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Conserved domains on  [gi|643016622|gb|AIA84894|]
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DUF847 [uncultured Leptothrix sp.]

Protein Classification

N-acetylmuramidase_GH108 domain-containing protein( domain architecture ID 10530764)

N-acetylmuramidase_GH108 domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ZliS super family cl34694
Lysozyme family protein [General function prediction only];
30-107 5.87e-27

Lysozyme family protein [General function prediction only];


The actual alignment was detected with superfamily member COG3926:

Pssm-ID: 443130 [Multi-domain]  Cd Length: 167  Bit Score: 97.62  E-value: 5.87e-27
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 643016622  30 DADTAVKLILRHEGGKVDNKNDPGGRTNRGVTQRVFTAWLKGQGKSSRDVWTITEAEAISIYKAQYLAPVRYDDLPPG 107
Cdd:COG3926    1 NFDQALDFILKHEGGYVNHPADPGGATNYGITQATLRAYRGLRDVTAGDVRALTREEAKAIYRRDYWDRPRGDELPQG 78
 
Name Accession Description Interval E-value
ZliS COG3926
Lysozyme family protein [General function prediction only];
30-107 5.87e-27

Lysozyme family protein [General function prediction only];


Pssm-ID: 443130 [Multi-domain]  Cd Length: 167  Bit Score: 97.62  E-value: 5.87e-27
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 643016622  30 DADTAVKLILRHEGGKVDNKNDPGGRTNRGVTQRVFTAWLKGQGKSSRDVWTITEAEAISIYKAQYLAPVRYDDLPPG 107
Cdd:COG3926    1 NFDQALDFILKHEGGYVNHPADPGGATNYGITQATLRAYRGLRDVTAGDVRALTREEAKAIYRRDYWDRPRGDELPQG 78
Glyco_hydro_108 pfam05838
Glycosyl hydrolase 108; This family acts as a lysozyme (N-acetylmuramidase), EC:3.2.1.17. It ...
 35-107 3.18e-26

Glycosyl hydrolase 108; This family acts as a lysozyme (N-acetylmuramidase), EC:3.2.1.17. It contains a conserved EGGY motif near the N-terminus, the glutamic acid within this motif is essential for catalytic activity. In bacteria, it may activate the secretion of large proteins via the breaking and rearrangement of the peptidoglycan layer during secretion. It is frequently found at the N-terminus of proteins containing a C-terminal pfam09374 domain.


Pssm-ID: 428646  Cd Length: 86  Bit Score: 93.01  E-value: 3.18e-26
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 643016622   35 VKLILRHEGGKVDNKNDPGGRTNRGVTQRVFTAWLKGQGKSSRDVWTITEAEAISIYKAQYLAPVRYDDLPPG 107
Cdd:pfam05838   1 LDFILAHEGGYVNDPADPGGATNYGITQATARAWGGRGGIDVADVRDLTRAEAAAIYRRDYWDPPRCDELPPP 73
N-acetylmuramidase_GH108 cd13926
N-acetylmuramidase domain of the glycosyl hydrolase 108 family; This domain acts as a lysozyme ...
 32-107 8.53e-23

N-acetylmuramidase domain of the glycosyl hydrolase 108 family; This domain acts as a lysozyme (N-acetylmuramidase), EC:3.2.1.17. It contains a conserved EGGY motif near the N-terminus, the glutamic acid within this motif is essential for catalytic activity. In bacteria, it may activate the secretion of large proteins via the breaking and rearrangement of the peptidoglycan layer during secretion. It is frequently found at the N-terminus of proteins containing a peptidoglycan binding domain.


Pssm-ID: 381608  Cd Length: 91  Bit Score: 84.52  E-value: 8.53e-23
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 643016622  32 DTAVKLILRHEGGKVDNKNDPGGRTNRGVTQRVFTAWlKGQGKSSRDVWTITEAEAISIYKAQYLAPVRYDDLPPG 107
Cdd:cd13926    4 DQAIERVLAHEGGYVNDPKDPGGETNYGITKRTARAL-GYRTVTKGDIKALTREQAVEIYRRDYWDAPRCDELPAG 78
 
Name Accession Description Interval E-value
ZliS COG3926
Lysozyme family protein [General function prediction only];
30-107 5.87e-27

Lysozyme family protein [General function prediction only];


Pssm-ID: 443130 [Multi-domain]  Cd Length: 167  Bit Score: 97.62  E-value: 5.87e-27
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 643016622  30 DADTAVKLILRHEGGKVDNKNDPGGRTNRGVTQRVFTAWLKGQGKSSRDVWTITEAEAISIYKAQYLAPVRYDDLPPG 107
Cdd:COG3926    1 NFDQALDFILKHEGGYVNHPADPGGATNYGITQATLRAYRGLRDVTAGDVRALTREEAKAIYRRDYWDRPRGDELPQG 78
Glyco_hydro_108 pfam05838
Glycosyl hydrolase 108; This family acts as a lysozyme (N-acetylmuramidase), EC:3.2.1.17. It ...
 35-107 3.18e-26

Glycosyl hydrolase 108; This family acts as a lysozyme (N-acetylmuramidase), EC:3.2.1.17. It contains a conserved EGGY motif near the N-terminus, the glutamic acid within this motif is essential for catalytic activity. In bacteria, it may activate the secretion of large proteins via the breaking and rearrangement of the peptidoglycan layer during secretion. It is frequently found at the N-terminus of proteins containing a C-terminal pfam09374 domain.


Pssm-ID: 428646  Cd Length: 86  Bit Score: 93.01  E-value: 3.18e-26
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 643016622   35 VKLILRHEGGKVDNKNDPGGRTNRGVTQRVFTAWLKGQGKSSRDVWTITEAEAISIYKAQYLAPVRYDDLPPG 107
Cdd:pfam05838   1 LDFILAHEGGYVNDPADPGGATNYGITQATARAWGGRGGIDVADVRDLTRAEAAAIYRRDYWDPPRCDELPPP 73
N-acetylmuramidase_GH108 cd13926
N-acetylmuramidase domain of the glycosyl hydrolase 108 family; This domain acts as a lysozyme ...
 32-107 8.53e-23

N-acetylmuramidase domain of the glycosyl hydrolase 108 family; This domain acts as a lysozyme (N-acetylmuramidase), EC:3.2.1.17. It contains a conserved EGGY motif near the N-terminus, the glutamic acid within this motif is essential for catalytic activity. In bacteria, it may activate the secretion of large proteins via the breaking and rearrangement of the peptidoglycan layer during secretion. It is frequently found at the N-terminus of proteins containing a peptidoglycan binding domain.


Pssm-ID: 381608  Cd Length: 91  Bit Score: 84.52  E-value: 8.53e-23
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 643016622  32 DTAVKLILRHEGGKVDNKNDPGGRTNRGVTQRVFTAWlKGQGKSSRDVWTITEAEAISIYKAQYLAPVRYDDLPPG 107
Cdd:cd13926    4 DQAIERVLAHEGGYVNDPKDPGGETNYGITKRTARAL-GYRTVTKGDIKALTREQAVEIYRRDYWDAPRCDELPAG 78
 
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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