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Conserved domains on  [gi|2054628280|tpg|DAM25255|]
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MAG TPA: lysozyme [Caudoviricetes sp.]

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 ...
15-153 3.73e-84

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: 243.28  E-value: 3.73e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2054628280  15 TSQAGLELIGNAEGCRRDPYKCPADVWTDGVGNTHGVKPGVRKTDQQIAADWKKNIIAAEQCVNRYAAGDKLSQGAFDAA 94
Cdd:cd16901     2 TSAAGLELIANAEGCRRDPYKCPAGVPTIGIGSTHGVKPGDRYTDEQAAKRLAKDIKKAERCVNRCFNGVPLPQGEFDAY 81
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2054628280  95 VSITFNAGCATMQKSTMFRLFRQGDAAAACEQFPRWVYASGVKLNGLVIRRDKERALCL 153
Cdd:cd16901    82 VSFAFNVGCGAFCKSTIYKKLQAGDYAAACNQLPRWVYAGGKVLPGLVTRRQKERALCL 140
 
Name Accession Description Interval E-value
lyz_P1 cd16901
P1 lysozyme Lyz-like proteins; Enterobacteria phage P1 lysozyme Lyz is secreted to the ...
15-153 3.73e-84

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: 243.28  E-value: 3.73e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2054628280  15 TSQAGLELIGNAEGCRRDPYKCPADVWTDGVGNTHGVKPGVRKTDQQIAADWKKNIIAAEQCVNRYAAGDKLSQGAFDAA 94
Cdd:cd16901     2 TSAAGLELIANAEGCRRDPYKCPAGVPTIGIGSTHGVKPGDRYTDEQAAKRLAKDIKKAERCVNRCFNGVPLPQGEFDAY 81
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2054628280  95 VSITFNAGCATMQKSTMFRLFRQGDAAAACEQFPRWVYASGVKLNGLVIRRDKERALCL 153
Cdd:cd16901    82 VSFAFNVGCGAFCKSTIYKKLQAGDYAAACNQLPRWVYAGGKVLPGLVTRRQKERALCL 140
RrrD COG3772
Phage-related lysozyme (muramidase), GH24 family [Cell wall/membrane/envelope biogenesis];
14-154 1.91e-60

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


Pssm-ID: 442986 [Multi-domain]  Cd Length: 146  Bit Score: 183.50  E-value: 1.91e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2054628280  14 KTSQAGLELIGNAEGCRRDPYKCPADVWTDGVGNT-HGVKPGVRKTDQQIAADWKKNIIAAEQCVNRYAaGDKLSQGAFD 92
Cdd:COG3772     3 KTSAAGLALIKEFEGFRLKAYRDPAGVWTIGYGHTgKDVKPGDTITEEEAEALLAADLAKAEAAVRRLV-KVPLTQNQFD 81
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2054628280  93 AAVSITFNAGCATMQKSTMFRLFRQGDAAAACEQFPRWVYASGVKLNGLVIRRDKERALCLA 154
Cdd:COG3772    82 ALVSFAYNVGAGAFCRSTLLRKLNAGDYAGACDELLRWVYAGGKVLPGLVRRREAERALCLG 143
Phage_lysozyme pfam00959
Phage lysozyme; This family includes lambda phage lysozyme and E. coli endolysin.
40-146 1.09e-31

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


Pssm-ID: 395766 [Multi-domain]  Cd Length: 107  Bit Score: 109.37  E-value: 1.09e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2054628280  40 VWTDGVG-NTHGVKPGVRKTDQQIAADWKKNIIAAEQCVNRYAAGDKLSQGAFDAAVSITFNAGCATMQKSTMFRLFRQG 118
Cdd:pfam00959   1 YWTIGIGhNGKDVSPHPRATKSEAAGRLQIDLDTAERCINQYHKVKDFNPNQQDALVSLAFNVGCGKRGFSTLLRAGNIG 80
                          90       100
                  ....*....|....*....|....*...
gi 2054628280 119 DAAAACEQFPRWVYAsGVKLNGLVIRRD 146
Cdd:pfam00959  81 QWIKACSAIWKSLKA-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 ...
15-153 3.73e-84

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: 243.28  E-value: 3.73e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2054628280  15 TSQAGLELIGNAEGCRRDPYKCPADVWTDGVGNTHGVKPGVRKTDQQIAADWKKNIIAAEQCVNRYAAGDKLSQGAFDAA 94
Cdd:cd16901     2 TSAAGLELIANAEGCRRDPYKCPAGVPTIGIGSTHGVKPGDRYTDEQAAKRLAKDIKKAERCVNRCFNGVPLPQGEFDAY 81
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2054628280  95 VSITFNAGCATMQKSTMFRLFRQGDAAAACEQFPRWVYASGVKLNGLVIRRDKERALCL 153
Cdd:cd16901    82 VSFAFNVGCGAFCKSTIYKKLQAGDYAAACNQLPRWVYAGGKVLPGLVTRRQKERALCL 140
RrrD COG3772
Phage-related lysozyme (muramidase), GH24 family [Cell wall/membrane/envelope biogenesis];
14-154 1.91e-60

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


Pssm-ID: 442986 [Multi-domain]  Cd Length: 146  Bit Score: 183.50  E-value: 1.91e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2054628280  14 KTSQAGLELIGNAEGCRRDPYKCPADVWTDGVGNT-HGVKPGVRKTDQQIAADWKKNIIAAEQCVNRYAaGDKLSQGAFD 92
Cdd:COG3772     3 KTSAAGLALIKEFEGFRLKAYRDPAGVWTIGYGHTgKDVKPGDTITEEEAEALLAADLAKAEAAVRRLV-KVPLTQNQFD 81
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2054628280  93 AAVSITFNAGCATMQKSTMFRLFRQGDAAAACEQFPRWVYASGVKLNGLVIRRDKERALCLA 154
Cdd:COG3772    82 ALVSFAYNVGAGAFCRSTLLRKLNAGDYAGACDELLRWVYAGGKVLPGLVRRREAERALCLG 143
lyz_endolysin_autolysin cd00737
endolysin and autolysin; The dsDNA phages of eubacteria use endolysins or muralytic enzymes in ...
19-153 1.39e-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: 153.06  E-value: 1.39e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2054628280  19 GLELIGNAEGCRRDPYKCPADVWTDGVGNTHGV--KPGVRKTDQQIAADWKKNIIAAEQCVNRyAAGDKLSQGAFDAAVS 96
Cdd:cd00737     1 GLDLIKEFEGLRLKAYRDPAGVWTIGYGHTGGVvvKPGDTITEAQAEALLRQDLARFEAAVNR-LVKVPLNQNQFDALVS 79
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2054628280  97 ITFNAGCATMQKSTMFRLFRQGDAAAACEQFPRWVYASGVKLNGLVIRRDKERALCL 153
Cdd:cd00737    80 FAFNVGAGAFKSSTLLRKLNAGDYAGAADEFLRWNKAGGKVLPGLVRRRAAEAALFL 136
Phage_lysozyme pfam00959
Phage lysozyme; This family includes lambda phage lysozyme and E. coli endolysin.
40-146 1.09e-31

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


Pssm-ID: 395766 [Multi-domain]  Cd Length: 107  Bit Score: 109.37  E-value: 1.09e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2054628280  40 VWTDGVG-NTHGVKPGVRKTDQQIAADWKKNIIAAEQCVNRYAAGDKLSQGAFDAAVSITFNAGCATMQKSTMFRLFRQG 118
Cdd:pfam00959   1 YWTIGIGhNGKDVSPHPRATKSEAAGRLQIDLDTAERCINQYHKVKDFNPNQQDALVSLAFNVGCGKRGFSTLLRAGNIG 80
                          90       100
                  ....*....|....*....|....*...
gi 2054628280 119 DAAAACEQFPRWVYAsGVKLNGLVIRRD 146
Cdd:pfam00959  81 QWIKACSAIWKSLKA-GKVYNGLVNRRE 107
endolysin_R21-like cd16900
endolysin R21-like proteins; Unlike T4 E phage lysozyme, the endolysin R21 from Enterobacteria ...
22-153 2.44e-31

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: 109.57  E-value: 2.44e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2054628280  22 LIGNAEGCRRDPYKCPADVWTDGVGNTHG-VKPGVRKTDQQIAADWKKNIIAAEQCVNRYAAgDKLSQGAFDAAVSITFN 100
Cdd:cd16900    11 LVGPWEGLRLTAYRDPVGVWTVCYGHTGGdVKPGMRYTPAECDALLAKDLQEAAAAVDRCVK-VPLPDPQRAALASFAYN 89
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2054628280 101 AGCATMQKSTMFRLFRQGDAAAACEQFPRWVYASGVKLNGLVIRRDKERALCL 153
Cdd:cd16900    90 VGVGAFCRSTLLRKLNAGDRRGACDELTRWVYAGGRVLRGLVNRREAERALCL 142
chitinase-like cd16889
chitinase-like domain; This family includes proteins such as chitinases, chitosanase, pesticin, ...
19-100 5.02e-09

chitinase-like domain; This family includes proteins such as chitinases, chitosanase, pesticin, and endolysin, which are involved in the degradation of 1,4-N-acetyl D-glucosamine linkages in chitin polymers and related activities. Chitinases are enzymes that catalyze the hydrolysis of the beta-1,4-N-acetyl-D-glucosamine linkages in chitin polymers. Chitosanase enzymes hydrolyze chitosan, a biopolymer of beta (1,4)-linked-D-glucosamine (GlcN) residues produced by partial or full deacetylation of chitin. Pesticin (Pst) is a anti-bacterial toxin produced by Yersinia pestis that acts through uptake by the target related bacteria and the hydrolysis of peptidoglycan in the periplasm. 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.


Pssm-ID: 381610  Cd Length: 105  Bit Score: 51.03  E-value: 5.02e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2054628280  19 GLELIGNAEGCRRDPYK-----CPADVWTDGVGNTHGVKPG----------------VRKTDQQIAADWKKNIIAAEQCV 77
Cdd:cd16889     1 WFLLITSLETKGLGPTAvygdgKDPRGYTRGIGVTHGMLRGstsrfpgvdtsnqtnnGASTDSQLAKLAMEGFDPAYRAL 80
                          90       100
                  ....*....|....*....|....*
gi 2054628280  78 NRYAAG--DKLSQGAFDAAVSITFN 100
Cdd:cd16889    81 MRTIAHrdDLSPHVNGCAVIFAGFN 105
T4-like_lys cd00735
bacteriophage T4-like lysozymes; Bacteriophage T4-like lysozymes hydrolyze the beta-1, ...
27-123 2.73e-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: 36.20  E-value: 2.73e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2054628280  27 EGCRRDPYKCPADVWTDGVGNTHGVKP----GVRKTDQQIAA----DWKKNIIAAEQCVNRYAAGDKLSQGAFDAAVSIT 98
Cdd:cd00735    10 EGYRLKAYKDTEGYPTIGIGHLIGKKGasltNGTITKDEAEAlfeqDVDRAVRDMLRNPKLAPVYAQLNAARRMALINMA 89
                          90       100
                  ....*....|....*....|....*.
gi 2054628280  99 FNAGCATMQK-STMFRLFRQGDAAAA 123
Cdd:cd00735    90 FQMGVGGLAKfKNMLAAIKAGDWEEA 115
 
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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