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Conserved domains on  [gi|1435434088|gb|RDE83061.1|]
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lysozyme [Haemophilus parahaemolyticus]

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 ...
 35-178 1.70e-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: 242.90  E-value: 1.70e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435434088  35 RTSKQGLEIIGDAEGCRRDPYQCPADVLTVGIGSTaasgEKIDPKHRYSDLEIAERWKNDIVIAEQCVNKYGNGKQLPQS 114
Cdd:cd16901     1 RTSAAGLELIANAEGCRRDPYKCPAGVPTIGIGST----HGVKPGDRYTDEQAAKRLAKDIKKAERCVNRCFNGVPLPQG 76

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1435434088 115 VFDAAVSITFNVGCGAVSRSTMFKHLQTGNYKQACNEFPRWVYAGGRKLPGLAARREKEKALCL 178
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 ...
 35-178 1.70e-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: 242.90  E-value: 1.70e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435434088  35 RTSKQGLEIIGDAEGCRRDPYQCPADVLTVGIGSTaasgEKIDPKHRYSDLEIAERWKNDIVIAEQCVNKYGNGKQLPQS 114
Cdd:cd16901     1 RTSAAGLELIANAEGCRRDPYKCPAGVPTIGIGST----HGVKPGDRYTDEQAAKRLAKDIKKAERCVNRCFNGVPLPQG 76

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1435434088 115 VFDAAVSITFNVGCGAVSRSTMFKHLQTGNYKQACNEFPRWVYAGGRKLPGLAARREKEKALCL 178
Cdd:cd16901    77 EFDAYVSFAFNVGCGAFCKSTIYKKLQAGDYAAACNQLPRWVYAGGKVLPGLVTRRQKERALCL 140
RrrD COG3772
Phage-related lysozyme (muramidase), GH24 family [Cell wall/membrane/envelope biogenesis];
35-178 8.69e-61

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


Pssm-ID: 442986 [Multi-domain]  Cd Length: 146  Bit Score: 185.43  E-value: 8.69e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435434088  35 RTSKQGLEIIGDAEGCRRDPYQCPADVLTVGIGSTaasGEKIDPKHRYSDLEIAERWKNDIVIAEQCVNKYGNGKqLPQS 114
Cdd:COG3772     3 KTSAAGLALIKEFEGFRLKAYRDPAGVWTIGYGHT---GKDVKPGDTITEEEAEALLAADLAKAEAAVRRLVKVP-LTQN 78

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1435434088 115 VFDAAVSITFNVGCGAVSRSTMFKHLQTGNYKQACNEFPRWVYAGGRKLPGLAARREKEKALCL 178
Cdd:COG3772    79 QFDALVSFAYNVGAGAFCRSTLLRKLNAGDYAGACDELLRWVYAGGKVLPGLVRRREAERALCL 142
Phage_lysozyme pfam00959
Phage lysozyme; This family includes lambda phage lysozyme and E. coli endolysin.
 61-171 2.65e-27

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


Pssm-ID: 395766 [Multi-domain]  Cd Length: 107  Bit Score: 98.97  E-value: 2.65e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435434088  61 VLTVGIGSTaasGEKIDPKHRYSDLEIAERWKNDIVIAEQCVNKYGNGKQLPQSVFDAAVSITFNVGCGAVSRSTMFKHL 140
Cdd:pfam00959   1 YWTIGIGHN---GKDVSPHPRATKSEAAGRLQIDLDTAERCINQYHKVKDFNPNQQDALVSLAFNVGCGKRGFSTLLRAG 77

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1435434088 141 QTGNYKQACNEFPRWVYAgGRKLPGLAARRE 171
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 ...
 35-178 1.70e-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: 242.90  E-value: 1.70e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435434088  35 RTSKQGLEIIGDAEGCRRDPYQCPADVLTVGIGSTaasgEKIDPKHRYSDLEIAERWKNDIVIAEQCVNKYGNGKQLPQS 114
Cdd:cd16901     1 RTSAAGLELIANAEGCRRDPYKCPAGVPTIGIGST----HGVKPGDRYTDEQAAKRLAKDIKKAERCVNRCFNGVPLPQG 76

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1435434088 115 VFDAAVSITFNVGCGAVSRSTMFKHLQTGNYKQACNEFPRWVYAGGRKLPGLAARREKEKALCL 178
Cdd:cd16901    77 EFDAYVSFAFNVGCGAFCKSTIYKKLQAGDYAAACNQLPRWVYAGGKVLPGLVTRRQKERALCL 140
RrrD COG3772
Phage-related lysozyme (muramidase), GH24 family [Cell wall/membrane/envelope biogenesis];
35-178 8.69e-61

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


Pssm-ID: 442986 [Multi-domain]  Cd Length: 146  Bit Score: 185.43  E-value: 8.69e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435434088  35 RTSKQGLEIIGDAEGCRRDPYQCPADVLTVGIGSTaasGEKIDPKHRYSDLEIAERWKNDIVIAEQCVNKYGNGKqLPQS 114
Cdd:COG3772     3 KTSAAGLALIKEFEGFRLKAYRDPAGVWTIGYGHT---GKDVKPGDTITEEEAEALLAADLAKAEAAVRRLVKVP-LTQN 78

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1435434088 115 VFDAAVSITFNVGCGAVSRSTMFKHLQTGNYKQACNEFPRWVYAGGRKLPGLAARREKEKALCL 178
Cdd:COG3772    79 QFDALVSFAYNVGAGAFCRSTLLRKLNAGDYAGACDELLRWVYAGGKVLPGLVRRREAERALCL 142
lyz_endolysin_autolysin cd00737
endolysin and autolysin; The dsDNA phages of eubacteria use endolysins or muralytic enzymes in ...
 40-178 1.31e-47

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: 151.90  E-value: 1.31e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435434088  40 GLEIIGDAEGCRRDPYQCPADVLTVGIGSTAASGEKidPKHRYSDLEIAERWKNDIVIAEQCVNKYGNgKQLPQSVFDAA 119
Cdd:cd00737     1 GLDLIKEFEGLRLKAYRDPAGVWTIGYGHTGGVVVK--PGDTITEAQAEALLRQDLARFEAAVNRLVK-VPLNQNQFDAL 77

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1435434088 120 VSITFNVGCGAVSRSTMFKHLQTGNYKQACNEFPRWVYAGGRKLPGLAARREKEKALCL 178
Cdd:cd00737    78 VSFAFNVGAGAFKSSTLLRKLNAGDYAGAADEFLRWNKAGGKVLPGLVRRRAAEAALFL 136
endolysin_R21-like cd16900
endolysin R21-like proteins; Unlike T4 E phage lysozyme, the endolysin R21 from Enterobacteria ...
 43-178 5.51e-30

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: 106.87  E-value: 5.51e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435434088  43 IIGDAEGCRRDPYQCPADVLTVGIGSTaasGEKIDPKHRYSDLEIAERWKNDIVIAEQCVNKYGNGKqLPQSVFDAAVSI 122
Cdd:cd16900    11 LVGPWEGLRLTAYRDPVGVWTVCYGHT---GGDVKPGMRYTPAECDALLAKDLQEAAAAVDRCVKVP-LPDPQRAALASF 86

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1435434088 123 TFNVGCGAVSRSTMFKHLQTGNYKQACNEFPRWVYAGGRKLPGLAARREKEKALCL 178
Cdd:cd16900    87 AYNVGVGAFCRSTLLRKLNAGDRRGACDELTRWVYAGGRVLRGLVNRREAERALCL 142
Phage_lysozyme pfam00959
Phage lysozyme; This family includes lambda phage lysozyme and E. coli endolysin.
 61-171 2.65e-27

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


Pssm-ID: 395766 [Multi-domain]  Cd Length: 107  Bit Score: 98.97  E-value: 2.65e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435434088  61 VLTVGIGSTaasGEKIDPKHRYSDLEIAERWKNDIVIAEQCVNKYGNGKQLPQSVFDAAVSITFNVGCGAVSRSTMFKHL 140
Cdd:pfam00959   1 YWTIGIGHN---GKDVSPHPRATKSEAAGRLQIDLDTAERCINQYHKVKDFNPNQQDALVSLAFNVGCGKRGFSTLLRAG 77

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1435434088 141 QTGNYKQACNEFPRWVYAgGRKLPGLAARRE 171
Cdd:pfam00959  78 NIGQWIKACSAIWKSLKA-GKVYNGLVNRRE 107
T4-like_lys cd00735
bacteriophage T4-like lysozymes; Bacteriophage T4-like lysozymes hydrolyze the beta-1, ...
 48-170 1.36e-03

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: 37.35  E-value: 1.36e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435434088  48 EGCRRDPYQCPADVLTVGIGSTAasGEKIDPKHRYS-DLEIAERW-KNDIVIA----EQCVNKYGNGKQLPQSVFDAAVS 121
Cdd:cd00735    10 EGYRLKAYKDTEGYPTIGIGHLI--GKKGASLTNGTiTKDEAEALfEQDVDRAvrdmLRNPKLAPVYAQLNAARRMALIN 87

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1435434088 122 ITFNVGCGAVSR-STMFKHLQTGNYKQACNEFPRwvYAGGRKLPGLAARR 170
Cdd:cd00735    88 MAFQMGVGGLAKfKNMLAAIKAGDWEEAADGMLN--SLWAKQTPNRANRV 135
 
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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