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Conserved domains on  [gi|1130464097|ref|WP_075630605|]
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glycoside hydrolase family 108 protein [Glaesserella parasuis]

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];
9-162 2.72e-71

Lysozyme family protein [General function prediction only];


:

Pssm-ID: 443130 [Multi-domain]  Cd Length: 167  Bit Score: 212.41  E-value: 2.72e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130464097   9 DFNKAFDRVIQHEGGYVNDPRDAGGETKFGITIHTARA-----NGYTGSMFTMTRDDAKQIYLKAFWQRYRCSEFPPELA 83
Cdd:COG3926     1 NFDQALDFILKHEGGYVNHPADPGGATNYGITQATLRAyrglrDVTAGDVRALTREEAKAIYRRDYWDRPRGDELPQGLA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130464097  84 FQFFDACVNHGSGNASRMLQRAVG----VVDDGIIGEITLAAIRKRSTVEVVTLFNAERLEFYTKL----SGFQHFGKGW 155
Cdd:COG3926    81 AEVFDFAVNSGPGRAIKLLQRALGalpdVTVDGIIGPKTLAALNAADPAVLIDAYCDARLAYYRSLverrPSQEKFLRGW 160


                  ....*..
gi 1130464097 156 IRRMAGN 162
Cdd:COG3926   161 LRRVESL 167
 
Name Accession Description Interval E-value
ZliS COG3926
Lysozyme family protein [General function prediction only];
9-162 2.72e-71

Lysozyme family protein [General function prediction only];


Pssm-ID: 443130 [Multi-domain]  Cd Length: 167  Bit Score: 212.41  E-value: 2.72e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130464097   9 DFNKAFDRVIQHEGGYVNDPRDAGGETKFGITIHTARA-----NGYTGSMFTMTRDDAKQIYLKAFWQRYRCSEFPPELA 83
Cdd:COG3926     1 NFDQALDFILKHEGGYVNHPADPGGATNYGITQATLRAyrglrDVTAGDVRALTREEAKAIYRRDYWDRPRGDELPQGLA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130464097  84 FQFFDACVNHGSGNASRMLQRAVG----VVDDGIIGEITLAAIRKRSTVEVVTLFNAERLEFYTKL----SGFQHFGKGW 155
Cdd:COG3926    81 AEVFDFAVNSGPGRAIKLLQRALGalpdVTVDGIIGPKTLAALNAADPAVLIDAYCDARLAYYRSLverrPSQEKFLRGW 160


                  ....*..
gi 1130464097 156 IRRMAGN 162
Cdd:COG3926   161 LRRVESL 167
N-acetylmuramidase_GH108 cd13926
N-acetylmuramidase domain of the glycosyl hydrolase 108 family; This domain acts as a lysozyme ...
 10-94 2.65e-40

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: 131.12  E-value: 2.65e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130464097  10 FNKAFDRVIQHEGGYVNDPRDAGGETKFGITIHTARANGY----TGSMFTMTRDDAKQIYLKAFWQRYRCSEFPPELAFQ 85
Cdd:cd13926     3 FDQAIERVLAHEGGYVNDPKDPGGETNYGITKRTARALGYrtvtKGDIKALTREQAVEIYRRDYWDAPRCDELPAGVALE 82


                  ....*....
gi 1130464097  86 FFDACVNHG 94
Cdd:cd13926    83 VFDAAVNSG 91
Glyco_hydro_108 pfam05838
Glycosyl hydrolase 108; This family acts as a lysozyme (N-acetylmuramidase), EC:3.2.1.17. It ...
 14-94 2.73e-37

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: 123.44  E-value: 2.73e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130464097  14 FDRVIQHEGGYVNDPRDAGGETKFGITIHTARANGYTG-----SMFTMTRDDAKQIYLKAFWQRYRCSEFPPELAFQFFD 88
Cdd:pfam05838   1 LDFILAHEGGYVNDPADPGGATNYGITQATARAWGGRGgidvaDVRDLTRAEAAAIYRRDYWDPPRCDELPPPLALVLFD 80


                  ....*.
gi 1130464097  89 ACVNHG 94
Cdd:pfam05838  81 AAVNSG 86
 
Name Accession Description Interval E-value
ZliS COG3926
Lysozyme family protein [General function prediction only];
9-162 2.72e-71

Lysozyme family protein [General function prediction only];


Pssm-ID: 443130 [Multi-domain]  Cd Length: 167  Bit Score: 212.41  E-value: 2.72e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130464097   9 DFNKAFDRVIQHEGGYVNDPRDAGGETKFGITIHTARA-----NGYTGSMFTMTRDDAKQIYLKAFWQRYRCSEFPPELA 83
Cdd:COG3926     1 NFDQALDFILKHEGGYVNHPADPGGATNYGITQATLRAyrglrDVTAGDVRALTREEAKAIYRRDYWDRPRGDELPQGLA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130464097  84 FQFFDACVNHGSGNASRMLQRAVG----VVDDGIIGEITLAAIRKRSTVEVVTLFNAERLEFYTKL----SGFQHFGKGW 155
Cdd:COG3926    81 AEVFDFAVNSGPGRAIKLLQRALGalpdVTVDGIIGPKTLAALNAADPAVLIDAYCDARLAYYRSLverrPSQEKFLRGW 160


                  ....*..
gi 1130464097 156 IRRMAGN 162
Cdd:COG3926   161 LRRVESL 167
N-acetylmuramidase_GH108 cd13926
N-acetylmuramidase domain of the glycosyl hydrolase 108 family; This domain acts as a lysozyme ...
 10-94 2.65e-40

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: 131.12  E-value: 2.65e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130464097  10 FNKAFDRVIQHEGGYVNDPRDAGGETKFGITIHTARANGY----TGSMFTMTRDDAKQIYLKAFWQRYRCSEFPPELAFQ 85
Cdd:cd13926     3 FDQAIERVLAHEGGYVNDPKDPGGETNYGITKRTARALGYrtvtKGDIKALTREQAVEIYRRDYWDAPRCDELPAGVALE 82


                  ....*....
gi 1130464097  86 FFDACVNHG 94
Cdd:cd13926    83 VFDAAVNSG 91
Glyco_hydro_108 pfam05838
Glycosyl hydrolase 108; This family acts as a lysozyme (N-acetylmuramidase), EC:3.2.1.17. It ...
 14-94 2.73e-37

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: 123.44  E-value: 2.73e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130464097  14 FDRVIQHEGGYVNDPRDAGGETKFGITIHTARANGYTG-----SMFTMTRDDAKQIYLKAFWQRYRCSEFPPELAFQFFD 88
Cdd:pfam05838   1 LDFILAHEGGYVNDPADPGGATNYGITQATARAWGGRGgidvaDVRDLTRAEAAAIYRRDYWDPPRCDELPPPLALVLFD 80


                  ....*.
gi 1130464097  89 ACVNHG 94
Cdd:pfam05838  81 AAVNSG 86
PG_binding_3 pfam09374
Predicted Peptidoglycan domain; This family contains a potential peptidoglycan binding domain.
 97-158 6.57e-06

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


Pssm-ID: 401356  Cd Length: 76  Bit Score: 42.11  E-value: 6.57e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1130464097  97 NASRMLQRAVG-----VVDDGIIGEITLAAIRKRSTV---EVVTLFNAERLEFYTKLSGFQH----FGKGWIRR 158
Cdd:pfam09374   1 NAVRILQRILGgmgpdVKVDGIIGPKTLNAVMSRNSAgeeVLCKAYGLARRRFYLRLAARRTtnarFLRGWVNR 74
 
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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