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Conserved domains on  [gi|1148817286|ref|WP_077542809|]
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lysozyme [Rodentibacter genomosp. 1]

Protein Classification

lysozyme( domain architecture ID 13014142)

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
lyz_P1 cd16901
P1 lysozyme Lyz-like proteins; Enterobacteria phage P1 lysozyme Lyz is secreted to the ...
 33-176 2.07e-83

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: 242.51  E-value: 2.07e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148817286  33 RISEKGMEIIGNAEGCRRDPYQCPADVLTVGIGSTEvsggSINPNKRYTDKEIADRWANDLRIAERCVNLYGNGRNLPQG 112
Cdd:cd16901     1 RTSAAGLELIANAEGCRRDPYKCPAGVPTIGIGSTH----GVKPGDRYTDEQAAKRLAKDIKKAERCVNRCFNGVPLPQG 76

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1148817286 113 TFDAMTSIVFNVGCGAMRKSTMFRKANAGDYIGACNELPKWVYAGGKKLRGLEIRRDKERQLCL 176
Cdd:cd16901    77 EFDAYVSFAFNVGCGAFCKSTIYKKLQAGDYAAACNQLPRWVYAGGKVLPGLVTRRQKERALCL 140
 
Name Accession Description Interval E-value
lyz_P1 cd16901
P1 lysozyme Lyz-like proteins; Enterobacteria phage P1 lysozyme Lyz is secreted to the ...
 33-176 2.07e-83

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: 242.51  E-value: 2.07e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148817286  33 RISEKGMEIIGNAEGCRRDPYQCPADVLTVGIGSTEvsggSINPNKRYTDKEIADRWANDLRIAERCVNLYGNGRNLPQG 112
Cdd:cd16901     1 RTSAAGLELIANAEGCRRDPYKCPAGVPTIGIGSTH----GVKPGDRYTDEQAAKRLAKDIKKAERCVNRCFNGVPLPQG 76

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1148817286 113 TFDAMTSIVFNVGCGAMRKSTMFRKANAGDYIGACNELPKWVYAGGKKLRGLEIRRDKERQLCL 176
Cdd:cd16901    77 EFDAYVSFAFNVGCGAFCKSTIYKKLQAGDYAAACNQLPRWVYAGGKVLPGLVTRRQKERALCL 140
RrrD COG3772
Phage-related lysozyme (muramidase), GH24 family [Cell wall/membrane/envelope biogenesis];
32-180 4.06e-63

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


Pssm-ID: 442986 [Multi-domain]  Cd Length: 146  Bit Score: 191.21  E-value: 4.06e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148817286  32 LRISEKGMEIIGNAEGCRRDPYQCPADVLTVGIGSTevsGGSINPNKRYTDKEIADRWANDLRIAERCVNLYGnGRNLPQ 111
Cdd:COG3772     2 MKTSAAGLALIKEFEGFRLKAYRDPAGVWTIGYGHT---GKDVKPGDTITEEEAEALLAADLAKAEAAVRRLV-KVPLTQ 77

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1148817286 112 GTFDAMTSIVFNVGCGAMRKSTMFRKANAGDYIGACNELPKWVYAGGKKLRGLEIRRDKERQLCLMELK 180
Cdd:COG3772    78 NQFDALVSFAYNVGAGAFCRSTLLRKLNAGDYAGACDELLRWVYAGGKVLPGLVRRREAERALCLGGLY 146
Phage_lysozyme pfam00959
Phage lysozyme; This family includes lambda phage lysozyme and E. coli endolysin.
 59-169 5.81e-39

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


Pssm-ID: 395766 [Multi-domain]  Cd Length: 107  Bit Score: 128.63  E-value: 5.81e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148817286  59 VLTVGIGsteVSGGSINPNKRYTDKEIADRWANDLRIAERCVNLYGNGRNLPQGTFDAMTSIVFNVGCGAMRKSTMFRKA 138
Cdd:pfam00959   1 YWTIGIG---HNGKDVSPHPRATKSEAAGRLQIDLDTAERCINQYHKVKDFNPNQQDALVSLAFNVGCGKRGFSTLLRAG 77

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1148817286 139 NAGDYIGACNELPKWVYAgGKKLRGLEIRRD 169
Cdd:pfam00959  78 NIGQWIKACSAIWKSLKA-GKVYNGLVNRRE 107
 
Name Accession Description Interval E-value
lyz_P1 cd16901
P1 lysozyme Lyz-like proteins; Enterobacteria phage P1 lysozyme Lyz is secreted to the ...
 33-176 2.07e-83

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: 242.51  E-value: 2.07e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148817286  33 RISEKGMEIIGNAEGCRRDPYQCPADVLTVGIGSTEvsggSINPNKRYTDKEIADRWANDLRIAERCVNLYGNGRNLPQG 112
Cdd:cd16901     1 RTSAAGLELIANAEGCRRDPYKCPAGVPTIGIGSTH----GVKPGDRYTDEQAAKRLAKDIKKAERCVNRCFNGVPLPQG 76

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1148817286 113 TFDAMTSIVFNVGCGAMRKSTMFRKANAGDYIGACNELPKWVYAGGKKLRGLEIRRDKERQLCL 176
Cdd:cd16901    77 EFDAYVSFAFNVGCGAFCKSTIYKKLQAGDYAAACNQLPRWVYAGGKVLPGLVTRRQKERALCL 140
RrrD COG3772
Phage-related lysozyme (muramidase), GH24 family [Cell wall/membrane/envelope biogenesis];
32-180 4.06e-63

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


Pssm-ID: 442986 [Multi-domain]  Cd Length: 146  Bit Score: 191.21  E-value: 4.06e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148817286  32 LRISEKGMEIIGNAEGCRRDPYQCPADVLTVGIGSTevsGGSINPNKRYTDKEIADRWANDLRIAERCVNLYGnGRNLPQ 111
Cdd:COG3772     2 MKTSAAGLALIKEFEGFRLKAYRDPAGVWTIGYGHT---GKDVKPGDTITEEEAEALLAADLAKAEAAVRRLV-KVPLTQ 77

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1148817286 112 GTFDAMTSIVFNVGCGAMRKSTMFRKANAGDYIGACNELPKWVYAGGKKLRGLEIRRDKERQLCLMELK 180
Cdd:COG3772    78 NQFDALVSFAYNVGAGAFCRSTLLRKLNAGDYAGACDELLRWVYAGGKVLPGLVRRREAERALCLGGLY 146
lyz_endolysin_autolysin cd00737
endolysin and autolysin; The dsDNA phages of eubacteria use endolysins or muralytic enzymes in ...
 38-176 2.87e-48

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: 153.44  E-value: 2.87e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148817286  38 GMEIIGNAEGCRRDPYQCPADVLTVGIGSTEVSGgsINPNKRYTDKEIADRWANDLRIAERCVNLYGNgRNLPQGTFDAM 117
Cdd:cd00737     1 GLDLIKEFEGLRLKAYRDPAGVWTIGYGHTGGVV--VKPGDTITEAQAEALLRQDLARFEAAVNRLVK-VPLNQNQFDAL 77

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1148817286 118 TSIVFNVGCGAMRKSTMFRKANAGDYIGACNELPKWVYAGGKKLRGLEIRRDKERQLCL 176
Cdd:cd00737    78 VSFAFNVGAGAFKSSTLLRKLNAGDYAGAADEFLRWNKAGGKVLPGLVRRRAAEAALFL 136
endolysin_R21-like cd16900
endolysin R21-like proteins; Unlike T4 E phage lysozyme, the endolysin R21 from Enterobacteria ...
 41-176 2.37e-40

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: 133.45  E-value: 2.37e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148817286  41 IIGNAEGCRRDPYQCPADVLTVGIGSTevsGGSINPNKRYTDKEIADRWANDLRIAE----RCVnlygnGRNLPQGTFDA 116
Cdd:cd16900    11 LVGPWEGLRLTAYRDPVGVWTVCYGHT---GGDVKPGMRYTPAECDALLAKDLQEAAaavdRCV-----KVPLPDPQRAA 82

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148817286 117 MTSIVFNVGCGAMRKSTMFRKANAGDYIGACNELPKWVYAGGKKLRGLEIRRDKERQLCL 176
Cdd:cd16900    83 LASFAYNVGVGAFCRSTLLRKLNAGDRRGACDELTRWVYAGGRVLRGLVNRREAERALCL 142
Phage_lysozyme pfam00959
Phage lysozyme; This family includes lambda phage lysozyme and E. coli endolysin.
 59-169 5.81e-39

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


Pssm-ID: 395766 [Multi-domain]  Cd Length: 107  Bit Score: 128.63  E-value: 5.81e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148817286  59 VLTVGIGsteVSGGSINPNKRYTDKEIADRWANDLRIAERCVNLYGNGRNLPQGTFDAMTSIVFNVGCGAMRKSTMFRKA 138
Cdd:pfam00959   1 YWTIGIG---HNGKDVSPHPRATKSEAAGRLQIDLDTAERCINQYHKVKDFNPNQQDALVSLAFNVGCGKRGFSTLLRAG 77

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1148817286 139 NAGDYIGACNELPKWVYAgGKKLRGLEIRRD 169
Cdd:pfam00959  78 NIGQWIKACSAIWKSLKA-GKVYNGLVNRRE 107
T4-like_lys cd00735
bacteriophage T4-like lysozymes; Bacteriophage T4-like lysozymes hydrolyze the beta-1, ...
 46-150 1.18e-06

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: 1.18e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148817286  46 EGCRRDPYQCPADVLTVGIGSTEVSGGSINPNKRYTDKEIADRWANDL----RIAERCVNLYGNGRNLPQGTFDAMTSIV 121
Cdd:cd00735    10 EGYRLKAYKDTEGYPTIGIGHLIGKKGASLTNGTITKDEAEALFEQDVdravRDMLRNPKLAPVYAQLNAARRMALINMA 89

                          90       100       110
                  ....*....|....*....|....*....|
gi 1148817286 122 FNVGCGAMRK-STMFRKANAGDYIGACNEL 150
Cdd:cd00735    90 FQMGVGGLAKfKNMLAAIKAGDWEEAADGM 119
 
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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