|
Name |
Accession |
Description |
Interval |
E-value |
| Acm |
COG3757 |
Lyzozyme M1 (1,4-beta-N-acetylmuramidase), GH25 family [Cell wall/membrane/envelope biogenesis] ... |
88-286 |
3.71e-72 |
|
Lyzozyme M1 (1,4-beta-N-acetylmuramidase), GH25 family [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442971 Cd Length: 208 Bit Score: 220.54 E-value: 3.71e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1559334836 88 GIDISQHQGNIAWDSVKyiknDIPISFVFVRATRGAYVQDAFFRKNWTNLKNKNLLRGAYHYYDVNRNSTDQAENFMKTV 167
Cdd:COG3757 13 GIDVSHYQGDIDWAAVK----AAGIDFAYIKATEGTDYVDPKFARNWAGARAAGLPRGAYHFFRPCSDAAAQADNFISTV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1559334836 168 TLEKGDLPPVLDIEELP-KNQSLELLKKGITNWLHLIEKQYQVKPIIYSNDAYFIHHIADMDLTEYPIWVANYNPRNSPK 246
Cdd:COG3757 89 PRDPGDLPPVLDLEENGyYGLSPAQLRAWLKAFLDEVEAHTGRKPIIYTSPSFYNDYLGNSDFSDYPLWIARYGSSPGYL 168
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1559334836 247 -HSRWSFWQFSEKGIIKGITSNfVDINIFNGNTNQLEKLTI 286
Cdd:COG3757 169 pGRNWTFWQYTSSGRVPGISGN-VDLNVFNGSRDELKALAL 208
|
|
| GH25_YegX-like |
cd06524 |
YegX is an uncharacterized bacterial protein with a glycosyl hydrolase family 25 (GH25) ... |
88-276 |
1.07e-70 |
|
YegX is an uncharacterized bacterial protein with a glycosyl hydrolase family 25 (GH25) catalytic domain that is similar in sequence to the CH-type (Chalaropsis-type) lysozymes of the GH25 family of endolysins.
Pssm-ID: 119384 Cd Length: 194 Bit Score: 216.44 E-value: 1.07e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1559334836 88 GIDISQHQGNIAWDSVKYIKNDIPISFVFVRATRGAYVQDAFFRKNWTNLKNKNLLRGAYHYYDVNRNSTDQAENFMKTV 167
Cdd:cd06524 2 GIDVSHYQGKIDWQKVKAKVKDSPVAFVFIKATEGVDIVDPDFPTNWEGAKEAGIIRGAYHFYRPNSDPKQQADNFLNTV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1559334836 168 TL-EKGDLPPVLDIEELPKNQSLELLKKGITNWLHLIEKQYQVKPIIYSNDAYFIHHIADMDLTEYPIWVANYNPRNSPK 246
Cdd:cd06524 82 KLlGPGDLPPVLDVEWDGRKSSAKQIQEGVLEWLDAVEKATGVKPIIYTNPSFWTDYLTDSSFSEYPLWIADYNPRRKKV 161
|
170 180 190
....*....|....*....|....*....|....
gi 1559334836 247 H----SRWSFWQFSEKGIIKGItSNFVDINIFNG 276
Cdd:cd06524 162 PpnesKKWLLWQYSDSGKVPGI-SGAVDLNVFNG 194
|
|
| Glyco_hydro_25 |
pfam01183 |
Glycosyl hydrolases family 25; |
89-264 |
1.25e-41 |
|
Glycosyl hydrolases family 25;
Pssm-ID: 426105 Cd Length: 180 Bit Score: 141.73 E-value: 1.25e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1559334836 89 IDISQHQGNIAWDSVKyiknDIPISFVFVRATRGAYVQDAFFRKNWTNLKNKNLLRGAYHYYDVNRNST--DQAENFMKT 166
Cdd:pfam01183 1 IDVSSYQGDIDWQKVK----ASGVSFVFIKATEGTDYVDPYFTTQYANARAAGLKVGAYHFARPCNSSTaaAQADYFLSN 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1559334836 167 VT---LEKGDLPPVLDIEELPKNQSLELLKKgITNWLHLIEKQYQVKPIIYSNDAYFIHHIADMDL-TEYPIWVANY--- 239
Cdd:pfam01183 77 VQglgLDAGTLPPVLDVEVTTGLTKAAATSN-ILRFLDRVKKQTGYKPVIYTGTSFWTNNLLYGQFiADYPLWIASYavt 155
|
170 180
....*....|....*....|....*
gi 1559334836 240 NPRNSPKHSRWSFWQFSEKGIIKGI 264
Cdd:pfam01183 156 PPKDYPGWTKWTFWQYTSSGSIPGV 180
|
|
| Glyco_25 |
smart00641 |
Glycosyl hydrolases family 25; |
88-181 |
1.23e-11 |
|
Glycosyl hydrolases family 25;
Pssm-ID: 128889 Cd Length: 109 Bit Score: 60.12 E-value: 1.23e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1559334836 88 GIDISQHQGNIAWDSVKyikNDIpISFVFVRATRGAYVQDAFFRKNWTNLKNKN-LLRGAYHY-YDVNRNSTDQAENFMK 165
Cdd:smart00641 3 GIDVSDYEGGIDGAKVR---NTG-ASFAFMKATEGAGYTPPYYSYQYFLADNAGyILRGFYHAaYPVSSSATAQANYFPS 78
|
90
....*....|....*....
gi 1559334836 166 TVTLEKGD---LPPVLDIE 181
Cdd:smart00641 79 MDGVRIFQftsNPFVLDLD 97
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| Acm |
COG3757 |
Lyzozyme M1 (1,4-beta-N-acetylmuramidase), GH25 family [Cell wall/membrane/envelope biogenesis] ... |
88-286 |
3.71e-72 |
|
Lyzozyme M1 (1,4-beta-N-acetylmuramidase), GH25 family [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442971 Cd Length: 208 Bit Score: 220.54 E-value: 3.71e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1559334836 88 GIDISQHQGNIAWDSVKyiknDIPISFVFVRATRGAYVQDAFFRKNWTNLKNKNLLRGAYHYYDVNRNSTDQAENFMKTV 167
Cdd:COG3757 13 GIDVSHYQGDIDWAAVK----AAGIDFAYIKATEGTDYVDPKFARNWAGARAAGLPRGAYHFFRPCSDAAAQADNFISTV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1559334836 168 TLEKGDLPPVLDIEELP-KNQSLELLKKGITNWLHLIEKQYQVKPIIYSNDAYFIHHIADMDLTEYPIWVANYNPRNSPK 246
Cdd:COG3757 89 PRDPGDLPPVLDLEENGyYGLSPAQLRAWLKAFLDEVEAHTGRKPIIYTSPSFYNDYLGNSDFSDYPLWIARYGSSPGYL 168
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1559334836 247 -HSRWSFWQFSEKGIIKGITSNfVDINIFNGNTNQLEKLTI 286
Cdd:COG3757 169 pGRNWTFWQYTSSGRVPGISGN-VDLNVFNGSRDELKALAL 208
|
|
| GH25_YegX-like |
cd06524 |
YegX is an uncharacterized bacterial protein with a glycosyl hydrolase family 25 (GH25) ... |
88-276 |
1.07e-70 |
|
YegX is an uncharacterized bacterial protein with a glycosyl hydrolase family 25 (GH25) catalytic domain that is similar in sequence to the CH-type (Chalaropsis-type) lysozymes of the GH25 family of endolysins.
Pssm-ID: 119384 Cd Length: 194 Bit Score: 216.44 E-value: 1.07e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1559334836 88 GIDISQHQGNIAWDSVKYIKNDIPISFVFVRATRGAYVQDAFFRKNWTNLKNKNLLRGAYHYYDVNRNSTDQAENFMKTV 167
Cdd:cd06524 2 GIDVSHYQGKIDWQKVKAKVKDSPVAFVFIKATEGVDIVDPDFPTNWEGAKEAGIIRGAYHFYRPNSDPKQQADNFLNTV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1559334836 168 TL-EKGDLPPVLDIEELPKNQSLELLKKGITNWLHLIEKQYQVKPIIYSNDAYFIHHIADMDLTEYPIWVANYNPRNSPK 246
Cdd:cd06524 82 KLlGPGDLPPVLDVEWDGRKSSAKQIQEGVLEWLDAVEKATGVKPIIYTNPSFWTDYLTDSSFSEYPLWIADYNPRRKKV 161
|
170 180 190
....*....|....*....|....*....|....
gi 1559334836 247 H----SRWSFWQFSEKGIIKGItSNFVDINIFNG 276
Cdd:cd06524 162 PpnesKKWLLWQYSDSGKVPGI-SGAVDLNVFNG 194
|
|
| GH25_muramidase |
cd00599 |
Endo-N-acetylmuramidases (muramidases) are lysozymes (also referred to as peptidoglycan ... |
88-274 |
1.35e-50 |
|
Endo-N-acetylmuramidases (muramidases) are lysozymes (also referred to as peptidoglycan hydrolases) that degrade bacterial cell walls by catalyzing the hydrolysis of 1,4-beta-linkages between N-acetylmuramic acid and N-acetyl-D-glucosamine residues. This family of muramidases contains a glycosyl hydrolase family 25 (GH25) catalytic domain and is found in bacteria, fungi, slime molds, round worms, protozoans and bacteriophages. The bacteriophage members are referred to as endolysins which are involved in lysing the host cell at the end of the replication cycle to allow release of mature phage particles. Endolysins are typically modular enzymes consisting of a catalytically active domain that hydrolyzes the peptidoglycan cell wall and a cell wall-binding domain that anchors the protein to the cell wall. Endolysins generally have narrow substrate specificities with either intra-species or intra-genus bacteriolytic activity.
Pssm-ID: 119373 [Multi-domain] Cd Length: 186 Bit Score: 164.83 E-value: 1.35e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1559334836 88 GIDISQHQGNIAWDSVKyiknDIPISFVFVRATRGAYVQDAFFRKNWTNLKNKNLLRGAYHYYDVNRNSTDQAENFMKTV 167
Cdd:cd00599 2 GIDVSSWQGSIDWNAVK----AAGIDFVFIKATEGTTYVDPKFATNRARARAAGLLVGAYHFARPCANAEAQADNFVNTV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1559334836 168 TLEKGDLPPVLDIEELPKNQSLELLKKGITNWLHLIEKQYQVKPIIYSNDAYFIHHIADMDLTEYPIWVANYN---PRNS 244
Cdd:cd00599 78 PRDPGSLPLVLDVEDTGGGCSAAALAAWLNAFLNEVEALTGKKPIIYTSPSFWDDYLASSQLSDYPLWIAHYRgepPPAP 157
|
170 180 190
....*....|....*....|....*....|
gi 1559334836 245 PKHSRWSFWQFSEKGIIKGITSNfVDINIF 274
Cdd:cd00599 158 GAWRPWTLWQYTSSGRVPGISGP-VDLNVF 186
|
|
| GH25_muramidase_1 |
cd06413 |
Uncharacterized bacterial muramidase containing a glycosyl hydrolase family 25 (GH25) ... |
88-276 |
8.14e-49 |
|
Uncharacterized bacterial muramidase containing a glycosyl hydrolase family 25 (GH25) catalytic domain. Endo-N-acetylmuramidases are lysozymes (also referred to as peptidoglycan hydrolases) that degrade bacterial cell walls by catalyzing the hydrolysis of 1,4-beta-linkages between N-acetylmuramic acid and N-acetyl-D-glucosamine residues.
Pssm-ID: 119375 Cd Length: 191 Bit Score: 160.52 E-value: 8.14e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1559334836 88 GIDISQHQGNIAWDSVKYIKndipISFVFVRATRGAYVQDAFFRKNWTNLKNKNLLRGAYHYYDVNRNSTDQAENFMKTV 167
Cdd:cd06413 5 GIDVSHHQGDIDWARVRAQG----VSFAYIKATEGGDHVDKRFAENWRGARAAGLPRGAYHFFTFCRSGAEQAANFIRNV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1559334836 168 TLEKGDLPPVLDIEELPK---NQSLELLKKGITNWLHLIEKQYQVKPIIYSNDAYFIHHIADmDLTEYPIWVANY--NPR 242
Cdd:cd06413 81 PKDPGALPPVVDVEWNGNsatCPSAEEVLAELQVFLDALEAHYGKRPIIYTTYDFYDDYLKG-EFPDYPLWIRSVagHPR 159
|
170 180 190
....*....|....*....|....*....|....
gi 1559334836 243 NSPKHsRWSFWQFSEKGIIKGITSnFVDINIFNG 276
Cdd:cd06413 160 LYEDR-PWTFWQYTNRGRVPGIEG-DVDLNVFNG 191
|
|
| Glyco_hydro_25 |
pfam01183 |
Glycosyl hydrolases family 25; |
89-264 |
1.25e-41 |
|
Glycosyl hydrolases family 25;
Pssm-ID: 426105 Cd Length: 180 Bit Score: 141.73 E-value: 1.25e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1559334836 89 IDISQHQGNIAWDSVKyiknDIPISFVFVRATRGAYVQDAFFRKNWTNLKNKNLLRGAYHYYDVNRNST--DQAENFMKT 166
Cdd:pfam01183 1 IDVSSYQGDIDWQKVK----ASGVSFVFIKATEGTDYVDPYFTTQYANARAAGLKVGAYHFARPCNSSTaaAQADYFLSN 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1559334836 167 VT---LEKGDLPPVLDIEELPKNQSLELLKKgITNWLHLIEKQYQVKPIIYSNDAYFIHHIADMDL-TEYPIWVANY--- 239
Cdd:pfam01183 77 VQglgLDAGTLPPVLDVEVTTGLTKAAATSN-ILRFLDRVKKQTGYKPVIYTGTSFWTNNLLYGQFiADYPLWIASYavt 155
|
170 180
....*....|....*....|....*
gi 1559334836 240 NPRNSPKHSRWSFWQFSEKGIIKGI 264
Cdd:pfam01183 156 PPKDYPGWTKWTFWQYTSSGSIPGV 180
|
|
| GH25_Lyc-like |
cd06525 |
Lyc muramidase is an autolytic lysozyme (autolysin) from Clostridium acetobutylicum encoded by ... |
88-274 |
1.48e-33 |
|
Lyc muramidase is an autolytic lysozyme (autolysin) from Clostridium acetobutylicum encoded by the lyc gene. Lyc has a glycosyl hydrolase family 25 (GH25) catalytic domain. Endo-N-acetylmuramidases are lysozymes (also referred to as peptidoglycan hydrolases) that degrade bacterial cell walls by catalyzing the hydrolysis of 1,4-beta-linkages between N-acetylmuramic acid and N-acetyl-D-glucosamine residues.
Pssm-ID: 119385 Cd Length: 184 Bit Score: 120.86 E-value: 1.48e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1559334836 88 GIDISQHQGNIAWDSVKyiknDIPISFVFVRATRGAYVQDAFFRKNWTNLKNKNLLRGAYHYYDVNRNSTDQAENFMKTV 167
Cdd:cd06525 2 GIDISNWQGNINFNAVK----DSGVEVVYIKATEGTTFVDSYFNENYNGAKAAGLKVGFYHFLVGTSNPEEQAENFYNTI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1559334836 168 TLEKGDLPPVLDIEelpknQSLELLKKGITN----WLHLIEKQYQVKPIIYSNdAYFIHHIADMDLTEYPIWVANYN--- 240
Cdd:cd06525 78 KGKKMDLKPALDVE-----VNFGLSKDELNDyvlrFIEEFEKLSGLKVGIYTY-TSFINNNLDSRLSSYPLWIANYGvsp 151
|
170 180 190
....*....|....*....|....*....|....
gi 1559334836 241 PRNSPKHSRWSFWQFSEKGIIKGITSNfVDINIF 274
Cdd:cd06525 152 PSSNGIWNSWVGFQYSETGRVNGVSGS-VDLDEF 184
|
|
| GH25_CH-type |
cd06412 |
CH-type (Chalaropsis-type) lysozymes represent one of four functionally-defined classes of ... |
88-281 |
1.60e-28 |
|
CH-type (Chalaropsis-type) lysozymes represent one of four functionally-defined classes of peptidoglycan hydrolases (also referred to as endo-N-acetylmuramidases) that cleave bacterial cell wall peptidoglycans. CH-type lysozymes exhibit both lysozyme (acetylmuramidase) and diacetylmuramidase activity. The first member of this family to be described was a muramidase from the fungus Chalaropsis. However, a majority of the CH-type lysozymes are found in bacteriophages and Gram-positive bacteria such as Streptomyces and Clostridium. CH-type lysozymes have a single glycosyl hydrolase family 25 (GH25) domain with an unusual beta/alpha-barrel fold in which the last strand of the barrel is antiparallel to strands beta7 and beta1. Most CH-type lysozymes appear to lack the cell wall-binding domain found in other GH25 muramidases.
Pssm-ID: 119374 Cd Length: 199 Bit Score: 108.18 E-value: 1.60e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1559334836 88 GIDISQHQGNIAWDSVKyiknDIPISFVFVRATRGAYVQDAFFRKNWTNLKNKNLLRGAYHYYDVNRNS-TDQAENFMKT 166
Cdd:cd06412 3 GIDVSGHQGSVDWSGAA----ANGARFAYVKATEGTSYTNPRFSSQYNGAYNAGLIRGAYHFALPDQSSgAAQADYFLDH 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1559334836 167 VTLEKGD---LPPVLDIEELPKNQSLE-LLKKGITNWLHLIEKQYQVK----PIIYS----------NDAYFihhiadmd 228
Cdd:cd06412 79 GGGWSPDgrtLPGVLDLEYNPYGATCYgLSPAQMVSWIKDFSDTYKARtgrdPVIYTttswwnqctgNSAGF-------- 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1559334836 229 lTEYPIWVANYNPRNSPK---HSRWSFWQFSEKGIIKGitsnfvDINIFNGNTNQL 281
Cdd:cd06412 151 -ANHPLWLARYGSSPGALpagWSAWTFWQYSDSGPFPG------DQNVFNGSRASL 199
|
|
| GH25_LytC-like |
cd06414 |
The LytC lysozyme of Streptococcus pneumoniae is a bacterial cell wall hydrolase that cleaves ... |
88-274 |
1.01e-26 |
|
The LytC lysozyme of Streptococcus pneumoniae is a bacterial cell wall hydrolase that cleaves the beta1-4-glycosydic bond located between the N-acetylmuramoyl-N-glucosaminyl residues of the cell wall polysaccharide chains. LytC is composed of a C-terminal glycosyl hydrolase family 25 (GH25) domain and an N-terminal choline-binding module (CBM) consisting of eleven homologous repeats that specifically recognizes the choline residues of pneumococcal lipoteichoic and teichoic acids. This domain arrangement is the reverse of the major pneumococcal autolysin, LytA, and the CPL-1-like lytic enzymes of the pneumococcal bacteriophages, in which the CBM (consisting of six repeats) is at the C-terminus. This model represents the C-terminal catalytic domain of the LytC-like enzymes.
Pssm-ID: 119376 Cd Length: 191 Bit Score: 103.03 E-value: 1.01e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1559334836 88 GIDISQHQGNIAWDSVKyiKNDIpiSFVFVRATRGAYVQ---DAFFRKNWTNLKNKNLLRGAYHY-YDVNRN-STDQAEN 162
Cdd:cd06414 3 GIDVSEWQGDIDWKKVK--ASGV--DFAIIRAGYGGYGElqeDKYFEENIKGAKAAGIPVGVYFYsYAVTVAeAREEAEF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1559334836 163 FMKTVTLEKGDLPPVLDIEELP---KNQSLELLKKGITNWLHLIEKQ-YqvKPIIYSNDAYFIHHIADMDLTEYPIWVAN 238
Cdd:cd06414 79 VLRLIKGYKLSYPVYYDLEDETqlgAGLSKDQRTDIANAFCETIEAAgY--YPGIYANLSWLTNKLDDERLSKYDVWVAQ 156
|
170 180 190
....*....|....*....|....*....|....*.
gi 1559334836 239 YNPRNSPKhSRWSFWQFSEKGIIKGITSNfVDINIF 274
Cdd:cd06414 157 YGNSPTYP-GNYGMWQYTSSGSVPGISGN-VDLNYC 190
|
|
| GH25_LysA-like |
cd06417 |
LysA is a cell wall endolysin produced by Lactobacillus fermentum, which degrades bacterial ... |
88-280 |
1.25e-12 |
|
LysA is a cell wall endolysin produced by Lactobacillus fermentum, which degrades bacterial cell walls by catalyzing the hydrolysis of 1,4-beta-linkages between N-acetylmuramic acid and N-acetyl-D-glucosamine residues. The N-terminal glycosyl hydrolase family 25 (GH25) domain of LysA has sequence similarity with other murein hydrolase catalytic domains while the C-terminal domain has sequence similarity with putative bacterial cell wall-binding SH3b domains. This domain family also includes LysL of Lactococcus lactis.
Pssm-ID: 119379 Cd Length: 195 Bit Score: 65.16 E-value: 1.25e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1559334836 88 GIDISQHQGNIawdsvkyIKNDIPISFVFVRATRGAYVQDAFFRKNWTNLKNKNLLRGAYHYYDVNrNSTDQAENFMKTV 167
Cdd:cd06417 3 GIDVSSWQSRI-------VTTVVPADFVIVKATQGTGYVNPSWRSQAAQAIAAGKLLGLYHYANGG-NAIAEADYFLNNI 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1559334836 168 TLEKGDLPPVLDIEElpKNQSLELLKKGITNWLHLIEKQYQVKPIIYSNDAYfIHHIADMDLTEYPIWVANY---NP--- 241
Cdd:cd06417 75 KGYVGKAVLVLDWES--YQNSAWGNSAWARQWVNRVHELTGVWPMVYVSKSV-TRQINWSVRADCGLWVAQYasnNPtgy 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1559334836 242 --RNSPKHSRWSF---WQFSEKGIIKGITSNfVDINIFNGNTNQ 280
Cdd:cd06417 152 qsQAGPWNAAWSGetiHQYTSNGSLNGYNGP-LDLNLFYGDREQ 194
|
|
| Glyco_25 |
smart00641 |
Glycosyl hydrolases family 25; |
88-181 |
1.23e-11 |
|
Glycosyl hydrolases family 25;
Pssm-ID: 128889 Cd Length: 109 Bit Score: 60.12 E-value: 1.23e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1559334836 88 GIDISQHQGNIAWDSVKyikNDIpISFVFVRATRGAYVQDAFFRKNWTNLKNKN-LLRGAYHY-YDVNRNSTDQAENFMK 165
Cdd:smart00641 3 GIDVSDYEGGIDGAKVR---NTG-ASFAFMKATEGAGYTPPYYSYQYFLADNAGyILRGFYHAaYPVSSSATAQANYFPS 78
|
90
....*....|....*....
gi 1559334836 166 TVTLEKGD---LPPVLDIE 181
Cdd:smart00641 79 MDGVRIFQftsNPFVLDLD 97
|
|
| GH25_muramidase_2 |
cd06419 |
Uncharacterized bacterial muramidase containing a glycosyl hydrolase family 25 (GH25) ... |
86-263 |
3.46e-10 |
|
Uncharacterized bacterial muramidase containing a glycosyl hydrolase family 25 (GH25) catalytic domain. Endo-N-acetylmuramidases are lysozymes (also referred to as peptidoglycan hydrolases) that degrade bacterial cell walls by catalyzing the hydrolysis of 1,4-beta-linkages between N-acetylmuramic acid and N-acetyl-D-glucosamine residues.
Pssm-ID: 119381 Cd Length: 190 Bit Score: 58.18 E-value: 3.46e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1559334836 86 AIGIDISQHQGNIAWDSVKyiKNDIpiSFVFVRATRGAYVQDAFFRKNWTNLKNKNLLRGAYHYYDVNRNSTDQAENFMK 165
Cdd:cd06419 8 VLGVQLSQDDGYIDFNSLQ--SNGI--SFVYLRATQGASYFDDNFLSNFSRAQGTGLSVGVIHTFSFSSTAAAQYRYFIR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1559334836 166 TVTLEKGDLPPVL-----DIEELPKNQSLELLKKGITnwlhLIEKQYQVKPIIYSndAYFIHHIADMDLTEYPIWVANyn 240
Cdd:cd06419 84 KVGNNTGNLPIAIyvsyyGDYNPDTKKSTQKLGLLVQ----LLEQHYNQSVIIRG--TPAVLKQVVKALKQLKYWLIE-- 155
|
170 180
....*....|....*....|....
gi 1559334836 241 pRNSPKH-SRWSFWQFSEKGIIKG 263
Cdd:cd06419 156 -DKLKGQgSKNQFWQYTANGKVKS 178
|
|
| GH25_PlyB-like |
cd06523 |
PlyB is a bacteriophage endolysin that displays potent lytic activity toward Bacillus ... |
89-272 |
1.30e-08 |
|
PlyB is a bacteriophage endolysin that displays potent lytic activity toward Bacillus anthracis. PlyB has an N-terminal glycosyl hydrolase family 25 (GH25) catalytic domain and a C-terminal bacterial SH3-like domain, SH3b. Both domains are required for effective catalytic activity. Endolysins are produced by bacteriophages at the end of their life cycle and participate in lysing the bacterial cell in order to release the newly formed progeny. Endolysins (also referred to as endo-N-acetylmuramidases or peptidoglycan hydrolases) degrade bacterial cell walls by catalyzing the hydrolysis of 1,4-beta-linkages between N-acetylmuramic acid and N-acetyl-D-glucosamine residues.
Pssm-ID: 119383 Cd Length: 177 Bit Score: 53.52 E-value: 1.30e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1559334836 89 IDISQHQGNIAWDsVKYIKNDipISFVFVRATRGAYVQDAFFRKNWTNLKNKNLLRGAYHYYDVNRNSTDQAE--NFMKt 166
Cdd:cd06523 3 VDISEWQGPINWD-YDTLSKQ--LDLVIIRVQYGSNYVDLKYKNNIKEFKKRGIPFGVYAFARGTSTADAKAEarDFYN- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1559334836 167 vtleKGDLPP---VLDIEElpknQSLELLKKGITNWLHLIEKQYQVKPIIYSNDAYFIHHIADMDLTEYpIWVANYNpRN 243
Cdd:cd06523 79 ----RANKKPtfyVLDVEV----TSMSDMNAGVQAFISELRRLGAKKVGLYIGHHFYTTFNLAVSKFDA-IWIPAYG-SN 148
|
170 180
....*....|....*....|....*....
gi 1559334836 244 SPKHSrWSFWQFSEKGIIKGITSNfVDIN 272
Cdd:cd06523 149 PGTYP-YDLWQYTDSGYLPGISGN-VDLN 175
|
|
| GH25_AtlA-like |
cd06522 |
AtlA is an autolysin found in Gram-positive lactic acid bacteria that degrades bacterial cell ... |
89-273 |
9.38e-03 |
|
AtlA is an autolysin found in Gram-positive lactic acid bacteria that degrades bacterial cell walls by catalyzing the hydrolysis of 1,4-beta-linkages between N-acetylmuramic acid and N-acetyl-D-glucosamine residues. This family includes the AtlA and Aml autolysins from Streptococcus mutans which have a C-terminal glycosyl hydrolase family 25 (GH25) catalytic domain as well as six tandem N-terminal repeats of the GBS (group B Streptococcus) Bsp-like peptidoglycan-binding domain. Other members of this family have one or more C-terminal peptidoglycan-binding domain(s) (SH3 or LysM) in addition to the GH25 domain.
Pssm-ID: 119382 Cd Length: 192 Bit Score: 36.58 E-value: 9.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1559334836 89 IDISQHQGNIAWDSVKYIKNdIPISFVFVRATRGAYVQDAFFRKNWTNLKNKNLLRGAYHYYDVNRNSTDQAE-----NF 163
Cdd:cd06522 4 VDVSSNNGIMSVADYNKLKN-YGVKAVIVKLTEGTTYRNPYAASQIANAKAAGLKVSAYHYAHYTSAADAQAEaryfaNT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1559334836 164 MKTVTLEKgDLPPVLDIEElpKNQSLELlkKGITN-WLHLIEKQYQVKPIIYSNDAYFIHHIADMDLTEYPIWVANYnPR 242
Cdd:cd06522 83 AKSLGLSK-NTVMVADMED--SSSSGNA--TANVNaFWQTMKAAGYKNTDVYTSASWLNSRADTSTLGAKRVWVAQY-PY 156
|
170 180 190
....*....|....*....|....*....|....*
gi 1559334836 243 NSPKHSRW----SFWQFSEKGIIKGITSNFvDINI 273
Cdd:cd06522 157 NPSSNNLWntnyGAWQWTSQAHFPGRSGGF-DVSI 190
|
|
| |
