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Conserved domains on  [gi|1879587989|gb|QLQ99307|]
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lysozyme [Providencia alcalifaciens]

Protein Classification

lysozyme( domain architecture ID 13014134)

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
endolysin_R21-like cd16900
endolysin R21-like proteins; Unlike T4 E phage lysozyme, the endolysin R21 from Enterobacteria ...
 10-151 4.08e-79

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: 232.06  E-value: 4.08e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879587989  10 AGGLISLTVGMIAYFEGVEYKPYKDVVGVTTVCFGHTGADIIPTKTYTESECLALLEKDLNKVRKGVDPLIKVDIDDNTR 89
Cdd:cd16900     1 AGALALAAAALVGPWEGLRLTAYRDPVGVWTVCYGHTGGDVKPGMRYTPAECDALLAKDLQEAAAAVDRCVKVPLPDPQR 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1879587989  90 AAIYSFAYNVGTGAFARSTMLKKLNAGDIDGACNELKRWTYAGGKEWKGLITRREIENAVCL 151
Cdd:cd16900    81 AALASFAYNVGVGAFCRSTLLRKLNAGDRRGACDELTRWVYAGGRVLRGLVNRREAERALCL 142
 
Name Accession Description Interval E-value
endolysin_R21-like cd16900
endolysin R21-like proteins; Unlike T4 E phage lysozyme, the endolysin R21 from Enterobacteria ...
 10-151 4.08e-79

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: 232.06  E-value: 4.08e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879587989  10 AGGLISLTVGMIAYFEGVEYKPYKDVVGVTTVCFGHTGADIIPTKTYTESECLALLEKDLNKVRKGVDPLIKVDIDDNTR 89
Cdd:cd16900     1 AGALALAAAALVGPWEGLRLTAYRDPVGVWTVCYGHTGGDVKPGMRYTPAECDALLAKDLQEAAAAVDRCVKVPLPDPQR 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1879587989  90 AAIYSFAYNVGTGAFARSTMLKKLNAGDIDGACNELKRWTYAGGKEWKGLITRREIENAVCL 151
Cdd:cd16900    81 AALASFAYNVGVGAFCRSTLLRKLNAGDRRGACDELTRWVYAGGRVLRGLVNRREAERALCL 142
RrrD COG3772
Phage-related lysozyme (muramidase), GH24 family [Cell wall/membrane/envelope biogenesis];
20-152 1.03e-66

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


Pssm-ID: 442986 [Multi-domain]  Cd Length: 146  Bit Score: 200.45  E-value: 1.03e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879587989  20 MIAYFEGVEYKPYKDVVGVTTVCFGHTGADIIPTKTYTESECLALLEKDLNKVRKGVDPLIKVDIDDNTRAAIYSFAYNV 99
Cdd:COG3772    11 LIKEFEGFRLKAYRDPAGVWTIGYGHTGKDVKPGDTITEEEAEALLAADLAKAEAAVRRLVKVPLTQNQFDALVSFAYNV 90

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1879587989 100 GTGAFARSTMLKKLNAGDIDGACNELKRWTYAGGKEWKGLITRREIENAVCLG 152
Cdd:COG3772    91 GAGAFCRSTLLRKLNAGDYAGACDELLRWVYAGGKVLPGLVRRREAERALCLG 143
Phage_lysozyme pfam00959
Phage lysozyme; This family includes lambda phage lysozyme and E. coli endolysin.
 40-144 1.78e-29

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


Pssm-ID: 395766 [Multi-domain]  Cd Length: 107  Bit Score: 104.74  E-value: 1.78e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879587989  40 TVCFGHTGADIIPTKTYTESECLALLEKDLNKVRKGVDPLIKV-DIDDNTRAAIYSFAYNVGTGAFARSTMLKKLNAGDI 118
Cdd:pfam00959   3 TIGIGHNGKDVSPHPRATKSEAAGRLQIDLDTAERCINQYHKVkDFNPNQQDALVSLAFNVGCGKRGFSTLLRAGNIGQW 82

                          90       100
                  ....*....|....*....|....*.
gi 1879587989 119 DGACNELKRWTYAgGKEWKGLITRRE 144
Cdd:pfam00959  83 IKACSAIWKSLKA-GKVYNGLVNRRE 107
5 PHA02596
baseplate hub subunit and tail lysozyme; Provisional
 20-131 2.43e-09

baseplate hub subunit and tail lysozyme; Provisional


Pssm-ID: 222900 [Multi-domain]  Cd Length: 576  Bit Score: 55.53  E-value: 2.43e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879587989  20 MIAYFEGVEYKPYKDVVGVTTVCFGHTgadIIPTKT----------------------YTESECLALLEKDLNKVRKGVD 77
Cdd:PHA02596  178 MLRRDEGIRLKVYWDSEGYPTIGIGHL---IIREKTrdmaqinkllskqvgrevtggrITAEEASKLFARDLAKVQRDIS 254

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879587989  78 PLIKV-----DIDDNTRAAIYSFAYNVGTGAFAR-STMLKKLNAGDIDGACNELKRWTYA 131
Cdd:PHA02596  255 RHSKVgpvynKLNRSRQMALENMAFQMGVGGVAKfKNMLAAMLAGDWKKAYDALRDSLWA 314
 
Name Accession Description Interval E-value
endolysin_R21-like cd16900
endolysin R21-like proteins; Unlike T4 E phage lysozyme, the endolysin R21 from Enterobacteria ...
 10-151 4.08e-79

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: 232.06  E-value: 4.08e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879587989  10 AGGLISLTVGMIAYFEGVEYKPYKDVVGVTTVCFGHTGADIIPTKTYTESECLALLEKDLNKVRKGVDPLIKVDIDDNTR 89
Cdd:cd16900     1 AGALALAAAALVGPWEGLRLTAYRDPVGVWTVCYGHTGGDVKPGMRYTPAECDALLAKDLQEAAAAVDRCVKVPLPDPQR 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1879587989  90 AAIYSFAYNVGTGAFARSTMLKKLNAGDIDGACNELKRWTYAGGKEWKGLITRREIENAVCL 151
Cdd:cd16900    81 AALASFAYNVGVGAFCRSTLLRKLNAGDRRGACDELTRWVYAGGRVLRGLVNRREAERALCL 142
RrrD COG3772
Phage-related lysozyme (muramidase), GH24 family [Cell wall/membrane/envelope biogenesis];
20-152 1.03e-66

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


Pssm-ID: 442986 [Multi-domain]  Cd Length: 146  Bit Score: 200.45  E-value: 1.03e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879587989  20 MIAYFEGVEYKPYKDVVGVTTVCFGHTGADIIPTKTYTESECLALLEKDLNKVRKGVDPLIKVDIDDNTRAAIYSFAYNV 99
Cdd:COG3772    11 LIKEFEGFRLKAYRDPAGVWTIGYGHTGKDVKPGDTITEEEAEALLAADLAKAEAAVRRLVKVPLTQNQFDALVSFAYNV 90

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1879587989 100 GTGAFARSTMLKKLNAGDIDGACNELKRWTYAGGKEWKGLITRREIENAVCLG 152
Cdd:COG3772    91 GAGAFCRSTLLRKLNAGDYAGACDELLRWVYAGGKVLPGLVRRREAERALCLG 143
lyz_endolysin_autolysin cd00737
endolysin and autolysin; The dsDNA phages of eubacteria use endolysins or muralytic enzymes in ...
 20-151 5.87e-52

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: 162.69  E-value: 5.87e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879587989  20 MIAYFEGVEYKPYKDVVGVTTVCFGHTGADII-PTKTYTESECLALLEKDLNKVRKGVDPLIKVDIDDNTRAAIYSFAYN 98
Cdd:cd00737     4 LIKEFEGLRLKAYRDPAGVWTIGYGHTGGVVVkPGDTITEAQAEALLRQDLARFEAAVNRLVKVPLNQNQFDALVSFAFN 83

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1879587989  99 VGTGAFARSTMLKKLNAGDIDGACNELKRWTYAGGKEWKGLITRREIENAVCL 151
Cdd:cd00737    84 VGAGAFKSSTLLRKLNAGDYAGAADEFLRWNKAGGKVLPGLVRRRAAEAALFL 136
lyz_P1 cd16901
P1 lysozyme Lyz-like proteins; Enterobacteria phage P1 lysozyme Lyz is secreted to the ...
 20-151 4.01e-40

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: 133.12  E-value: 4.01e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879587989  20 MIAYFEGVEYKPYKDVVGVTTVCFGHTGAdIIPTKTYTESECLALLEKDLNKVRKGV-DPLIKVDIDDNTRAAIYSFAYN 98
Cdd:cd16901     9 LIANAEGCRRDPYKCPAGVPTIGIGSTHG-VKPGDRYTDEQAAKRLAKDIKKAERCVnRCFNGVPLPQGEFDAYVSFAFN 87

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1879587989  99 VGTGAFARSTMLKKLNAGDIDGACNELKRWTYAGGKEWKGLITRREIENAVCL 151
Cdd:cd16901    88 VGCGAFCKSTIYKKLQAGDYAAACNQLPRWVYAGGKVLPGLVTRRQKERALCL 140
Phage_lysozyme pfam00959
Phage lysozyme; This family includes lambda phage lysozyme and E. coli endolysin.
 40-144 1.78e-29

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


Pssm-ID: 395766 [Multi-domain]  Cd Length: 107  Bit Score: 104.74  E-value: 1.78e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879587989  40 TVCFGHTGADIIPTKTYTESECLALLEKDLNKVRKGVDPLIKV-DIDDNTRAAIYSFAYNVGTGAFARSTMLKKLNAGDI 118
Cdd:pfam00959   3 TIGIGHNGKDVSPHPRATKSEAAGRLQIDLDTAERCINQYHKVkDFNPNQQDALVSLAFNVGCGKRGFSTLLRAGNIGQW 82

                          90       100
                  ....*....|....*....|....*.
gi 1879587989 119 DGACNELKRWTYAgGKEWKGLITRRE 144
Cdd:pfam00959  83 IKACSAIWKSLKA-GKVYNGLVNRRE 107
T4-like_lys cd00735
bacteriophage T4-like lysozymes; Bacteriophage T4-like lysozymes hydrolyze the beta-1, ...
 20-131 9.30e-14

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: 65.09  E-value: 9.30e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879587989  20 MIAYFEGVEYKPYKDVVGVTTVCFGHTgadIIPTK------TYTESECLALLEKDLNKVRKGVDPLIKVDI-----DDNT 88
Cdd:cd00735     5 MLRQDEGYRLKAYKDTEGYPTIGIGHL---IGKKGasltngTITKDEAEALFEQDVDRAVRDMLRNPKLAPvyaqlNAAR 81

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1879587989  89 RAAIYSFAYNVGTGAFAR-STMLKKLNAGDIDGACNELKRWTYA 131
Cdd:cd00735    82 RMALINMAFQMGVGGLAKfKNMLAAIKAGDWEEAADGMLNSLWA 125
5 PHA02596
baseplate hub subunit and tail lysozyme; Provisional
 20-131 2.43e-09

baseplate hub subunit and tail lysozyme; Provisional


Pssm-ID: 222900 [Multi-domain]  Cd Length: 576  Bit Score: 55.53  E-value: 2.43e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879587989  20 MIAYFEGVEYKPYKDVVGVTTVCFGHTgadIIPTKT----------------------YTESECLALLEKDLNKVRKGVD 77
Cdd:PHA02596  178 MLRRDEGIRLKVYWDSEGYPTIGIGHL---IIREKTrdmaqinkllskqvgrevtggrITAEEASKLFARDLAKVQRDIS 254

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879587989  78 PLIKV-----DIDDNTRAAIYSFAYNVGTGAFAR-STMLKKLNAGDIDGACNELKRWTYA 131
Cdd:PHA02596  255 RHSKVgpvynKLNRSRQMALENMAFQMGVGGVAKfKNMLAAMLAGDWKKAYDALRDSLWA 314
 
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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