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Conserved domains on  [gi|446431999|ref|WP_000509854|]
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MULTISPECIES: GH25 family lysozyme [Bacillus]

Protein Classification

glycoside hydrolase family 25 domain-containing protein; glycoside hydrolase family 25 protein( domain architecture ID 10158189)

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_PlyB-like cd06523
PlyB is a bacteriophage endolysin that displays potent lytic activity toward Bacillus ...
 4-176 7.84e-93

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: 271.16  E-value: 7.84e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446431999   4 IIDISKWNGDINWS--IAKQHIDFIIARVQDGSNYVDPLYKGYVQAMKQHGIPFGNYAFCRFVSIADAKKEAQDFWNRGD 81
Cdd:cd06523    2 IVDISEWQGPINWDydTLSKQLDLVIIRVQYGSNYVDLKYKNNIKEFKKRGIPFGVYAFARGTSTADAKAEARDFYNRAN 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446431999  82 KSATVWVADVEVKTMNDMRAGTQAFIDELYRLGAKKVGLYVGHHMYTPFGMANVKSDFVWIPRYGGNKPAYPCDIWQYTE 161
Cdd:cd06523   82 KKPTFYVLDVEVTSMSDMNAGVQAFISELRRLGAKKVGLYIGHHFYTTFNLAVSKFDAIWIPAYGSNPGTYPYDLWQYTD 161

                        170
                 ....*....|....*.
gi 446431999 162 TGNVPGI-GKCDLNSL 176
Cdd:cd06523  162 SGYLPGIsGNVDLNRL 177
CBD_PlyG pfam12123
PlyG Cell wall binding domain; This domain is found in bacteria and viruses. This domain is ...
 221-264 2.55e-21

PlyG Cell wall binding domain; This domain is found in bacteria and viruses. This domain is about 50 amino acids in length. This domain is thought to be a cell wall binding domain.


:

Pssm-ID: 338253  Cd Length: 44  Bit Score: 84.08  E-value: 2.55e-21
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 446431999  221 SLKMTAKFILKPDGLTYFISDPTSDAQLNAMKEYLDRKGWWYEV 264
Cdd:pfam12123   1 SLGMTGKIILQPDGLTYFITDPTSDTQLDKFTAWLDRKGWWYEY 44
 
Name Accession Description Interval E-value
GH25_PlyB-like cd06523
PlyB is a bacteriophage endolysin that displays potent lytic activity toward Bacillus ...
 4-176 7.84e-93

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: 271.16  E-value: 7.84e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446431999   4 IIDISKWNGDINWS--IAKQHIDFIIARVQDGSNYVDPLYKGYVQAMKQHGIPFGNYAFCRFVSIADAKKEAQDFWNRGD 81
Cdd:cd06523    2 IVDISEWQGPINWDydTLSKQLDLVIIRVQYGSNYVDLKYKNNIKEFKKRGIPFGVYAFARGTSTADAKAEARDFYNRAN 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446431999  82 KSATVWVADVEVKTMNDMRAGTQAFIDELYRLGAKKVGLYVGHHMYTPFGMANVKSDFVWIPRYGGNKPAYPCDIWQYTE 161
Cdd:cd06523   82 KKPTFYVLDVEVTSMSDMNAGVQAFISELRRLGAKKVGLYIGHHFYTTFNLAVSKFDAIWIPAYGSNPGTYPYDLWQYTD 161

                        170
                 ....*....|....*.
gi 446431999 162 TGNVPGI-GKCDLNSL 176
Cdd:cd06523  162 SGYLPGIsGNVDLNRL 177
Acm COG3757
Lyzozyme M1 (1,4-beta-N-acetylmuramidase), GH25 family [Cell wall/membrane/envelope biogenesis] ...
 3-181 4.29e-54

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


Pssm-ID: 442971  Cd Length: 208  Bit Score: 173.93  E-value: 4.29e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446431999   3 HIIDISKWNGDINWS-IAKQHIDFIIARVQDGSNYVDPLYKGYVQAMKQHGIPFGNYAFCRFVSiaDAKKEAQDFWNR-- 79
Cdd:COG3757   12 HGIDVSHYQGDIDWAaVKAAGIDFAYIKATEGTDYVDPKFARNWAGARAAGLPRGAYHFFRPCS--DAAAQADNFISTvp 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446431999  80 GDKSATVWVADVEVKTMN-----DMRAGTQAFIDELYRLGAKKVGLYVGHHMYTPF-GMANVKSDFVWIPRYGGN---KP 150
Cdd:COG3757   90 RDPGDLPPVLDLEENGYYglspaQLRAWLKAFLDEVEAHTGRKPIIYTSPSFYNDYlGNSDFSDYPLWIARYGSSpgyLP 169

                        170       180       190
                 ....*....|....*....|....*....|..
gi 446431999 151 AYPCDIWQYTETGNVPGI-GKCDLNSLIGNKS 181
Cdd:COG3757  170 GRNWTFWQYTSSGRVPGIsGNVDLNVFNGSRD 201
Glyco_hydro_25 pfam01183
Glycosyl hydrolases family 25;
5-168 1.25e-30

Glycosyl hydrolases family 25;


Pssm-ID: 426105  Cd Length: 180  Bit Score: 112.46  E-value: 1.25e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446431999    5 IDISKWNGDINWSIAKQH-IDFIIARVQDGSNYVDPLYKGYVQAMKQHGIPFGNYAFCRFVSIADAKKEAQDFWNRG--- 80
Cdd:pfam01183   1 IDVSSYQGDIDWQKVKASgVSFVFIKATEGTDYVDPYFTTQYANARAAGLKVGAYHFARPCNSSTAAAQADYFLSNVqgl 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446431999   81 --DKSATVWVADVEVK---TMNDMRAGTQAFIDELYRLGAKKVGLYVGHHMYT-PFGMANVKSDF-VWIPRYGGNKPAYP 153
Cdd:pfam01183  81 glDAGTLPPVLDVEVTtglTKAAATSNILRFLDRVKKQTGYKPVIYTGTSFWTnNLLYGQFIADYpLWIASYAVTPPKDY 160

                         170       180
                  ....*....|....*....|
gi 446431999  154 CD-----IWQYTETGNVPGI 168
Cdd:pfam01183 161 PGwtkwtFWQYTSSGSIPGV 180
CBD_PlyG pfam12123
PlyG Cell wall binding domain; This domain is found in bacteria and viruses. This domain is ...
 221-264 2.55e-21

PlyG Cell wall binding domain; This domain is found in bacteria and viruses. This domain is about 50 amino acids in length. This domain is thought to be a cell wall binding domain.


Pssm-ID: 338253  Cd Length: 44  Bit Score: 84.08  E-value: 2.55e-21
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 446431999  221 SLKMTAKFILKPDGLTYFISDPTSDAQLNAMKEYLDRKGWWYEV 264
Cdd:pfam12123   1 SLGMTGKIILQPDGLTYFITDPTSDTQLDKFTAWLDRKGWWYEY 44
 
Name Accession Description Interval E-value
GH25_PlyB-like cd06523
PlyB is a bacteriophage endolysin that displays potent lytic activity toward Bacillus ...
 4-176 7.84e-93

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: 271.16  E-value: 7.84e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446431999   4 IIDISKWNGDINWS--IAKQHIDFIIARVQDGSNYVDPLYKGYVQAMKQHGIPFGNYAFCRFVSIADAKKEAQDFWNRGD 81
Cdd:cd06523    2 IVDISEWQGPINWDydTLSKQLDLVIIRVQYGSNYVDLKYKNNIKEFKKRGIPFGVYAFARGTSTADAKAEARDFYNRAN 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446431999  82 KSATVWVADVEVKTMNDMRAGTQAFIDELYRLGAKKVGLYVGHHMYTPFGMANVKSDFVWIPRYGGNKPAYPCDIWQYTE 161
Cdd:cd06523   82 KKPTFYVLDVEVTSMSDMNAGVQAFISELRRLGAKKVGLYIGHHFYTTFNLAVSKFDAIWIPAYGSNPGTYPYDLWQYTD 161

                        170
                 ....*....|....*.
gi 446431999 162 TGNVPGI-GKCDLNSL 176
Cdd:cd06523  162 SGYLPGIsGNVDLNRL 177
Acm COG3757
Lyzozyme M1 (1,4-beta-N-acetylmuramidase), GH25 family [Cell wall/membrane/envelope biogenesis] ...
 3-181 4.29e-54

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


Pssm-ID: 442971  Cd Length: 208  Bit Score: 173.93  E-value: 4.29e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446431999   3 HIIDISKWNGDINWS-IAKQHIDFIIARVQDGSNYVDPLYKGYVQAMKQHGIPFGNYAFCRFVSiaDAKKEAQDFWNR-- 79
Cdd:COG3757   12 HGIDVSHYQGDIDWAaVKAAGIDFAYIKATEGTDYVDPKFARNWAGARAAGLPRGAYHFFRPCS--DAAAQADNFISTvp 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446431999  80 GDKSATVWVADVEVKTMN-----DMRAGTQAFIDELYRLGAKKVGLYVGHHMYTPF-GMANVKSDFVWIPRYGGN---KP 150
Cdd:COG3757   90 RDPGDLPPVLDLEENGYYglspaQLRAWLKAFLDEVEAHTGRKPIIYTSPSFYNDYlGNSDFSDYPLWIARYGSSpgyLP 169

                        170       180       190
                 ....*....|....*....|....*....|..
gi 446431999 151 AYPCDIWQYTETGNVPGI-GKCDLNSLIGNKS 181
Cdd:COG3757  170 GRNWTFWQYTSSGRVPGIsGNVDLNVFNGSRD 201
GH25_muramidase cd00599
Endo-N-acetylmuramidases (muramidases) are lysozymes (also referred to as peptidoglycan ...
 3-174 1.70e-41

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: 140.95  E-value: 1.70e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446431999   3 HIIDISKWNGDINWSIAKQ-HIDFIIARVQDGSNYVDPLYKGYVQAMKQHGIPFGNYAFCRFVSiaDAKKEAQDFWN--R 79
Cdd:cd00599    1 KGIDVSSWQGSIDWNAVKAaGIDFVFIKATEGTTYVDPKFATNRARARAAGLLVGAYHFARPCA--NAEAQADNFVNtvP 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446431999  80 GDKSATVWVADVEVKTM----NDMRAGTQAFIDELYRLGAKKVGLYVGHHMYTPFGMANVKSDFV-WIPRYGGNKPAY-- 152
Cdd:cd00599   79 RDPGSLPLVLDVEDTGGgcsaAALAAWLNAFLNEVEALTGKKPIIYTSPSFWDDYLASSQLSDYPlWIAHYRGEPPPApg 158

                        170       180
                 ....*....|....*....|....*.
gi 446431999 153 ---PCDIWQYTETGNVPGI-GKCDLN 174
Cdd:cd00599  159 awrPWTLWQYTSSGRVPGIsGPVDLN 184
GH25_LytC-like cd06414
The LytC lysozyme of Streptococcus pneumoniae is a bacterial cell wall hydrolase that cleaves ...
 5-174 3.70e-31

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: 114.20  E-value: 3.70e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446431999   5 IDISKWNGDINWSIAKQ-HIDFIIARV---QDGSNYVDPLYKGYVQAMKQHGIPFGNYAFCRFVSIADAKKEAQDF-WNR 79
Cdd:cd06414    4 IDVSEWQGDIDWKKVKAsGVDFAIIRAgygGYGELQEDKYFEENIKGAKAAGIPVGVYFYSYAVTVAEAREEAEFVlRLI 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446431999  80 GDKSATVWVA-DVEVKTMNDMRAGTQ-------AFIDELYRLGAkKVGLYVGHHMYT-PFGMANVKSDFVWIPRYgGNKP 150
Cdd:cd06414   84 KGYKLSYPVYyDLEDETQLGAGLSKDqrtdianAFCETIEAAGY-YPGIYANLSWLTnKLDDERLSKYDVWVAQY-GNSP 161

                        170       180
                 ....*....|....*....|....*..
gi 446431999 151 AYP--CDIWQYTETGNVPGI-GKCDLN 174
Cdd:cd06414  162 TYPgnYGMWQYTSSGSVPGIsGNVDLN 188
Glyco_hydro_25 pfam01183
Glycosyl hydrolases family 25;
5-168 1.25e-30

Glycosyl hydrolases family 25;


Pssm-ID: 426105  Cd Length: 180  Bit Score: 112.46  E-value: 1.25e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446431999    5 IDISKWNGDINWSIAKQH-IDFIIARVQDGSNYVDPLYKGYVQAMKQHGIPFGNYAFCRFVSIADAKKEAQDFWNRG--- 80
Cdd:pfam01183   1 IDVSSYQGDIDWQKVKASgVSFVFIKATEGTDYVDPYFTTQYANARAAGLKVGAYHFARPCNSSTAAAQADYFLSNVqgl 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446431999   81 --DKSATVWVADVEVK---TMNDMRAGTQAFIDELYRLGAKKVGLYVGHHMYT-PFGMANVKSDF-VWIPRYGGNKPAYP 153
Cdd:pfam01183  81 glDAGTLPPVLDVEVTtglTKAAATSNILRFLDRVKKQTGYKPVIYTGTSFWTnNLLYGQFIADYpLWIASYAVTPPKDY 160

                         170       180
                  ....*....|....*....|
gi 446431999  154 CD-----IWQYTETGNVPGI 168
Cdd:pfam01183 161 PGwtkwtFWQYTSSGSIPGV 180
GH25_Lyc-like cd06525
Lyc muramidase is an autolytic lysozyme (autolysin) from Clostridium acetobutylicum encoded by ...
 5-174 2.13e-24

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: 96.21  E-value: 2.13e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446431999   5 IDISKWNGDINWSIAKQH-IDFIIARVQDGSNYVDPLYKGYVQAMKQHGIPFGNYAFcrFVSIADAKKEAQDFWN--RGD 81
Cdd:cd06525    3 IDISNWQGNINFNAVKDSgVEVVYIKATEGTTFVDSYFNENYNGAKAAGLKVGFYHF--LVGTSNPEEQAENFYNtiKGK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446431999  82 KSATVWVADVEVktmNDMRAGTQA------FIDELYRLGAKKVGLYVghhmYTPFGMANVKSDF----VWIPRYGGNKPA 151
Cdd:cd06525   81 KMDLKPALDVEV---NFGLSKDELndyvlrFIEEFEKLSGLKVGIYT----YTSFINNNLDSRLssypLWIANYGVSPPS 153

                        170       180
                 ....*....|....*....|....*....
gi 446431999 152 -----YPCDIWQYTETGNVPGI-GKCDLN 174
Cdd:cd06525  154 sngiwNSWVGFQYSETGRVNGVsGSVDLD 182
CBD_PlyG pfam12123
PlyG Cell wall binding domain; This domain is found in bacteria and viruses. This domain is ...
 221-264 2.55e-21

PlyG Cell wall binding domain; This domain is found in bacteria and viruses. This domain is about 50 amino acids in length. This domain is thought to be a cell wall binding domain.


Pssm-ID: 338253  Cd Length: 44  Bit Score: 84.08  E-value: 2.55e-21
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 446431999  221 SLKMTAKFILKPDGLTYFISDPTSDAQLNAMKEYLDRKGWWYEV 264
Cdd:pfam12123   1 SLGMTGKIILQPDGLTYFITDPTSDTQLDKFTAWLDRKGWWYEY 44
GH25_YegX-like cd06524
YegX is an uncharacterized bacterial protein with a glycosyl hydrolase family 25 (GH25) ...
 5-174 3.18e-18

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: 80.08  E-value: 3.18e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446431999   5 IDISKWNGDINWS-----IAKQHIDFIIARVQDGSNYVDPLYKGYVQAMKQHGIPFGNYAFcrFVSIADAKKEAQDFWN- 78
Cdd:cd06524    3 IDVSHYQGKIDWQkvkakVKDSPVAFVFIKATEGVDIVDPDFPTNWEGAKEAGIIRGAYHF--YRPNSDPKQQADNFLNt 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446431999  79 -----RGDKSAtvwVADVEV----KTMNDMRAGTQAFIDELYRLGAKKVGLYVGHHMYTPFGMANVKSDF-VWI----PR 144
Cdd:cd06524   81 vkllgPGDLPP---VLDVEWdgrkSSAKQIQEGVLEWLDAVEKATGVKPIIYTNPSFWTDYLTDSSFSEYpLWIadynPR 157

                        170       180       190
                 ....*....|....*....|....*....|...
gi 446431999 145 YGGNKPAY--PCDIWQYTETGNVPGIGKC-DLN 174
Cdd:cd06524  158 RKKVPPNEskKWLLWQYSDSGKVPGISGAvDLN 190
GH25_muramidase_1 cd06413
Uncharacterized bacterial muramidase containing a glycosyl hydrolase family 25 (GH25) ...
 3-178 3.61e-18

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: 80.02  E-value: 3.61e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446431999   3 HIIDISKWNGDINWS-IAKQHIDFIIARVQDGSNYVDPLYKGYVQAMKQHGIPFGNYAFCRFVSiaDAKKEAQDFWNR-- 79
Cdd:cd06413    4 RGIDVSHHQGDIDWArVRAQGVSFAYIKATEGGDHVDKRFAENWRGARAAGLPRGAYHFFTFCR--SGAEQAANFIRNvp 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446431999  80 GDKSATVWVADVEV-------KTMNDMRAGTQAFIDELYRLGAKKVGLYVGHHMYTPFGMANVKSDFVWIPRYGGNKPAY 152
Cdd:cd06413   82 KDPGALPPVVDVEWngnsatcPSAEEVLAELQVFLDALEAHYGKRPIIYTTYDFYDDYLKGEFPDYPLWIRSVAGHPRLY 161

                        170       180       190
                 ....*....|....*....|....*....|
gi 446431999 153 PCD---IWQYTETGNVPGI-GKCDLNSLIG 178
Cdd:cd06413  162 EDRpwtFWQYTNRGRVPGIeGDVDLNVFNG 191
GH25_AtlA-like cd06522
AtlA is an autolysin found in Gram-positive lactic acid bacteria that degrades bacterial cell ...
 5-167 3.93e-16

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: 74.33  E-value: 3.93e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446431999   5 IDISKWNGDI---NW-SIAKQHIDFIIARVQDGSNYVDPLYKGYVQAMKQHGIPFGNYAFCRFVSIADAKKEAQDFWNRG 80
Cdd:cd06522    4 VDVSSNNGIMsvaDYnKLKNYGVKAVIVKLTEGTTYRNPYAASQIANAKAAGLKVSAYHYAHYTSAADAQAEARYFANTA 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446431999  81 DKSA----TVWVADVE-VKTMNDMRAGTQAFIDELYRLGAKKVGLYV-GHHMYTPFGMANVKSDFVWIPRYGGNKPA--- 151
Cdd:cd06522   84 KSLGlsknTVMVADMEdSSSSGNATANVNAFWQTMKAAGYKNTDVYTsASWLNSRADTSTLGAKRVWVAQYPYNPSSnnl 163

                        170
                 ....*....|....*...
gi 446431999 152 YPCDI--WQYTETGNVPG 167
Cdd:cd06522  164 WNTNYgaWQWTSQAHFPG 181
GH25_Cpl1-like cd06415
Cpl-1 lysin (also known as Cpl-9 lysozyme / muramidase) is a bacterial cell wall endolysin ...
 3-167 4.49e-09

Cpl-1 lysin (also known as Cpl-9 lysozyme / muramidase) is a bacterial cell wall endolysin encoded by the pneumococcal bacteriophage Cp-1, which cleaves the glycosidic N-acetylmuramoyl-(beta1,4)-N-acetylglucosamine bonds of the pneumococcal glycan chain, thus acting as an enzymatic antimicrobial agent (an enzybiotic) against streptococcal infections. Cpl-1 belongs to the CP family of lysozymes (CPL lysozymes) which includes the Cpl-7 lysin. Cpl-1 has a glycosyl hydrolase family 25 (GH25) catalytic domain with an irregular (beta/alpha)5-beta3 barrel and a C-terminal cell wall-anchoring module formed by six similar choline-binding repeats (ChBr's). The ChBr's facilitate the anchoring of Cpl-1 to the choline-containing teichoic acid of the pneumococcal cell wall. Other members of this domain family have an N-terminal CHAP (cysteine, histidine-dependent amidohydrolases/peptidases) domain similar to that of the firmicute CHAP lysins and associated with endopeptidase activity. The Cpl-7 lysin is also included here as is LysB of Lactococcus phage, and the Mur lysin of Lactobacillus phage.


Pssm-ID: 119377  Cd Length: 196  Bit Score: 54.71  E-value: 4.49e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446431999   3 HIIDISKWNGDINWSIAKQHIDFIIARVQDGSNYVDPLYKGYVQAMKQHGIPFGNYAFCRFV-SIADAKKEAQDFWNR-- 79
Cdd:cd06415    2 YGVDVASYQGTDLTAYGQAGAKFAIVKISEGTNYVNPKASAQVSSAIANGKMTGGYHFARFGgSVSQAKYEADYFLNSaq 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446431999  80 --GDKSATVWVADVEVKTMNDMRAGTQA---FIDELYRLGAKKvGLYvghhMYTPFGMANVKS--------DFVWIPRY- 145
Cdd:cd06415   82 qaGLPKGSYLALDYEQGSGNSKAANTSAilaFMDTIKDAGYKP-MLY----SYKPLLLNNVDYsqiiakypNSLWVAAYp 156

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 446431999 146 ---GGNKPAYP-------CDIWQYTET---GNVPG 167
Cdd:cd06415  157 tygVQDTPDFNyfpsmdgVAIWQFTSNwrgGGVDG 191
GH25_CH-type cd06412
CH-type (Chalaropsis-type) lysozymes represent one of four functionally-defined classes of ...
 5-167 7.38e-05

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: 42.69  E-value: 7.38e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446431999   5 IDISKWNGDINWSIAKQH-IDFIIARVQDGSNYVDPLYKGYVQAMKQHGIPFGNYAFCRfVSIADAKKEAQDFWNRGDK- 82
Cdd:cd06412    4 IDVSGHQGSVDWSGAAANgARFAYVKATEGTSYTNPRFSSQYNGAYNAGLIRGAYHFAL-PDQSSGAAQADYFLDHGGGw 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446431999  83 SATVW----VADVEV---------KTMNDMRAGTQAFIDELYRLGAKKVGLYVGHH---MYTpfGMANVKSDF-VWIPRY 145
Cdd:cd06412   83 SPDGRtlpgVLDLEYnpygatcygLSPAQMVSWIKDFSDTYKARTGRDPVIYTTTSwwnQCT--GNSAGFANHpLWLARY 160

                        170       180
                 ....*....|....*....|....*..
gi 446431999 146 GGNKPAYPC-----DIWQYTETGNVPG 167
Cdd:cd06412  161 GSSPGALPAgwsawTFWQYSDSGPFPG 187
GH25_LysA-like cd06417
LysA is a cell wall endolysin produced by Lactobacillus fermentum, which degrades bacterial ...
 5-181 2.41e-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: 40.89  E-value: 2.41e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446431999   5 IDISKWNGDINWSIAKQhiDFIIARVQDGSNYVDPLYKGYVQAMKQHGIPFGNYAFCrfvSIADAKKEAQDFWNRGDK-- 82
Cdd:cd06417    4 IDVSSWQSRIVTTVVPA--DFVIVKATQGTGYVNPSWRSQAAQAIAAGKLLGLYHYA---NGGNAIAEADYFLNNIKGyv 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446431999  83 SATVWVADVEvKTMNDMR---AGTQAFIDELYRLGAKKVGLYVGHHMytpfgMANVKSDF-----VWIPRYGGNKPA--- 151
Cdd:cd06417   79 GKAVLVLDWE-SYQNSAWgnsAWARQWVNRVHELTGVWPMVYVSKSV-----TRQINWSVradcgLWVAQYASNNPTgyq 152

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 446431999 152 ----------YPCDIWQYTETGNVPG-IGKCDLNSLIGNKS 181
Cdd:cd06417  153 sqagpwnaawSGETIHQYTSNGSLNGyNGPLDLNLFYGDRE 193
PBP1_Qymf-like cd06291
ligand binding domain of the lacI-like transcription regulator from a novel metal-reducing ...
 41-118 7.97e-03

ligand binding domain of the lacI-like transcription regulator from a novel metal-reducing bacterium Alkaliphilus Metalliredigens (strain Qymf) and its close homologs; This group includes the ligand binding domain of the lacI-like transcription regulator from a novel metal-reducing bacterium Alkaliphilus metalliredigens (strain Qymf) and its close homologs. Qymf is a strict anaerobe that could be grown in the presence of borax and its cells are straight rods that produce endospores. This group is a member of the LacI-GalR family repressors that are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the sugar-binding domain of ABC-type transport systems that contain the type 1 periplasmic binding protein-like fold. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor.


Pssm-ID: 380514 [Multi-domain]  Cd Length: 264  Bit Score: 36.73  E-value: 7.97e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446431999  41 YKGYVQAMKQHGIPFGNYAFCRFV-SIADAKKEAQDFWNRGDKSATVWvadvevkTMNDMRAgtQAFIDELYRLGaKKV 118
Cdd:cd06291  131 YRGFEDALKEAGIEYEIIEIDENDfSEEDAYELAKELLEKYPDIDGIF-------ASNDLLA--IGVLKALQKLG-IRV 199
 
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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