNQFDALVSFA 87

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 662242620 102 FNVGQTAMCSSTLVRKLNAGDLQGASAEFPRWNRSGGKVLPGLTNRRAAERKLFDTGAY 160
Cdd:COG3772   88 YNVGAGAFCRSTLLRKLNAGDYAGACDELLRWVYAGGKVLPGLVRRREAERALCLGGLY 146
 
Name Accession Description Interval E-value
RrrD COG3772
Phage-related lysozyme (muramidase), GH24 family [Cell wall/membrane/envelope biogenesis];
22-160 1.94e-64

Phage-related lysozyme (muramidase), GH24 family [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442986 [Multi-domain]  Cd Length: 146  Bit Score: 193.90  E-value: 1.94e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 662242620  22 FIATHEGTVQQSYADPAlgwKVPTICTGHTGPDVYRGQVATKEMCRAWLQQDSASAAKAVHRCVSYRLNQPQFDALVSFT 101
Cdd:COG3772   11 LIKEFEGFRLKAYRDPA---GVWTIGYGHTGKDVKPGDTITEEEAEALLAADLAKAEAAVRRLVKVPLTQNQFDALVSFA 87

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 662242620 102 FNVGQTAMCSSTLVRKLNAGDLQGASAEFPRWNRSGGKVLPGLTNRRAAERKLFDTGAY 160
Cdd:COG3772   88 YNVGAGAFCRSTLLRKLNAGDYAGACDELLRWVYAGGKVLPGLVRRREAERALCLGGLY 146
lyz_endolysin_autolysin cd00737
endolysin and autolysin; The dsDNA phages of eubacteria use endolysins or muralytic enzymes in ...
 22-156 1.33e-58

endolysin and autolysin; The dsDNA phages of eubacteria use endolysins or muralytic enzymes in conjunction with hollin, a small membrane protein, to degrade the peptidoglycan found in bacterial cell walls. Similarly, bacteria produce autolysins to facilitate the biosynthesis of its cell wall heteropolymer peptidoglycan and cell division. Endolysins and autolysins are found in viruses and bacteria, respectively. Both endolysin and autolysin enzymes cleave the glycosidic beta 1,4-bonds between the N-acetylmuramic acid and the N-acetylglucosamine of the peptidoglycan.


Pssm-ID: 381599 [Multi-domain]  Cd Length: 136  Bit Score: 178.87  E-value: 1.33e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 662242620  22 FIATHEGTVQQSYADPAlgwKVPTICTGHTGPDVYR-GQVATKEMCRAWLQQDSASAAKAVHRCVSYRLNQPQFDALVSF 100
Cdd:cd00737    4 LIKEFEGLRLKAYRDPA---GVWTIGYGHTGGVVVKpGDTITEAQAEALLRQDLARFEAAVNRLVKVPLNQNQFDALVSF 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 662242620 101 TFNVGQTAMCSSTLVRKLNAGDLQGASAEFPRWNRSGGKVLPGLTNRRAAERKLFD 156
Cdd:cd00737   81 AFNVGAGAFKSSTLLRKLNAGDYAGAADEFLRWNKAGGKVLPGLVRRRAAEAALFL 136
Phage_lysozyme pfam00959
Phage lysozyme; This family includes lambda phage lysozyme and E. coli endolysin.
 43-149 1.17e-23

Phage lysozyme; This family includes lambda phage lysozyme and E. coli endolysin.


Pssm-ID: 395766 [Multi-domain]  Cd Length: 107  Bit Score: 88.95  E-value: 1.17e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 662242620   43 VPTICTGHTGPDVYRGQVATKEMCRAWLQQDSASAAKAVHRCVSYR-LNQPQFDALVSFTFNVGQTAMCSSTLVRKLNAG 121
Cdd:pfam00959   1 YWTIGIGHNGKDVSPHPRATKSEAAGRLQIDLDTAERCINQYHKVKdFNPNQQDALVSLAFNVGCGKRGFSTLLRAGNIG 80

                          90       100
                  ....*....|....*....|....*...
gi 662242620  122 DLQGASAEFPRWNRSgGKVLPGLTNRRA 149
Cdd:pfam00959  81 QWIKACSAIWKSLKA-GKVYNGLVNRRE 107
 
Name Accession Description Interval E-value
RrrD COG3772
Phage-related lysozyme (muramidase), GH24 family [Cell wall/membrane/envelope biogenesis];
22-160 1.94e-64

Phage-related lysozyme (muramidase), GH24 family [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442986 [Multi-domain]  Cd Length: 146  Bit Score: 193.90  E-value: 1.94e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 662242620  22 FIATHEGTVQQSYADPAlgwKVPTICTGHTGPDVYRGQVATKEMCRAWLQQDSASAAKAVHRCVSYRLNQPQFDALVSFT 101
Cdd:COG3772   11 LIKEFEGFRLKAYRDPA---GVWTIGYGHTGKDVKPGDTITEEEAEALLAADLAKAEAAVRRLVKVPLTQNQFDALVSFA 87

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 662242620 102 FNVGQTAMCSSTLVRKLNAGDLQGASAEFPRWNRSGGKVLPGLTNRRAAERKLFDTGAY 160
Cdd:COG3772   88 YNVGAGAFCRSTLLRKLNAGDYAGACDELLRWVYAGGKVLPGLVRRREAERALCLGGLY 146
lyz_endolysin_autolysin cd00737
endolysin and autolysin; The dsDNA phages of eubacteria use endolysins or muralytic enzymes in ...
 22-156 1.33e-58

endolysin and autolysin; The dsDNA phages of eubacteria use endolysins or muralytic enzymes in conjunction with hollin, a small membrane protein, to degrade the peptidoglycan found in bacterial cell walls. Similarly, bacteria produce autolysins to facilitate the biosynthesis of its cell wall heteropolymer peptidoglycan and cell division. Endolysins and autolysins are found in viruses and bacteria, respectively. Both endolysin and autolysin enzymes cleave the glycosidic beta 1,4-bonds between the N-acetylmuramic acid and the N-acetylglucosamine of the peptidoglycan.


Pssm-ID: 381599 [Multi-domain]  Cd Length: 136  Bit Score: 178.87  E-value: 1.33e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 662242620  22 FIATHEGTVQQSYADPAlgwKVPTICTGHTGPDVYR-GQVATKEMCRAWLQQDSASAAKAVHRCVSYRLNQPQFDALVSF 100
Cdd:cd00737    4 LIKEFEGLRLKAYRDPA---GVWTIGYGHTGGVVVKpGDTITEAQAEALLRQDLARFEAAVNRLVKVPLNQNQFDALVSF 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 662242620 101 TFNVGQTAMCSSTLVRKLNAGDLQGASAEFPRWNRSGGKVLPGLTNRRAAERKLFD 156
Cdd:cd00737   81 AFNVGAGAFKSSTLLRKLNAGDYAGAADEFLRWNKAGGKVLPGLVRRRAAEAALFL 136
endolysin_R21-like cd16900
endolysin R21-like proteins; Unlike T4 E phage lysozyme, the endolysin R21 from Enterobacteria ...
 21-154 2.55e-57

endolysin R21-like proteins; Unlike T4 E phage lysozyme, the endolysin R21 from Enterobacteria phage P21 has an N-terminal SAR (signal-arrest-release) domain that anchors the endolysin to the membrane in an inactive form, which act to prevent premature lysis of the infected bacterium. The dsDNA phages of eubacteria use endolysins or muralytic enzymes in conjunction with hollin, a small membrane protein, to degrade the peptidoglycan found in bacterial cell walls. Similarly, bacteria produce autolysins to facilitate the biosynthesis of its cell wall heteropolymer peptidoglycan and cell division. Endolysins and autolysins are found in viruses and bacteria, respectively. Both endolysin and autolysin enzymes cleave the glycosidic beta 1,4-bonds between the N-acetylmuramic acid and the N-acetylglucosamine of the peptidoglycan.


Pssm-ID: 381619 [Multi-domain]  Cd Length: 142  Bit Score: 175.82  E-value: 2.55e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 662242620  21 TFIATHEGTVQQSYADPAlgwKVPTICTGHTGPDVYRGQVATKEMCRAWLQQDSASAAKAVHRCVSYRLNQPQFDALVSF 100
Cdd:cd16900   10 ALVGPWEGLRLTAYRDPV---GVWTVCYGHTGGDVKPGMRYTPAECDALLAKDLQEAAAAVDRCVKVPLPDPQRAALASF 86

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 662242620 101 TFNVGQTAMCSSTLVRKLNAGDLQGASAEFPRWNRSGGKVLPGLTNRRAAERKL 154
Cdd:cd16900   87 AYNVGVGAFCRSTLLRKLNAGDRRGACDELTRWVYAGGRVLRGLVNRREAERAL 140
lyz_P1 cd16901
P1 lysozyme Lyz-like proteins; Enterobacteria phage P1 lysozyme Lyz is secreted to the ...
 22-154 1.09e-41

P1 lysozyme Lyz-like proteins; Enterobacteria phage P1 lysozyme Lyz is secreted to the Escherichia coli periplasm where it is membrane bound and inactive. Activation involves the release from the membrane, an intramolecular thiol-disulfide isomerization and extensive structural rearrangement of the N-terminal region. The dsDNA phages of eubacteria use endolysins or muralytic enzymes in conjunction with hollin, a small membrane protein, to degrade the peptidoglycan found in bacterial cell walls. Similarly, bacteria produce autolysins to facilitate the biosynthesis of its cell wall heteropolymer peptidoglycan and cell division. Endolysins and autolysins are found in viruses and bacteria, respectively. Both endolysin and autolysin enzymes cleave the glycosidic beta 1,4-bonds between the N-acetylmuramic acid and the N-acetylglucosamine of the peptidoglycan.


Pssm-ID: 381620 [Multi-domain]  Cd Length: 140  Bit Score: 135.81  E-value: 1.09e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 662242620  22 FIATHEGTVQQSYADPAlgwKVPTICTGHTGpDVYRGQVATKEMCRAWLQQDSASAAKAVHRCVS-YRLNQPQFDALVSF 100
Cdd:cd16901    9 LIANAEGCRRDPYKCPA---GVPTIGIGSTH-GVKPGDRYTDEQAAKRLAKDIKKAERCVNRCFNgVPLPQGEFDAYVSF 84

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 662242620 101 TFNVGQTAMCSSTLVRKLNAGDLQGASAEFPRWNRSGGKVLPGLTNRRAAERKL 154
Cdd:cd16901   85 AFNVGCGAFCKSTIYKKLQAGDYAAACNQLPRWVYAGGKVLPGLVTRRQKERAL 138
Phage_lysozyme pfam00959
Phage lysozyme; This family includes lambda phage lysozyme and E. coli endolysin.
 43-149 1.17e-23

Phage lysozyme; This family includes lambda phage lysozyme and E. coli endolysin.


Pssm-ID: 395766 [Multi-domain]  Cd Length: 107  Bit Score: 88.95  E-value: 1.17e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 662242620   43 VPTICTGHTGPDVYRGQVATKEMCRAWLQQDSASAAKAVHRCVSYR-LNQPQFDALVSFTFNVGQTAMCSSTLVRKLNAG 121
Cdd:pfam00959   1 YWTIGIGHNGKDVSPHPRATKSEAAGRLQIDLDTAERCINQYHKVKdFNPNQQDALVSLAFNVGCGKRGFSTLLRAGNIG 80

                          90       100
                  ....*....|....*....|....*...
gi 662242620  122 DLQGASAEFPRWNRSgGKVLPGLTNRRA 149
Cdd:pfam00959  81 QWIKACSAIWKSLKA-GKVYNGLVNRRE 107
T4-like_lys cd00735
bacteriophage T4-like lysozymes; Bacteriophage T4-like lysozymes hydrolyze the beta-1, ...
 27-161 9.13e-07

bacteriophage T4-like lysozymes; Bacteriophage T4-like lysozymes hydrolyze the beta-1,4-glycosidic bond between N-acetylmuramic acid (MurNAc) and N-acetylglucosamine (GlcNAc) in peptidoglycan heteropolymers of prokaryotic cell walls. Members include a variety of bacteriophages (T4, RB49, RB69, Aeh1), as well as Dictyostelium.


Pssm-ID: 381597  Cd Length: 146  Bit Score: 45.83  E-value: 9.13e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 662242620  27 EGTVQQSYADpALGWkvPTICTGHT---GPDVYRGQVATKEMCRAWLQQDSASAAKAVHRCVSYR-----LNQPQFDALV 98
Cdd:cd00735   10 EGYRLKAYKD-TEGY--PTIGIGHLigkKGASLTNGTITKDEAEALFEQDVDRAVRDMLRNPKLApvyaqLNAARRMALI 86

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 662242620  99 SFTFNVGQTAMCS-STLVRKLNAGDLQGASAEFprWNRSGGKVLPGLTNRRAAerkLFDTGAYE 161
Cdd:cd00735   87 NMAFQMGVGGLAKfKNMLAAIKAGDWEEAADGM--LNSLWAKQTPNRANRVSA---VMRTGTWA 145
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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