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Conserved domains on  [gi|2588604132|ref|WP_314396908|]
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glycosyl hydrolase 108 family protein [Leptotrichia shahii]

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];
5-166 4.72e-58

Lysozyme family protein [General function prediction only];


:

Pssm-ID: 443130 [Multi-domain]  Cd Length: 167  Bit Score: 178.90  E-value: 4.72e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2588604132   5 RFLKFFNYILLVEGSYSNDKNDKGGETKYGITKERAREC-----GYKGNMKDLTKAMAQKIYEEKYYKARKLDQVkNDKV 79
Cdd:COG3926     1 NFDQALDFILKHEGGYVNHPADPGGATNYGITQATLRAYrglrdVTAGDVRALTREEAKAIYRRDYWDRPRGDEL-PQGL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2588604132  80 ALSIFDFSVNAG-RYGIKKAQEAVNKVYgknVVSMDGAIGTQTLKYLNEVNPDKFLVVYHSLQREYYKYLAKRDATQNDF 158
Cdd:COG3926    80 AAEVFDFAVNSGpGRAIKLLQRALGALP---DVTVDGIIGPKTLAALNAADPAVLIDAYCDARLAYYRSLVERRPSQEKF 156


                  ....*...
gi 2588604132 159 LTGWLNRV 166
Cdd:COG3926   157 LRGWLRRV 164
 
Name Accession Description Interval E-value
ZliS COG3926
Lysozyme family protein [General function prediction only];
5-166 4.72e-58

Lysozyme family protein [General function prediction only];


Pssm-ID: 443130 [Multi-domain]  Cd Length: 167  Bit Score: 178.90  E-value: 4.72e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2588604132   5 RFLKFFNYILLVEGSYSNDKNDKGGETKYGITKERAREC-----GYKGNMKDLTKAMAQKIYEEKYYKARKLDQVkNDKV 79
Cdd:COG3926     1 NFDQALDFILKHEGGYVNHPADPGGATNYGITQATLRAYrglrdVTAGDVRALTREEAKAIYRRDYWDRPRGDEL-PQGL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2588604132  80 ALSIFDFSVNAG-RYGIKKAQEAVNKVYgknVVSMDGAIGTQTLKYLNEVNPDKFLVVYHSLQREYYKYLAKRDATQNDF 158
Cdd:COG3926    80 AAEVFDFAVNSGpGRAIKLLQRALGALP---DVTVDGIIGPKTLAALNAADPAVLIDAYCDARLAYYRSLVERRPSQEKF 156


                  ....*...
gi 2588604132 159 LTGWLNRV 166
Cdd:COG3926   157 LRGWLRRV 164
N-acetylmuramidase_GH108 cd13926
N-acetylmuramidase domain of the glycosyl hydrolase 108 family; This domain acts as a lysozyme ...
 4-91 7.26e-33

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: 112.63  E-value: 7.26e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2588604132   4 SRFLKFFNYILLVEGSYSNDKNDKGGETKYGITKERARECGY----KGNMKDLTKAMAQKIYEEKYYKARKLDQVkNDKV 79
Cdd:cd13926     1 ATFDQAIERVLAHEGGYVNDPKDPGGETNYGITKRTARALGYrtvtKGDIKALTREQAVEIYRRDYWDAPRCDEL-PAGV 79

                          90
                  ....*....|..
gi 2588604132  80 ALSIFDFSVNAG 91
Cdd:cd13926    80 ALEVFDAAVNSG 91
Glyco_hydro_108 pfam05838
Glycosyl hydrolase 108; This family acts as a lysozyme (N-acetylmuramidase), EC:3.2.1.17. It ...
 10-91 2.80e-29

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: 103.03  E-value: 2.80e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2588604132  10 FNYILLVEGSYSNDKNDKGGETKYGITKERARECGYKG-----NMKDLTKAMAQKIYEEKYYKARKLDQVKnDKVALSIF 84
Cdd:pfam05838   1 LDFILAHEGGYVNDPADPGGATNYGITQATARAWGGRGgidvaDVRDLTRAEAAAIYRRDYWDPPRCDELP-PPLALVLF 79


                  ....*..
gi 2588604132  85 DFSVNAG 91
Cdd:pfam05838  80 DAAVNSG 86
 
Name Accession Description Interval E-value
ZliS COG3926
Lysozyme family protein [General function prediction only];
5-166 4.72e-58

Lysozyme family protein [General function prediction only];


Pssm-ID: 443130 [Multi-domain]  Cd Length: 167  Bit Score: 178.90  E-value: 4.72e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2588604132   5 RFLKFFNYILLVEGSYSNDKNDKGGETKYGITKERAREC-----GYKGNMKDLTKAMAQKIYEEKYYKARKLDQVkNDKV 79
Cdd:COG3926     1 NFDQALDFILKHEGGYVNHPADPGGATNYGITQATLRAYrglrdVTAGDVRALTREEAKAIYRRDYWDRPRGDEL-PQGL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2588604132  80 ALSIFDFSVNAG-RYGIKKAQEAVNKVYgknVVSMDGAIGTQTLKYLNEVNPDKFLVVYHSLQREYYKYLAKRDATQNDF 158
Cdd:COG3926    80 AAEVFDFAVNSGpGRAIKLLQRALGALP---DVTVDGIIGPKTLAALNAADPAVLIDAYCDARLAYYRSLVERRPSQEKF 156


                  ....*...
gi 2588604132 159 LTGWLNRV 166
Cdd:COG3926   157 LRGWLRRV 164
N-acetylmuramidase_GH108 cd13926
N-acetylmuramidase domain of the glycosyl hydrolase 108 family; This domain acts as a lysozyme ...
 4-91 7.26e-33

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: 112.63  E-value: 7.26e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2588604132   4 SRFLKFFNYILLVEGSYSNDKNDKGGETKYGITKERARECGY----KGNMKDLTKAMAQKIYEEKYYKARKLDQVkNDKV 79
Cdd:cd13926     1 ATFDQAIERVLAHEGGYVNDPKDPGGETNYGITKRTARALGYrtvtKGDIKALTREQAVEIYRRDYWDAPRCDEL-PAGV 79

                          90
                  ....*....|..
gi 2588604132  80 ALSIFDFSVNAG 91
Cdd:cd13926    80 ALEVFDAAVNSG 91
Glyco_hydro_108 pfam05838
Glycosyl hydrolase 108; This family acts as a lysozyme (N-acetylmuramidase), EC:3.2.1.17. It ...
 10-91 2.80e-29

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: 103.03  E-value: 2.80e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2588604132  10 FNYILLVEGSYSNDKNDKGGETKYGITKERARECGYKG-----NMKDLTKAMAQKIYEEKYYKARKLDQVKnDKVALSIF 84
Cdd:pfam05838   1 LDFILAHEGGYVNDPADPGGATNYGITQATARAWGGRGgidvaDVRDLTRAEAAAIYRRDYWDPPRCDELP-PPLALVLF 79


                  ....*..
gi 2588604132  85 DFSVNAG 91
Cdd:pfam05838  80 DAAVNSG 86
PG_binding_3 pfam09374
Predicted Peptidoglycan domain; This family contains a potential peptidoglycan binding domain.
 93-165 1.21e-08

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


Pssm-ID: 401356  Cd Length: 76  Bit Score: 49.43  E-value: 1.21e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2588604132  93 YGIKKAQEAVNKVYGKnvVSMDGAIGTQTLKYLNEVN---PDKFLVVYHSLQREYYKYLAKRDATQNDFLTGWLNR 165
Cdd:pfam09374   1 NAVRILQRILGGMGPD--VKVDGIIGPKTLNAVMSRNsagEEVLCKAYGLARRRFYLRLAARRTTNARFLRGWVNR 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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