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Conserved domains on  [gi|493016613|ref|WP_006093933|]
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MULTISPECIES: LysM peptidoglycan-binding domain-containing protein [Bacillus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
CwlJ COG3773
Cell wall hydrolase CwlJ, involved in spore germination [Cell cycle control, cell division, ...
 144-265 6.28e-50

Cell wall hydrolase CwlJ, involved in spore germination [Cell cycle control, cell division, chromosome partitioning, Cell wall/membrane/envelope biogenesis];


:

Pssm-ID: 442987  Cd Length: 124  Bit Score: 160.34  E-value: 6.28e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493016613 144 ISEQELDLMARLVTAEAGGEPYAGKVAVAKVILNRVDAVEFPNTITDVIYEPikygYAFTPVTDGRIDQPATREARMAVE 223
Cdd:COG3773    3 YSDSDLDLLARAIYAEARGEPYEGQVAVAAVVLNRVRSPRFPNTICGVVYQP----GQFSPVCDGQINRPPEEEARRAAR 78

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 493016613 224 EAIS------TKGinsdWLYFYNPKTSTDKWITTRQTVAVIGNHVFAK 265
Cdd:COG3773   79 DALNgwrrdpTGG----ALYFHNPATVTPSWARSRPKTARIGNHVFYR 122
PRK06347 super family cl32140
1,4-beta-N-acetylmuramoylhydrolase;
21-145 4.47e-17

1,4-beta-N-acetylmuramoylhydrolase;


The actual alignment was detected with superfamily member PRK06347:

Pssm-ID: 180536 [Multi-domain]  Cd Length: 592  Bit Score: 80.51  E-value: 4.47e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493016613  21 SNQGTADAATVYTVKKNDTLGGISIHYGVSVQAIKQANHKTNDRIYIGEQLTIPVSPSSSESTQQKDVAASNHSAQI--- 97
Cdd:PRK06347 322 SNTGNTSNAKIYTVVKGDSLWRIANNHKVTVANLKAWNNLKSDFIYPGQKLKVSAGSTTSDTNTSKPSTGTSTSKPStgt 401

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 493016613  98 -----VYQVQRGDTLEAIAKRYNVSIQSIRQANNTNGDRIYAGQHLIITTGIS 145
Cdd:PRK06347 402 stnakVYTVVKGDSLWRIANNNKVTIANLKSWNNLKSDFIYPGQKLKVSAGST 454
 
Name Accession Description Interval E-value
CwlJ COG3773
Cell wall hydrolase CwlJ, involved in spore germination [Cell cycle control, cell division, ...
 144-265 6.28e-50

Cell wall hydrolase CwlJ, involved in spore germination [Cell cycle control, cell division, chromosome partitioning, Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442987  Cd Length: 124  Bit Score: 160.34  E-value: 6.28e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493016613 144 ISEQELDLMARLVTAEAGGEPYAGKVAVAKVILNRVDAVEFPNTITDVIYEPikygYAFTPVTDGRIDQPATREARMAVE 223
Cdd:COG3773    3 YSDSDLDLLARAIYAEARGEPYEGQVAVAAVVLNRVRSPRFPNTICGVVYQP----GQFSPVCDGQINRPPEEEARRAAR 78

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 493016613 224 EAIS------TKGinsdWLYFYNPKTSTDKWITTRQTVAVIGNHVFAK 265
Cdd:COG3773   79 DALNgwrrdpTGG----ALYFHNPATVTPSWARSRPKTARIGNHVFYR 122
spore_SleB TIGR02869
spore cortex-lytic enzyme; Members of this protein family are the spore cortex-lytic enzyme ...
 143-265 3.27e-43

spore cortex-lytic enzyme; Members of this protein family are the spore cortex-lytic enzyme SleB from Bacillus subtilis and other Gram-positive, endospore-forming bacterial species. This protein is stored in an inactive form in the spore and activated during germination. [Cellular processes, Sporulation and germination]


Pssm-ID: 213747 [Multi-domain]  Cd Length: 200  Bit Score: 145.59  E-value: 3.27e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493016613  143 GISEQELDLMARLVTAEAGGEPYAGKVAVAKVILNRVDAVEFPNTITDVIYEPikygYAFTPVTDGRIDQPATREARMAV 222
Cdd:TIGR02869  82 GYSQNDIQLLARLVNGEARGEPYEGQVAVAAVILNRVRDPRFPNTIAGVIYQP----GAFTAVADGQIWLTPTETSKKAA 157

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 493016613  223 EEAISTKGINSDWLYFYNPKTSTDKWITTRQTVAVIGNHVFAK 265
Cdd:TIGR02869 158 LDALNGWDPSGGALYYFNPATATSSWIWTRPIIKRIGKHIFCK 200
Hydrolase_2 pfam07486
Cell Wall Hydrolase; These enzymes have been implicated in cell wall hydrolysis, most ...
 162-264 3.13e-39

Cell Wall Hydrolase; These enzymes have been implicated in cell wall hydrolysis, most extensively in Bacillus subtilis. For instance Swiss:P50739 is expressed during sporulation as an inactive form and then deposited on the cell outer cortex. During germination the the enzyme is activated and hydrolyses the cortex. A similar role is carried out by the partially redundant Swiss:P42249. It is not clear whether these enzymes are amidases or peptidases.


Pssm-ID: 462179  Cd Length: 101  Bit Score: 131.87  E-value: 3.13e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493016613  162 GEPYAGKVAVAKVILNRVDAVEFPNTITDVIYEPikygYAFTPVTDGRIDQPATREARMAVEEAISTKGINS-DWLYFYN 240
Cdd:pfam07486   1 GEPYEGQVAVANVILNRVRSPRFPNTICGVVYQP----GQFSPVCDGRINLPPSEEAIRAARDALAGERDPTgGALYFHN 76

                          90       100
                  ....*....|....*....|....*
gi 493016613  241 PKTSTDKWITTRQT-VAVIGNHVFA 264
Cdd:pfam07486  77 PSVAPSSWIWSRGVrTARIGNHVFY 101
PRK06347 PRK06347
1,4-beta-N-acetylmuramoylhydrolase;
21-145 4.47e-17

1,4-beta-N-acetylmuramoylhydrolase;


Pssm-ID: 180536 [Multi-domain]  Cd Length: 592  Bit Score: 80.51  E-value: 4.47e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493016613  21 SNQGTADAATVYTVKKNDTLGGISIHYGVSVQAIKQANHKTNDRIYIGEQLTIPVSPSSSESTQQKDVAASNHSAQI--- 97
Cdd:PRK06347 322 SNTGNTSNAKIYTVVKGDSLWRIANNHKVTVANLKAWNNLKSDFIYPGQKLKVSAGSTTSDTNTSKPSTGTSTSKPStgt 401

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 493016613  98 -----VYQVQRGDTLEAIAKRYNVSIQSIRQANNTNGDRIYAGQHLIITTGIS 145
Cdd:PRK06347 402 stnakVYTVVKGDSLWRIANNNKVTIANLKSWNNLKSDFIYPGQKLKVSAGST 454
LysM COG1388
LysM repeat [Cell wall/membrane/envelope biogenesis];
1-140 1.09e-15

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


Pssm-ID: 440998 [Multi-domain]  Cd Length: 156  Bit Score: 72.43  E-value: 1.09e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493016613   1 MKLHKMKHLLPISAATITLVSNQGTADAATVYTVKKNDTLGGISIHYGVSVQAIKQANHKTNDRIYIGEQLTIPVSPSSS 80
Cdd:COG1388   14 AAVLTLLAALLLLAAALAAVALLLLAALAPAGLSLAAALNGEALLLLLPAAAAAAKAALAAAPEAAAAAAARYTVKSGDT 93

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 493016613  81 ESTQQKDVAASNHSAQIVYQVQRGDTLEAIAKRYNVSIQSIRQANNTNGDRIYAGQHLII 140
Cdd:COG1388   94 LSGIARRYGAAAAPSPVTYTVKKGDTLWSIARRYGVSVEELKRWNGLSSDTIRPGQKLKI 153
LysM cd00118
Lysin Motif is a small domain involved in binding peptidoglycan; LysM, a small globular domain ...
 97-140 3.47e-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: 62.50  E-value: 3.47e-13
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 493016613  97 IVYQVQRGDTLEAIAKRYNVSIQSIRQANN-TNGDRIYAGQHLII 140
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 ...
 99-141 4.72e-13

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: 62.03  E-value: 4.72e-13
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 493016613   99 YQVQRGDTLEAIAKRYNVSIQSIRQANNTNGDRIYAGQHLIIT 141
Cdd:pfam01476   1 YTVKKGDTLSSIAKRYGITVEQLAELNGLSSPNLYVGQKLKIP 43
LysM smart00257
Lysin motif;
99-140 2.94e-10

Lysin motif;


Pssm-ID: 197609 [Multi-domain]  Cd Length: 44  Bit Score: 54.37  E-value: 2.94e-10
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 493016613    99 YQVQRGDTLEAIAKRYNVSIQSIRQANNT-NGDRIYAGQHLII 140
Cdd:smart00257   2 YTVKKGDTLSSIARRYGISVSDLLELNNIlDPDNLQVGQKLKI 44
 
Name Accession Description Interval E-value
CwlJ COG3773
Cell wall hydrolase CwlJ, involved in spore germination [Cell cycle control, cell division, ...
 144-265 6.28e-50

Cell wall hydrolase CwlJ, involved in spore germination [Cell cycle control, cell division, chromosome partitioning, Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442987  Cd Length: 124  Bit Score: 160.34  E-value: 6.28e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493016613 144 ISEQELDLMARLVTAEAGGEPYAGKVAVAKVILNRVDAVEFPNTITDVIYEPikygYAFTPVTDGRIDQPATREARMAVE 223
Cdd:COG3773    3 YSDSDLDLLARAIYAEARGEPYEGQVAVAAVVLNRVRSPRFPNTICGVVYQP----GQFSPVCDGQINRPPEEEARRAAR 78

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 493016613 224 EAIS------TKGinsdWLYFYNPKTSTDKWITTRQTVAVIGNHVFAK 265
Cdd:COG3773   79 DALNgwrrdpTGG----ALYFHNPATVTPSWARSRPKTARIGNHVFYR 122
spore_SleB TIGR02869
spore cortex-lytic enzyme; Members of this protein family are the spore cortex-lytic enzyme ...
 143-265 3.27e-43

spore cortex-lytic enzyme; Members of this protein family are the spore cortex-lytic enzyme SleB from Bacillus subtilis and other Gram-positive, endospore-forming bacterial species. This protein is stored in an inactive form in the spore and activated during germination. [Cellular processes, Sporulation and germination]


Pssm-ID: 213747 [Multi-domain]  Cd Length: 200  Bit Score: 145.59  E-value: 3.27e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493016613  143 GISEQELDLMARLVTAEAGGEPYAGKVAVAKVILNRVDAVEFPNTITDVIYEPikygYAFTPVTDGRIDQPATREARMAV 222
Cdd:TIGR02869  82 GYSQNDIQLLARLVNGEARGEPYEGQVAVAAVILNRVRDPRFPNTIAGVIYQP----GAFTAVADGQIWLTPTETSKKAA 157

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 493016613  223 EEAISTKGINSDWLYFYNPKTSTDKWITTRQTVAVIGNHVFAK 265
Cdd:TIGR02869 158 LDALNGWDPSGGALYYFNPATATSSWIWTRPIIKRIGKHIFCK 200
Hydrolase_2 pfam07486
Cell Wall Hydrolase; These enzymes have been implicated in cell wall hydrolysis, most ...
 162-264 3.13e-39

Cell Wall Hydrolase; These enzymes have been implicated in cell wall hydrolysis, most extensively in Bacillus subtilis. For instance Swiss:P50739 is expressed during sporulation as an inactive form and then deposited on the cell outer cortex. During germination the the enzyme is activated and hydrolyses the cortex. A similar role is carried out by the partially redundant Swiss:P42249. It is not clear whether these enzymes are amidases or peptidases.


Pssm-ID: 462179  Cd Length: 101  Bit Score: 131.87  E-value: 3.13e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493016613  162 GEPYAGKVAVAKVILNRVDAVEFPNTITDVIYEPikygYAFTPVTDGRIDQPATREARMAVEEAISTKGINS-DWLYFYN 240
Cdd:pfam07486   1 GEPYEGQVAVANVILNRVRSPRFPNTICGVVYQP----GQFSPVCDGRINLPPSEEAIRAARDALAGERDPTgGALYFHN 76

                          90       100
                  ....*....|....*....|....*
gi 493016613  241 PKTSTDKWITTRQT-VAVIGNHVFA 264
Cdd:pfam07486  77 PSVAPSSWIWSRGVrTARIGNHVFY 101
PRK06347 PRK06347
1,4-beta-N-acetylmuramoylhydrolase;
21-145 4.47e-17

1,4-beta-N-acetylmuramoylhydrolase;


Pssm-ID: 180536 [Multi-domain]  Cd Length: 592  Bit Score: 80.51  E-value: 4.47e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493016613  21 SNQGTADAATVYTVKKNDTLGGISIHYGVSVQAIKQANHKTNDRIYIGEQLTIPVSPSSSESTQQKDVAASNHSAQI--- 97
Cdd:PRK06347 322 SNTGNTSNAKIYTVVKGDSLWRIANNHKVTVANLKAWNNLKSDFIYPGQKLKVSAGSTTSDTNTSKPSTGTSTSKPStgt 401

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 493016613  98 -----VYQVQRGDTLEAIAKRYNVSIQSIRQANNTNGDRIYAGQHLIITTGIS 145
Cdd:PRK06347 402 stnakVYTVVKGDSLWRIANNNKVTIANLKSWNNLKSDFIYPGQKLKVSAGST 454
PRK06347 PRK06347
1,4-beta-N-acetylmuramoylhydrolase;
13-145 5.87e-17

1,4-beta-N-acetylmuramoylhydrolase;


Pssm-ID: 180536 [Multi-domain]  Cd Length: 592  Bit Score: 80.12  E-value: 5.87e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493016613  13 SAATITLVSNQGTADAATVYTVKKNDTLGGISIHYGVSVQAIKQANHKTNDRIYIGEQLTIPVSPSSSESTQQ------- 85
Cdd:PRK06347 389 STGTSTSKPSTGTSTNAKVYTVVKGDSLWRIANNNKVTIANLKSWNNLKSDFIYPGQKLKVSAGSTSNTNTSKpstntnt 468

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 493016613  86 -KDVAASNHSAQiVYQVQRGDTLEAIAKRYNVSIQSIRQANNTNGDRIYAGQHLIITTGIS 145
Cdd:PRK06347 469 sKPSTNTNTNAK-VYTVAKGDSLWRIANNNKVTIANLKSWNNLKSDFIYPGQKLKVSAGST 528
LysM COG1388
LysM repeat [Cell wall/membrane/envelope biogenesis];
1-140 1.09e-15

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


Pssm-ID: 440998 [Multi-domain]  Cd Length: 156  Bit Score: 72.43  E-value: 1.09e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493016613   1 MKLHKMKHLLPISAATITLVSNQGTADAATVYTVKKNDTLGGISIHYGVSVQAIKQANHKTNDRIYIGEQLTIPVSPSSS 80
Cdd:COG1388   14 AAVLTLLAALLLLAAALAAVALLLLAALAPAGLSLAAALNGEALLLLLPAAAAAAKAALAAAPEAAAAAAARYTVKSGDT 93

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 493016613  81 ESTQQKDVAASNHSAQIVYQVQRGDTLEAIAKRYNVSIQSIRQANNTNGDRIYAGQHLII 140
Cdd:COG1388   94 LSGIARRYGAAAAPSPVTYTVKKGDTLWSIARRYGVSVEELKRWNGLSSDTIRPGQKLKI 153
PRK06347 PRK06347
1,4-beta-N-acetylmuramoylhydrolase;
13-140 2.99e-15

1,4-beta-N-acetylmuramoylhydrolase;


Pssm-ID: 180536 [Multi-domain]  Cd Length: 592  Bit Score: 75.12  E-value: 2.99e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493016613  13 SAATITLVSNQGTADAATVYTVKKNDTLGGISIHYGVSVQAIKQANHKTNDRIYIGEQLTIPVSPSSSE-STQQKDVAAS 91
Cdd:PRK06347 463 STNTNTSKPSTNTNTNAKVYTVAKGDSLWRIANNNKVTIANLKSWNNLKSDFIYPGQKLKVSAGSTTNNtNTAKPSTNKP 542

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 493016613  92 NHSAQIVYQVQRGDTLEAIAKRYNVSIQSIRQANNTNGDRIYAGQHLII 140
Cdd:PRK06347 543 SNSTVKTYTVKKGDSLWAISRQYKTTVDNIKAWNKLTSNMIHVGQKLTI 591
LysM COG1388
LysM repeat [Cell wall/membrane/envelope biogenesis];
11-76 5.83e-14

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


Pssm-ID: 440998 [Multi-domain]  Cd Length: 156  Bit Score: 67.81  E-value: 5.83e-14
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 493016613  11 PISAATITLVSNQGTADAATVYTVKKNDTLGGISIHYGVSVQAIKQANHKTNDRIYIGEQLTIPVS 76
Cdd:COG1388   91 GDTLSGIARRYGAAAAPSPVTYTVKKGDTLWSIARRYGVSVEELKRWNGLSSDTIRPGQKLKIPAS 156
mltD PRK10783
membrane-bound lytic murein transglycosylase D; Provisional
 14-138 9.85e-14

membrane-bound lytic murein transglycosylase D; Provisional


Pssm-ID: 182727 [Multi-domain]  Cd Length: 456  Bit Score: 70.53  E-value: 9.85e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493016613  14 AATITLVSNQGTADAATVYTVKKNDTLGGISIHYGVSVQAIKQANHKTNDRIYIGEQLTIPVSPSSSEStqqkdvaaSNH 93
Cdd:PRK10783 328 AAVQSTLVADNTPLNSRSYKVRSGDTLSGIASRLNVSTKDLQQWNNLRGSKLKVGQTLTIGAGSSAQRL--------ANN 399

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 493016613  94 SAQIVYQVQRGDTLEAIAKRYNVSIQSIRQANNTNGDRIYAGQHL 138
Cdd:PRK10783 400 SDSITYRVRKGDSLSSIAKRHGVNIKDVMRWNSDTAKNLQPGDKL 444
LysM cd00118
Lysin Motif is a small domain involved in binding peptidoglycan; LysM, a small globular domain ...
 97-140 3.47e-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: 62.50  E-value: 3.47e-13
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 493016613  97 IVYQVQRGDTLEAIAKRYNVSIQSIRQANN-TNGDRIYAGQHLII 140
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 ...
 99-141 4.72e-13

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: 62.03  E-value: 4.72e-13
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 493016613   99 YQVQRGDTLEAIAKRYNVSIQSIRQANNTNGDRIYAGQHLIIT 141
Cdd:pfam01476   1 YTVKKGDTLSSIAKRYGITVEQLAELNGLSSPNLYVGQKLKIP 43
LysM pfam01476
LysM domain; The LysM (lysin motif) domain is about 40 residues long. It is found in a variety ...
 32-74 3.65e-12

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: 59.33  E-value: 3.65e-12
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 493016613   32 YTVKKNDTLGGISIHYGVSVQAIKQANHKTNDRIYIGEQLTIP 74
Cdd:pfam01476   1 YTVKKGDTLSSIAKRYGITVEQLAELNGLSSPNLYVGQKLKIP 43
mltD PRK10783
membrane-bound lytic murein transglycosylase D; Provisional
 82-149 1.82e-10

membrane-bound lytic murein transglycosylase D; Provisional


Pssm-ID: 182727 [Multi-domain]  Cd Length: 456  Bit Score: 60.52  E-value: 1.82e-10
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 493016613  82 STQQKDVAASNHSAQIVYQVQRGDTLEAIAKRYNVSIQSIRQANNTNGDRIYAGQHLIITTGISEQEL 149
Cdd:PRK10783 329 AVQSTLVADNTPLNSRSYKVRSGDTLSGIASRLNVSTKDLQQWNNLRGSKLKVGQTLTIGAGSSAQRL 396
LysM cd00118
Lysin Motif is a small domain involved in binding peptidoglycan; LysM, a small globular domain ...
 30-73 2.81e-10

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: 54.41  E-value: 2.81e-10
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 493016613  30 TVYTVKKNDTLGGISIHYGVSVQAIKQANH-KTNDRIYIGEQLTI 73
Cdd:cd00118    1 KTYTVKPGDTLWSIAKKYGVTVEELAAANPlINPDCIYPGQKLKI 45
LysM smart00257
Lysin motif;
99-140 2.94e-10

Lysin motif;


Pssm-ID: 197609 [Multi-domain]  Cd Length: 44  Bit Score: 54.37  E-value: 2.94e-10
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 493016613    99 YQVQRGDTLEAIAKRYNVSIQSIRQANNT-NGDRIYAGQHLII 140
Cdd:smart00257   2 YTVKKGDTLSSIARRYGISVSDLLELNNIlDPDNLQVGQKLKI 44
LysM smart00257
Lysin motif;
32-73 1.31e-09

Lysin motif;


Pssm-ID: 197609 [Multi-domain]  Cd Length: 44  Bit Score: 52.45  E-value: 1.31e-09
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 493016613    32 YTVKKNDTLGGISIHYGVSVQAIKQANHKTN-DRIYIGEQLTI 73
Cdd:smart00257   2 YTVKKGDTLSSIARRYGISVSDLLELNNILDpDNLQVGQKLKI 44
XkdP COG1652
Cytoplasmic potassium-binding protein Kbp/XkdP/YgaU, contains LysM domain [Inorganic ion ...
 1-74 3.29e-07

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: 48.85  E-value: 3.29e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493016613   1 MKLHKMKHLLPISAATITLVSN--QGTADAATVYTVKKNDTLGGISIHY---GVSVQAIKQANHK--TN-DRIYIGEQLT 72
Cdd:COG1652   79 MRAGAAAKLSPAVTVAEEAAAPsaELAPDAPKTYTVKPGDTLWGIAKRFygdPARWPEIAEANRDqiKNpDLIYPGQVLR 158


                 ..
gi 493016613  73 IP 74
Cdd:COG1652  159 IP 160
PRK13914 PRK13914
invasion associated endopeptidase;
29-124 1.26e-06

invasion associated endopeptidase;


Pssm-ID: 237555 [Multi-domain]  Cd Length: 481  Bit Score: 49.03  E-value: 1.26e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493016613  29 ATVYTVKKNDTLGGISIHYGVSVQAIKQANHKTNDRIYIGEQLTIP-----VSPSSSESTQQKdvAASNHSAQIVYQVQR 103
Cdd:PRK13914 199 ATTHAVKSGDTIWALSVKYGVSVQDIMSWNNLSSSSIYVGQKLAIKqtantATPKAEVKTEAP--AAEKQAAPVVKENTN 276

                         90       100
                 ....*....|....*....|.
gi 493016613 104 GDTLEAIAKRYNVSIQSIRQA 124
Cdd:PRK13914 277 TNTATTEKKETTTQQQTAPKA 297
PRK06347 PRK06347
1,4-beta-N-acetylmuramoylhydrolase;
78-145 1.69e-06

1,4-beta-N-acetylmuramoylhydrolase;


Pssm-ID: 180536 [Multi-domain]  Cd Length: 592  Bit Score: 48.92  E-value: 1.69e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 493016613  78 SSSESTQQKDVAASNHSAQIVYQVQRGDTLEAIAKRYNVSIQSIRQANNTNGDRIYAGQHLIITTGIS 145
Cdd:PRK06347 312 SGSTGNSSNSSNTGNTSNAKIYTVVKGDSLWRIANNHKVTVANLKAWNNLKSDFIYPGQKLKVSAGST 379
PRK06347 PRK06347
1,4-beta-N-acetylmuramoylhydrolase;
10-73 2.04e-06

1,4-beta-N-acetylmuramoylhydrolase;


Pssm-ID: 180536 [Multi-domain]  Cd Length: 592  Bit Score: 48.54  E-value: 2.04e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 493016613  10 LPISAATITlvSNQGTADAAT---------VYTVKKNDTLGGISIHYGVSVQAIKQANHKTNDRIYIGEQLTI 73
Cdd:PRK06347 521 LKVSAGSTT--NNTNTAKPSTnkpsnstvkTYTVKKGDSLWAISRQYKTTVDNIKAWNKLTSNMIHVGQKLTI 591
XkdP COG1652
Cytoplasmic potassium-binding protein Kbp/XkdP/YgaU, contains LysM domain [Inorganic ion ...
 77-140 5.17e-06

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: 45.38  E-value: 5.17e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493016613  77 PSSSESTQQKDVAASNHSAQIVYQVQRGDTLEAIAKRY---NVSIQSIRQANN---TNGDRIYAGQHLII 140
Cdd:COG1652   90 AVTVAEEAAAPSAELAPDAPKTYTVKPGDTLWGIAKRFygdPARWPEIAEANRdqiKNPDLIYPGQVLRI 159
PRK13914 PRK13914
invasion associated endopeptidase;
26-91 4.92e-05

invasion associated endopeptidase;


Pssm-ID: 237555 [Multi-domain]  Cd Length: 481  Bit Score: 44.02  E-value: 4.92e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 493016613  26 ADAATVyTVKKNDTLGGISIHYGVSVQAIKQANHKTNDRIYIGEQLTipVSPSSSESTQQKDVAAS 91
Cdd:PRK13914  25 ASASTV-VVEAGDTLWGIAQSKGTTVDAIKKANNLTTDKIVPGQKLQ--VNEVAAAEKTEKSVSAT 87
PRK13914 PRK13914
invasion associated endopeptidase;
72-140 2.97e-04

invasion associated endopeptidase;


Pssm-ID: 237555 [Multi-domain]  Cd Length: 481  Bit Score: 41.71  E-value: 2.97e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 493016613  72 TIPVSPSSSESTQQKDVAASNHSAQiVYQVQRGDTLEAIAKRYNVSIQSIRQANNTNGDRIYAGQHLII 140
Cdd:PRK13914 176 TTQATTPAPKVAETKETPVVDQNAT-THAVKSGDTIWALSVKYGVSVQDIMSWNNLSSSSIYVGQKLAI 243
PRK14125 PRK14125
cell division suppressor protein YneA; Provisional
 1-85 1.03e-03

cell division suppressor protein YneA; Provisional


Pssm-ID: 184523 [Multi-domain]  Cd Length: 103  Bit Score: 37.70  E-value: 1.03e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493016613   1 MKLHKMKHLLPISA------ATITLVSNQGTADAATVYTVKKNDTLGGISIHYGVSVQAIKQA--------NHKTNDRIY 66
Cdd:PRK14125   2 KLKESKIHVSIFFVltalvlLIFVYATVPVDKNQYVEITVQEGDTLWALADQYAGKHHMAKNEfiewvedvNNLPSGHIK 81

                         90
                 ....*....|....*....
gi 493016613  67 IGEQLTIPVSPSSSESTQQ 85
Cdd:PRK14125  82 AGDKLVIPVLKSKSDSYIL 100
PRK11198 PRK11198
LysM domain/BON superfamily protein; Provisional
 99-140 1.59e-03

LysM domain/BON superfamily protein; Provisional


Pssm-ID: 236880 [Multi-domain]  Cd Length: 147  Bit Score: 37.97  E-value: 1.59e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 493016613  99 YQVQRGDTLEAIAK-------RYNVsiqsIRQANN---TNGDRIYAGQHLII 140
Cdd:PRK11198  98 YTVKSGDTLSAIAKkvygnanKYNK----IFEANKpmlKSPDKIYPGQVLRI 145
PRK11198 PRK11198
LysM domain/BON superfamily protein; Provisional
 24-74 2.52e-03

LysM domain/BON superfamily protein; Provisional


Pssm-ID: 236880 [Multi-domain]  Cd Length: 147  Bit Score: 37.59  E-value: 2.52e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 493016613  24 GTADAATVYTVKKNDTLGGIS-IHYGVSVQ--AIKQANH---KTNDRIYIGEQLTIP 74
Cdd:PRK11198  90 TPAPESQFYTVKSGDTLSAIAkKVYGNANKynKIFEANKpmlKSPDKIYPGQVLRIP 146
mltD PRK10783
membrane-bound lytic murein transglycosylase D; Provisional
 15-83 8.56e-03

membrane-bound lytic murein transglycosylase D; Provisional


Pssm-ID: 182727 [Multi-domain]  Cd Length: 456  Bit Score: 37.02  E-value: 8.56e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 493016613  15 ATITLVSNQGTADAATVYTVKKNDTLGGISIHYGVSVQAIKQANHKTNDRIYIGEQLTIPVSPSSSEST 83
Cdd:PRK10783 388 GAGSSAQRLANNSDSITYRVRKGDSLSSIAKRHGVNIKDVMRWNSDTAKNLQPGDKLTLFVKNNSTPDS 456
 
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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