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Conserved domains on  [gi|937129024|ref|WP_054563767|]
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MULTISPECIES: transglycosylase SLT domain-containing protein [Pseudoalteromonas]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK11619 super family cl42930
lytic murein transglycosylase; Provisional
 1-619 3.81e-74

lytic murein transglycosylase; Provisional


The actual alignment was detected with superfamily member PRK11619:

Pssm-ID: 183236 [Multi-domain]  Cd Length: 644  Bit Score: 249.98  E-value: 3.81e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937129024   1 MKKQLLGWTAAALLFPFFAAEAN-DKHDaflkaEKKARYG------DYQDMKEAASGL----DHPLKPYVEkaYWQRNPS 69
Cdd:PRK11619   4 AKMGKWRLLAAGVCLLTVSGVARaDSLD-----EQRQRYQqikqawDNRQMDVVEQLMptlkDYPLYPYLE--YRQLTQD 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937129024  70 LKHQT--EIENYLNVYQNTPlewPVRKAWLNYLkkyNKKAAyirnyRETSNNELT------------CPYLSFQLDLGAP 135
Cdd:PRK11619  77 LMNQPavQVTNFIRANPTLP---PARSLQSRFV---NELAR-----REDWRGLLAfspekpkpvearCNYYYAKWATGQQ 145

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937129024 136 EKAiMNQVTDLWVVGKSQPKECDKLFSLWKKKGYQTEERVWQRISLAAEGGSSSLIPYLKTLLPRADQYLADLYLKVRKD 215
Cdd:PRK11619 146 QEA-WQGAKELWLTGKSLPNACDKLFSVWQQSGKQDPLAYLERIRLAMKAGNTGLVTYLAKQLPADYQTIASALIKLQND 224

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937129024 216 PSASAGLYRYKKKSAKEGQIAIYGVKRLVWRDKDLALRAWEKLETMFDYTDEQKADVYYSFALSLASSG--HQQARfWLN 293
Cdd:PRK11619 225 PNTVETFARTTGPTDFTRQMAAVAFASVARQDAENARLMIPSLVRAQKLNEDQRQELRDIVAWRLMGNDvtDEQAK-WRD 303

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937129024 294 KVPKDRQTRKLMQWQLGNMLERQDWSGIVAFFT--GKENLSLGQ-QYWLAYSLNQRGEVERAREIWQTVAKERDYYGFLA 370
Cdd:PRK11619 304 DVIMRSQSTSLLERRVRMALGTGDRRGLNTWLArlPMEAKEKDEwRYWQADLLLEQGRKAEAEEILRQLMQQRGFYPMVA 383

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937129024 371 SARLGIPVSLNnkeINISNKLKLEVANAPGFKRARALYELERFTSARREWNYLTGTSTKEEKLAASLLAAELDWYDSTIY 450
Cdd:PRK11619 384 AQRLGEEYPLK---IDKAPKPDSALTQGPEMARVRELMYWNMDNTARSEWANLVASRSKTEQAQLARYAFNQQWWDLSVQ 460

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937129024 451 TLAQLKEWDYVDLRFPFAFKDVFATYSSRSHIDVAWSIAISRRESSFAPDARSHANAHGLMQLLPSTAKYMNKSS----- 525
Cdd:PRK11619 461 ATIAGKLWDHLEERFPLAWNDEFRRYTSGKGIPQSYAMAIARQESAWNPKARSPVGASGLMQIMPGTATHTVKMFsipgy 540

                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937129024 526 VSRKQLYQPRTNIRLGSEYLQYLKKKNHGNEILATASYNAGYHRIKRWIPEQA--MPAELWIELIPYTETRNYVKNVFAY 603
Cdd:PRK11619 541 SSSSQLLDPETNINIGTSYLEYVYQQFGNNRILASAAYNAGPGRVRTWLGNSAgrIDAVAFVESIPFSETRGYVKNVLAY 620

                        650
                 ....*....|....*.
gi 937129024 604 RQVYHTRLGRDGNVLA 619
Cdd:PRK11619 621 DAYYRYFMGQKPTLLS 636
 
Name Accession Description Interval E-value
PRK11619 PRK11619
lytic murein transglycosylase; Provisional
 1-619 3.81e-74

lytic murein transglycosylase; Provisional


Pssm-ID: 183236 [Multi-domain]  Cd Length: 644  Bit Score: 249.98  E-value: 3.81e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937129024   1 MKKQLLGWTAAALLFPFFAAEAN-DKHDaflkaEKKARYG------DYQDMKEAASGL----DHPLKPYVEkaYWQRNPS 69
Cdd:PRK11619   4 AKMGKWRLLAAGVCLLTVSGVARaDSLD-----EQRQRYQqikqawDNRQMDVVEQLMptlkDYPLYPYLE--YRQLTQD 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937129024  70 LKHQT--EIENYLNVYQNTPlewPVRKAWLNYLkkyNKKAAyirnyRETSNNELT------------CPYLSFQLDLGAP 135
Cdd:PRK11619  77 LMNQPavQVTNFIRANPTLP---PARSLQSRFV---NELAR-----REDWRGLLAfspekpkpvearCNYYYAKWATGQQ 145

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937129024 136 EKAiMNQVTDLWVVGKSQPKECDKLFSLWKKKGYQTEERVWQRISLAAEGGSSSLIPYLKTLLPRADQYLADLYLKVRKD 215
Cdd:PRK11619 146 QEA-WQGAKELWLTGKSLPNACDKLFSVWQQSGKQDPLAYLERIRLAMKAGNTGLVTYLAKQLPADYQTIASALIKLQND 224

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937129024 216 PSASAGLYRYKKKSAKEGQIAIYGVKRLVWRDKDLALRAWEKLETMFDYTDEQKADVYYSFALSLASSG--HQQARfWLN 293
Cdd:PRK11619 225 PNTVETFARTTGPTDFTRQMAAVAFASVARQDAENARLMIPSLVRAQKLNEDQRQELRDIVAWRLMGNDvtDEQAK-WRD 303

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937129024 294 KVPKDRQTRKLMQWQLGNMLERQDWSGIVAFFT--GKENLSLGQ-QYWLAYSLNQRGEVERAREIWQTVAKERDYYGFLA 370
Cdd:PRK11619 304 DVIMRSQSTSLLERRVRMALGTGDRRGLNTWLArlPMEAKEKDEwRYWQADLLLEQGRKAEAEEILRQLMQQRGFYPMVA 383

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937129024 371 SARLGIPVSLNnkeINISNKLKLEVANAPGFKRARALYELERFTSARREWNYLTGTSTKEEKLAASLLAAELDWYDSTIY 450
Cdd:PRK11619 384 AQRLGEEYPLK---IDKAPKPDSALTQGPEMARVRELMYWNMDNTARSEWANLVASRSKTEQAQLARYAFNQQWWDLSVQ 460

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937129024 451 TLAQLKEWDYVDLRFPFAFKDVFATYSSRSHIDVAWSIAISRRESSFAPDARSHANAHGLMQLLPSTAKYMNKSS----- 525
Cdd:PRK11619 461 ATIAGKLWDHLEERFPLAWNDEFRRYTSGKGIPQSYAMAIARQESAWNPKARSPVGASGLMQIMPGTATHTVKMFsipgy 540

                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937129024 526 VSRKQLYQPRTNIRLGSEYLQYLKKKNHGNEILATASYNAGYHRIKRWIPEQA--MPAELWIELIPYTETRNYVKNVFAY 603
Cdd:PRK11619 541 SSSSQLLDPETNINIGTSYLEYVYQQFGNNRILASAAYNAGPGRVRTWLGNSAgrIDAVAFVESIPFSETRGYVKNVLAY 620

                        650
                 ....*....|....*.
gi 937129024 604 RQVYHTRLGRDGNVLA 619
Cdd:PRK11619 621 DAYYRYFMGQKPTLLS 636
Slt70-like cd13401
70kDa soluble lytic transglycosylase (Slt70) and similar proteins; Catalytic domain of the ...
 464-610 2.71e-64

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: 208.48  E-value: 2.71e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937129024 464 RFPFAFKDVFATYSSRSHIDVAWSIAISRRESSFAPDARSHANAHGLMQLLPSTAKYMNK----SSVSRKQLYQPRTNIR 539
Cdd:cd13401    1 RYPLPYRDLVERAAKKNGLDPALVYAIIRQESAFDPDAVSPAGALGLMQLMPATAKDVAKklglPYYSPRDLFDPEYNIR 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 937129024 540 LGSEYLQYLKKKNHGNEILATASYNAGYHRIKRWIPEQ-AMPAELWIELIPYTETRNYVKNVFAYRQVYHTR 610
Cdd:cd13401   81 LGSAYLAELLDRFDGNPVLALAAYNAGPGRVRRWLKRRgDLDPDLWIETIPFSETRNYVKRVLENYVVYRAL 152
MltE COG0741
Soluble lytic murein transglycosylase or regulatory protein s ( may contain LysM/invasin ...
 391-607 3.32e-46

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: 163.63  E-value: 3.32e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937129024 391 LKLEVANAPGFKRARALYELERFTSARREWNYLTGTSTKEEKLAASLLAAELDWYDSTIYTLAQLKEWDYVD--LRFPFA 468
Cdd:COG0741   23 LALLAAAAAAAALAAAAAALAAAAAAAAGAAAAAASAAAGGPALAAALAAADALAAFAAIAALAAELLALAAllLRRPLP 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937129024 469 FKDVFATYSSRSHIDVAWSIAISRRESSFAPDARSHANAHGLMQLLPSTAKYMNKS---SVSRKQLYQPRTNIRLGSEYL 545
Cdd:COG0741  103 YLPLIEEAAKKYGVDPALVLALIRQESAFNPNAVSPAGARGLMQLMPATARRLGLKlglGPSPDDLFDPETNIRAGAAYL 182

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 937129024 546 QYLKKKNHGNEILATASYNAGYHRIKRWIPEQampAELWIELIPYTETRNYVKNVFAYRQVY 607
Cdd:COG0741  183 RELLDRFDGDLVLALAAYNAGPGRVRRWLRRN---GDRDGEIIPYAETRNYVKKVLANYAIY 241
SLT pfam01464
Transglycosylase SLT domain; This family is distantly related to pfam00062. Members are found ...
 476-574 7.69e-20

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: 85.05  E-value: 7.69e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937129024  476 YSSRSHIDVAWSIAISRRESSFAPDARSHANAHGLMQLLPSTAK-YMNKSSVSRKQLYQPRTNIRLGSEYLQYLKKKNHG 554
Cdd:pfam01464   4 AAQKYGVDPSLLLAIAQQESGFNPKAVSKSGAVGLMQIMPSTAKrLGLRVNPGVDDLFDPEKNIKAGTKYLKELYKQYGG 83

                          90       100
                  ....*....|....*....|
gi 937129024  555 NEILATASYNAGYHRIKRWI 574
Cdd:pfam01464  84 DLWLALAAYNAGPGRVRKWI 103
 
Name Accession Description Interval E-value
PRK11619 PRK11619
lytic murein transglycosylase; Provisional
 1-619 3.81e-74

lytic murein transglycosylase; Provisional


Pssm-ID: 183236 [Multi-domain]  Cd Length: 644  Bit Score: 249.98  E-value: 3.81e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937129024   1 MKKQLLGWTAAALLFPFFAAEAN-DKHDaflkaEKKARYG------DYQDMKEAASGL----DHPLKPYVEkaYWQRNPS 69
Cdd:PRK11619   4 AKMGKWRLLAAGVCLLTVSGVARaDSLD-----EQRQRYQqikqawDNRQMDVVEQLMptlkDYPLYPYLE--YRQLTQD 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937129024  70 LKHQT--EIENYLNVYQNTPlewPVRKAWLNYLkkyNKKAAyirnyRETSNNELT------------CPYLSFQLDLGAP 135
Cdd:PRK11619  77 LMNQPavQVTNFIRANPTLP---PARSLQSRFV---NELAR-----REDWRGLLAfspekpkpvearCNYYYAKWATGQQ 145

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937129024 136 EKAiMNQVTDLWVVGKSQPKECDKLFSLWKKKGYQTEERVWQRISLAAEGGSSSLIPYLKTLLPRADQYLADLYLKVRKD 215
Cdd:PRK11619 146 QEA-WQGAKELWLTGKSLPNACDKLFSVWQQSGKQDPLAYLERIRLAMKAGNTGLVTYLAKQLPADYQTIASALIKLQND 224

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937129024 216 PSASAGLYRYKKKSAKEGQIAIYGVKRLVWRDKDLALRAWEKLETMFDYTDEQKADVYYSFALSLASSG--HQQARfWLN 293
Cdd:PRK11619 225 PNTVETFARTTGPTDFTRQMAAVAFASVARQDAENARLMIPSLVRAQKLNEDQRQELRDIVAWRLMGNDvtDEQAK-WRD 303

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937129024 294 KVPKDRQTRKLMQWQLGNMLERQDWSGIVAFFT--GKENLSLGQ-QYWLAYSLNQRGEVERAREIWQTVAKERDYYGFLA 370
Cdd:PRK11619 304 DVIMRSQSTSLLERRVRMALGTGDRRGLNTWLArlPMEAKEKDEwRYWQADLLLEQGRKAEAEEILRQLMQQRGFYPMVA 383

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937129024 371 SARLGIPVSLNnkeINISNKLKLEVANAPGFKRARALYELERFTSARREWNYLTGTSTKEEKLAASLLAAELDWYDSTIY 450
Cdd:PRK11619 384 AQRLGEEYPLK---IDKAPKPDSALTQGPEMARVRELMYWNMDNTARSEWANLVASRSKTEQAQLARYAFNQQWWDLSVQ 460

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937129024 451 TLAQLKEWDYVDLRFPFAFKDVFATYSSRSHIDVAWSIAISRRESSFAPDARSHANAHGLMQLLPSTAKYMNKSS----- 525
Cdd:PRK11619 461 ATIAGKLWDHLEERFPLAWNDEFRRYTSGKGIPQSYAMAIARQESAWNPKARSPVGASGLMQIMPGTATHTVKMFsipgy 540

                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937129024 526 VSRKQLYQPRTNIRLGSEYLQYLKKKNHGNEILATASYNAGYHRIKRWIPEQA--MPAELWIELIPYTETRNYVKNVFAY 603
Cdd:PRK11619 541 SSSSQLLDPETNINIGTSYLEYVYQQFGNNRILASAAYNAGPGRVRTWLGNSAgrIDAVAFVESIPFSETRGYVKNVLAY 620

                        650
                 ....*....|....*.
gi 937129024 604 RQVYHTRLGRDGNVLA 619
Cdd:PRK11619 621 DAYYRYFMGQKPTLLS 636
Slt70-like cd13401
70kDa soluble lytic transglycosylase (Slt70) and similar proteins; Catalytic domain of the ...
 464-610 2.71e-64

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: 208.48  E-value: 2.71e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937129024 464 RFPFAFKDVFATYSSRSHIDVAWSIAISRRESSFAPDARSHANAHGLMQLLPSTAKYMNK----SSVSRKQLYQPRTNIR 539
Cdd:cd13401    1 RYPLPYRDLVERAAKKNGLDPALVYAIIRQESAFDPDAVSPAGALGLMQLMPATAKDVAKklglPYYSPRDLFDPEYNIR 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 937129024 540 LGSEYLQYLKKKNHGNEILATASYNAGYHRIKRWIPEQ-AMPAELWIELIPYTETRNYVKNVFAYRQVYHTR 610
Cdd:cd13401   81 LGSAYLAELLDRFDGNPVLALAAYNAGPGRVRRWLKRRgDLDPDLWIETIPFSETRNYVKRVLENYVVYRAL 152
MltE COG0741
Soluble lytic murein transglycosylase or regulatory protein s ( may contain LysM/invasin ...
 391-607 3.32e-46

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: 163.63  E-value: 3.32e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937129024 391 LKLEVANAPGFKRARALYELERFTSARREWNYLTGTSTKEEKLAASLLAAELDWYDSTIYTLAQLKEWDYVD--LRFPFA 468
Cdd:COG0741   23 LALLAAAAAAAALAAAAAALAAAAAAAAGAAAAAASAAAGGPALAAALAAADALAAFAAIAALAAELLALAAllLRRPLP 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937129024 469 FKDVFATYSSRSHIDVAWSIAISRRESSFAPDARSHANAHGLMQLLPSTAKYMNKS---SVSRKQLYQPRTNIRLGSEYL 545
Cdd:COG0741  103 YLPLIEEAAKKYGVDPALVLALIRQESAFNPNAVSPAGARGLMQLMPATARRLGLKlglGPSPDDLFDPETNIRAGAAYL 182

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 937129024 546 QYLKKKNHGNEILATASYNAGYHRIKRWIPEQampAELWIELIPYTETRNYVKNVFAYRQVY 607
Cdd:COG0741  183 RELLDRFDGDLVLALAAYNAGPGRVRRWLRRN---GDRDGEIIPYAETRNYVKKVLANYAIY 241
LT_Slt70-like cd16896
uncharacterized lytic transglycosylase subfamily with similarity to Slt70; Uncharacterized ...
 466-606 6.68e-39

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: 139.95  E-value: 6.68e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937129024 466 PFAFKDVFATYSSRSHIDVAWSIAISRRESSFAPDARSHANAHGLMQLLPSTAKY----MNKSSVSRKQLYQPRTNIRLG 541
Cdd:cd16896    1 PLKYREYIEKYAKEYGVDPLLVAAVIKVESNFNPNAVSSKGAIGLMQIMPETAEWiaekLGLEDFSEDDLYDPETNIRLG 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 937129024 542 SEYLQYLKKKNHGNEILATASYNAGYHRIKRWIPEQAM-PAELWIELIPYTETRNYVKNVFAYRQV 606
Cdd:cd16896   81 TWYLSYLLKEFDGNLVLALAAYNAGPGNVDKWLKDGGWsGDGKTLDQIPFPETRHYVKKVLKNYKI 146
LT-like cd00254
lytic transglycosylase(LT)-like domain; Members include the soluble and insoluble ...
 489-605 3.31e-30

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: 114.62  E-value: 3.31e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937129024 489 AISRRESSFAPDARSHANAHGLMQLLPSTAKYMNKSSVSRkqLYQPRTNIRLGSEYLQYLKKKNHGNEILATASYNAGYH 568
Cdd:cd00254    6 AVIRVESGFNPRAVSPAGARGLMQLMPGTARDLGRRGVDD--LFDPEENIRAGARYLRELLDRFGGDLELALAAYNAGPG 83

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 937129024 569 RIKRWipeqampaeLWIELIPYTETRNYVKNVFAYRQ 605
Cdd:cd00254   84 AVDRW---------GGGEVPPYKETRNYVQRVLAYYQ 111
LT_MltC_MltE cd16893
membrane-bound lytic murein transglycosylases MltC and MltE, and similar proteins; MltC and ...
 475-605 4.26e-25

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: 101.87  E-value: 4.26e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937129024 475 TYSSRSHIDVAWSIAISRRESSFAPDARSHANAHGLMQLLPSTA-------KYMNKSSVSRKQLYQPRTNIRLGSEYL-- 545
Cdd:cd16893    5 KYAKKYGVDPALILAIIETESSFNPYAVSHSPAYGLMQIVPSTAgrdvyrlLGGKGGLPSKSYLFDPENNIDIGTAYLhi 84

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 937129024 546 ---QYLKKKNH--GNEILATASYNAGYHRIKRWI---PEQAM-------PAELWIELI---PYTETRNYVKNVFAYRQ 605
Cdd:cd16893   85 lqnRYLKGIKNpkSREYCAIAAYNGGAGNVLRTFssdRKKAIskinrlsPDEVYQHLTkklPAAETRNYLKKVLKAKK 162
MltF COG4623
Membrane-bound lytic murein transglycosylase MltF [Cell wall/membrane/envelope biogenesis, ...
 469-607 4.90e-20

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


Pssm-ID: 443662 [Multi-domain]  Cd Length: 421  Bit Score: 92.82  E-value: 4.90e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937129024 469 FKDVFATYSSRSHIDVAWSIAISRRESSFAPDARSHANAHGLMQLLPSTAKYMNKssvsrKQLYQPRTNIRLGSEYLQYL 548
Cdd:COG4623  264 YDPLFEKYAEEYGLDWRLLAALAYQESHWNPRARSPTGARGLMQLMPATAKELGV-----DDRLDPEQSIRAGAKYLRWL 338

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937129024 549 KKK--NHGNEI----LATASYNAGYHRIKR---------------WIPEQAMPAELWIELIPYTETRNYVKNVFAYRQVY 607
Cdd:COG4623  339 YDRfpEAIDEPdrwwFALAAYNAGPGHVQDarrlakkqgldpdrwFDVEKSQPKYYDTGYARGRETVNYVPNIRAYYDIY 418
SLT pfam01464
Transglycosylase SLT domain; This family is distantly related to pfam00062. Members are found ...
 476-574 7.69e-20

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: 85.05  E-value: 7.69e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937129024  476 YSSRSHIDVAWSIAISRRESSFAPDARSHANAHGLMQLLPSTAK-YMNKSSVSRKQLYQPRTNIRLGSEYLQYLKKKNHG 554
Cdd:pfam01464   4 AAQKYGVDPSLLLAIAQQESGFNPKAVSKSGAVGLMQIMPSTAKrLGLRVNPGVDDLFDPEKNIKAGTKYLKELYKQYGG 83

                          90       100
                  ....*....|....*....|
gi 937129024  555 NEILATASYNAGYHRIKRWI 574
Cdd:pfam01464  84 DLWLALAAYNAGPGRVRKWI 103
MLTF-like cd13403
membrane-bound lytic murein transglycosylase F (MLTF) and similar proteins; This subfamily ...
 489-607 5.59e-17

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: 78.73  E-value: 5.59e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937129024 489 AISRRESSFAPDARSHANAHGLMQLLPSTAKymnksSVSRKQLYQPRTNIRLGSEYLQYLKKKNHGNE------ILATAS 562
Cdd:cd13403   17 AQAYQESRFNPNARSPAGARGLMQLMPSTAR-----ELGVNDRLDPEQNIHAGAKYLRYLRDRFPPDIdepdrlKFALAA 91

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 937129024 563 YNAGYHRI--------------------KRWIPEQAMPAELWIELIPYT---ETRNYVKNVFAYRQVY 607
Cdd:cd13403   92 YNAGPGHVrdarrlakkyglnpnvwfdnVEVLPLLKSPYYDPVVKYGYArgrETVNYVRNIRKYYDAY 159
MltD-like cd16894
Membrane-bound lytic murein transglycosylase D and similar proteins; Lytic transglycosylases ...
 494-605 3.04e-14

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: 69.85  E-value: 3.04e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937129024 494 ESSFAPDARSHANAHGLMQLLPSTAK-YMNKSSVSRKQLYQPRTNIRLGSEYLQYLKKKNhGNEILATASYNAGYHRIKR 572
Cdd:cd16894   17 ESGFNPDAVSSAGAAGLWQFMPATAReYGLRVDSWVDERRDPEKSTRAAARYLKDLYKRF-GDWLLALAAYNAGEGRVRR 95

                         90       100       110
                 ....*....|....*....|....*....|....
gi 937129024 573 WIPEQAMPAELWIELIPY-TETRNYVKNVFAYRQ 605
Cdd:cd16894   96 AIKRAGTDKWEDYYRLYLpAETRRYVPKFLAAKI 129
SLT_L pfam14718
Soluble lytic murein transglycosylase L domain; Soluble lytic murein transglycosylase (SLT) ...
 394-461 1.37e-13

Soluble lytic murein transglycosylase L domain; Soluble lytic murein transglycosylase (SLT) consists of three domains, an N-terminal U domain, an L domain (linker domain) and a C-terminal domain (C). The L domain may be involved in the interaction of the enzyme with peptidoglycan.


Pssm-ID: 434154 [Multi-domain]  Cd Length: 68  Bit Score: 65.70  E-value: 1.37e-13
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 937129024  394 EVANAPGFKRARALYELERFTSARREWNYLTGTSTKEEKLAASLLAAELDWYDSTIYTLAQLKEWDYV 461
Cdd:pfam14718   1 KVAQLPALARIRELLALGRDAEARREWRHLLARLDKEQQLALARLALDWGWHDLAIQATIQAKLWDDL 68
mltD PRK10783
membrane-bound lytic murein transglycosylase D; Provisional
 494-602 2.27e-09

membrane-bound lytic murein transglycosylase D; Provisional


Pssm-ID: 182727 [Multi-domain]  Cd Length: 456  Bit Score: 60.13  E-value: 2.27e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937129024 494 ESSFAPDARSHANAHGLMQLLPSTAKYMnksSVSRKQLYQPR------TNIRLgsEYLQYLKKKNHGNEILATASYNAGY 567
Cdd:PRK10783 128 ESAFDPHATSGANAAGIWQIIPSTGRNY---GLKQTRWYDARrdvvasTTAAL--DMMQRLNKMFDGDWLLTVAAYNSGE 202

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 937129024 568 HRIKRWIPE---QAMPAELWIELIPYtETRNYVKNVFA 602
Cdd:PRK10783 203 GRVMKAIKAnkaKGKPTDFWSLSLPR-ETKIYVPKMLA 239
PRK10859 PRK10859
membrane-bound lytic murein transglycosylase MltF;
451-567 1.30e-08

membrane-bound lytic murein transglycosylase MltF;


Pssm-ID: 236778 [Multi-domain]  Cd Length: 482  Bit Score: 57.58  E-value: 1.30e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937129024 451 TLAQLKE--------WDYVDLR-FPFAFKDVFATYssRSHI-----DVAWSI--AISRRESSFAPDARSHANAHGLMQLL 514
Cdd:PRK10859 256 TLARLEEkyfghvdrFDYVDTRtFLRAIDNRLPKY--QPLFekyagELDWRLlaAIAYQESHWNPQATSPTGVRGLMMLT 333

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 937129024 515 PSTAKYMNkssVSRKqlYQPRTNIRLGSEYLQYLKKK-----NHGNEI-LATASYNAGY 567
Cdd:PRK10859 334 RNTAQSMG---VTDR--LDPEQSIRGGARYLQDLMERlpesiPEPERIwFALAAYNIGY 387
mltC PRK11671
membrane-bound lytic murein transglycosylase MltC;
477-551 1.47e-08

membrane-bound lytic murein transglycosylase MltC;


Pssm-ID: 183271 [Multi-domain]  Cd Length: 359  Bit Score: 56.98  E-value: 1.47e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937129024 477 SSRSHIDVAWSIAISRRESSFAPDARSHANAHGLMQLLPSTA-----KYMNKSSV-SRKQLYQPRTNIRLGSEYLQYLKK 550
Cdd:PRK11671 200 SRKYGVDESLILAIMQTESSFNPYAVSRSDALGLMQVVQHTAgkdvfRMKGKSGQpSRSYLFDPANNIDTGTAYLAILQN 279


                 .
gi 937129024 551 K 551
Cdd:PRK11671 280 V 280
Slt35-like cd13399
Slt35-like lytic transglycosylase; Lytic transglycosylase similar to Escherichia coli lytic ...
 484-566 2.44e-05

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: 43.84  E-value: 2.44e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937129024 484 VAWSI--AISRRESSFAPDA-RSHANAHGLMQLLPSTAKYMNKSSVS--RKQLYQPRTNIRLGSEYLQYLKKKNHGNEI- 557
Cdd:cd13399    3 VPPGIlaAILGVESGFGPNAgGSPAGAQGIAQFMPSTWKAYGVDGNGdgKADPFNPEDAIASAANYLCRHGWDLNAFLGe 82

                         90
                 ....*....|..
gi 937129024 558 ---LATASYNAG 566
Cdd:cd13399   83 dnfLALAAYNAG 94
LT_IagB-like cd13400
Escherichia coli invasion protein IagB and similar proteins; Lytic transglycosylase-like ...
 489-573 2.25e-04

Escherichia coli invasion protein IagB and similar proteins; Lytic transglycosylase-like protein, similar to Escherichia coli invasion protein IagB. IagB is encoded within a pathogenicity island in Salmonella enterica and has been shown to degrade polymeric peptidoglycan. IagB-like invasion proteins are implicated in the invasion of eukaryotic host cells by bacteria. 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. Members of this family resemble the soluble and insoluble membrane-bound LTs in bacteria and the LTs in bacteriophage lambda.


Pssm-ID: 381603 [Multi-domain]  Cd Length: 109  Bit Score: 40.98  E-value: 2.25e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937129024 489 AISRRESSFAPDARSHAN----AHGLMQL----LPSTAKYmnkSSVSRKQLYQPRTNIRLGSEYLQYLKKKnHGNEILAT 560
Cdd:cd13400   10 AIAKVESGFNPNAINRNKngsyDIGLMQInsiwLPELARY---GITREELLNDPCTNIYVGAWILARNIKR-YGNTWKAV 85

                         90
                 ....*....|...
gi 937129024 561 ASYNAGYHRIKRW 573
Cdd:cd13400   86 GAYNSGTPKKNDK 98
emtA PRK15470
membrane-bound lytic murein transglycosylase EmtA;
485-549 4.76e-04

membrane-bound lytic murein transglycosylase EmtA;


Pssm-ID: 185367 [Multi-domain]  Cd Length: 203  Bit Score: 41.87  E-value: 4.76e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 937129024 485 AWSI------AISRRESSFAPDARSHANAHGLMQLLPSTA-----KYMN-KSSVSRKQLYQPRTNIRLGSEYLQYLK 549
Cdd:PRK15470  49 AWGVdpqlitAIIAIESGGNPNAVSKSNAIGLMQLKASTSgrdvyRRMGwSGEPTTSELKNPERNISMGAAYLNILE 125
PHA00368 PHA00368
internal virion protein D
 494-599 7.08e-04

internal virion protein D


Pssm-ID: 222785 [Multi-domain]  Cd Length: 1315  Bit Score: 42.85  E-value: 7.08e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937129024  494 ESSFAPDARSHANAHGLMQLLPSTAKYMNKsSVSRKQLYQPRTNIRLGSEYLQYLKKKNHGNEILATASYNAGYHRIKRw 573
Cdd:PHA00368   36 ESRFNPTAKSPTGPKGLMQFTKATAKALGL-IVDDDDRLDPELAIDAGARYLADLVGKYDGDELKAALAYNQGEGRLGA- 113

                          90       100
                  ....*....|....*....|....*.
gi 937129024  574 ipEQAMPAELWIELIPYTETRNYVKN 599
Cdd:PHA00368  114 --PQLEAYDKGDFASISEEGRNYLRN 137
PRK15328 PRK15328
type III secretion system invasion protein IagB;
463-566 8.70e-03

type III secretion system invasion protein IagB;


Pssm-ID: 185228 [Multi-domain]  Cd Length: 160  Bit Score: 37.54  E-value: 8.70e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937129024 463 LRFPFAFKDVFATYSSRSHIDVAWSIAISRRESSFAPDA--RSHANAH--GLMQLLPSTAKYMNKSSVSRKQLYQ-PRTN 537
Cdd:PRK15328  12 LSINTAWADCWLQAEKMFNIESELLYAIAQQESAMKPGAigHNRDGSTdlGLMQINSFHMKRLKKMGISEKQLLQdPCIS 91

                         90       100
                 ....*....|....*....|....*....
gi 937129024 538 IRLGSEYLQYLKKKnHGNEILATASYNAG 566
Cdd:PRK15328  92 VIVGASILSDMMKI-YGYSWEAVGAYNAG 119
 
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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