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Conserved domains on  [gi|1859645326|ref|YP_009833673|]
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endolysin [Bacillus phage Deep-Purple]

Protein Classification

glycoside hydrolase family 25 protein( domain architecture ID 10158183)

glycoside hydrolase family 25 protein similar to PlyB, a bacteriophage endolysin active against Bacillus anthracis; 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

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 ...
 3-173 1.62e-80

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: 239.96  E-value: 1.62e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859645326   3 KILDISHHN-TINW--DKVAGNVEFIIARVQDGSNTVDTKYKSFVANMKQRGIPFGNYAFCRFVSVNDARVEARDFWARG 79
Cdd:cd06523     1 AIVDISEWQgPINWdyDTLSKQLDLVIIRVQYGSNYVDLKYKNNIKEFKKRGIPFGVYAFARGTSTADAKAEARDFYNRA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859645326  80 DKDAKFWVADVEVKTMSDMRAGTQAFIDELRALGAKKVGLYVGHHTYEEFNASQIKADFVWIPRYGGKNPAYPCDIWQHS 159
Cdd:cd06523    81 NKKPTFYVLDVEVTSMSDMNAGVQAFISELRRLGAKKVGLYIGHHFYTTFNLAVSKFDAIWIPAYGSNPGTYPYDLWQYT 160

                         170
                  ....*....|....*
gi 1859645326 160 EDEWIDGI-GECDSN 173
Cdd:cd06523   161 DSGYLPGIsGNVDLN 175
YraI super family cl28549
Uncharacterized conserved protein YraI [Function unknown];
190-257 4.71e-04

Uncharacterized conserved protein YraI [Function unknown];


The actual alignment was detected with superfamily member COG4991:

Pssm-ID: 444015 [Multi-domain]  Cd Length: 92  Bit Score: 38.51  E-value: 4.71e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1859645326 190 APSISNGSTVVergvirTTDRANVRTGPSLSDPVVKTLPINTdweywSIELKG---DYNWFNVGA----GYVRGD 257
Cdd:COG4991    16 APAAAAAATAV------ATDDLNLRSGPGTGYPVVGTLPAGA-----TVTVLGctsGGGWCKVSYggqrGWVSAR 79
 
Name Accession Description Interval E-value
GH25_PlyB-like cd06523
PlyB is a bacteriophage endolysin that displays potent lytic activity toward Bacillus ...
 3-173 1.62e-80

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: 239.96  E-value: 1.62e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859645326   3 KILDISHHN-TINW--DKVAGNVEFIIARVQDGSNTVDTKYKSFVANMKQRGIPFGNYAFCRFVSVNDARVEARDFWARG 79
Cdd:cd06523     1 AIVDISEWQgPINWdyDTLSKQLDLVIIRVQYGSNYVDLKYKNNIKEFKKRGIPFGVYAFARGTSTADAKAEARDFYNRA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859645326  80 DKDAKFWVADVEVKTMSDMRAGTQAFIDELRALGAKKVGLYVGHHTYEEFNASQIKADFVWIPRYGGKNPAYPCDIWQHS 159
Cdd:cd06523    81 NKKPTFYVLDVEVTSMSDMNAGVQAFISELRRLGAKKVGLYIGHHFYTTFNLAVSKFDAIWIPAYGSNPGTYPYDLWQYT 160

                         170
                  ....*....|....*
gi 1859645326 160 EDEWIDGI-GECDSN 173
Cdd:cd06523   161 DSGYLPGIsGNVDLN 175
Acm COG3757
Lyzozyme M1 (1,4-beta-N-acetylmuramidase), GH25 family [Cell wall/membrane/envelope biogenesis] ...
 3-179 4.71e-44

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


Pssm-ID: 442971  Cd Length: 208  Bit Score: 147.74  E-value: 4.71e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859645326   3 KILDISHHN-TINWDKVAG-NVEFIIARVQDGSNTVDTKYKSFVANMKQRGIPFGNYAFCRFVSvnDARVEARDFWARGD 80
Cdd:COG3757    12 HGIDVSHYQgDIDWAAVKAaGIDFAYIKATEGTDYVDPKFARNWAGARAAGLPRGAYHFFRPCS--DAAAQADNFISTVP 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859645326  81 KDAK--FWVADVEVKTM-----SDMRAGTQAFIDELRALGAKKVGLYVGHHTYEEF-NASQIKADFVWIPRYGGKNPAYP 152
Cdd:COG3757    90 RDPGdlPPVLDLEENGYyglspAQLRAWLKAFLDEVEAHTGRKPIIYTSPSFYNDYlGNSDFSDYPLWIARYGSSPGYLP 169

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1859645326 153 ---CDIWQHSEDEWIDGI-GECDSNTLLGSK 179
Cdd:COG3757   170 grnWTFWQYTSSGRVPGIsGNVDLNVFNGSR 200
Glyco_hydro_25 pfam01183
Glycosyl hydrolases family 25;
6-167 1.12e-21

Glycosyl hydrolases family 25;


Pssm-ID: 426105  Cd Length: 180  Bit Score: 88.96  E-value: 1.12e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859645326   6 DISHHN-TINWDKV-AGNVEFIIARVQDGSNTVDTKYKSFVANMKQRGIPFGNYAFCRFVSVNDARVEARDFWARGD--- 80
Cdd:pfam01183   2 DVSSYQgDIDWQKVkASGVSFVFIKATEGTDYVDPYFTTQYANARAAGLKVGAYHFARPCNSSTAAAQADYFLSNVQglg 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859645326  81 KDAKFW--VADVEVK---TMSDMRAGTQAFIDELRALGAKKVGLYVGHH-TYEEFNASQIKADF-VWIPRYGGKNPAYPC 153
Cdd:pfam01183  82 LDAGTLppVLDVEVTtglTKAAATSNILRFLDRVKKQTGYKPVIYTGTSfWTNNLLYGQFIADYpLWIASYAVTPPKDYP 161

                         170
                  ....*....|....*....
gi 1859645326 154 D-----IWQHSEDEWIDGI 167
Cdd:pfam01183 162 GwtkwtFWQYTSSGSIPGV 180
YraI COG4991
Uncharacterized conserved protein YraI [Function unknown];
190-257 4.71e-04

Uncharacterized conserved protein YraI [Function unknown];


Pssm-ID: 444015 [Multi-domain]  Cd Length: 92  Bit Score: 38.51  E-value: 4.71e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1859645326 190 APSISNGSTVVergvirTTDRANVRTGPSLSDPVVKTLPINTdweywSIELKG---DYNWFNVGA----GYVRGD 257
Cdd:COG4991    16 APAAAAAATAV------ATDDLNLRSGPGTGYPVVGTLPAGA-----TVTVLGctsGGGWCKVSYggqrGWVSAR 79
 
Name Accession Description Interval E-value
GH25_PlyB-like cd06523
PlyB is a bacteriophage endolysin that displays potent lytic activity toward Bacillus ...
 3-173 1.62e-80

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: 239.96  E-value: 1.62e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859645326   3 KILDISHHN-TINW--DKVAGNVEFIIARVQDGSNTVDTKYKSFVANMKQRGIPFGNYAFCRFVSVNDARVEARDFWARG 79
Cdd:cd06523     1 AIVDISEWQgPINWdyDTLSKQLDLVIIRVQYGSNYVDLKYKNNIKEFKKRGIPFGVYAFARGTSTADAKAEARDFYNRA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859645326  80 DKDAKFWVADVEVKTMSDMRAGTQAFIDELRALGAKKVGLYVGHHTYEEFNASQIKADFVWIPRYGGKNPAYPCDIWQHS 159
Cdd:cd06523    81 NKKPTFYVLDVEVTSMSDMNAGVQAFISELRRLGAKKVGLYIGHHFYTTFNLAVSKFDAIWIPAYGSNPGTYPYDLWQYT 160

                         170
                  ....*....|....*
gi 1859645326 160 EDEWIDGI-GECDSN 173
Cdd:cd06523   161 DSGYLPGIsGNVDLN 175
Acm COG3757
Lyzozyme M1 (1,4-beta-N-acetylmuramidase), GH25 family [Cell wall/membrane/envelope biogenesis] ...
 3-179 4.71e-44

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


Pssm-ID: 442971  Cd Length: 208  Bit Score: 147.74  E-value: 4.71e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859645326   3 KILDISHHN-TINWDKVAG-NVEFIIARVQDGSNTVDTKYKSFVANMKQRGIPFGNYAFCRFVSvnDARVEARDFWARGD 80
Cdd:COG3757    12 HGIDVSHYQgDIDWAAVKAaGIDFAYIKATEGTDYVDPKFARNWAGARAAGLPRGAYHFFRPCS--DAAAQADNFISTVP 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859645326  81 KDAK--FWVADVEVKTM-----SDMRAGTQAFIDELRALGAKKVGLYVGHHTYEEF-NASQIKADFVWIPRYGGKNPAYP 152
Cdd:COG3757    90 RDPGdlPPVLDLEENGYyglspAQLRAWLKAFLDEVEAHTGRKPIIYTSPSFYNDYlGNSDFSDYPLWIARYGSSPGYLP 169

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1859645326 153 ---CDIWQHSEDEWIDGI-GECDSNTLLGSK 179
Cdd:COG3757   170 grnWTFWQYTSSGRVPGIsGNVDLNVFNGSR 200
GH25_muramidase cd00599
Endo-N-acetylmuramidases (muramidases) are lysozymes (also referred to as peptidoglycan ...
 3-173 2.34e-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: 119.76  E-value: 2.34e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859645326   3 KILDISHHNT-INWDKVAGN-VEFIIARVQDGSNTVDTKYKSFVANMKQRGIPFGNYAFCRFVSvnDARVEARDFW--AR 78
Cdd:cd00599     1 KGIDVSSWQGsIDWNAVKAAgIDFVFIKATEGTTYVDPKFATNRARARAAGLLVGAYHFARPCA--NAEAQADNFVntVP 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859645326  79 GDKDAKFWVADVEVKTM----SDMRAGTQAFIDELRALGAKKVGLYVGHHTYEEF-NASQIKADFVWIPRYGG-----KN 148
Cdd:cd00599    79 RDPGSLPLVLDVEDTGGgcsaAALAAWLNAFLNEVEALTGKKPIIYTSPSFWDDYlASSQLSDYPLWIAHYRGepppaPG 158

                         170       180
                  ....*....|....*....|....*.
gi 1859645326 149 PAYPCDIWQHSEDEWIDGI-GECDSN 173
Cdd:cd00599   159 AWRPWTLWQYTSSGRVPGIsGPVDLN 184
GH25_LytC-like cd06414
The LytC lysozyme of Streptococcus pneumoniae is a bacterial cell wall hydrolase that cleaves ...
 2-173 4.41e-24

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: 95.33  E-value: 4.41e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859645326   2 KKILDISHHN-TINWDKV-AGNVEFIIARV---QDGSNTVDTKYKSFVANMKQRGIPFGNYAFCRFVSVNDARVEARDF- 75
Cdd:cd06414     1 KKGIDVSEWQgDIDWKKVkASGVDFAIIRAgygGYGELQEDKYFEENIKGAKAAGIPVGVYFYSYAVTVAEAREEAEFVl 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859645326  76 WARGDKDAKFWVA-DVEVKTMSDMRAGTQ-------AFIDELRALGAkKVGLYVGHHTYE-EFNASQIKADFVWIPRYGG 146
Cdd:cd06414    81 RLIKGYKLSYPVYyDLEDETQLGAGLSKDqrtdianAFCETIEAAGY-YPGIYANLSWLTnKLDDERLSKYDVWVAQYGN 159

                         170       180
                  ....*....|....*....|....*....
gi 1859645326 147 KNPAYP-CDIWQHSEDEWIDGI-GECDSN 173
Cdd:cd06414   160 SPTYPGnYGMWQYTSSGSVPGIsGNVDLN 188
Glyco_hydro_25 pfam01183
Glycosyl hydrolases family 25;
6-167 1.12e-21

Glycosyl hydrolases family 25;


Pssm-ID: 426105  Cd Length: 180  Bit Score: 88.96  E-value: 1.12e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859645326   6 DISHHN-TINWDKV-AGNVEFIIARVQDGSNTVDTKYKSFVANMKQRGIPFGNYAFCRFVSVNDARVEARDFWARGD--- 80
Cdd:pfam01183   2 DVSSYQgDIDWQKVkASGVSFVFIKATEGTDYVDPYFTTQYANARAAGLKVGAYHFARPCNSSTAAAQADYFLSNVQglg 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859645326  81 KDAKFW--VADVEVK---TMSDMRAGTQAFIDELRALGAKKVGLYVGHH-TYEEFNASQIKADF-VWIPRYGGKNPAYPC 153
Cdd:pfam01183  82 LDAGTLppVLDVEVTtglTKAAATSNILRFLDRVKKQTGYKPVIYTGTSfWTNNLLYGQFIADYpLWIASYAVTPPKDYP 161

                         170
                  ....*....|....*....
gi 1859645326 154 D-----IWQHSEDEWIDGI 167
Cdd:pfam01183 162 GwtkwtFWQYTSSGSIPGV 180
GH25_muramidase_1 cd06413
Uncharacterized bacterial muramidase containing a glycosyl hydrolase family 25 (GH25) ...
 5-177 5.41e-14

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: 68.46  E-value: 5.41e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859645326   5 LDISHHNT-INWDKV-AGNVEFIIARVQDGSNTVDTKYKSFVANMKQRGIPFGNYAFCRFVSvnDARVEARDFWAR--GD 80
Cdd:cd06413     6 IDVSHHQGdIDWARVrAQGVSFAYIKATEGGDHVDKRFAENWRGARAAGLPRGAYHFFTFCR--SGAEQAANFIRNvpKD 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859645326  81 KDAKFWVADVEV-------KTMSDMRAGTQAFIDELRALGAKKVGLYVGHHTYEEFNASQIKADFVWIPRYGGKNPAYPC 153
Cdd:cd06413    84 PGALPPVVDVEWngnsatcPSAEEVLAELQVFLDALEAHYGKRPIIYTTYDFYDDYLKGEFPDYPLWIRSVAGHPRLYED 163

                         170       180
                  ....*....|....*....|....*...
gi 1859645326 154 D---IWQHSEDEWIDGI-GECDSNTLLG 177
Cdd:cd06413   164 RpwtFWQYTNRGRVPGIeGDVDLNVFNG 191
GH25_YegX-like cd06524
YegX is an uncharacterized bacterial protein with a glycosyl hydrolase family 25 (GH25) ...
 6-170 6.45e-13

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: 65.44  E-value: 6.45e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859645326   6 DISHHNT-INWDKVAG-----NVEFIIARVQDGSNTVDTKYKSFVANMKQRGIPFGNYAFCRFVSvnDARVEAR------ 73
Cdd:cd06524     4 DVSHYQGkIDWQKVKAkvkdsPVAFVFIKATEGVDIVDPDFPTNWEGAKEAGIIRGAYHFYRPNS--DPKQQADnflntv 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859645326  74 DFWARGDKDAkfwVADVEV----KTMSDMRAGTQAFIDEL-RALGAKKVgLYVGHHTYEEFNASQIKADF-VWIPRYGGK 147
Cdd:cd06524    82 KLLGPGDLPP---VLDVEWdgrkSSAKQIQEGVLEWLDAVeKATGVKPI-IYTNPSFWTDYLTDSSFSEYpLWIADYNPR 157

                         170       180
                  ....*....|....*....|....*....
gi 1859645326 148 NPAYPCD------IWQHSEDEWIDGIGEC 170
Cdd:cd06524   158 RKKVPPNeskkwlLWQYSDSGKVPGISGA 186
GH25_Lyc-like cd06525
Lyc muramidase is an autolytic lysozyme (autolysin) from Clostridium acetobutylicum encoded by ...
 3-173 1.90e-12

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: 63.85  E-value: 1.90e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859645326   3 KILDISHHN-TINWDKVAGN-VEFIIARVQDGSNTVDTKYKSFVANMKQRGIPFGNYAFcrFVSVNDARVEARDFWAR-G 79
Cdd:cd06525     1 KGIDISNWQgNINFNAVKDSgVEVVYIKATEGTTFVDSYFNENYNGAKAAGLKVGFYHF--LVGTSNPEEQAENFYNTiK 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859645326  80 DK--DAKFWVaDVEVktmSDMRAGTQA------FIDELRALGAKKVGLYVGHHTYEEFNASQIKADFVWIPRYGGKNPA- 150
Cdd:cd06525    79 GKkmDLKPAL-DVEV---NFGLSKDELndyvlrFIEEFEKLSGLKVGIYTYTSFINNNLDSRLSSYPLWIANYGVSPPSs 154

                         170       180
                  ....*....|....*....|....*...
gi 1859645326 151 ----YPCDIWQHSEDEWIDGI-GECDSN 173
Cdd:cd06525   155 ngiwNSWVGFQYSETGRVNGVsGSVDLD 182
GH25_AtlA-like cd06522
AtlA is an autolysin found in Gram-positive lactic acid bacteria that degrades bacterial cell ...
 6-145 2.07e-08

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: 52.76  E-value: 2.07e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859645326   6 DISHHNTI----NWDKVAG-NVEFIIARVQDGSNTVDTKYKSFVANMKQRGIPFGNYAFCRFVSVNDARVEARdFWARGD 80
Cdd:cd06522     5 DVSSNNGImsvaDYNKLKNyGVKAVIVKLTEGTTYRNPYAASQIANAKAAGLKVSAYHYAHYTSAADAQAEAR-YFANTA 83

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1859645326  81 KDAKF-----WVADVEVKTMS-DMRAGTQAFIDELRALGAKKVGLYV-GHHTYEEFNASQIKADFVWIPRYG 145
Cdd:cd06522    84 KSLGLskntvMVADMEDSSSSgNATANVNAFWQTMKAAGYKNTDVYTsASWLNSRADTSTLGAKRVWVAQYP 155
GH25_CH-type cd06412
CH-type (Chalaropsis-type) lysozymes represent one of four functionally-defined classes of ...
 5-178 3.05e-04

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: 40.77  E-value: 3.05e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859645326   5 LDISHHN-TINWDKVAGN-VEFIIARVQDGSNTVDTKYKSFVANMKQRGIPFGNYAFcrfvsvndarveARDFWARGDKD 82
Cdd:cd06412     4 IDVSGHQgSVDWSGAAANgARFAYVKATEGTSYTNPRFSSQYNGAYNAGLIRGAYHF------------ALPDQSSGAAQ 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859645326  83 AKFWVA----------------DVEV---------KTMSDMRAGTQAFIDELRALGAKKVGLYVGHHTYEEFNASQikAD 137
Cdd:cd06412    72 ADYFLDhgggwspdgrtlpgvlDLEYnpygatcygLSPAQMVSWIKDFSDTYKARTGRDPVIYTTTSWWNQCTGNS--AG 149

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1859645326 138 FV----WIPRYGGKNPAYPC-----DIWQHSEdewiDGIGECDSNTLLGS 178
Cdd:cd06412   150 FAnhplWLARYGSSPGALPAgwsawTFWQYSD----SGPFPGDQNVFNGS 195
YraI COG4991
Uncharacterized conserved protein YraI [Function unknown];
190-257 4.71e-04

Uncharacterized conserved protein YraI [Function unknown];


Pssm-ID: 444015 [Multi-domain]  Cd Length: 92  Bit Score: 38.51  E-value: 4.71e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1859645326 190 APSISNGSTVVergvirTTDRANVRTGPSLSDPVVKTLPINTdweywSIELKG---DYNWFNVGA----GYVRGD 257
Cdd:COG4991    16 APAAAAAATAV------ATDDLNLRSGPGTGYPVVGTLPAGA-----TVTVLGctsGGGWCKVSYggqrGWVSAR 79
 
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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