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Conserved domains on  [gi|602192080|gb|EYT21245|]
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glycosyl hydrolase 108 family protein [Acinetobacter sp. 1592897]

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];
3-181 5.45e-57

Lysozyme family protein [General function prediction only];


:

Pssm-ID: 443130 [Multi-domain]  Cd Length: 167  Bit Score: 176.59  E-value: 5.45e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602192080   3 VEQYLDALIKREGGYVNDTLDSGHATKFGITQAVARSY-----GYQGEMEDLPLETARDIYKKQYWLEPRFDQINlisPI 77
Cdd:COG3926    2 FDQALDFILKHEGGYVNHPADPGGATNYGITQATLRAYrglrdVTAGDVRALTREEAKAIYRRDYWDRPRGDELP---QG 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602192080  78 IAEELLDTGVNCGLGFTKPLLQRALNLLnrqgkegwSDLKLDGQYGTSTLQALSLYiknrgqeGERVMVRLLNIMQGQRY 157
Cdd:COG3926   79 LAAEVFDFAVNSGPGRAIKLLQRALGAL--------PDVTVDGIIGPKTLAALNAA-------DPAVLIDAYCDARLAYY 143

                        170       180
                 ....*....|....*....|....
gi 602192080 158 IEITEKNPKYEQFFYGWLANRVSF 181
Cdd:COG3926  144 RSLVERRPSQEKFLRGWLRRVESL 167
 
Name Accession Description Interval E-value
ZliS COG3926
Lysozyme family protein [General function prediction only];
3-181 5.45e-57

Lysozyme family protein [General function prediction only];


Pssm-ID: 443130 [Multi-domain]  Cd Length: 167  Bit Score: 176.59  E-value: 5.45e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602192080   3 VEQYLDALIKREGGYVNDTLDSGHATKFGITQAVARSY-----GYQGEMEDLPLETARDIYKKQYWLEPRFDQINlisPI 77
Cdd:COG3926    2 FDQALDFILKHEGGYVNHPADPGGATNYGITQATLRAYrglrdVTAGDVRALTREEAKAIYRRDYWDRPRGDELP---QG 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602192080  78 IAEELLDTGVNCGLGFTKPLLQRALNLLnrqgkegwSDLKLDGQYGTSTLQALSLYiknrgqeGERVMVRLLNIMQGQRY 157
Cdd:COG3926   79 LAAEVFDFAVNSGPGRAIKLLQRALGAL--------PDVTVDGIIGPKTLAALNAA-------DPAVLIDAYCDARLAYY 143

                        170       180
                 ....*....|....*....|....
gi 602192080 158 IEITEKNPKYEQFFYGWLANRVSF 181
Cdd:COG3926  144 RSLVERRPSQEKFLRGWLRRVESL 167
N-acetylmuramidase_GH108 cd13926
N-acetylmuramidase domain of the glycosyl hydrolase 108 family; This domain acts as a lysozyme ...
 1-90 9.39e-34

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: 114.95  E-value: 9.39e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602192080   1 MKVEQYLDALIKREGGYVNDTLDSGHATKFGITQAVARSYGY----QGEMEDLPLETARDIYKKQYWLEPRFDQinlISP 76
Cdd:cd13926    1 ATFDQAIERVLAHEGGYVNDPKDPGGETNYGITKRTARALGYrtvtKGDIKALTREQAVEIYRRDYWDAPRCDE---LPA 77

                         90
                 ....*....|....
gi 602192080  77 IIAEELLDTGVNCG 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 3.73e-30

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: 105.73  E-value: 3.73e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602192080    7 LDALIKREGGYVNDTLDSGHATKFGITQAVARSYGYQG-----EMEDLPLETARDIYKKQYWLEPRFDQinlISPIIAEE 81
Cdd:pfam05838   1 LDFILAHEGGYVNDPADPGGATNYGITQATARAWGGRGgidvaDVRDLTRAEAAAIYRRDYWDPPRCDE---LPPPLALV 77


                  ....*....
gi 602192080   82 LLDTGVNCG 90
Cdd:pfam05838  78 LFDAAVNSG 86
 
Name Accession Description Interval E-value
ZliS COG3926
Lysozyme family protein [General function prediction only];
3-181 5.45e-57

Lysozyme family protein [General function prediction only];


Pssm-ID: 443130 [Multi-domain]  Cd Length: 167  Bit Score: 176.59  E-value: 5.45e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602192080   3 VEQYLDALIKREGGYVNDTLDSGHATKFGITQAVARSY-----GYQGEMEDLPLETARDIYKKQYWLEPRFDQINlisPI 77
Cdd:COG3926    2 FDQALDFILKHEGGYVNHPADPGGATNYGITQATLRAYrglrdVTAGDVRALTREEAKAIYRRDYWDRPRGDELP---QG 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602192080  78 IAEELLDTGVNCGLGFTKPLLQRALNLLnrqgkegwSDLKLDGQYGTSTLQALSLYiknrgqeGERVMVRLLNIMQGQRY 157
Cdd:COG3926   79 LAAEVFDFAVNSGPGRAIKLLQRALGAL--------PDVTVDGIIGPKTLAALNAA-------DPAVLIDAYCDARLAYY 143

                        170       180
                 ....*....|....*....|....
gi 602192080 158 IEITEKNPKYEQFFYGWLANRVSF 181
Cdd:COG3926  144 RSLVERRPSQEKFLRGWLRRVESL 167
N-acetylmuramidase_GH108 cd13926
N-acetylmuramidase domain of the glycosyl hydrolase 108 family; This domain acts as a lysozyme ...
 1-90 9.39e-34

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: 114.95  E-value: 9.39e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602192080   1 MKVEQYLDALIKREGGYVNDTLDSGHATKFGITQAVARSYGY----QGEMEDLPLETARDIYKKQYWLEPRFDQinlISP 76
Cdd:cd13926    1 ATFDQAIERVLAHEGGYVNDPKDPGGETNYGITKRTARALGYrtvtKGDIKALTREQAVEIYRRDYWDAPRCDE---LPA 77

                         90
                 ....*....|....
gi 602192080  77 IIAEELLDTGVNCG 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 3.73e-30

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: 105.73  E-value: 3.73e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602192080    7 LDALIKREGGYVNDTLDSGHATKFGITQAVARSYGYQG-----EMEDLPLETARDIYKKQYWLEPRFDQinlISPIIAEE 81
Cdd:pfam05838   1 LDFILAHEGGYVNDPADPGGATNYGITQATARAWGGRGgidvaDVRDLTRAEAAAIYRRDYWDPPRCDE---LPPPLALV 77


                  ....*....
gi 602192080   82 LLDTGVNCG 90
Cdd:pfam05838  78 LFDAAVNSG 86
PG_binding_3 pfam09374
Predicted Peptidoglycan domain; This family contains a potential peptidoglycan binding domain.
 98-179 5.51e-12

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


Pssm-ID: 401356  Cd Length: 76  Bit Score: 58.67  E-value: 5.51e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602192080   98 LQRALnllnrqGKEGWsDLKLDGQYGTSTLQALslyiKNRGQEGERVMVRLLNIMQGQRYIEITEKNPKYEQFFYGWLAN 177
Cdd:pfam09374   6 LQRIL------GGMGP-DVKVDGIIGPKTLNAV----MSRNSAGEEVLCKAYGLARRRFYLRLAARRTTNARFLRGWVNR 74


                  ..
gi 602192080  178 RV 179
Cdd:pfam09374  75 LV 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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