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Conserved domains on  [gi|1728663866|gb|TXU91353|]
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lysozyme [Klebsiella oxytoca]

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];
1-163 1.10e-48

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


:

Pssm-ID: 442986 [Multi-domain]  Cd Length: 146  Bit Score: 154.23  E-value: 1.10e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728663866   1 MLGLIAAGAsapVLMAQFqhekEGTSLTAYQDkSRGIWTICGGVTyvdGKPVIKGMTLTRAQCDKIDKAEQAKALAWVDR 80
Cdd:COG3772     1 MMKTSAAGL---ALIKEF----EGFRLKAYRD-PAGVWTIGYGHT---GKDVKPGDTITEEEAEALLAADLAKAEAAVRR 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728663866  81 NVHVQLTEPQKVGIASFCpWNIGPGKCFPSGFYRDLNAGNFKGACAQIKRWVWDAGRDCRirenncyGQVIRRDQESELT 160
Cdd:COG3772    70 LVKVPLTQNQFDALVSFA-YNVGAGAFCRSTLLRKLNAGDYAGACDELLRWVYAGGKVLP-------GLVRRREAERALC 141


                  ...
gi 1728663866 161 CWG 163
Cdd:COG3772   142 LGG 144
 
Name Accession Description Interval E-value
RrrD COG3772
Phage-related lysozyme (muramidase), GH24 family [Cell wall/membrane/envelope biogenesis];
1-163 1.10e-48

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


Pssm-ID: 442986 [Multi-domain]  Cd Length: 146  Bit Score: 154.23  E-value: 1.10e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728663866   1 MLGLIAAGAsapVLMAQFqhekEGTSLTAYQDkSRGIWTICGGVTyvdGKPVIKGMTLTRAQCDKIDKAEQAKALAWVDR 80
Cdd:COG3772     1 MMKTSAAGL---ALIKEF----EGFRLKAYRD-PAGVWTIGYGHT---GKDVKPGDTITEEEAEALLAADLAKAEAAVRR 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728663866  81 NVHVQLTEPQKVGIASFCpWNIGPGKCFPSGFYRDLNAGNFKGACAQIKRWVWDAGRDCRirenncyGQVIRRDQESELT 160
Cdd:COG3772    70 LVKVPLTQNQFDALVSFA-YNVGAGAFCRSTLLRKLNAGDYAGACDELLRWVYAGGKVLP-------GLVRRREAERALC 141


                  ...
gi 1728663866 161 CWG 163
Cdd:COG3772   142 LGG 144
endolysin_R21-like cd16900
endolysin R21-like proteins; Unlike T4 E phage lysozyme, the endolysin R21 from Enterobacteria ...
 7-161 2.40e-47

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: 150.40  E-value: 2.40e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728663866   7 AGASAPVLmAQFQHEKEGTSLTAYQDkSRGIWTICGGVTyvdGKPVIKGMTLTRAQCDKIDKAEQAKALAWVDRNVHVQL 86
Cdd:cd16900     1 AGALALAA-AALVGPWEGLRLTAYRD-PVGVWTVCYGHT---GGDVKPGMRYTPAECDALLAKDLQEAAAAVDRCVKVPL 75

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1728663866  87 TEPQKVGIASFCpWNIGPGKCFPSGFYRDLNAGNFKGACAQIKRWVWDAGRdcrirenNCYGQVIRRDQESELTC 161
Cdd:cd16900    76 PDPQRAALASFA-YNVGVGAFCRSTLLRKLNAGDRRGACDELTRWVYAGGR-------VLRGLVNRREAERALCL 142
Phage_lysozyme pfam00959
Phage lysozyme; This family includes lambda phage lysozyme and E. coli endolysin.
 37-154 9.11e-19

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


Pssm-ID: 395766 [Multi-domain]  Cd Length: 107  Bit Score: 76.62  E-value: 9.11e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728663866  37 IWTICGGVtyvDGKPVIKGMTLTRAQCDKIDKAEQAKALAWVDRNVHVQLTEPQKVGIASFCPWNIGPGKCFPSGFYRDL 116
Cdd:pfam00959   1 YWTIGIGH---NGKDVSPHPRATKSEAAGRLQIDLDTAERCINQYHKVKDFNPNQQDALVSLAFNVGCGKRGFSTLLRAG 77

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1728663866 117 NAGNFKGACAQIKRWVwDAGRdcrirenNCYGQVIRRD 154
Cdd:pfam00959  78 NIGQWIKACSAIWKSL-KAGK-------VYNGLVNRRE 107
 
Name Accession Description Interval E-value
RrrD COG3772
Phage-related lysozyme (muramidase), GH24 family [Cell wall/membrane/envelope biogenesis];
1-163 1.10e-48

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


Pssm-ID: 442986 [Multi-domain]  Cd Length: 146  Bit Score: 154.23  E-value: 1.10e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728663866   1 MLGLIAAGAsapVLMAQFqhekEGTSLTAYQDkSRGIWTICGGVTyvdGKPVIKGMTLTRAQCDKIDKAEQAKALAWVDR 80
Cdd:COG3772     1 MMKTSAAGL---ALIKEF----EGFRLKAYRD-PAGVWTIGYGHT---GKDVKPGDTITEEEAEALLAADLAKAEAAVRR 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728663866  81 NVHVQLTEPQKVGIASFCpWNIGPGKCFPSGFYRDLNAGNFKGACAQIKRWVWDAGRDCRirenncyGQVIRRDQESELT 160
Cdd:COG3772    70 LVKVPLTQNQFDALVSFA-YNVGAGAFCRSTLLRKLNAGDYAGACDELLRWVYAGGKVLP-------GLVRRREAERALC 141


                  ...
gi 1728663866 161 CWG 163
Cdd:COG3772   142 LGG 144
endolysin_R21-like cd16900
endolysin R21-like proteins; Unlike T4 E phage lysozyme, the endolysin R21 from Enterobacteria ...
 7-161 2.40e-47

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: 150.40  E-value: 2.40e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728663866   7 AGASAPVLmAQFQHEKEGTSLTAYQDkSRGIWTICGGVTyvdGKPVIKGMTLTRAQCDKIDKAEQAKALAWVDRNVHVQL 86
Cdd:cd16900     1 AGALALAA-AALVGPWEGLRLTAYRD-PVGVWTVCYGHT---GGDVKPGMRYTPAECDALLAKDLQEAAAAVDRCVKVPL 75

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1728663866  87 TEPQKVGIASFCpWNIGPGKCFPSGFYRDLNAGNFKGACAQIKRWVWDAGRdcrirenNCYGQVIRRDQESELTC 161
Cdd:cd16900    76 PDPQRAALASFA-YNVGVGAFCRSTLLRKLNAGDRRGACDELTRWVYAGGR-------VLRGLVNRREAERALCL 142
lyz_endolysin_autolysin cd00737
endolysin and autolysin; The dsDNA phages of eubacteria use endolysins or muralytic enzymes in ...
 14-137 1.29e-24

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: 92.58  E-value: 1.29e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728663866  14 LMAQFqhekEGTSLTAYQDkSRGIWTIcgGVTYVDGKPVIKGMTLTRAQCDKIDKAEQAKALAWVDRNVHVQLTEPQKVG 93
Cdd:cd00737     4 LIKEF----EGLRLKAYRD-PAGVWTI--GYGHTGGVVVKPGDTITEAQAEALLRQDLARFEAAVNRLVKVPLNQNQFDA 76

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1728663866  94 IASFCpWNIGPGKCFPSGFYRDLNAGNFKGACAQIKRWVWDAGR 137
Cdd:cd00737    77 LVSFA-FNVGAGAFKSSTLLRKLNAGDYAGAADEFLRWNKAGGK 119
Phage_lysozyme pfam00959
Phage lysozyme; This family includes lambda phage lysozyme and E. coli endolysin.
 37-154 9.11e-19

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


Pssm-ID: 395766 [Multi-domain]  Cd Length: 107  Bit Score: 76.62  E-value: 9.11e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728663866  37 IWTICGGVtyvDGKPVIKGMTLTRAQCDKIDKAEQAKALAWVDRNVHVQLTEPQKVGIASFCPWNIGPGKCFPSGFYRDL 116
Cdd:pfam00959   1 YWTIGIGH---NGKDVSPHPRATKSEAAGRLQIDLDTAERCINQYHKVKDFNPNQQDALVSLAFNVGCGKRGFSTLLRAG 77

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1728663866 117 NAGNFKGACAQIKRWVwDAGRdcrirenNCYGQVIRRD 154
Cdd:pfam00959  78 NIGQWIKACSAIWKSL-KAGK-------VYNGLVNRRE 107
lyz_P1 cd16901
P1 lysozyme Lyz-like proteins; Enterobacteria phage P1 lysozyme Lyz is secreted to the ...
 23-159 2.10e-16

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: 71.48  E-value: 2.10e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728663866  23 EGTSLTAYQDkSRGIWTICGGVTYvdgkPVIKGMTLTRAQCDK-----IDKAEQAkalawVDRNVH-VQLTEPQKVGIAS 96
Cdd:cd16901    14 EGCRRDPYKC-PAGVPTIGIGSTH----GVKPGDRYTDEQAAKrlakdIKKAERC-----VNRCFNgVPLPQGEFDAYVS 83

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1728663866  97 FCpWNIGPGKCFPSGFYRDLNAGNFKGACAQIKRWVWDAGRDcrirennCYGQVIRRDQESEL 159
Cdd:cd16901    84 FA-FNVGCGAFCKSTIYKKLQAGDYAAACNQLPRWVYAGGKV-------LPGLVTRRQKERAL 138
T4-like_lys cd00735
bacteriophage T4-like lysozymes; Bacteriophage T4-like lysozymes hydrolyze the beta-1, ...
 21-133 9.22e-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: 34.66  E-value: 9.22e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728663866  21 EKEGTSLTAYQDkSRGIWTICGGVTYVDGKPVIKGMTLTRAQCDKIDKAEQAKALAWVDRN-----VHVQLTEPQKVGIA 95
Cdd:cd00735     8 QDEGYRLKAYKD-TEGYPTIGIGHLIGKKGASLTNGTITKDEAEALFEQDVDRAVRDMLRNpklapVYAQLNAARRMALI 86

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1728663866  96 SFCpWNIGPGKC--FPsGFYRDLNAGNFKGACAQIKRWVW 133
Cdd:cd00735    87 NMA-FQMGVGGLakFK-NMLAAIKAGDWEEAADGMLNSLW 124
 
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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