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Conserved domains on  [gi|510997722|ref|WP_016265563|]
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GH25 family lysozyme [Latilactobacillus sakei]

Protein Classification

glycoside hydrolase family 25 domain-containing protein; glycoside hydrolase family 25 protein( domain architecture ID 10157525)

glycoside hydrolase family 25 domain-containing protein is a peptidoglycan hydrolase (also called lysozyme) that degrades bacterial cell walls by catalyzing the hydrolysis of 1,4-beta-linkages between N-acetylmuramic acid and N-acetyl-D-glucosamine residues| glycoside hydrolase family 25 protein similar to Escherichia coli protein YegX that is similar in sequence to the CH-type (Chalaropsis-type) lysozymes of the GH25 family of endolysins

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
GH25_muramidase_2 cd06419
Uncharacterized bacterial muramidase containing a glycosyl hydrolase family 25 (GH25) ...
 46-238 5.89e-99

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: 286.60  E-value: 5.89e-99
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510997722  46 PNEQQYPVLGAQISQEDGYQDYQILKKEGLKFVYLKATEGASYKDDNFDSNYSRAEGSGISVGVYHFFSFDSSPEDQAQQ 125
Cdd:cd06419    1 PALSNYPVLGVQLSQDDGYIDFNSLQSNGISFVYLRATQGASYFDDNFLSNFSRAQGTGLSVGVIHTFSFSSTAAAQYRY 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510997722 126 FIKSVGQDTGHLPIMVYLSYYNDYAqkpPAKAKTQRAIARFVTLINQYYHQDCIIGGAPALLKRYVPTKGTYPLWQTTQQ 205
Cdd:cd06419   81 FIRKVGNNTGNLPIAIYVSYYGDYN---PDTKKSTQKLGLLVQLLEQHYNQSVIIRGTPAVLKQVVKALKQLKYWLIEDK 157

                        170       180       190
                 ....*....|....*....|....*....|...
gi 510997722 206 RPTVGTKNGFWQYTTASKIPGGRDDSEYQLAVF 238
Cdd:cd06419  158 LKGQGSKNQFWQYTANGKVKSGGNSAELPLAVF 190
 
Name Accession Description Interval E-value
GH25_muramidase_2 cd06419
Uncharacterized bacterial muramidase containing a glycosyl hydrolase family 25 (GH25) ...
 46-238 5.89e-99

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: 286.60  E-value: 5.89e-99
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510997722  46 PNEQQYPVLGAQISQEDGYQDYQILKKEGLKFVYLKATEGASYKDDNFDSNYSRAEGSGISVGVYHFFSFDSSPEDQAQQ 125
Cdd:cd06419    1 PALSNYPVLGVQLSQDDGYIDFNSLQSNGISFVYLRATQGASYFDDNFLSNFSRAQGTGLSVGVIHTFSFSSTAAAQYRY 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510997722 126 FIKSVGQDTGHLPIMVYLSYYNDYAqkpPAKAKTQRAIARFVTLINQYYHQDCIIGGAPALLKRYVPTKGTYPLWQTTQQ 205
Cdd:cd06419   81 FIRKVGNNTGNLPIAIYVSYYGDYN---PDTKKSTQKLGLLVQLLEQHYNQSVIIRGTPAVLKQVVKALKQLKYWLIEDK 157

                        170       180       190
                 ....*....|....*....|....*....|...
gi 510997722 206 RPTVGTKNGFWQYTTASKIPGGRDDSEYQLAVF 238
Cdd:cd06419  158 LKGQGSKNQFWQYTANGKVKSGGNSAELPLAVF 190
Acm COG3757
Lyzozyme M1 (1,4-beta-N-acetylmuramidase), GH25 family [Cell wall/membrane/envelope biogenesis] ...
 49-248 9.00e-44

Lyzozyme M1 (1,4-beta-N-acetylmuramidase), GH25 family [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442971  Cd Length: 208  Bit Score: 146.58  E-value: 9.00e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510997722  49 QQYPVLGAQISQEDGYQDYQILKKEGLKFVYLKATEGASYKDDNFDSNYSRAEGSGISVGVYHFFSFDSSPEDQAQQFIK 128
Cdd:COG3757    7 AAYPVHGIDVSHYQGDIDWAAVKAAGIDFAYIKATEGTDYVDPKFARNWAGARAAGLPRGAYHFFRPCSDAAAQADNFIS 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510997722 129 SVGQDTGHLPIMVYLSYYNDYaqkPPAKAKTQRAIARFVTLINQYYHQDCIIGGAPALLKRYVPTK--GTYPLW--QTTQ 204
Cdd:COG3757   87 TVPRDPGDLPPVLDLEENGYY---GLSPAQLRAWLKAFLDEVEAHTGRKPIIYTSPSFYNDYLGNSdfSDYPLWiaRYGS 163

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 510997722 205 QRPTVGTKN-GFWQYTTASKIPG--GRDDseyqLAVFTGTPQEWQKL 248
Cdd:COG3757  164 SPGYLPGRNwTFWQYTSSGRVPGisGNVD----LNVFNGSRDELKAL 206
Glyco_hydro_25 pfam01183
Glycosyl hydrolases family 25;
58-226 4.60e-23

Glycosyl hydrolases family 25;


Pssm-ID: 426105  Cd Length: 180  Bit Score: 92.04  E-value: 4.60e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510997722   58 ISQEDGYQDYQILKKEGLKFVYLKATEGASYKDDNFDSNYSRAEGSGISVGVYHFFSFD--SSPEDQAQQF---IKSVGQ 132
Cdd:pfam01183   3 VSSYQGDIDWQKVKASGVSFVFIKATEGTDYVDPYFTTQYANARAAGLKVGAYHFARPCnsSTAAAQADYFlsnVQGLGL 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510997722  133 DTGHLPIMvylsyyNDY-AQKPPAKAKTQRAIARFVTLINQYYHQDCII-GGAPALLKR--YVPTKGTYPLW-----QTT 203
Cdd:pfam01183  83 DAGTLPPV------LDVeVTTGLTKAAATSNILRFLDRVKKQTGYKPVIyTGTSFWTNNllYGQFIADYPLWiasyaVTP 156

                         170       180
                  ....*....|....*....|...
gi 510997722  204 QQRPTVGTKNGFWQYTTASKIPG 226
Cdd:pfam01183 157 PKDYPGWTKWTFWQYTSSGSIPG 179
Glyco_25 smart00641
Glycosyl hydrolases family 25;
58-131 3.29e-07

Glycosyl hydrolases family 25;


Pssm-ID: 128889  Cd Length: 109  Bit Score: 47.41  E-value: 3.29e-07
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 510997722    58 ISQEDGYQDYQILKKEGLKFVYLKATEGASYKDDNFDSNYSRAEGSG-ISVGVYHFFSFDS-SPEDQAQQFIKSVG 131
Cdd:smart00641   6 VSDYEGGIDGAKVRNTGASFAFMKATEGAGYTPPYYSYQYFLADNAGyILRGFYHAAYPVSsSATAQANYFPSMDG 81
 
Name Accession Description Interval E-value
GH25_muramidase_2 cd06419
Uncharacterized bacterial muramidase containing a glycosyl hydrolase family 25 (GH25) ...
 46-238 5.89e-99

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: 286.60  E-value: 5.89e-99
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510997722  46 PNEQQYPVLGAQISQEDGYQDYQILKKEGLKFVYLKATEGASYKDDNFDSNYSRAEGSGISVGVYHFFSFDSSPEDQAQQ 125
Cdd:cd06419    1 PALSNYPVLGVQLSQDDGYIDFNSLQSNGISFVYLRATQGASYFDDNFLSNFSRAQGTGLSVGVIHTFSFSSTAAAQYRY 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510997722 126 FIKSVGQDTGHLPIMVYLSYYNDYAqkpPAKAKTQRAIARFVTLINQYYHQDCIIGGAPALLKRYVPTKGTYPLWQTTQQ 205
Cdd:cd06419   81 FIRKVGNNTGNLPIAIYVSYYGDYN---PDTKKSTQKLGLLVQLLEQHYNQSVIIRGTPAVLKQVVKALKQLKYWLIEDK 157

                        170       180       190
                 ....*....|....*....|....*....|...
gi 510997722 206 RPTVGTKNGFWQYTTASKIPGGRDDSEYQLAVF 238
Cdd:cd06419  158 LKGQGSKNQFWQYTANGKVKSGGNSAELPLAVF 190
Acm COG3757
Lyzozyme M1 (1,4-beta-N-acetylmuramidase), GH25 family [Cell wall/membrane/envelope biogenesis] ...
 49-248 9.00e-44

Lyzozyme M1 (1,4-beta-N-acetylmuramidase), GH25 family [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442971  Cd Length: 208  Bit Score: 146.58  E-value: 9.00e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510997722  49 QQYPVLGAQISQEDGYQDYQILKKEGLKFVYLKATEGASYKDDNFDSNYSRAEGSGISVGVYHFFSFDSSPEDQAQQFIK 128
Cdd:COG3757    7 AAYPVHGIDVSHYQGDIDWAAVKAAGIDFAYIKATEGTDYVDPKFARNWAGARAAGLPRGAYHFFRPCSDAAAQADNFIS 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510997722 129 SVGQDTGHLPIMVYLSYYNDYaqkPPAKAKTQRAIARFVTLINQYYHQDCIIGGAPALLKRYVPTK--GTYPLW--QTTQ 204
Cdd:COG3757   87 TVPRDPGDLPPVLDLEENGYY---GLSPAQLRAWLKAFLDEVEAHTGRKPIIYTSPSFYNDYLGNSdfSDYPLWiaRYGS 163

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 510997722 205 QRPTVGTKN-GFWQYTTASKIPG--GRDDseyqLAVFTGTPQEWQKL 248
Cdd:COG3757  164 SPGYLPGRNwTFWQYTSSGRVPGisGNVD----LNVFNGSRDELKAL 206
GH25_muramidase_1 cd06413
Uncharacterized bacterial muramidase containing a glycosyl hydrolase family 25 (GH25) ...
 51-240 2.68e-33

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: 119.31  E-value: 2.68e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510997722  51 YPVLGAQISQEDGYQDYQILKKEGLKFVYLKATEGASYKDDNFDSNYSRAEGSGISVGVYHFFSFDSSPEDQAQQFIKSV 130
Cdd:cd06413    1 YPVRGIDVSHHQGDIDWARVRAQGVSFAYIKATEGGDHVDKRFAENWRGARAAGLPRGAYHFFTFCRSGAEQAANFIRNV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510997722 131 GQDTGHLPIMVYLSYYNDYAQKPPAkAKTQRAIARFVTLINQYYHQDCIIGGAPALLKRYVptKGT---YPLW-QTTQQR 206
Cdd:cd06413   81 PKDPGALPPVVDVEWNGNSATCPSA-EEVLAELQVFLDALEAHYGKRPIIYTTYDFYDDYL--KGEfpdYPLWiRSVAGH 157

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 510997722 207 PTVGTKNG--FWQYTTASKIPGGRDDSEyqLAVFTG 240
Cdd:cd06413  158 PRLYEDRPwtFWQYTNRGRVPGIEGDVD--LNVFNG 191
GH25_muramidase cd00599
Endo-N-acetylmuramidases (muramidases) are lysozymes (also referred to as peptidoglycan ...
 55-230 3.05e-33

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: 118.99  E-value: 3.05e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510997722  55 GAQISQEDGYQDYQILKKEGLKFVYLKATEGASYKDDNFDSNYSRAEGSGISVGVYHFFSFDSSPEDQAQQFIKSVGQDT 134
Cdd:cd00599    2 GIDVSSWQGSIDWNAVKAAGIDFVFIKATEGTTYVDPKFATNRARARAAGLLVGAYHFARPCANAEAQADNFVNTVPRDP 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510997722 135 GHLPIMVYLSYYNDYaqkpPAKAKTQRAIARFVTLINQYYHQDCIIGGAPALLKRYV--PTKGTYPLW-----QTTQQRP 207
Cdd:cd00599   82 GSLPLVLDVEDTGGG----CSAAALAAWLNAFLNEVEALTGKKPIIYTSPSFWDDYLasSQLSDYPLWiahyrGEPPPAP 157

                        170       180
                 ....*....|....*....|...
gi 510997722 208 TVGTKNGFWQYTTASKIPGGRDD 230
Cdd:cd00599  158 GAWRPWTLWQYTSSGRVPGISGP 180
Glyco_hydro_25 pfam01183
Glycosyl hydrolases family 25;
58-226 4.60e-23

Glycosyl hydrolases family 25;


Pssm-ID: 426105  Cd Length: 180  Bit Score: 92.04  E-value: 4.60e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510997722   58 ISQEDGYQDYQILKKEGLKFVYLKATEGASYKDDNFDSNYSRAEGSGISVGVYHFFSFD--SSPEDQAQQF---IKSVGQ 132
Cdd:pfam01183   3 VSSYQGDIDWQKVKASGVSFVFIKATEGTDYVDPYFTTQYANARAAGLKVGAYHFARPCnsSTAAAQADYFlsnVQGLGL 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510997722  133 DTGHLPIMvylsyyNDY-AQKPPAKAKTQRAIARFVTLINQYYHQDCII-GGAPALLKR--YVPTKGTYPLW-----QTT 203
Cdd:pfam01183  83 DAGTLPPV------LDVeVTTGLTKAAATSNILRFLDRVKKQTGYKPVIyTGTSFWTNNllYGQFIADYPLWiasyaVTP 156

                         170       180
                  ....*....|....*....|...
gi 510997722  204 QQRPTVGTKNGFWQYTTASKIPG 226
Cdd:pfam01183 157 PKDYPGWTKWTFWQYTSSGSIPG 179
GH25_Lyc-like cd06525
Lyc muramidase is an autolytic lysozyme (autolysin) from Clostridium acetobutylicum encoded by ...
 55-226 1.84e-21

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: 88.12  E-value: 1.84e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510997722  55 GAQISQEDGYQDYQILKKEGLKFVYLKATEGASYKDDNFDSNYSRAEGSGISVGVYHFFSFDSSPEDQAQQFIKSVGQDT 134
Cdd:cd06525    2 GIDISNWQGNINFNAVKDSGVEVVYIKATEGTTFVDSYFNENYNGAKAAGLKVGFYHFLVGTSNPEEQAENFYNTIKGKK 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510997722 135 GHLPIMVylsyynDYAQKPPAKAKTQRAIA-RFVTLINQYYHQDCII----GGAPALLKRYVPtkgTYPLW--QTTQQRP 207
Cdd:cd06525   82 MDLKPAL------DVEVNFGLSKDELNDYVlRFIEEFEKLSGLKVGIytytSFINNNLDSRLS---SYPLWiaNYGVSPP 152

                        170       180
                 ....*....|....*....|..
gi 510997722 208 T---VGTKNGFWQYTTASKIPG 226
Cdd:cd06525  153 SsngIWNSWVGFQYSETGRVNG 174
GH25_YegX-like cd06524
YegX is an uncharacterized bacterial protein with a glycosyl hydrolase family 25 (GH25) ...
 54-226 8.08e-20

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: 83.93  E-value: 8.08e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510997722  54 LGAQISQEDGYQDYQILKKE----GLKFVYLKATEGASYKDDNFDSNYSRAEGSGISVGVYHFFSFDSSPEDQAQQFIKS 129
Cdd:cd06524    1 FGIDVSHYQGKIDWQKVKAKvkdsPVAFVFIKATEGVDIVDPDFPTNWEGAKEAGIIRGAYHFYRPNSDPKQQADNFLNT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510997722 130 VG-QDTGHLPIMVYLSyYNDYAQKPpakAKTQRAIARFVTLINQYYHQDCIIGGAPALLKRYVPTKG--TYPLW------ 200
Cdd:cd06524   81 VKlLGPGDLPPVLDVE-WDGRKSSA---KQIQEGVLEWLDAVEKATGVKPIIYTNPSFWTDYLTDSSfsEYPLWiadynp 156

                        170       180
                 ....*....|....*....|....*.
gi 510997722 201 QTTQQRPTVGTKNGFWQYTTASKIPG 226
Cdd:cd06524  157 RRKKVPPNESKKWLLWQYSDSGKVPG 182
GH25_CH-type cd06412
CH-type (Chalaropsis-type) lysozymes represent one of four functionally-defined classes of ...
 53-229 4.33e-16

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: 74.28  E-value: 4.33e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510997722  53 VLGAQISQEDGYQDYQILKKEGLKFVYLKATEGASYKDDNFDSNYSRAEGSGISVGVYHF-FSFDSSPEDQAQQFIKSVG 131
Cdd:cd06412    1 VPGIDVSGHQGSVDWSGAAANGARFAYVKATEGTSYTNPRFSSQYNGAYNAGLIRGAYHFaLPDQSSGAAQADYFLDHGG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510997722 132 QDTGH---LPIMVYLSyYNDYAQKPPAKAKTQRA--IARFVTLINQYYHQDCIIGGAPALLKRYV---PTKGTYPLWqTT 203
Cdd:cd06412   81 GWSPDgrtLPGVLDLE-YNPYGATCYGLSPAQMVswIKDFSDTYKARTGRDPVIYTTTSWWNQCTgnsAGFANHPLW-LA 158

                        170       180       190
                 ....*....|....*....|....*....|..
gi 510997722 204 QQRPTVGTKNG------FWQYTTASKIPGGRD 229
Cdd:cd06412  159 RYGSSPGALPAgwsawtFWQYSDSGPFPGDQN 190
Glyco_25 smart00641
Glycosyl hydrolases family 25;
58-131 3.29e-07

Glycosyl hydrolases family 25;


Pssm-ID: 128889  Cd Length: 109  Bit Score: 47.41  E-value: 3.29e-07
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 510997722    58 ISQEDGYQDYQILKKEGLKFVYLKATEGASYKDDNFDSNYSRAEGSG-ISVGVYHFFSFDS-SPEDQAQQFIKSVG 131
Cdd:smart00641   6 VSDYEGGIDGAKVRNTGASFAFMKATEGAGYTPPYYSYQYFLADNAGyILRGFYHAAYPVSsSATAQANYFPSMDG 81
GH25_LytC-like cd06414
The LytC lysozyme of Streptococcus pneumoniae is a bacterial cell wall hydrolase that cleaves ...
 55-226 4.16e-06

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: 46.02  E-value: 4.16e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510997722  55 GAQISQEDGYQDYQILKKEGLKFVYLKA---TEGASYKDDNFDSNYSRAEGSGISVGVYHfFSFDSSPED---QAQQFIK 128
Cdd:cd06414    3 GIDVSEWQGDIDWKKVKASGVDFAIIRAgygGYGELQEDKYFEENIKGAKAAGIPVGVYF-YSYAVTVAEareEAEFVLR 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510997722 129 SVGQDTGHLPImvylsYYnDYAQKPPAKAKTQR----AIAR-FVTLINQ--YYhqdCIIGGAPALLKRYV--PTKGTYPL 199
Cdd:cd06414   82 LIKGYKLSYPV-----YY-DLEDETQLGAGLSKdqrtDIANaFCETIEAagYY---PGIYANLSWLTNKLddERLSKYDV 152

                        170       180
                 ....*....|....*....|....*....
gi 510997722 200 W--QTTQQrPTVGTKNGFWQYTTASKIPG 226
Cdd:cd06414  153 WvaQYGNS-PTYPGNYGMWQYTSSGSVPG 180
GH25_AtlA-like cd06522
AtlA is an autolysin found in Gram-positive lactic acid bacteria that degrades bacterial cell ...
 66-135 9.47e-06

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: 45.05  E-value: 9.47e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 510997722  66 DYQILKKEGLKFVYLKATEGASYKDDNFDSNYSRAEGSGISVGVYHFFSFDSSPEDQAQ-----QFIKSVGQDTG 135
Cdd:cd06522   17 DYNKLKNYGVKAVIVKLTEGTTYRNPYAASQIANAKAAGLKVSAYHYAHYTSAADAQAEaryfaNTAKSLGLSKN 91
GH25_LysA-like cd06417
LysA is a cell wall endolysin produced by Lactobacillus fermentum, which degrades bacterial ...
 77-245 4.25e-04

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: 40.12  E-value: 4.25e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510997722  77 FVYLKATEGASYKDDNFDSNYSRAEGSGISVGVYHFFSfDSSPEDQAQQFIKSVGQDTGHLPIMVYLSYYNDYAQKPPAK 156
Cdd:cd06417   22 FVIVKATQGTGYVNPSWRSQAAQAIAAGKLLGLYHYAN-GGNAIAEADYFLNNIKGYVGKAVLVLDWESYQNSAWGNSAW 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510997722 157 AKtqraiaRFVTLINQ-------YYHQDCIIGGAPAllkryvPTKGTYPLW--------QTTQQRPTvGTKNGFW----- 216
Cdd:cd06417  101 AR------QWVNRVHEltgvwpmVYVSKSVTRQINW------SVRADCGLWvaqyasnnPTGYQSQA-GPWNAAWsgeti 167

                        170       180       190
                 ....*....|....*....|....*....|
gi 510997722 217 -QYTTASKIPGGRDDSEyqLAVFTGTPQEW 245
Cdd:cd06417  168 hQYTSNGSLNGYNGPLD--LNLFYGDREQW 195
GH25_Lys1-like cd06416
Lys-1 is a lysozyme encoded by the Caenorhabditis elegans lys-1 gene. This gene is one of a ...
 53-133 9.20e-04

Lys-1 is a lysozyme encoded by the Caenorhabditis elegans lys-1 gene. This gene is one of a several lysozyme genes upregulated upon infection by the Gram-negative bacterial pathogen Serratia marcescens. Lys-1 contains a glycosyl hydrolase family 25 (GH25) catalytic domain. This family also includes Lys-5 from Caenorhabditis elegans.


Pssm-ID: 119378  Cd Length: 196  Bit Score: 39.23  E-value: 9.20e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510997722  53 VLGAQISQEDGYQDYQILKKEGLKFVYLKATEGASYKDDNFDSNYSRAEGSGISVGVYHF--FSFDSSPEDQAQQFIKSV 130
Cdd:cd06416    1 ILGVDISQPTSVSTFQCLKNNGYSFAIIRAYRSNGSFDPNSVTNIKNARAAGLSTDVYFFpcINCCGSAAGQVQTFLQYL 80


                 ...
gi 510997722 131 GQD 133
Cdd:cd06416   81 KAN 83
 
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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