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Conserved domains on  [gi|798945400|ref|WP_045909861|]
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MULTISPECIES: murein transglycosylase D [Enterobacter]

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
 1-454 0e+00

membrane-bound lytic murein transglycosylase D; Provisional


:

Pssm-ID: 182727 [Multi-domain]  Cd Length: 456  Bit Score: 934.54  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 798945400   1 MKAKAILLASVLLVGCQ-SQNGSNVQQHAQSLSAAGQGEAGKFTSSARWMDDGTSFAQDQDLWTSIGDELKMGIPENTRI 79
Cdd:PRK10783   1 MKAKAILLASVLLVGCQsSKNDATVQQHAQSLSSAGQGEAGKYTSQARWMDDGTSIAPDQDLWAFIGDELKMGIPENSRI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 798945400  80 REQKQKYLSNKSYLHDVTLRAEPYMYWIAGQVKKRNMPMELVLLPIVESAFDPHATSGANAAGIWQIIPSTGRNYGLKQT 159
Cdd:PRK10783  81 REQKQKYLRNKSYLHDVTLRAEPYMYWIVGQIKKRNMPMELVLLPIVESAFDPHATSGANAAGIWQIIPSTGRNYGLKQT 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 798945400 160 RNYDARRDVVASTTAALDMMQRLNKMFDGDWLLTVAAYNSGEGRVLKAMKANKARGKSTDFWSLSLPQETKIYVPKMLAL 239
Cdd:PRK10783 161 RWYDARRDVVASTTAALDMMQRLNKMFDGDWLLTVAAYNSGEGRVMKAIKANKAKGKPTDFWSLSLPRETKIYVPKMLAL 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 798945400 240 SDILKNSKRYGVQLPTPDESRALARVRLSNPVDIQQVADMTGMSVSKLKTFNAGVKGSTLGASGPQYVMVPQKHAEQLRE 319
Cdd:PRK10783 241 SDILKNSKRYGVRLPTTDESRALARVDLGQQIELAQAAEMAGMSLTKLKTFNAGYKRSTTAPSGPHYIMVPKKHADQLRE 320

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 798945400 320 SLASGEIAAVQSTLIADASPVNSRSYKVRSGDTLSGIASRLGVSAKDLQQWNNLRGSGLKVGQNLTVGAGSSAQRLANNS 399
Cdd:PRK10783 321 SLASGEIAAVQSTLVADNTPLNSRSYKVRSGDTLSGIASRLNVSTKDLQQWNNLRGSKLKVGQTLTIGAGSSAQRLANNS 400

                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 798945400 400 DSITYRVRKGDSLSSIAKRHGVNIKDVMRWNNDTD-NLKPGDQLTLFVKNSATPDS 454
Cdd:PRK10783 401 DSITYRVRKGDSLSSIAKRHGVNIKDVMRWNSDTAkNLQPGDKLTLFVKNNSTPDS 456
 
Name Accession Description Interval E-value
mltD PRK10783
membrane-bound lytic murein transglycosylase D; Provisional
 1-454 0e+00

membrane-bound lytic murein transglycosylase D; Provisional


Pssm-ID: 182727 [Multi-domain]  Cd Length: 456  Bit Score: 934.54  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 798945400   1 MKAKAILLASVLLVGCQ-SQNGSNVQQHAQSLSAAGQGEAGKFTSSARWMDDGTSFAQDQDLWTSIGDELKMGIPENTRI 79
Cdd:PRK10783   1 MKAKAILLASVLLVGCQsSKNDATVQQHAQSLSSAGQGEAGKYTSQARWMDDGTSIAPDQDLWAFIGDELKMGIPENSRI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 798945400  80 REQKQKYLSNKSYLHDVTLRAEPYMYWIAGQVKKRNMPMELVLLPIVESAFDPHATSGANAAGIWQIIPSTGRNYGLKQT 159
Cdd:PRK10783  81 REQKQKYLRNKSYLHDVTLRAEPYMYWIVGQIKKRNMPMELVLLPIVESAFDPHATSGANAAGIWQIIPSTGRNYGLKQT 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 798945400 160 RNYDARRDVVASTTAALDMMQRLNKMFDGDWLLTVAAYNSGEGRVLKAMKANKARGKSTDFWSLSLPQETKIYVPKMLAL 239
Cdd:PRK10783 161 RWYDARRDVVASTTAALDMMQRLNKMFDGDWLLTVAAYNSGEGRVMKAIKANKAKGKPTDFWSLSLPRETKIYVPKMLAL 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 798945400 240 SDILKNSKRYGVQLPTPDESRALARVRLSNPVDIQQVADMTGMSVSKLKTFNAGVKGSTLGASGPQYVMVPQKHAEQLRE 319
Cdd:PRK10783 241 SDILKNSKRYGVRLPTTDESRALARVDLGQQIELAQAAEMAGMSLTKLKTFNAGYKRSTTAPSGPHYIMVPKKHADQLRE 320

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 798945400 320 SLASGEIAAVQSTLIADASPVNSRSYKVRSGDTLSGIASRLGVSAKDLQQWNNLRGSGLKVGQNLTVGAGSSAQRLANNS 399
Cdd:PRK10783 321 SLASGEIAAVQSTLVADNTPLNSRSYKVRSGDTLSGIASRLNVSTKDLQQWNNLRGSKLKVGQTLTIGAGSSAQRLANNS 400

                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 798945400 400 DSITYRVRKGDSLSSIAKRHGVNIKDVMRWNNDTD-NLKPGDQLTLFVKNSATPDS 454
Cdd:PRK10783 401 DSITYRVRKGDSLSSIAKRHGVNIKDVMRWNSDTAkNLQPGDKLTLFVKNNSTPDS 456
MltD-like cd16894
Membrane-bound lytic murein transglycosylase D and similar proteins; Lytic transglycosylases ...
 111-241 8.52e-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: 196.58  E-value: 8.52e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 798945400 111 VKKRNMPMELVLLPIVESAFDPHATSGANAAGIWQIIPSTGRNYGLKQTRNYDARRDVVASTTAALDMMQRLNKMFdGDW 190
Cdd:cd16894    1 LLKEGLPEELKYLALVESGFNPDAVSSAGAAGLWQFMPATAREYGLRVDSWVDERRDPEKSTRAAARYLKDLYKRF-GDW 79

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 798945400 191 LLTVAAYNSGEGRVLKAMKANKArGKSTDFWSLSLPQETKIYVPKMLALSD 241
Cdd:cd16894   80 LLALAAYNAGEGRVRRAIKRAGT-DKWEDYYRLYLPAETRRYVPKFLAAKI 129
MltE COG0741
Soluble lytic murein transglycosylase or regulatory protein s ( may contain LysM/invasin ...
 28-246 9.67e-41

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: 145.91  E-value: 9.67e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 798945400  28 AQSLSAAGQGEAGKFTSSARWMDDGTSFAQDQDLWTSIGDELKMGIPENTRIREQKQKYLSNKSYLHDVTLRAEPYMYWI 107
Cdd:COG0741   28 AAAAAAALAAAAAALAAAAAAAAGAAAAAASAAAGGPALAAALAAADALAAFAAIAALAAELLALAALLLRRPLPYLPLI 107

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 798945400 108 AGQVKKRNMPMELVL-LPIVESAFDPHATSGANAAGIWQIIPSTGRNYGLKQ--TRNYDARRDVVASTTAALDMMQRLNK 184
Cdd:COG0741  108 EEAAKKYGVDPALVLaLIRQESAFNPNAVSPAGARGLMQLMPATARRLGLKLglGPSPDDLFDPETNIRAGAAYLRELLD 187

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 798945400 185 MFDGDWLLTVAAYNSGEGRVLKAMKANKARGKStdfwslSLP-QETKIYVPKMLALSDILKNS 246
Cdd:COG0741  188 RFDGDLVLALAAYNAGPGRVRRWLRRNGDRDGE------IIPyAETRNYVKKVLANYAIYRAG 244
SLT pfam01464
Transglycosylase SLT domain; This family is distantly related to pfam00062. Members are found ...
 106-219 2.25e-35

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: 127.04  E-value: 2.25e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 798945400  106 WIAGQVKKRNMPMELVLLPIVESAFDPHATSGANAAGIWQIIPSTGRNYGLKQTRNYDARRDVVASTTAALDMMQRLNKM 185
Cdd:pfam01464   1 IIKAAQKYGVDPSLLLAIAQQESGFNPKAVSKSGAVGLMQIMPSTAKRLGLRVNPGVDDLFDPEKNIKAGTKYLKELYKQ 80

                          90       100       110
                  ....*....|....*....|....*....|....
gi 798945400  186 FDGDWLLTVAAYNSGEGRVLKAMKANKARGKSTD 219
Cdd:pfam01464  81 YGGDLWLALAAYNAGPGRVRKWIKNAGAKDKKLL 114
LysM smart00257
Lysin motif;
403-444 1.33e-11

Lysin motif;


Pssm-ID: 197609 [Multi-domain]  Cd Length: 44  Bit Score: 59.00  E-value: 1.33e-11
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 798945400   403 TYRVRKGDSLSSIAKRHGVNIKDVMRWNN--DTDNLKPGDQLTL 444
Cdd:smart00257   1 TYTVKKGDTLSSIARRYGISVSDLLELNNilDPDNLQVGQKLKI 44
 
Name Accession Description Interval E-value
mltD PRK10783
membrane-bound lytic murein transglycosylase D; Provisional
 1-454 0e+00

membrane-bound lytic murein transglycosylase D; Provisional


Pssm-ID: 182727 [Multi-domain]  Cd Length: 456  Bit Score: 934.54  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 798945400   1 MKAKAILLASVLLVGCQ-SQNGSNVQQHAQSLSAAGQGEAGKFTSSARWMDDGTSFAQDQDLWTSIGDELKMGIPENTRI 79
Cdd:PRK10783   1 MKAKAILLASVLLVGCQsSKNDATVQQHAQSLSSAGQGEAGKYTSQARWMDDGTSIAPDQDLWAFIGDELKMGIPENSRI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 798945400  80 REQKQKYLSNKSYLHDVTLRAEPYMYWIAGQVKKRNMPMELVLLPIVESAFDPHATSGANAAGIWQIIPSTGRNYGLKQT 159
Cdd:PRK10783  81 REQKQKYLRNKSYLHDVTLRAEPYMYWIVGQIKKRNMPMELVLLPIVESAFDPHATSGANAAGIWQIIPSTGRNYGLKQT 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 798945400 160 RNYDARRDVVASTTAALDMMQRLNKMFDGDWLLTVAAYNSGEGRVLKAMKANKARGKSTDFWSLSLPQETKIYVPKMLAL 239
Cdd:PRK10783 161 RWYDARRDVVASTTAALDMMQRLNKMFDGDWLLTVAAYNSGEGRVMKAIKANKAKGKPTDFWSLSLPRETKIYVPKMLAL 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 798945400 240 SDILKNSKRYGVQLPTPDESRALARVRLSNPVDIQQVADMTGMSVSKLKTFNAGVKGSTLGASGPQYVMVPQKHAEQLRE 319
Cdd:PRK10783 241 SDILKNSKRYGVRLPTTDESRALARVDLGQQIELAQAAEMAGMSLTKLKTFNAGYKRSTTAPSGPHYIMVPKKHADQLRE 320

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 798945400 320 SLASGEIAAVQSTLIADASPVNSRSYKVRSGDTLSGIASRLGVSAKDLQQWNNLRGSGLKVGQNLTVGAGSSAQRLANNS 399
Cdd:PRK10783 321 SLASGEIAAVQSTLVADNTPLNSRSYKVRSGDTLSGIASRLNVSTKDLQQWNNLRGSKLKVGQTLTIGAGSSAQRLANNS 400

                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 798945400 400 DSITYRVRKGDSLSSIAKRHGVNIKDVMRWNNDTD-NLKPGDQLTLFVKNSATPDS 454
Cdd:PRK10783 401 DSITYRVRKGDSLSSIAKRHGVNIKDVMRWNSDTAkNLQPGDKLTLFVKNNSTPDS 456
MltD-like cd16894
Membrane-bound lytic murein transglycosylase D and similar proteins; Lytic transglycosylases ...
 111-241 8.52e-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: 196.58  E-value: 8.52e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 798945400 111 VKKRNMPMELVLLPIVESAFDPHATSGANAAGIWQIIPSTGRNYGLKQTRNYDARRDVVASTTAALDMMQRLNKMFdGDW 190
Cdd:cd16894    1 LLKEGLPEELKYLALVESGFNPDAVSSAGAAGLWQFMPATAREYGLRVDSWVDERRDPEKSTRAAARYLKDLYKRF-GDW 79

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 798945400 191 LLTVAAYNSGEGRVLKAMKANKArGKSTDFWSLSLPQETKIYVPKMLALSD 241
Cdd:cd16894   80 LLALAAYNAGEGRVRRAIKRAGT-DKWEDYYRLYLPAETRRYVPKFLAAKI 129
MltE COG0741
Soluble lytic murein transglycosylase or regulatory protein s ( may contain LysM/invasin ...
 28-246 9.67e-41

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: 145.91  E-value: 9.67e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 798945400  28 AQSLSAAGQGEAGKFTSSARWMDDGTSFAQDQDLWTSIGDELKMGIPENTRIREQKQKYLSNKSYLHDVTLRAEPYMYWI 107
Cdd:COG0741   28 AAAAAAALAAAAAALAAAAAAAAGAAAAAASAAAGGPALAAALAAADALAAFAAIAALAAELLALAALLLRRPLPYLPLI 107

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 798945400 108 AGQVKKRNMPMELVL-LPIVESAFDPHATSGANAAGIWQIIPSTGRNYGLKQ--TRNYDARRDVVASTTAALDMMQRLNK 184
Cdd:COG0741  108 EEAAKKYGVDPALVLaLIRQESAFNPNAVSPAGARGLMQLMPATARRLGLKLglGPSPDDLFDPETNIRAGAAYLRELLD 187

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 798945400 185 MFDGDWLLTVAAYNSGEGRVLKAMKANKARGKStdfwslSLP-QETKIYVPKMLALSDILKNS 246
Cdd:COG0741  188 RFDGDLVLALAAYNAGPGRVRRWLRRNGDRDGE------IIPyAETRNYVKKVLANYAIYRAG 244
MltF COG4623
Membrane-bound lytic murein transglycosylase MltF [Cell wall/membrane/envelope biogenesis, ...
 73-245 1.68e-36

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


Pssm-ID: 443662 [Multi-domain]  Cd Length: 421  Bit Score: 139.04  E-value: 1.68e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 798945400  73 IPENTRIREQKQKYLSN-----KSYLHDVTLRAEPYMYWIAGQVKKRNMPME-LVLLPIVESAFDPHATSGANAAGIWQI 146
Cdd:COG4623  229 IKKGGTLARLYERYFGHvkrdtRAFLRRIEGRLPPYDPLFEKYAEEYGLDWRlLAALAYQESHWNPRARSPTGARGLMQL 308

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 798945400 147 IPSTGRNYGLKQtrnydaRRDVVASTTAALDMMQRLNKMFD------GDWLLTVAAYNSGEGRVLKAMKANKARGKSTDF 220
Cdd:COG4623  309 MPATAKELGVDD------RLDPEQSIRAGAKYLRWLYDRFPeaidepDRWWFALAAYNAGPGHVQDARRLAKKQGLDPDR 382

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 798945400 221 WSLS-------------LPQETKIYVPKMLALSDILKN 245
Cdd:COG4623  383 WFDVeksqpkyydtgyaRGRETVNYVPNIRAYYDIYKR 420
SLT pfam01464
Transglycosylase SLT domain; This family is distantly related to pfam00062. Members are found ...
 106-219 2.25e-35

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: 127.04  E-value: 2.25e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 798945400  106 WIAGQVKKRNMPMELVLLPIVESAFDPHATSGANAAGIWQIIPSTGRNYGLKQTRNYDARRDVVASTTAALDMMQRLNKM 185
Cdd:pfam01464   1 IIKAAQKYGVDPSLLLAIAQQESGFNPKAVSKSGAVGLMQIMPSTAKRLGLRVNPGVDDLFDPEKNIKAGTKYLKELYKQ 80

                          90       100       110
                  ....*....|....*....|....*....|....
gi 798945400  186 FDGDWLLTVAAYNSGEGRVLKAMKANKARGKSTD 219
Cdd:pfam01464  81 YGGDLWLALAAYNAGPGRVRKWIKNAGAKDKKLL 114
LT-like cd00254
lytic transglycosylase(LT)-like domain; Members include the soluble and insoluble ...
 126-238 2.85e-19

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: 83.03  E-value: 2.85e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 798945400 126 VESAFDPHATSGANAAGIWQIIPSTGRNYGLKQTRNydaRRDVVASTTAALDMMQRLNKMFDGDWLLTVAAYNSGEGRVL 205
Cdd:cd00254   10 VESGFNPRAVSPAGARGLMQLMPGTARDLGRRGVDD---LFDPEENIRAGARYLRELLDRFGGDLELALAAYNAGPGAVD 86

                         90       100       110
                 ....*....|....*....|....*....|...
gi 798945400 206 KAMKANKargkstdfwslSLPQETKIYVPKMLA 238
Cdd:cd00254   87 RWGGGEV-----------PPYKETRNYVQRVLA 108
Slt70-like cd13401
70kDa soluble lytic transglycosylase (Slt70) and similar proteins; Catalytic domain of the ...
 102-238 8.59e-17

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: 77.13  E-value: 8.59e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 798945400 102 PYMYWIAGQVKKRNMPMELVLlPIV--ESAFDPHATSGANAAGIWQIIPSTGRNYGLKQTRNYDARRDV-VASTTAALDM 178
Cdd:cd13401    5 PYRDLVERAAKKNGLDPALVY-AIIrqESAFDPDAVSPAGALGLMQLMPATAKDVAKKLGLPYYSPRDLfDPEYNIRLGS 83

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 798945400 179 --MQRLNKMFDGDWLLTVAAYNSGEGRVLKAMKANkaRGKSTDFWSLSLP-QETKIYVPKMLA 238
Cdd:cd13401   84 ayLAELLDRFDGNPVLALAAYNAGPGRVRRWLKRR--GDLDPDLWIETIPfSETRNYVKRVLE 144
LysM COG1388
LysM repeat [Cell wall/membrane/envelope biogenesis];
292-444 9.85e-17

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


Pssm-ID: 440998 [Multi-domain]  Cd Length: 156  Bit Score: 77.44  E-value: 9.85e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 798945400 292 AGVKGSTLGASGPQYVMVPQKHAEQLRESLASGEIAAVQSTLIADASPVNSRSYKVRSGDTLSGIASRLGVSAKdlqqwn 371
Cdd:COG1388   33 VALLLLAALAPAGLSLAAALNGEALLLLLPAAAAAAKAALAAAPEAAAAAAARYTVKSGDTLSGIARRYGAAAA------ 106

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 798945400 372 nlrgsglkvgqnltvgagssaqrlannSDSITYRVRKGDSLSSIAKRHGVNIKDVMRWNN-DTDNLKPGDQLTL 444
Cdd:COG1388  107 ---------------------------PSPVTYTVKKGDTLWSIARRYGVSVEELKRWNGlSSDTIRPGQKLKI 153
LysM COG1388
LysM repeat [Cell wall/membrane/envelope biogenesis];
230-386 6.48e-16

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


Pssm-ID: 440998 [Multi-domain]  Cd Length: 156  Bit Score: 75.13  E-value: 6.48e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 798945400 230 KIYVPKMLALSDILKNSKRYGVQLPTPDESRALARVRLSNPVDIQQVADMTGMSVSKLKTFNAGVKGSTLGASGPQYVMV 309
Cdd:COG1388    3 LLALSANAALLAAVLTLLAALLLLAAALAAVALLLLAALAPAGLSLAAALNGEALLLLLPAAAAAAKAALAAAPEAAAAA 82

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 798945400 310 PQKHAEQLRESLasGEIAAVQSTliadASPVNSRSYKVRSGDTLSGIASRLGVSAKDLQQWNNLRGSGLKVGQNLTV 386
Cdd:COG1388   83 AARYTVKSGDTL--SGIARRYGA----AAAPSPVTYTVKKGDTLWSIARRYGVSVEELKRWNGLSSDTIRPGQKLKI 153
MLTF-like cd13403
membrane-bound lytic murein transglycosylase F (MLTF) and similar proteins; This subfamily ...
 127-222 2.54e-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: 73.34  E-value: 2.54e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 798945400 127 ESAFDPHATSGANAAGIWQIIPSTGRNYGLKQtrnydaRRDVVASTTAALDMMQRLNKMFDGD------WLLTVAAYNSG 200
Cdd:cd13403   22 ESRFNPNARSPAGARGLMQLMPSTARELGVND------RLDPEQNIHAGAKYLRYLRDRFPPDidepdrLKFALAAYNAG 95

                         90       100
                 ....*....|....*....|..
gi 798945400 201 EGRVLKAMKANKARGKSTDFWS 222
Cdd:cd13403   96 PGHVRDARRLAKKYGLNPNVWF 117
PRK06347 PRK06347
1,4-beta-N-acetylmuramoylhydrolase;
337-442 3.06e-14

1,4-beta-N-acetylmuramoylhydrolase;


Pssm-ID: 180536 [Multi-domain]  Cd Length: 592  Bit Score: 74.73  E-value: 3.06e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 798945400 337 ASPVNSRSYKVRSGDTLSGIASRLGVSAKDLQQWNNLRGSGLKVGQNLTVGAGSSAQ---------------RLANNSDS 401
Cdd:PRK06347 400 GTSTNAKVYTVVKGDSLWRIANNNKVTIANLKSWNNLKSDFIYPGQKLKVSAGSTSNtntskpstntntskpSTNTNTNA 479

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 798945400 402 ITYRVRKGDSLSSIAKRHGVNIKDVMRWNN-DTDNLKPGDQL 442
Cdd:PRK06347 480 KVYTVAKGDSLWRIANNNKVTIANLKSWNNlKSDFIYPGQKL 521
PRK06347 PRK06347
1,4-beta-N-acetylmuramoylhydrolase;
341-442 3.65e-14

1,4-beta-N-acetylmuramoylhydrolase;


Pssm-ID: 180536 [Multi-domain]  Cd Length: 592  Bit Score: 74.73  E-value: 3.65e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 798945400 341 NSRSYKVRSGDTLSGIASRLGVSAKDLQQWNNLRGSGLKVGQNLTVGAGSSAQ----------------RLANNSDSITY 404
Cdd:PRK06347 329 NAKIYTVVKGDSLWRIANNHKVTVANLKAWNNLKSDFIYPGQKLKVSAGSTTSdtntskpstgtstskpSTGTSTNAKVY 408

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 798945400 405 RVRKGDSLSSIAKRHGVNIKDVMRWNN-DTDNLKPGDQL 442
Cdd:PRK06347 409 TVVKGDSLWRIANNNKVTIANLKSWNNlKSDFIYPGQKL 447
PRK06347 PRK06347
1,4-beta-N-acetylmuramoylhydrolase;
341-444 6.26e-14

1,4-beta-N-acetylmuramoylhydrolase;


Pssm-ID: 180536 [Multi-domain]  Cd Length: 592  Bit Score: 73.96  E-value: 6.26e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 798945400 341 NSRSYKVRSGDTLSGIASRLGVSAKDLQQWNNLRGSGLKVGQNLTVGAGSSAQRLA---------NNSDSITYRVRKGDS 411
Cdd:PRK06347 478 NAKVYTVAKGDSLWRIANNNKVTIANLKSWNNLKSDFIYPGQKLKVSAGSTTNNTNtakpstnkpSNSTVKTYTVKKGDS 557

                         90       100       110
                 ....*....|....*....|....*....|....
gi 798945400 412 LSSIAKRHGVNIKDVMRWNNDTDN-LKPGDQLTL 444
Cdd:PRK06347 558 LWAISRQYKTTVDNIKAWNKLTSNmIHVGQKLTI 591
LT_Slt70-like cd16896
uncharacterized lytic transglycosylase subfamily with similarity to Slt70; Uncharacterized ...
 126-248 6.52e-14

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: 68.69  E-value: 6.52e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 798945400 126 VESAFDPHATSGANAAGIWQIIPSTGR----NYGLKQTRN---YDARRDVVASTTaaldMMQRLNKMFDGDWLLTVAAYN 198
Cdd:cd16896   28 VESNFNPNAVSSKGAIGLMQIMPETAEwiaeKLGLEDFSEddlYDPETNIRLGTW----YLSYLLKEFDGNLVLALAAYN 103

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 798945400 199 SGEGRVLKAMKANKARGKSTDFWSLSLPqETKIYVPKmlalsdILKNSKR 248
Cdd:cd16896  104 AGPGNVDKWLKDGGWSGDGKTLDQIPFP-ETRHYVKK------VLKNYKI 146
LysM pfam01476
LysM domain; The LysM (lysin motif) domain is about 40 residues long. It is found in a variety ...
 345-386 4.52e-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: 63.18  E-value: 4.52e-13
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 798945400  345 YKVRSGDTLSGIASRLGVSAKDLQQWNNLRGSGLKVGQNLTV 386
Cdd:pfam01476   1 YTVKKGDTLSSIAKRYGITVEQLAELNGLSSPNLYVGQKLKI 42
LysM pfam01476
LysM domain; The LysM (lysin motif) domain is about 40 residues long. It is found in a variety ...
 404-444 1.58e-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: 61.64  E-value: 1.58e-12
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 798945400  404 YRVRKGDSLSSIAKRHGVNIKDVMRWNN-DTDNLKPGDQLTL 444
Cdd:pfam01476   1 YTVKKGDTLSSIAKRYGITVEQLAELNGlSSPNLYVGQKLKI 42
LysM cd00118
Lysin Motif is a small domain involved in binding peptidoglycan; LysM, a small globular domain ...
 402-444 1.71e-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: 61.73  E-value: 1.71e-12
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 798945400 402 ITYRVRKGDSLSSIAKRHGVNIKDVMRWNN--DTDNLKPGDQLTL 444
Cdd:cd00118    1 KTYTVKPGDTLWSIAKKYGVTVEELAAANPliNPDCIYPGQKLKI 45
LysM cd00118
Lysin Motif is a small domain involved in binding peptidoglycan; LysM, a small globular domain ...
 343-386 7.27e-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: 59.81  E-value: 7.27e-12
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 798945400 343 RSYKVRSGDTLSGIASRLGVSAKDLQQWNNLRGSG-LKVGQNLTV 386
Cdd:cd00118    1 KTYTVKPGDTLWSIAKKYGVTVEELAAANPLINPDcIYPGQKLKI 45
LysM smart00257
Lysin motif;
403-444 1.33e-11

Lysin motif;


Pssm-ID: 197609 [Multi-domain]  Cd Length: 44  Bit Score: 59.00  E-value: 1.33e-11
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 798945400   403 TYRVRKGDSLSSIAKRHGVNIKDVMRWNN--DTDNLKPGDQLTL 444
Cdd:smart00257   1 TYTVKKGDTLSSIARRYGISVSDLLELNNilDPDNLQVGQKLKI 44
LysM smart00257
Lysin motif;
345-386 9.57e-11

Lysin motif;


Pssm-ID: 197609 [Multi-domain]  Cd Length: 44  Bit Score: 56.69  E-value: 9.57e-11
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 798945400   345 YKVRSGDTLSGIASRLGVSAKDLQQWNNLRGSG-LKVGQNLTV 386
Cdd:smart00257   2 YTVKKGDTLSSIARRYGISVSDLLELNNILDPDnLQVGQKLKI 44
LT_MltC_MltE cd16893
membrane-bound lytic murein transglycosylases MltC and MltE, and similar proteins; MltC and ...
 112-239 3.78e-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: 55.64  E-value: 3.78e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 798945400 112 KKRNMPMELVLLPI-VESAFDPHATSGANAAGIWQIIPSTG------RNYGLKQ--TRNY--DARRDVVAStTAALDMMQ 180
Cdd:cd16893    8 KKYGVDPALILAIIeTESSFNPYAVSHSPAYGLMQIVPSTAgrdvyrLLGGKGGlpSKSYlfDPENNIDIG-TAYLHILQ 86

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 798945400 181 R---------LNKMFdgdwlLTVAAYNSGEGRVLKAMKANKARG------KSTD--FWSLS--LP-QETKIYVPKMLAL 239
Cdd:cd16893   87 NrylkgiknpKSREY-----CAIAAYNGGAGNVLRTFSSDRKKAiskinrLSPDevYQHLTkkLPaAETRNYLKKVLKA 160
Lyz-like cd00442
lysozyme-like domains; This family contains several members, including soluble lytic ...
 119-176 7.34e-08

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: 48.95  E-value: 7.34e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 798945400 119 ELVLLPIVESAFDPHA--TSGANAAGIWQIIPSTGRNYGLKQTRNydaRRDVVASTTAAL 176
Cdd:cd00442    1 VLAAIIGQESGGNKPAnaGSGSGAAGLFQFMPGTWKAYGKNSSSD---LNDPEASIEAAA 57
PRK13914 PRK13914
invasion associated endopeptidase;
322-386 1.64e-07

invasion associated endopeptidase;


Pssm-ID: 237555 [Multi-domain]  Cd Length: 481  Bit Score: 53.27  E-value: 1.64e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 798945400 322 ASGEIAAVQSTLIADASPVNSRSYKVRSGDTLSGIASRLGVSAKDLQQWNNLRGSGLKVGQNLTV 386
Cdd:PRK13914 179 ATTPAPKVAETKETPVVDQNATTHAVKSGDTIWALSVKYGVSVQDIMSWNNLSSSSIYVGQKLAI 243
PRK06347 PRK06347
1,4-beta-N-acetylmuramoylhydrolase;
341-442 1.87e-07

1,4-beta-N-acetylmuramoylhydrolase;


Pssm-ID: 180536 [Multi-domain]  Cd Length: 592  Bit Score: 53.55  E-value: 1.87e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 798945400 341 NSRSYKvRSGDTLSGI-------ASRLG--VSAKDLQQWNNLRGSGlkvGQNLTVGAGSSAQRLANNSDSITYRVRKGDS 411
Cdd:PRK06347 265 NTTSYK-DATKALTGTyatdtayATKLNdlISRYNLTQYDSGKTTG---GNSGSTGNSSNSSNTGNTSNAKIYTVVKGDS 340

                         90       100       110
                 ....*....|....*....|....*....|..
gi 798945400 412 LSSIAKRHGVNIKDVMRWNN-DTDNLKPGDQL 442
Cdd:PRK06347 341 LWRIANNHKVTVANLKAWNNlKSDFIYPGQKL 372
Slt35-like cd13399
Slt35-like lytic transglycosylase; Lytic transglycosylase similar to Escherichia coli lytic ...
 126-207 5.89e-07

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: 47.69  E-value: 5.89e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 798945400 126 VESAFDPHA-TSGANAAGIWQIIPSTGRNYGLkqTRNYDARRDVV----ASTTAALDMMQR---LNKMFDGDWLLTVAAY 197
Cdd:cd13399   14 VESGFGPNAgGSPAGAQGIAQFMPSTWKAYGV--DGNGDGKADPFnpedAIASAANYLCRHgwdLNAFLGEDNFLALAAY 91

                         90
                 ....*....|
gi 798945400 198 NSGEGRVLKA 207
Cdd:cd13399   92 NAGPGAYANA 101
OapA COG3061
Cell division protein YtfB/OapA (opacity-associated protein A) [Cell cycle control, cell ...
 396-444 9.89e-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: 47.74  E-value: 9.89e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 798945400 396 ANNSDSITYRVRKGDSLSSIAKRHGVNIKDVMR------WNNDTDNLKPGDQLTL 444
Cdd:COG3061   64 APEGEWQEYTVQSGDTLSQIFRRLGLSASDLYAllaaegDAKPLSRLKPGQELRF 118
XkdP COG1652
Cytoplasmic potassium-binding protein Kbp/XkdP/YgaU, contains LysM domain [Inorganic ion ...
 294-444 1.01e-05

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: 45.77  E-value: 1.01e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 798945400 294 VKGSTLGASGPQYVMVPQKHAEQLRESLASGEIAAVQSTLIADASPVNSRSYKVRSGDTLSGIASRLGVSAKDLQQWNNL 373
Cdd:COG1652    1 VAAAAAAAALAALLPAVSAAAATVLALAAAAALAVVAGLGAAVGAGGALAAALPLAAGLAAAVAAAAAAAVLIAPVAVMR 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 798945400 374 RGSGLKVGQNLTVGAGSSAQRLANNSDSI-TYRVRKGDSLSSIAKRH---GVNIKDVMRWN----NDTDNLKPGDQLTL 444
Cdd:COG1652   81 AGAAAKLSPAVTVAEEAAAPSAELAPDAPkTYTVKPGDTLWGIAKRFygdPARWPEIAEANrdqiKNPDLIYPGQVLRI 159
PHA00368 PHA00368
internal virion protein D
 126-237 1.55e-05

internal virion protein D


Pssm-ID: 222785 [Multi-domain]  Cd Length: 1315  Bit Score: 47.47  E-value: 1.55e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 798945400  126 VESAFDPHATSGANAAGIWQIIPSTGRNYGLKQTRnyDARRDVVASTTAALDMMQRLNKMFDGDWLLTVAAYNSGEGRVL 205
Cdd:PHA00368   35 DESRFNPTAKSPTGPKGLMQFTKATAKALGLIVDD--DDRLDPELAIDAGARYLADLVGKYDGDELKAALAYNQGEGRLG 112

                          90       100       110
                  ....*....|....*....|....*....|..
gi 798945400  206 KAMKANKARGkstDFWSLSlpQETKIYVPKML 237
Cdd:PHA00368  113 APQLEAYDKG---DFASIS--EEGRNYLRNLL 139
mltC PRK11671
membrane-bound lytic murein transglycosylase MltC;
99-214 4.28e-05

membrane-bound lytic murein transglycosylase MltC;


Pssm-ID: 183271 [Multi-domain]  Cd Length: 359  Bit Score: 45.43  E-value: 4.28e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 798945400  99 RAEPYMYWIAGQVKKRNMPMELVLLPI-VESAFDPHATSGANAAGIWQIIPST---------------GRNYGLKQTRNY 162
Cdd:PRK11671 188 RAHKYLPMVRKASRKYGVDESLILAIMqTESSFNPYAVSRSDALGLMQVVQHTagkdvfrmkgksgqpSRSYLFDPANNI 267

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 798945400 163 DArrdvvasTTAALDMMQrlNKMFDGDWLLT------VAAYNSGEGRVLKAMKANKAR 214
Cdd:PRK11671 268 DT-------GTAYLAILQ--NVYLGGITNPTsrryavITAYNGGAGSVLRVFSNDKIQ 316
OapA COG3061
Cell division protein YtfB/OapA (opacity-associated protein A) [Cell cycle control, cell ...
 328-386 1.08e-04

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: 44.27  E-value: 1.08e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 798945400 328 AVQSTLIADASPVNSRSYKVRSGDTLSGIASRLGVSAKDLQQWNNLRGSG-----LKVGQNLTV 386
Cdd:COG3061   55 AAAAPAAPAAPEGEWQEYTVQSGDTLSQIFRRLGLSASDLYALLAAEGDAkplsrLKPGQELRF 118
PHA00658 PHA00658
putative lysin
 135-277 2.72e-04

putative lysin


Pssm-ID: 106967 [Multi-domain]  Cd Length: 720  Bit Score: 43.27  E-value: 2.72e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 798945400 135 TSGANAAGIWQIIPSTG----RNYGLKQTRNyDARRDVVASTTAALDMMQRLNKMFDGDWLLTVAAYNSGEGRVLKAMKA 210
Cdd:PHA00658 325 TSPKGAVGIAQVMPDTApeaaKLAGLPWDEN-RYRNDAAYNRALGMAYFQKQLRDFGGDLPKAYAAYNAGPGALQSALKD 403

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 798945400 211 NKARGkstdfWSLSLPQETKIYV-------------PKMLALSDI---LKNSKRygvqLPTPDESRALARVRLSNPVDIQ 274
Cdd:PHA00658 404 AKDGN-----WLALLPKETQDYVvknmqaynagqgrPARPTLADIeaqLQNDPR----LAGNPERLKIARVEAERQFNMQ 474


                 ...
gi 798945400 275 QVA 277
Cdd:PHA00658 475 TAA 477
 
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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