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Conserved domains on  [gi|1378935781|gb|AWA52602|]
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hypothetical protein CLQ69_16860 [Klebsiella pneumoniae subsp. pneumoniae]

Protein Classification

glycoside hydrolase family 108 protein( domain architecture ID 11467621)

glycoside hydrolase family 108 protein may function as a lysozyme (N-acetylmuramidase), catalyzing the hydrolysis of (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
ZliS COG3926
Lysozyme family protein [General function prediction only];
4-178 1.47e-64

Lysozyme family protein [General function prediction only];


:

Pssm-ID: 443130 [Multi-domain]  Cd Length: 167  Bit Score: 195.46  E-value: 1.47e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1378935781   4 DQIIEGILGKEDGYVDHPSDKGGPTRWGITQTTARAH-----GYTGDMRNLPRETAKQILLSDYWTGPRFDQVAAlstLL 78
Cdd:COG3926     3 DQALDFILKHEGGYVNHPADPGGATNYGITQATLRAYrglrdVTAGDVRALTREEAKAIYRRDYWDRPRGDELPQ---GL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1378935781  79 ADELCDTGVNMGPSVASKFFQRWLTAMnmrgklyPDLIPDGAIGPRTITALKGYlsargkeGEQVLVRALNCSQGARYLE 158
Cdd:COG3926    80 AAEVFDFAVNSGPGRAIKLLQRALGAL-------PDVTVDGIIGPKTLAALNAA-------DPAVLIDAYCDARLAYYRS 145

                         170       180
                  ....*....|....*....|
gi 1378935781 159 LAEGREANEDFLYGWVKERV 178
Cdd:COG3926   146 LVERRPSQEKFLRGWLRRVE 165
 
Name Accession Description Interval E-value
ZliS COG3926
Lysozyme family protein [General function prediction only];
4-178 1.47e-64

Lysozyme family protein [General function prediction only];


Pssm-ID: 443130 [Multi-domain]  Cd Length: 167  Bit Score: 195.46  E-value: 1.47e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1378935781   4 DQIIEGILGKEDGYVDHPSDKGGPTRWGITQTTARAH-----GYTGDMRNLPRETAKQILLSDYWTGPRFDQVAAlstLL 78
Cdd:COG3926     3 DQALDFILKHEGGYVNHPADPGGATNYGITQATLRAYrglrdVTAGDVRALTREEAKAIYRRDYWDRPRGDELPQ---GL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1378935781  79 ADELCDTGVNMGPSVASKFFQRWLTAMnmrgklyPDLIPDGAIGPRTITALKGYlsargkeGEQVLVRALNCSQGARYLE 158
Cdd:COG3926    80 AAEVFDFAVNSGPGRAIKLLQRALGAL-------PDVTVDGIIGPKTLAALNAA-------DPAVLIDAYCDARLAYYRS 145

                         170       180
                  ....*....|....*....|
gi 1378935781 159 LAEGREANEDFLYGWVKERV 178
Cdd:COG3926   146 LVERRPSQEKFLRGWLRRVE 165
N-acetylmuramidase_GH108 cd13926
N-acetylmuramidase domain of the glycosyl hydrolase 108 family; This domain acts as a lysozyme ...
 1-90 2.19e-37

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: 124.19  E-value: 2.19e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1378935781   1 MTADQIIEGILGKEDGYVDHPSDKGGPTRWGITQTTARAHGY----TGDMRNLPRETAKQILLSDYWTGPRFDqvaALST 76
Cdd:cd13926     1 ATFDQAIERVLAHEGGYVNDPKDPGGETNYGITKRTARALGYrtvtKGDIKALTREQAVEIYRRDYWDAPRCD---ELPA 77

                          90
                  ....*....|....
gi 1378935781  77 LLADELCDTGVNMG 90
Cdd:cd13926    78 GVALEVFDAAVNSG 91
Glyco_hydro_108 pfam05838
Glycosyl hydrolase 108; This family acts as a lysozyme (N-acetylmuramidase), EC:3.2.1.17. It ...
 7-90 6.27e-32

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: 109.96  E-value: 6.27e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1378935781   7 IEGILGKEDGYVDHPSDKGGPTRWGITQTTARAHGYTG-----DMRNLPRETAKQILLSDYWTGPRFDQVAAlstLLADE 81
Cdd:pfam05838   1 LDFILAHEGGYVNDPADPGGATNYGITQATARAWGGRGgidvaDVRDLTRAEAAAIYRRDYWDPPRCDELPP---PLALV 77


                  ....*....
gi 1378935781  82 LCDTGVNMG 90
Cdd:pfam05838  78 LFDAAVNSG 86
 
Name Accession Description Interval E-value
ZliS COG3926
Lysozyme family protein [General function prediction only];
4-178 1.47e-64

Lysozyme family protein [General function prediction only];


Pssm-ID: 443130 [Multi-domain]  Cd Length: 167  Bit Score: 195.46  E-value: 1.47e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1378935781   4 DQIIEGILGKEDGYVDHPSDKGGPTRWGITQTTARAH-----GYTGDMRNLPRETAKQILLSDYWTGPRFDQVAAlstLL 78
Cdd:COG3926     3 DQALDFILKHEGGYVNHPADPGGATNYGITQATLRAYrglrdVTAGDVRALTREEAKAIYRRDYWDRPRGDELPQ---GL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1378935781  79 ADELCDTGVNMGPSVASKFFQRWLTAMnmrgklyPDLIPDGAIGPRTITALKGYlsargkeGEQVLVRALNCSQGARYLE 158
Cdd:COG3926    80 AAEVFDFAVNSGPGRAIKLLQRALGAL-------PDVTVDGIIGPKTLAALNAA-------DPAVLIDAYCDARLAYYRS 145

                         170       180
                  ....*....|....*....|
gi 1378935781 159 LAEGREANEDFLYGWVKERV 178
Cdd:COG3926   146 LVERRPSQEKFLRGWLRRVE 165
N-acetylmuramidase_GH108 cd13926
N-acetylmuramidase domain of the glycosyl hydrolase 108 family; This domain acts as a lysozyme ...
 1-90 2.19e-37

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: 124.19  E-value: 2.19e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1378935781   1 MTADQIIEGILGKEDGYVDHPSDKGGPTRWGITQTTARAHGY----TGDMRNLPRETAKQILLSDYWTGPRFDqvaALST 76
Cdd:cd13926     1 ATFDQAIERVLAHEGGYVNDPKDPGGETNYGITKRTARALGYrtvtKGDIKALTREQAVEIYRRDYWDAPRCD---ELPA 77

                          90
                  ....*....|....
gi 1378935781  77 LLADELCDTGVNMG 90
Cdd:cd13926    78 GVALEVFDAAVNSG 91
Glyco_hydro_108 pfam05838
Glycosyl hydrolase 108; This family acts as a lysozyme (N-acetylmuramidase), EC:3.2.1.17. It ...
 7-90 6.27e-32

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: 109.96  E-value: 6.27e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1378935781   7 IEGILGKEDGYVDHPSDKGGPTRWGITQTTARAHGYTG-----DMRNLPRETAKQILLSDYWTGPRFDQVAAlstLLADE 81
Cdd:pfam05838   1 LDFILAHEGGYVNDPADPGGATNYGITQATARAWGGRGgidvaDVRDLTRAEAAAIYRRDYWDPPRCDELPP---PLALV 77


                  ....*....
gi 1378935781  82 LCDTGVNMG 90
Cdd:pfam05838  78 LFDAAVNSG 86
PG_binding_3 pfam09374
Predicted Peptidoglycan domain; This family contains a potential peptidoglycan binding domain.
 93-178 2.41e-25

Predicted Peptidoglycan domain; This family contains a potential peptidoglycan binding domain.


Pssm-ID: 401356  Cd Length: 76  Bit Score: 92.95  E-value: 2.41e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1378935781  93 VASKFFQRWLtamnmrGKLYPDLIPDGAIGPRTITALKgylsARGKEGEQVLVRALNCSQGARYLELAEGREANEDFLYG 172
Cdd:pfam09374   1 NAVRILQRIL------GGMGPDVKVDGIIGPKTLNAVM----SRNSAGEEVLCKAYGLARRRFYLRLAARRTTNARFLRG 70


                  ....*.
gi 1378935781 173 WVKERV 178
Cdd:pfam09374  71 WVNRLV 76
 
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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