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Conserved domains on  [gi|1786405|gb|AAC73316|]
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membrane-bound lytic murein transglycosylase D [Escherichia coli str. K-12 substr. MG1655]

Protein Classification

murein transglycosylase D( domain architecture ID 11484940)

membrane-bound lytic murein transglycosylase D catalyzes the cleavage of the beta-1,4-glycosidic bond between N-acetylmuramic acetyl-D-glucosamine (GlcNAc)

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
mltD PRK10783
membrane-bound lytic murein transglycosylase D; Provisional
 1-452 0e+00

membrane-bound lytic murein transglycosylase D; Provisional


:

Pssm-ID: 182727 [Multi-domain]  Cd Length: 456  Bit Score: 931.84  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786405     1 MKAKAILLASVLLVGCQST---GNVQQHAQSLSAAGQGEAAKFTSQARWMDDGTSIAPDGDLWAFIGDELKMGIPENDRI 77
Cdd:PRK10783   1 MKAKAILLASVLLVGCQSSkndATVQQHAQSLSSAGQGEAGKYTSQARWMDDGTSIAPDQDLWAFIGDELKMGIPENSRI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786405    78 REQKQKYLRNKSYLHDVTLRAEPYMYWIAGQVKKRNMPMELVLLPIVESAFDPHATSGANAAGIWQIIPSTGRNYGLKQT 157
Cdd:PRK10783  81 REQKQKYLRNKSYLHDVTLRAEPYMYWIVGQIKKRNMPMELVLLPIVESAFDPHATSGANAAGIWQIIPSTGRNYGLKQT 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786405   158 RNYDARRDVVASTTAALNMMQRLNKMFDGDWLLTVAAYNSGEGRVMKAIKTNKARGKSTDFWSLPLPQETKQYVPKMLAL 237
Cdd:PRK10783 161 RWYDARRDVVASTTAALDMMQRLNKMFDGDWLLTVAAYNSGEGRVMKAIKANKAKGKPTDFWSLSLPRETKIYVPKMLAL 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786405   238 SDILKNSKRYGVRLPTTDESRALARVHLSSPVEMAKVADMAGISVSKLKTFNAGVKGSTLGASGPQYVMVPKKHADQLRE 317
Cdd:PRK10783 241 SDILKNSKRYGVRLPTTDESRALARVDLGQQIELAQAAEMAGMSLTKLKTFNAGYKRSTTAPSGPHYIMVPKKHADQLRE 320

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786405   318 SLASGEIAAVQSTLVADNTPLNSRVYTVRSGDTLSSIASRLGVSTKDLQQWNKLRGSKLKPGQSLTIGAGSSAQRLANNS 397
Cdd:PRK10783 321 SLASGEIAAVQSTLVADNTPLNSRSYKVRSGDTLSGIASRLNVSTKDLQQWNNLRGSKLKVGQTLTIGAGSSAQRLANNS 400

                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 1786405   398 DSITYRVRKGDSLSSIAKRHGVNIKDVMRWNSDTA-NLQPGDKLTLFVKNNNMPDS 452
Cdd:PRK10783 401 DSITYRVRKGDSLSSIAKRHGVNIKDVMRWNSDTAkNLQPGDKLTLFVKNNSTPDS 456
 
Name Accession Description Interval E-value
mltD PRK10783
membrane-bound lytic murein transglycosylase D; Provisional
 1-452 0e+00

membrane-bound lytic murein transglycosylase D; Provisional


Pssm-ID: 182727 [Multi-domain]  Cd Length: 456  Bit Score: 931.84  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786405     1 MKAKAILLASVLLVGCQST---GNVQQHAQSLSAAGQGEAAKFTSQARWMDDGTSIAPDGDLWAFIGDELKMGIPENDRI 77
Cdd:PRK10783   1 MKAKAILLASVLLVGCQSSkndATVQQHAQSLSSAGQGEAGKYTSQARWMDDGTSIAPDQDLWAFIGDELKMGIPENSRI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786405    78 REQKQKYLRNKSYLHDVTLRAEPYMYWIAGQVKKRNMPMELVLLPIVESAFDPHATSGANAAGIWQIIPSTGRNYGLKQT 157
Cdd:PRK10783  81 REQKQKYLRNKSYLHDVTLRAEPYMYWIVGQIKKRNMPMELVLLPIVESAFDPHATSGANAAGIWQIIPSTGRNYGLKQT 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786405   158 RNYDARRDVVASTTAALNMMQRLNKMFDGDWLLTVAAYNSGEGRVMKAIKTNKARGKSTDFWSLPLPQETKQYVPKMLAL 237
Cdd:PRK10783 161 RWYDARRDVVASTTAALDMMQRLNKMFDGDWLLTVAAYNSGEGRVMKAIKANKAKGKPTDFWSLSLPRETKIYVPKMLAL 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786405   238 SDILKNSKRYGVRLPTTDESRALARVHLSSPVEMAKVADMAGISVSKLKTFNAGVKGSTLGASGPQYVMVPKKHADQLRE 317
Cdd:PRK10783 241 SDILKNSKRYGVRLPTTDESRALARVDLGQQIELAQAAEMAGMSLTKLKTFNAGYKRSTTAPSGPHYIMVPKKHADQLRE 320

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786405   318 SLASGEIAAVQSTLVADNTPLNSRVYTVRSGDTLSSIASRLGVSTKDLQQWNKLRGSKLKPGQSLTIGAGSSAQRLANNS 397
Cdd:PRK10783 321 SLASGEIAAVQSTLVADNTPLNSRSYKVRSGDTLSGIASRLNVSTKDLQQWNNLRGSKLKVGQTLTIGAGSSAQRLANNS 400

                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 1786405   398 DSITYRVRKGDSLSSIAKRHGVNIKDVMRWNSDTA-NLQPGDKLTLFVKNNNMPDS 452
Cdd:PRK10783 401 DSITYRVRKGDSLSSIAKRHGVNIKDVMRWNSDTAkNLQPGDKLTLFVKNNSTPDS 456
MltD-like cd16894
Membrane-bound lytic murein transglycosylase D and similar proteins; Lytic transglycosylases ...
 109-239 2.80e-62

Membrane-bound lytic murein transglycosylase D and similar proteins; Lytic transglycosylases (LT) catalyze the cleavage of the beta-1,4-glycosidic bond between N-acetylmuramic acid (MurNAc) and N-acetyl-D-glucosamine (GlcNAc). Membrane-bound lytic murein transglycosylase D protein (MltD) family members may have one or more small LysM domains, which may contribute to peptidoglycan binding. Unlike the similar "goose-type" lysozymes, LTs also make a new glycosidic bond with the C6 hydroxyl group of the same muramic acid residue. Proteins similar to this family include the soluble and insoluble membrane-bound LTs in bacteria, the LTs in bacteriophage lambda, as well as the eukaryotic "goose-type" lysozymes (goose egg-white lysozyme; GEWL).


Pssm-ID: 381615 [Multi-domain]  Cd Length: 129  Bit Score: 198.13  E-value: 2.80e-62
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786405  109 VKKRNMPMELVLLPIVESAFDPHATSGANAAGIWQIIPSTGRNYGLKQTRNYDARRDVVASTTAALNMMQRLNKMFdGDW 188
Cdd:cd16894   1 LLKEGLPEELKYLALVESGFNPDAVSSAGAAGLWQFMPATAREYGLRVDSWVDERRDPEKSTRAAARYLKDLYKRF-GDW 79

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|.
gi 1786405  189 LLTVAAYNSGEGRVMKAIKTNKArGKSTDFWSLPLPQETKQYVPKMLALSD 239
Cdd:cd16894  80 LLALAAYNAGEGRVRRAIKRAGT-DKWEDYYRLYLPAETRRYVPKFLAAKI 129
MltE COG0741
Soluble lytic murein transglycosylase or regulatory protein s ( may contain LysM/invasin ...
 26-244 9.41e-42

Soluble lytic murein transglycosylase or regulatory protein s ( may contain LysM/invasin domain) [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440504 [Multi-domain]  Cd Length: 244  Bit Score: 148.60  E-value: 9.41e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786405   26 AQSLSAAGQGEAAKFTSQARWMDDGTSIAPDGDLWAFIGDELKMGIPENDRIREQKQKYLRNKSYLHDVTLRAEPYMYWI 105
Cdd:COG0741  28 AAAAAAALAAAAAALAAAAAAAAGAAAAAASAAAGGPALAAALAAADALAAFAAIAALAAELLALAALLLRRPLPYLPLI 107

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786405  106 AGQVKKRNMPMELVL-LPIVESAFDPHATSGANAAGIWQIIPSTGRNYGLKQ--TRNYDARRDVVASTTAALNMMQRLNK 182
Cdd:COG0741 108 EEAAKKYGVDPALVLaLIRQESAFNPNAVSPAGARGLMQLMPATARRLGLKLglGPSPDDLFDPETNIRAGAAYLRELLD 187

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1786405  183 MFDGDWLLTVAAYNSGEGRVMKAIKTNKARgkstdFWSLPLPQETKQYVPKMLALSDILKNS 244
Cdd:COG0741 188 RFDGDLVLALAAYNAGPGRVRRWLRRNGDR-----DGEIIPYAETRNYVKKVLANYAIYRAG 244
SLT pfam01464
Transglycosylase SLT domain; This family is distantly related to pfam00062. Members are found ...
 104-217 2.54e-37

Transglycosylase SLT domain; This family is distantly related to pfam00062. Members are found in phages, type II, type III and type IV secretion systems.


Pssm-ID: 396169 [Multi-domain]  Cd Length: 114  Bit Score: 132.05  E-value: 2.54e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786405    104 WIAGQVKKRNMPMELVLLPIVESAFDPHATSGANAAGIWQIIPSTGRNYGLKQTRNYDARRDVVASTTAALNMMQRLNKM 183
Cdd:pfam01464   1 IIKAAQKYGVDPSLLLAIAQQESGFNPKAVSKSGAVGLMQIMPSTAKRLGLRVNPGVDDLFDPEKNIKAGTKYLKELYKQ 80

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1786405    184 FDGDWLLTVAAYNSGEGRVMKAIKTNKARGKSTD 217
Cdd:pfam01464  81 YGGDLWLALAAYNAGPGRVRKWIKNAGAKDKKLL 114
LysM smart00257
Lysin motif;
343-384 2.32e-12

Lysin motif;


Pssm-ID: 197609 [Multi-domain]  Cd Length: 44  Bit Score: 61.31  E-value: 2.32e-12
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 1786405     343 YTVRSGDTLSSIASRLGVSTKDLQQWNKLRGS-KLKPGQSLTI 384
Cdd:smart00257   2 YTVKKGDTLSSIARRYGISVSDLLELNNILDPdNLQVGQKLKI 44
 
Name Accession Description Interval E-value
mltD PRK10783
membrane-bound lytic murein transglycosylase D; Provisional
 1-452 0e+00

membrane-bound lytic murein transglycosylase D; Provisional


Pssm-ID: 182727 [Multi-domain]  Cd Length: 456  Bit Score: 931.84  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786405     1 MKAKAILLASVLLVGCQST---GNVQQHAQSLSAAGQGEAAKFTSQARWMDDGTSIAPDGDLWAFIGDELKMGIPENDRI 77
Cdd:PRK10783   1 MKAKAILLASVLLVGCQSSkndATVQQHAQSLSSAGQGEAGKYTSQARWMDDGTSIAPDQDLWAFIGDELKMGIPENSRI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786405    78 REQKQKYLRNKSYLHDVTLRAEPYMYWIAGQVKKRNMPMELVLLPIVESAFDPHATSGANAAGIWQIIPSTGRNYGLKQT 157
Cdd:PRK10783  81 REQKQKYLRNKSYLHDVTLRAEPYMYWIVGQIKKRNMPMELVLLPIVESAFDPHATSGANAAGIWQIIPSTGRNYGLKQT 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786405   158 RNYDARRDVVASTTAALNMMQRLNKMFDGDWLLTVAAYNSGEGRVMKAIKTNKARGKSTDFWSLPLPQETKQYVPKMLAL 237
Cdd:PRK10783 161 RWYDARRDVVASTTAALDMMQRLNKMFDGDWLLTVAAYNSGEGRVMKAIKANKAKGKPTDFWSLSLPRETKIYVPKMLAL 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786405   238 SDILKNSKRYGVRLPTTDESRALARVHLSSPVEMAKVADMAGISVSKLKTFNAGVKGSTLGASGPQYVMVPKKHADQLRE 317
Cdd:PRK10783 241 SDILKNSKRYGVRLPTTDESRALARVDLGQQIELAQAAEMAGMSLTKLKTFNAGYKRSTTAPSGPHYIMVPKKHADQLRE 320

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786405   318 SLASGEIAAVQSTLVADNTPLNSRVYTVRSGDTLSSIASRLGVSTKDLQQWNKLRGSKLKPGQSLTIGAGSSAQRLANNS 397
Cdd:PRK10783 321 SLASGEIAAVQSTLVADNTPLNSRSYKVRSGDTLSGIASRLNVSTKDLQQWNNLRGSKLKVGQTLTIGAGSSAQRLANNS 400

                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 1786405   398 DSITYRVRKGDSLSSIAKRHGVNIKDVMRWNSDTA-NLQPGDKLTLFVKNNNMPDS 452
Cdd:PRK10783 401 DSITYRVRKGDSLSSIAKRHGVNIKDVMRWNSDTAkNLQPGDKLTLFVKNNSTPDS 456
MltD-like cd16894
Membrane-bound lytic murein transglycosylase D and similar proteins; Lytic transglycosylases ...
 109-239 2.80e-62

Membrane-bound lytic murein transglycosylase D and similar proteins; Lytic transglycosylases (LT) catalyze the cleavage of the beta-1,4-glycosidic bond between N-acetylmuramic acid (MurNAc) and N-acetyl-D-glucosamine (GlcNAc). Membrane-bound lytic murein transglycosylase D protein (MltD) family members may have one or more small LysM domains, which may contribute to peptidoglycan binding. Unlike the similar "goose-type" lysozymes, LTs also make a new glycosidic bond with the C6 hydroxyl group of the same muramic acid residue. Proteins similar to this family include the soluble and insoluble membrane-bound LTs in bacteria, the LTs in bacteriophage lambda, as well as the eukaryotic "goose-type" lysozymes (goose egg-white lysozyme; GEWL).


Pssm-ID: 381615 [Multi-domain]  Cd Length: 129  Bit Score: 198.13  E-value: 2.80e-62
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786405  109 VKKRNMPMELVLLPIVESAFDPHATSGANAAGIWQIIPSTGRNYGLKQTRNYDARRDVVASTTAALNMMQRLNKMFdGDW 188
Cdd:cd16894   1 LLKEGLPEELKYLALVESGFNPDAVSSAGAAGLWQFMPATAREYGLRVDSWVDERRDPEKSTRAAARYLKDLYKRF-GDW 79

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|.
gi 1786405  189 LLTVAAYNSGEGRVMKAIKTNKArGKSTDFWSLPLPQETKQYVPKMLALSD 239
Cdd:cd16894  80 LLALAAYNAGEGRVRRAIKRAGT-DKWEDYYRLYLPAETRRYVPKFLAAKI 129
MltE COG0741
Soluble lytic murein transglycosylase or regulatory protein s ( may contain LysM/invasin ...
 26-244 9.41e-42

Soluble lytic murein transglycosylase or regulatory protein s ( may contain LysM/invasin domain) [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440504 [Multi-domain]  Cd Length: 244  Bit Score: 148.60  E-value: 9.41e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786405   26 AQSLSAAGQGEAAKFTSQARWMDDGTSIAPDGDLWAFIGDELKMGIPENDRIREQKQKYLRNKSYLHDVTLRAEPYMYWI 105
Cdd:COG0741  28 AAAAAAALAAAAAALAAAAAAAAGAAAAAASAAAGGPALAAALAAADALAAFAAIAALAAELLALAALLLRRPLPYLPLI 107

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786405  106 AGQVKKRNMPMELVL-LPIVESAFDPHATSGANAAGIWQIIPSTGRNYGLKQ--TRNYDARRDVVASTTAALNMMQRLNK 182
Cdd:COG0741 108 EEAAKKYGVDPALVLaLIRQESAFNPNAVSPAGARGLMQLMPATARRLGLKLglGPSPDDLFDPETNIRAGAAYLRELLD 187

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1786405  183 MFDGDWLLTVAAYNSGEGRVMKAIKTNKARgkstdFWSLPLPQETKQYVPKMLALSDILKNS 244
Cdd:COG0741 188 RFDGDLVLALAAYNAGPGRVRRWLRRNGDR-----DGEIIPYAETRNYVKKVLANYAIYRAG 244
SLT pfam01464
Transglycosylase SLT domain; This family is distantly related to pfam00062. Members are found ...
 104-217 2.54e-37

Transglycosylase SLT domain; This family is distantly related to pfam00062. Members are found in phages, type II, type III and type IV secretion systems.


Pssm-ID: 396169 [Multi-domain]  Cd Length: 114  Bit Score: 132.05  E-value: 2.54e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786405    104 WIAGQVKKRNMPMELVLLPIVESAFDPHATSGANAAGIWQIIPSTGRNYGLKQTRNYDARRDVVASTTAALNMMQRLNKM 183
Cdd:pfam01464   1 IIKAAQKYGVDPSLLLAIAQQESGFNPKAVSKSGAVGLMQIMPSTAKRLGLRVNPGVDDLFDPEKNIKAGTKYLKELYKQ 80

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1786405    184 FDGDWLLTVAAYNSGEGRVMKAIKTNKARGKSTD 217
Cdd:pfam01464  81 YGGDLWLALAAYNAGPGRVRKWIKNAGAKDKKLL 114
MltF COG4623
Membrane-bound lytic murein transglycosylase MltF [Cell wall/membrane/envelope biogenesis, ...
 61-243 9.32e-37

Membrane-bound lytic murein transglycosylase MltF [Cell wall/membrane/envelope biogenesis, Signal transduction mechanisms];


Pssm-ID: 443662 [Multi-domain]  Cd Length: 421  Bit Score: 139.43  E-value: 9.32e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786405   61 AFIGDELKMGIPENDRIREQKQKYLRNKSYLHDVTLRAEPYMYWIAGQVKKRNMPME-LVLLPIVESAFDPHATSGANAA 139
Cdd:COG4623 224 EFFAKIKKGGTLARLYERYFGHVKRDTRAFLRRIEGRLPPYDPLFEKYAEEYGLDWRlLAALAYQESHWNPRARSPTGAR 303

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786405  140 GIWQIIPSTGRNYGLKQtrnydaRRDVVASTTAALNMMQRLNKMFD------GDWLLTVAAYNSGEGRVMKAIKTNKARG 213
Cdd:COG4623 304 GLMQLMPATAKELGVDD------RLDPEQSIRAGAKYLRWLYDRFPeaidepDRWWFALAAYNAGPGHVQDARRLAKKQG 377

                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
gi 1786405  214 KSTDFWSLP-------------LPQETKQYVPKMLALSDILKN 243
Cdd:COG4623 378 LDPDRWFDVeksqpkyydtgyaRGRETVNYVPNIRAYYDIYKR 420
LT-like cd00254
lytic transglycosylase(LT)-like domain; Members include the soluble and insoluble ...
 124-236 1.14e-20

lytic transglycosylase(LT)-like domain; Members include the soluble and insoluble membrane-bound LTs in bacteria and LTs in bacteriophage lambda. LTs catalyze the cleavage of the beta-1,4-glycosidic bond between N-acetylmuramic acid (MurNAc) and N-acetyl-D-glucosamine (GlcNAc), as do "goose-type" lysozymes. However, in addition to this, they also make a new glycosidic bond with the C6 hydroxyl group of the same muramic acid residue.


Pssm-ID: 381594 [Multi-domain]  Cd Length: 111  Bit Score: 86.88  E-value: 1.14e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786405  124 VESAFDPHATSGANAAGIWQIIPSTGRNYGLKQTRNydaRRDVVASTTAALNMMQRLNKMFDGDWLLTVAAYNSGEGRVM 203
Cdd:cd00254  10 VESGFNPRAVSPAGARGLMQLMPGTARDLGRRGVDD---LFDPEENIRAGARYLRELLDRFGGDLELALAAYNAGPGAVD 86

                        90       100       110
                ....*....|....*....|....*....|...
gi 1786405  204 KAIKTNKargkstdfwslPLPQETKQYVPKMLA 236
Cdd:cd00254  87 RWGGGEV-----------PPYKETRNYVQRVLA 108
Slt70-like cd13401
70kDa soluble lytic transglycosylase (Slt70) and similar proteins; Catalytic domain of the ...
 100-236 1.91e-19

70kDa soluble lytic transglycosylase (Slt70) and similar proteins; Catalytic domain of the 70kda soluble lytic transglycosylase (LT)-like proteins, which also have an N-terminal U-shaped U-domain and a linker L-domain. LTs catalyze the cleavage of the beta-1,4-glycosidic bond between N-acetylmuramic acid (MurNAc) and N-acetyl-D-glucosamine (GlcNAc), as do "goose-type" lysozymes. However, in addition to this, they also make a new glycosidic bond with the C6 hydroxyl group of the same muramic acid residue. Proteins similar to this family include the soluble and insoluble membrane-bound LTs in bacteria and the LTs in bacteriophage lambda.


Pssm-ID: 381604 [Multi-domain]  Cd Length: 152  Bit Score: 84.84  E-value: 1.91e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786405  100 PYMYWIAGQVKKRNMPMELVLlPIV--ESAFDPHATSGANAAGIWQIIPSTGRNYGLKQTRNYDARRDVvasTTAALNM- 176
Cdd:cd13401   5 PYRDLVERAAKKNGLDPALVY-AIIrqESAFDPDAVSPAGALGLMQLMPATAKDVAKKLGLPYYSPRDL---FDPEYNIr 80

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1786405  177 -----MQRLNKMFDGDWLLTVAAYNSGEGRVMKAIKTNkaRGKSTDFW--SLPLpQETKQYVPKMLA 236
Cdd:cd13401  81 lgsayLAELLDRFDGNPVLALAAYNAGPGRVRRWLKRR--GDLDPDLWieTIPF-SETRNYVKRVLE 144
LT_Slt70-like cd16896
uncharacterized lytic transglycosylase subfamily with similarity to Slt70; Uncharacterized ...
 124-246 3.63e-17

uncharacterized lytic transglycosylase subfamily with similarity to Slt70; Uncharacterized lytic transglycosylase (LT) with a conserved sequence pattern suggesting similarity to the Slt70, a 70kda soluble lytic transglycosylase which also has an N-terminal U-shaped U-domain and a linker L-domain. LTs catalyze the cleavage of the beta-1,4-glycosidic bond between N-acetylmuramic acid (MurNAc) and N-acetyl-D-glucosamine (GlcNAc), as do "goose-type" lysozymes. However, in addition to this, they also make a new glycosidic bond with the C6 hydroxyl group of the same muramic acid residue.


Pssm-ID: 381617 [Multi-domain]  Cd Length: 146  Bit Score: 77.94  E-value: 3.63e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786405  124 VESAFDPHATSGANAAGIWQIIPSTGR----NYGLKQTRNYDARrdvvastTAALNM------MQRLNKMFDGDWLLTVA 193
Cdd:cd16896  28 VESNFNPNAVSSKGAIGLMQIMPETAEwiaeKLGLEDFSEDDLY-------DPETNIrlgtwyLSYLLKEFDGNLVLALA 100

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|...
gi 1786405  194 AYNSGEGRVMKAIKTNKARGKSTDFWSLPLPqETKQYVPKmlalsdILKNSKR 246
Cdd:cd16896 101 AYNAGPGNVDKWLKDGGWSGDGKTLDQIPFP-ETRHYVKK------VLKNYKI 146
LysM COG1388
LysM repeat [Cell wall/membrane/envelope biogenesis];
307-384 4.62e-17

LysM repeat [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440998 [Multi-domain]  Cd Length: 156  Bit Score: 78.21  E-value: 4.62e-17
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1786405  307 VPKKHADQLRESLASGEIAAVQSTLVADNTPLNSRVYTVRSGDTLSSIASRLGVSTKDLQQWNKLRGSKLKPGQSLTI 384
Cdd:COG1388  76 PEAAAAAAARYTVKSGDTLSGIARRYGAAAAPSPVTYTVKKGDTLWSIARRYGVSVEELKRWNGLSSDTIRPGQKLKI 153
PRK06347 PRK06347
1,4-beta-N-acetylmuramoylhydrolase;
335-442 2.31e-16

1,4-beta-N-acetylmuramoylhydrolase;


Pssm-ID: 180536 [Multi-domain]  Cd Length: 592  Bit Score: 81.28  E-value: 2.31e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786405   335 NTPLNSRVYTVRSGDTLSSIASRLGVSTKDLQQWNKLRGSKLKPGQSLTIGAGSSAQRLA---------NNSDSITYRVR 405
Cdd:PRK06347 474 NTNTNAKVYTVAKGDSLWRIANNNKVTIANLKSWNNLKSDFIYPGQKLKVSAGSTTNNTNtakpstnkpSNSTVKTYTVK 553

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 1786405   406 KGDSLSSIAKRHGVNIKDVMRWNSDTAN-LQPGDKLTL 442
Cdd:PRK06347 554 KGDSLWAISRQYKTTVDNIKAWNKLTSNmIHVGQKLTI 591
LysM COG1388
LysM repeat [Cell wall/membrane/envelope biogenesis];
258-442 9.96e-16

LysM repeat [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440998 [Multi-domain]  Cd Length: 156  Bit Score: 74.36  E-value: 9.96e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786405  258 RALARVHLSSPVEMAKVADMAGISVSKLKTFNAGVKGSTLGASGPQYVMVPKKHADQLRESLASGEIAAVQSTLVADNTP 337
Cdd:COG1388   1 GLLLALSANAALLAAVLTLLAALLLLAAALAAVALLLLAALAPAGLSLAAALNGEALLLLLPAAAAAAKAALAAAPEAAA 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786405  338 LNSRVYTVRSGDTLSSIASRLGVSTKdlqqwnklrgsklkpgqsltigagssaqrlannSDSITYRVRKGDSLSSIAKRH 417
Cdd:COG1388  81 AAAARYTVKSGDTLSGIARRYGAAAA---------------------------------PSPVTYTVKKGDTLWSIARRY 127

                       170       180
                ....*....|....*....|....*.
gi 1786405  418 GVNIKDVMRWNS-DTANLQPGDKLTL 442
Cdd:COG1388 128 GVSVEELKRWNGlSSDTIRPGQKLKI 153
MLTF-like cd13403
membrane-bound lytic murein transglycosylase F (MLTF) and similar proteins; This subfamily ...
 125-243 2.98e-15

membrane-bound lytic murein transglycosylase F (MLTF) and similar proteins; This subfamily includes membrane-bound lytic murein transglycosylase F (MltF, murein lyase F) that degrades murein glycan strands. It is responsible for catalyzing the release of 1,6-anhydromuropeptides from peptidoglycan. Lytic transglycosylase catalyzes the cleavage of the beta-1,4-glycosidic bond between N-acetylmuramic acid (MurNAc) and N-acetyl-D-glucosamine (GlcNAc) as do goose-type lysozymes. However, in addition, it also makes a new glycosidic bond with the C6 hydroxyl group of the same muramic acid residue.


Pssm-ID: 381606 [Multi-domain]  Cd Length: 161  Bit Score: 72.95  E-value: 2.98e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786405  125 ESAFDPHATSGANAAGIWQIIPSTGRNYGLKQtrnydaRRDVVASTTAALNMMQRLNKMFDGD------WLLTVAAYNSG 198
Cdd:cd13403  22 ESRFNPNARSPAGARGLMQLMPSTARELGVND------RLDPEQNIHAGAKYLRYLRDRFPPDidepdrLKFALAAYNAG 95

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1786405  199 EGRVMKAIKTNKARGKSTDFWS-----LPLP----------------QETKQYVPKMLALSDILKN 243
Cdd:cd13403  96 PGHVRDARRLAKKYGLNPNVWFdnvevLPLLkspyydpvvkygyargRETVNYVRNIRKYYDAYKQ 161
PRK06347 PRK06347
1,4-beta-N-acetylmuramoylhydrolase;
335-440 9.53e-15

1,4-beta-N-acetylmuramoylhydrolase;


Pssm-ID: 180536 [Multi-domain]  Cd Length: 592  Bit Score: 76.27  E-value: 9.53e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786405   335 NTPLNSRVYTVRSGDTLSSIASRLGVSTKDLQQWNKLRGSKLKPGQSLTIGAGSSAQ---------------RLANNSDS 399
Cdd:PRK06347 400 GTSTNAKVYTVVKGDSLWRIANNNKVTIANLKSWNNLKSDFIYPGQKLKVSAGSTSNtntskpstntntskpSTNTNTNA 479

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 1786405   400 ITYRVRKGDSLSSIAKRHGVNIKDVMRWNS-DTANLQPGDKL 440
Cdd:PRK06347 480 KVYTVAKGDSLWRIANNNKVTIANLKSWNNlKSDFIYPGQKL 521
LysM pfam01476
LysM domain; The LysM (lysin motif) domain is about 40 residues long. It is found in a variety ...
 343-384 1.60e-14

LysM domain; The LysM (lysin motif) domain is about 40 residues long. It is found in a variety of enzymes involved in bacterial cell wall degradation. This domain may have a general peptidoglycan binding function. The structure of this domain is known.


Pssm-ID: 396179 [Multi-domain]  Cd Length: 43  Bit Score: 67.42  E-value: 1.60e-14
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1786405    343 YTVRSGDTLSSIASRLGVSTKDLQQWNKLRGSKLKPGQSLTI 384
Cdd:pfam01476   1 YTVKKGDTLSSIAKRYGITVEQLAELNGLSSPNLYVGQKLKI 42
PRK06347 PRK06347
1,4-beta-N-acetylmuramoylhydrolase;
339-440 7.01e-14

1,4-beta-N-acetylmuramoylhydrolase;


Pssm-ID: 180536 [Multi-domain]  Cd Length: 592  Bit Score: 73.58  E-value: 7.01e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786405   339 NSRVYTVRSGDTLSSIASRLGVSTKDLQQWNKLRGSKLKPGQSLTIGAGSSAQ----------------RLANNSDSITY 402
Cdd:PRK06347 329 NAKIYTVVKGDSLWRIANNHKVTVANLKAWNNLKSDFIYPGQKLKVSAGSTTSdtntskpstgtstskpSTGTSTNAKVY 408

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 1786405   403 RVRKGDSLSSIAKRHGVNIKDVMRWNS-DTANLQPGDKL 440
Cdd:PRK06347 409 TVVKGDSLWRIANNNKVTIANLKSWNNlKSDFIYPGQKL 447
LysM cd00118
Lysin Motif is a small domain involved in binding peptidoglycan; LysM, a small globular domain ...
 341-384 4.69e-13

Lysin Motif is a small domain involved in binding peptidoglycan; LysM, a small globular domain with approximately 40 amino acids, is a widespread protein module involved in binding peptidoglycan in bacteria and chitin in eukaryotes. The domain was originally identified in enzymes that degrade bacterial cell walls, but proteins involved in many other biological functions also contain this domain. It has been reported that the LysM domain functions as a signal for specific plant-bacteria recognition in bacterial pathogenesis. Many of these enzymes are modular and are composed of catalytic units linked to one or several repeats of LysM domains. LysM domains are found in bacteria and eukaryotes.


Pssm-ID: 212030 [Multi-domain]  Cd Length: 45  Bit Score: 63.27  E-value: 4.69e-13
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*
gi 1786405  341 RVYTVRSGDTLSSIASRLGVSTKDLQQWNKLRG-SKLKPGQSLTI 384
Cdd:cd00118   1 KTYTVKPGDTLWSIAKKYGVTVEELAAANPLINpDCIYPGQKLKI 45
LysM smart00257
Lysin motif;
343-384 2.32e-12

Lysin motif;


Pssm-ID: 197609 [Multi-domain]  Cd Length: 44  Bit Score: 61.31  E-value: 2.32e-12
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 1786405     343 YTVRSGDTLSSIASRLGVSTKDLQQWNKLRGS-KLKPGQSLTI 384
Cdd:smart00257   2 YTVKKGDTLSSIARRYGISVSDLLELNNILDPdNLQVGQKLKI 44
LysM cd00118
Lysin Motif is a small domain involved in binding peptidoglycan; LysM, a small globular domain ...
 400-442 5.51e-12

Lysin Motif is a small domain involved in binding peptidoglycan; LysM, a small globular domain with approximately 40 amino acids, is a widespread protein module involved in binding peptidoglycan in bacteria and chitin in eukaryotes. The domain was originally identified in enzymes that degrade bacterial cell walls, but proteins involved in many other biological functions also contain this domain. It has been reported that the LysM domain functions as a signal for specific plant-bacteria recognition in bacterial pathogenesis. Many of these enzymes are modular and are composed of catalytic units linked to one or several repeats of LysM domains. LysM domains are found in bacteria and eukaryotes.


Pssm-ID: 212030 [Multi-domain]  Cd Length: 45  Bit Score: 60.19  E-value: 5.51e-12
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*
gi 1786405  400 ITYRVRKGDSLSSIAKRHGVNIKDVMRWN--SDTANLQPGDKLTL 442
Cdd:cd00118   1 KTYTVKPGDTLWSIAKKYGVTVEELAAANplINPDCIYPGQKLKI 45
LysM pfam01476
LysM domain; The LysM (lysin motif) domain is about 40 residues long. It is found in a variety ...
 402-442 1.55e-11

LysM domain; The LysM (lysin motif) domain is about 40 residues long. It is found in a variety of enzymes involved in bacterial cell wall degradation. This domain may have a general peptidoglycan binding function. The structure of this domain is known.


Pssm-ID: 396179 [Multi-domain]  Cd Length: 43  Bit Score: 58.95  E-value: 1.55e-11
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1786405    402 YRVRKGDSLSSIAKRHGVNIKDVMRWNS-DTANLQPGDKLTL 442
Cdd:pfam01476   1 YTVKKGDTLSSIAKRYGITVEQLAELNGlSSPNLYVGQKLKI 42
LysM smart00257
Lysin motif;
401-442 6.07e-11

Lysin motif;


Pssm-ID: 197609 [Multi-domain]  Cd Length: 44  Bit Score: 57.07  E-value: 6.07e-11
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 1786405     401 TYRVRKGDSLSSIAKRHGVNIKDVMRWN--SDTANLQPGDKLTL 442
Cdd:smart00257   1 TYTVKKGDTLSSIARRYGISVSDLLELNniLDPDNLQVGQKLKI 44
LT_MltC_MltE cd16893
membrane-bound lytic murein transglycosylases MltC and MltE, and similar proteins; MltC and ...
 110-205 5.41e-09

membrane-bound lytic murein transglycosylases MltC and MltE, and similar proteins; MltC and MltE are periplasmic, outer membrane attached lytic transglycosylases (LTs), which cleave beta-1,4-glycosidic bonds joining N-acetylmuramic acid and N-acetylglucosamine in the cell wall peptidoglycan, yielding 1,6-anhydromuropeptides. Proteins similar to this family include the soluble and insoluble membrane-bound LTs in bacteria and the LTs in bacteriophage lambda


Pssm-ID: 381614 [Multi-domain]  Cd Length: 162  Bit Score: 54.87  E-value: 5.41e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786405  110 KKRNMPMELVLLPI-VESAFDPHATSGANAAGIWQIIPSTG------RNYGLKQ--TRNY--DARRDVVAStTAALNMMQ 178
Cdd:cd16893   8 KKYGVDPALILAIIeTESSFNPYAVSHSPAYGLMQIVPSTAgrdvyrLLGGKGGlpSKSYlfDPENNIDIG-TAYLHILQ 86

                        90       100       110
                ....*....|....*....|....*....|....*.
gi 1786405  179 R---------LNKMFdgdwlLTVAAYNSGEGRVMKA 205
Cdd:cd16893  87 NrylkgiknpKSREY-----CAIAAYNGGAGNVLRT 117
Lyz-like cd00442
lysozyme-like domains; This family contains several members, including soluble lytic ...
 117-176 9.90e-09

lysozyme-like domains; This family contains several members, including soluble lytic transglycosylases (SLT), goose egg-white lysozymes (GEWL), hen egg-white lysozymes (HEWL), chitinases, bacteriophage lambda lysozymes, endolysins, autolysins, chitosanases, and pesticin. Typical members are involved in the hydrolysis of beta-1,4- linked polysaccharides.


Pssm-ID: 381596 [Multi-domain]  Cd Length: 59  Bit Score: 51.26  E-value: 9.90e-09
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1786405  117 ELVLLPIVESAFDPHA--TSGANAAGIWQIIPSTGRNYGLKQTRNydaRRDVVASTTAALNM 176
Cdd:cd00442   1 VLAAIIGQESGGNKPAnaGSGSGAAGLFQFMPGTWKAYGKNSSSD---LNDPEASIEAAAKY 59
Slt35-like cd13399
Slt35-like lytic transglycosylase; Lytic transglycosylase similar to Escherichia coli lytic ...
 124-206 3.67e-08

Slt35-like lytic transglycosylase; Lytic transglycosylase similar to Escherichia coli lytic transglycosylase Slt35 and Pseudomonas aeruginosa Sltb1. Lytic transglycosylase (LT) catalyzes the cleavage of the beta-1,4-glycosidic bond between N-acetylmuramic acid (MurNAc) and N-acetyl-D-glucosamine (GlcNAc) as do "goose-type" lysozymes. However, in addition to this, they also make a new glycosidic bond with the C6 hydroxyl group of the same muramic acid residue. Proteins similar to this this family include the soluble and insoluble membrane-bound LTs in bacteria, the LTs in bacteriophage lambda, as well as the eukaryotic "goose-type" lysozymes (goose egg-white lysozyme; GEWL).


Pssm-ID: 381602 [Multi-domain]  Cd Length: 108  Bit Score: 51.16  E-value: 3.67e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786405  124 VESAFDPHA-TSGANAAGIWQIIPSTGRNYGLkqTRNYDARRDVV----ASTTAAlNMMQR----LNKMFDGDWLLTVAA 194
Cdd:cd13399  14 VESGFGPNAgGSPAGAQGIAQFMPSTWKAYGV--DGNGDGKADPFnpedAIASAA-NYLCRhgwdLNAFLGEDNFLALAA 90

                        90
                ....*....|..
gi 1786405  195 YNSGEGRVMKAI 206
Cdd:cd13399  91 YNAGPGAYANAV 102
OapA COG3061
Cell division protein YtfB/OapA (opacity-associated protein A) [Cell cycle control, cell ...
 326-384 2.08e-06

Cell division protein YtfB/OapA (opacity-associated protein A) [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 442295 [Multi-domain]  Cd Length: 425  Bit Score: 49.67  E-value: 2.08e-06
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1786405  326 AVQSTLVADNTPLNSRVYTVRSGDTLSSIASRLGVSTKDLQQWNKLRG-----SKLKPGQSLTI 384
Cdd:COG3061  55 AAAAPAAPAAPEGEWQEYTVQSGDTLSQIFRRLGLSASDLYALLAAEGdakplSRLKPGQELRF 118
PRK06347 PRK06347
1,4-beta-N-acetylmuramoylhydrolase;
350-440 2.51e-06

1,4-beta-N-acetylmuramoylhydrolase;


Pssm-ID: 180536 [Multi-domain]  Cd Length: 592  Bit Score: 49.69  E-value: 2.51e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786405   350 TLSSIASRLG--VSTKDLQQWNKlrgSKLKPGQSLTIGAGSSAQRLANNSDSITYRVRKGDSLSSIAKRHGVNIKDVMRW 427
Cdd:PRK06347 282 TDTAYATKLNdlISRYNLTQYDS---GKTTGGNSGSTGNSSNSSNTGNTSNAKIYTVVKGDSLWRIANNHKVTVANLKAW 358

                         90
                 ....*....|....
gi 1786405   428 NS-DTANLQPGDKL 440
Cdd:PRK06347 359 NNlKSDFIYPGQKL 372
PRK13914 PRK13914
invasion associated endopeptidase;
320-384 1.14e-05

invasion associated endopeptidase;


Pssm-ID: 237555 [Multi-domain]  Cd Length: 481  Bit Score: 47.49  E-value: 1.14e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1786405   320 ASGEIAAVQSTLVADNTPLNSRVYTVRSGDTLSSIASRLGVSTKDLQQWNKLRGSKLKPGQSLTI 384
Cdd:PRK13914 179 ATTPAPKVAETKETPVVDQNATTHAVKSGDTIWALSVKYGVSVQDIMSWNNLSSSSIYVGQKLAI 243
OapA COG3061
Cell division protein YtfB/OapA (opacity-associated protein A) [Cell cycle control, cell ...
 394-448 3.15e-05

Cell division protein YtfB/OapA (opacity-associated protein A) [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 442295 [Multi-domain]  Cd Length: 425  Bit Score: 46.20  E-value: 3.15e-05
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1786405  394 ANNSDSITYRVRKGDSLSSIAKRHGVNIKDVMR------WNSDTANLQPGDKLTlFVKNNN 448
Cdd:COG3061  64 APEGEWQEYTVQSGDTLSQIFRRLGLSASDLYAllaaegDAKPLSRLKPGQELR-FQLDAD 123
PHA00368 PHA00368
internal virion protein D
 124-235 3.42e-05

internal virion protein D


Pssm-ID: 222785 [Multi-domain]  Cd Length: 1315  Bit Score: 46.31  E-value: 3.42e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786405    124 VESAFDPHATSGANAAGIWQIIPSTGRNYGLKQTRnyDARRDVVASTTAALNMMQRLNKMFDGDWLLTVAAYNSGEGRVM 203
Cdd:PHA00368   35 DESRFNPTAKSPTGPKGLMQFTKATAKALGLIVDD--DDRLDPELAIDAGARYLADLVGKYDGDELKAALAYNQGEGRLG 112

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1786405    204 KAIKTNKARGkstDFWSlpLPQETKQYVPKML 235
Cdd:PHA00368  113 APQLEAYDKG---DFAS--ISEEGRNYLRNLL 139
PHA00658 PHA00658
putative lysin
 133-275 1.12e-04

putative lysin


Pssm-ID: 106967 [Multi-domain]  Cd Length: 720  Bit Score: 44.81  E-value: 1.12e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786405   133 TSGANAAGIWQIIPSTG----RNYGLKQTRNyDARRDVVASTTAALNMMQRLNKMFDGDWLLTVAAYNSGEGRVMKAIKT 208
Cdd:PHA00658 325 TSPKGAVGIAQVMPDTApeaaKLAGLPWDEN-RYRNDAAYNRALGMAYFQKQLRDFGGDLPKAYAAYNAGPGALQSALKD 403

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786405   209 NKARGkstdfWSLPLPQETKQYV-------------PKMLALSDI---LKNSKrygvRLPTTDESRALARVHLSSPVEMA 272
Cdd:PHA00658 404 AKDGN-----WLALLPKETQDYVvknmqaynagqgrPARPTLADIeaqLQNDP----RLAGNPERLKIARVEAERQFNMQ 474


                 ...
gi 1786405   273 KVA 275
Cdd:PHA00658 475 TAA 477
mltC PRK11671
membrane-bound lytic murein transglycosylase MltC;
97-212 1.39e-04

membrane-bound lytic murein transglycosylase MltC;


Pssm-ID: 183271 [Multi-domain]  Cd Length: 359  Bit Score: 43.89  E-value: 1.39e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786405    97 RAEPYMYWIAGQVKKRNMPMELVLLPI-VESAFDPHATSGANAAGIWQIIPST---------------GRNYGLKQTRNY 160
Cdd:PRK11671 188 RAHKYLPMVRKASRKYGVDESLILAIMqTESSFNPYAVSRSDALGLMQVVQHTagkdvfrmkgksgqpSRSYLFDPANNI 267

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 1786405   161 DArrdvvasTTAALNMMQrlNKMFDGDWLLT------VAAYNSGEGRVMKAIKTNKAR 212
Cdd:PRK11671 268 DT-------GTAYLAILQ--NVYLGGITNPTsrryavITAYNGGAGSVLRVFSNDKIQ 316
XkdP COG1652
Cytoplasmic potassium-binding protein Kbp/XkdP/YgaU, contains LysM domain [Inorganic ion ...
 287-384 1.41e-04

Cytoplasmic potassium-binding protein Kbp/XkdP/YgaU, contains LysM domain [Inorganic ion transport and metabolism];


Pssm-ID: 441258 [Multi-domain]  Cd Length: 163  Bit Score: 42.30  E-value: 1.41e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786405  287 TFNAGVKGSTLGASGPQYVMVPKKHADQLRESLASGEIAAVQSTLVADNTplnsRVYTVRSGDTLSSIASR-LGvstkDL 365
Cdd:COG1652  60 AAAVAAAAAAAVLIAPVAVMRAGAAAKLSPAVTVAEEAAAPSAELAPDAP----KTYTVKPGDTLWGIAKRfYG----DP 131

                        90       100
                ....*....|....*....|....*...
gi 1786405  366 QQWNKLRG---------SKLKPGQSLTI 384
Cdd:COG1652 132 ARWPEIAEanrdqiknpDLIYPGQVLRI 159
XkdP COG1652
Cytoplasmic potassium-binding protein Kbp/XkdP/YgaU, contains LysM domain [Inorganic ion ...
 360-442 1.45e-04

Cytoplasmic potassium-binding protein Kbp/XkdP/YgaU, contains LysM domain [Inorganic ion transport and metabolism];


Pssm-ID: 441258 [Multi-domain]  Cd Length: 163  Bit Score: 42.30  E-value: 1.45e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786405  360 VSTKDLQQWNKLRGSKLKPGQSLTIGAGSSAQRLANNSDSiTYRVRKGDSLSSIAKRH---GVNIKDVMRWN----SDTA 432
Cdd:COG1652  71 VLIAPVAVMRAGAAAKLSPAVTVAEEAAAPSAELAPDAPK-TYTVKPGDTLWGIAKRFygdPARWPEIAEANrdqiKNPD 149

                        90
                ....*....|
gi 1786405  433 NLQPGDKLTL 442
Cdd:COG1652 150 LIYPGQVLRI 159
PRK11619 PRK11619
lytic murein transglycosylase; Provisional
 125-236 1.76e-03

lytic murein transglycosylase; Provisional


Pssm-ID: 183236 [Multi-domain]  Cd Length: 644  Bit Score: 40.82  E-value: 1.76e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786405   125 ESAFDPHATSGANAAGIWQIIPSTGRN----YGLKQTRNYDARRDVVASTTAALNMMQRLNKMFDGDWLLTVAAYNSGEG 200
Cdd:PRK11619 504 ESAWNPKARSPVGASGLMQIMPGTATHtvkmFSIPGYSSSSQLLDPETNINIGTSYLEYVYQQFGNNRILASAAYNAGPG 583

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 1786405   201 RVMKAIKTNKARGKSTDFW-SLPLpQETKQYVPKMLA 236
Cdd:PRK11619 584 RVRTWLGNSAGRIDAVAFVeSIPF-SETRGYVKNVLA 619
PRK11649 PRK11649
putative peptidase; Provisional
 332-443 4.57e-03

putative peptidase; Provisional


Pssm-ID: 236946 [Multi-domain]  Cd Length: 439  Bit Score: 39.26  E-value: 4.57e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786405   332 VADNTPLNSrvYTVRSGDTLSSIASRLGVSTKDLQQWNK----LRGskLKPGQSL--TIGAGSSAQRL---ANNSDSITY 402
Cdd:PRK11649  89 IAGEAGVHE--YVVSTGDTLSSILNQYGIDMSDISQLAAqdkeLRN--LKIGQQLswTLTADGDLQRLtweVSRRETRTY 164

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786405   403 -----------RVRKGD------------SLSSIAKRHGVN---IKDVMR---WNSDTANLQPGDKLTLF 443
Cdd:PRK11649 165 drtgngfketsEMQQGEwvnsvlkgtvggSFVASAKNAGLTsaeISAVIKalqWQMDFRKLKKGDEFSVL 234
 
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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