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Conserved domains on  [gi|446557896|ref|WP_000635242|]
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MULTISPECIES: lytic transglycosylase domain-containing protein [Bacillus cereus group]

Protein Classification

lytic transglycosylase domain-containing protein( domain architecture ID 11432856)

lytic transglycosylase domain-containing protein similar to Bacillus subtilis bifunctional muramidase/lytic transglycosylase CwlQ that cleaves the beta-1,4-glycosidic bond between N-acetylmuramic acid and N-acetylglucosamine (MurNAc-GlcNAc) in peptidoglycan, producing both N-acetylmuramic acid and 1,6-anhydro-N-acetylmuramic acid

Gene Ontology:  GO:0016787|GO:0000270|GO:0008933|GO:0071555
PubMed:  8765311|7479697|9723170

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
MltE COG0741
Soluble lytic murein transglycosylase or regulatory protein s ( may contain LysM/invasin ...
 134-251 1.12e-47

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: 158.23  E-value: 1.12e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557896 134 KYEDIIDRTSRTYGIPKSLIQKMIEVESDFNPKTVSHAGAKGLMQLMPANVKEMGIK--------NPFSPAESIEGGVKE 205
Cdd:COG0741  102 PYLPLIEEAAKKYGVDPALVLALIRQESAFNPNAVSPAGARGLMQLMPATARRLGLKlglgpspdDLFDPETNIRAGAAY 181

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 446557896 206 LSGYLKKNNGDLVLALASYNAGPGNVRKY--------GGVPPFKETQGYIKKIL 251
Cdd:COG0741  182 LRELLDRFDGDLVLALAAYNAGPGRVRRWlrrngdrdGEIIPYAETRNYVKKVL 235
 
Name Accession Description Interval E-value
MltE COG0741
Soluble lytic murein transglycosylase or regulatory protein s ( may contain LysM/invasin ...
 134-251 1.12e-47

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: 158.23  E-value: 1.12e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557896 134 KYEDIIDRTSRTYGIPKSLIQKMIEVESDFNPKTVSHAGAKGLMQLMPANVKEMGIK--------NPFSPAESIEGGVKE 205
Cdd:COG0741  102 PYLPLIEEAAKKYGVDPALVLALIRQESAFNPNAVSPAGARGLMQLMPATARRLGLKlglgpspdDLFDPETNIRAGAAY 181

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 446557896 206 LSGYLKKNNGDLVLALASYNAGPGNVRKY--------GGVPPFKETQGYIKKIL 251
Cdd:COG0741  182 LRELLDRFDGDLVLALAAYNAGPGRVRRWlrrngdrdGEIIPYAETRNYVKKVL 235
LT-like cd00254
lytic transglycosylase(LT)-like domain; Members include the soluble and insoluble ...
 151-251 1.33e-47

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: 153.52  E-value: 1.33e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557896 151 SLIQKMIEVESDFNPKTVSHAGAKGLMQLMPANVKEMGIK---NPFSPAESIEGGVKELSGYLKKNNGDLVLALASYNAG 227
Cdd:cd00254    2 ALVLAVIRVESGFNPRAVSPAGARGLMQLMPGTARDLGRRgvdDLFDPEENIRAGARYLRELLDRFGGDLELALAAYNAG 81

                         90       100
                 ....*....|....*....|....*.
gi 446557896 228 PGNVRKYGG--VPPFKETQGYIKKIL 251
Cdd:cd00254   82 PGAVDRWGGgeVPPYKETRNYVQRVL 107
SLT pfam01464
Transglycosylase SLT domain; This family is distantly related to pfam00062. Members are found ...
 143-244 1.73e-27

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: 102.00  E-value: 1.73e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557896  143 SRTYGIPKSLIQKMIEVESDFNPKTVSHAGAKGLMQLMPANVKEMGIK------NPFSPAESIEGGVKELSGYLKKNNGD 216
Cdd:pfam01464   5 AQKYGVDPSLLLAIAQQESGFNPKAVSKSGAVGLMQIMPSTAKRLGLRvnpgvdDLFDPEKNIKAGTKYLKELYKQYGGD 84

                          90       100
                  ....*....|....*....|....*...
gi 446557896  217 LVLALASYNAGPGNVRKYGGVPPFKETQ 244
Cdd:pfam01464  85 LWLALAAYNAGPGRVRKWIKNAGAKDKK 112
PRK11619 PRK11619
lytic murein transglycosylase; Provisional
 135-255 7.94e-17

lytic murein transglycosylase; Provisional


Pssm-ID: 183236 [Multi-domain]  Cd Length: 644  Bit Score: 79.33  E-value: 7.94e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557896 135 YEDIIDRTSRTYGIPKSLIQKMIEVESDFNPKTVSHAGAKGLMQLMPA----NVKEMGIK---NP---FSPAESIEGGVK 204
Cdd:PRK11619 479 WNDEFRRYTSGKGIPQSYAMAIARQESAWNPKARSPVGASGLMQIMPGtathTVKMFSIPgysSSsqlLDPETNINIGTS 558

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446557896 205 ELSGYLKKNNGDLVLALASYNAGPGNVRKYGGVP-------------PFKETQGYIKKILNIDV 255
Cdd:PRK11619 559 YLEYVYQQFGNNRILASAAYNAGPGRVRTWLGNSagridavafvesiPFSETRGYVKNVLAYDA 622
 
Name Accession Description Interval E-value
MltE COG0741
Soluble lytic murein transglycosylase or regulatory protein s ( may contain LysM/invasin ...
 134-251 1.12e-47

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: 158.23  E-value: 1.12e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557896 134 KYEDIIDRTSRTYGIPKSLIQKMIEVESDFNPKTVSHAGAKGLMQLMPANVKEMGIK--------NPFSPAESIEGGVKE 205
Cdd:COG0741  102 PYLPLIEEAAKKYGVDPALVLALIRQESAFNPNAVSPAGARGLMQLMPATARRLGLKlglgpspdDLFDPETNIRAGAAY 181

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 446557896 206 LSGYLKKNNGDLVLALASYNAGPGNVRKY--------GGVPPFKETQGYIKKIL 251
Cdd:COG0741  182 LRELLDRFDGDLVLALAAYNAGPGRVRRWlrrngdrdGEIIPYAETRNYVKKVL 235
LT-like cd00254
lytic transglycosylase(LT)-like domain; Members include the soluble and insoluble ...
 151-251 1.33e-47

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: 153.52  E-value: 1.33e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557896 151 SLIQKMIEVESDFNPKTVSHAGAKGLMQLMPANVKEMGIK---NPFSPAESIEGGVKELSGYLKKNNGDLVLALASYNAG 227
Cdd:cd00254    2 ALVLAVIRVESGFNPRAVSPAGARGLMQLMPGTARDLGRRgvdDLFDPEENIRAGARYLRELLDRFGGDLELALAAYNAG 81

                         90       100
                 ....*....|....*....|....*.
gi 446557896 228 PGNVRKYGG--VPPFKETQGYIKKIL 251
Cdd:cd00254   82 PGAVDRWGGgeVPPYKETRNYVQRVL 107
Slt70-like cd13401
70kDa soluble lytic transglycosylase (Slt70) and similar proteins; Catalytic domain of the ...
 135-251 3.19e-37

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: 128.36  E-value: 3.19e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557896 135 YEDIIDRTSRTYGIPKSLIQKMIEVESDFNPKTVSHAGAKGLMQLMPANVKEM----GIKNP-----FSPAESIEGGVKE 205
Cdd:cd13401    6 YRDLVERAAKKNGLDPALVYAIIRQESAFDPDAVSPAGALGLMQLMPATAKDVakklGLPYYsprdlFDPEYNIRLGSAY 85

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 446557896 206 LSGYLKKNNGDLVLALASYNAGPGNVRK----YGGVP--------PFKETQGYIKKIL 251
Cdd:cd13401   86 LAELLDRFDGNPVLALAAYNAGPGRVRRwlkrRGDLDpdlwietiPFSETRNYVKRVL 143
LT_Slt70-like cd16896
uncharacterized lytic transglycosylase subfamily with similarity to Slt70; Uncharacterized ...
 134-251 2.50e-35

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: 123.39  E-value: 2.50e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557896 134 KYEDIIDRTSRTYGIPKSLIQKMIEVESDFNPKTVSHAGAKGLMQLMP--AN--VKEMGIKNP-----FSPAESIEGGVK 204
Cdd:cd16896    3 KYREYIEKYAKEYGVDPLLVAAVIKVESNFNPNAVSSKGAIGLMQIMPetAEwiAEKLGLEDFseddlYDPETNIRLGTW 82

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 446557896 205 ELSGYLKKNNGDLVLALASYNAGPGNVRKYGGVP------------PFKETQGYIKKIL 251
Cdd:cd16896   83 YLSYLLKEFDGNLVLALAAYNAGPGNVDKWLKDGgwsgdgktldqiPFPETRHYVKKVL 141
MltF COG4623
Membrane-bound lytic murein transglycosylase MltF [Cell wall/membrane/envelope biogenesis, ...
 134-251 1.97e-30

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


Pssm-ID: 443662 [Multi-domain]  Cd Length: 421  Bit Score: 117.08  E-value: 1.97e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557896 134 KYEDIIDRTSRTYGIPKSLIQKMIEVESDFNPKTVSHAGAKGLMQLMPANVKEMGIKNPFSPAESIEGGVKelsgYLKK- 212
Cdd:COG4623  263 PYDPLFEKYAEEYGLDWRLLAALAYQESHWNPRARSPTGARGLMQLMPATAKELGVDDRLDPEQSIRAGAK----YLRWl 338

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446557896 213 ---------NNGDLVLALASYNAGPGNVR-------KYGGVPPF-------------------KETQGYIKKIL 251
Cdd:COG4623  339 ydrfpeaidEPDRWWFALAAYNAGPGHVQdarrlakKQGLDPDRwfdveksqpkyydtgyargRETVNYVPNIR 412
SLT pfam01464
Transglycosylase SLT domain; This family is distantly related to pfam00062. Members are found ...
 143-244 1.73e-27

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: 102.00  E-value: 1.73e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557896  143 SRTYGIPKSLIQKMIEVESDFNPKTVSHAGAKGLMQLMPANVKEMGIK------NPFSPAESIEGGVKELSGYLKKNNGD 216
Cdd:pfam01464   5 AQKYGVDPSLLLAIAQQESGFNPKAVSKSGAVGLMQIMPSTAKRLGLRvnpgvdDLFDPEKNIKAGTKYLKELYKQYGGD 84

                          90       100
                  ....*....|....*....|....*...
gi 446557896  217 LVLALASYNAGPGNVRKYGGVPPFKETQ 244
Cdd:pfam01464  85 LWLALAAYNAGPGRVRKWIKNAGAKDKK 112
MLTF-like cd13403
membrane-bound lytic murein transglycosylase F (MLTF) and similar proteins; This subfamily ...
 141-238 6.86e-27

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: 101.84  E-value: 6.86e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557896 141 RTSRTYGIPKSLIQKMIEVESDFNPKTVSHAGAKGLMQLMPANVKEMGIKNPFSPAESIEGGVKELSgYLKKNNGD---- 216
Cdd:cd13403    3 KYAEKYGFDWRLLAAQAYQESRFNPNARSPAGARGLMQLMPSTARELGVNDRLDPEQNIHAGAKYLR-YLRDRFPPdide 81

                         90       100       110
                 ....*....|....*....|....*....|..
gi 446557896 217 ---LVLALASYNAGPGNVR-------KYGGVP 238
Cdd:cd13403   82 pdrLKFALAAYNAGPGHVRdarrlakKYGLNP 113
MltD-like cd16894
Membrane-bound lytic murein transglycosylase D and similar proteins; Lytic transglycosylases ...
 146-253 8.94e-22

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: 87.57  E-value: 8.94e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557896 146 YGIPKSLiqKMI-EVESDFNPKTVSHAGAKGLMQLMPANVKEMGIKNP------FSPAESIEGGVKelsgYLKKNN---G 215
Cdd:cd16894    4 EGLPEEL--KYLaLVESGFNPDAVSSAGAAGLWQFMPATAREYGLRVDswvderRDPEKSTRAAAR----YLKDLYkrfG 77

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 446557896 216 DLVLALASYNAGPGNVRK----YGGVPPF--------KETQGYIKKILNI 253
Cdd:cd16894   78 DWLLALAAYNAGEGRVRRaikrAGTDKWEdyyrlylpAETRRYVPKFLAA 127
LT_MltC_MltE cd16893
membrane-bound lytic murein transglycosylases MltC and MltE, and similar proteins; MltC and ...
 137-252 1.24e-18

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: 80.30  E-value: 1.24e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557896 137 DIIDRTSRTYGIPKSLIQKMIEVESDFNPKTVSHAGAKGLMQLMPA----NVKEMGIKNP--------FSPAESIEGGVK 204
Cdd:cd16893    1 PIVEKYAKKYGVDPALILAIIETESSFNPYAVSHSPAYGLMQIVPStagrDVYRLLGGKGglpsksylFDPENNIDIGTA 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446557896 205 ELS----GYLKKNNGDLVL---ALASYNAGPGNVRKYGGVP------------------------PFKETQGYIKKILN 252
Cdd:cd16893   81 YLHilqnRYLKGIKNPKSReycAIAAYNGGAGNVLRTFSSDrkkaiskinrlspdevyqhltkklPAAETRNYLKKVLK 159
PRK11619 PRK11619
lytic murein transglycosylase; Provisional
 135-255 7.94e-17

lytic murein transglycosylase; Provisional


Pssm-ID: 183236 [Multi-domain]  Cd Length: 644  Bit Score: 79.33  E-value: 7.94e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557896 135 YEDIIDRTSRTYGIPKSLIQKMIEVESDFNPKTVSHAGAKGLMQLMPA----NVKEMGIK---NP---FSPAESIEGGVK 204
Cdd:PRK11619 479 WNDEFRRYTSGKGIPQSYAMAIARQESAWNPKARSPVGASGLMQIMPGtathTVKMFSIPgysSSsqlLDPETNINIGTS 558

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446557896 205 ELSGYLKKNNGDLVLALASYNAGPGNVRKYGGVP-------------PFKETQGYIKKILNIDV 255
Cdd:PRK11619 559 YLEYVYQQFGNNRILASAAYNAGPGRVRTWLGNSagridavafvesiPFSETRGYVKNVLAYDA 622
Slt35-like cd13399
Slt35-like lytic transglycosylase; Lytic transglycosylase similar to Escherichia coli lytic ...
 146-230 2.27e-16

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: 72.73  E-value: 2.27e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557896 146 YGIPKSLIQKMIEVESDFNPKTV-SHAGAKGLMQLMPANVKEMGI-------KNPFSPAESIEGGVKELS---GYLKKNN 214
Cdd:cd13399    1 YGVPPGILAAILGVESGFGPNAGgSPAGAQGIAQFMPSTWKAYGVdgngdgkADPFNPEDAIASAANYLCrhgWDLNAFL 80

                         90
                 ....*....|....*..
gi 446557896 215 GDLV-LALASYNAGPGN 230
Cdd:cd13399   81 GEDNfLALAAYNAGPGA 97
PHA00368 PHA00368
internal virion protein D
 135-229 3.66e-12

internal virion protein D


Pssm-ID: 222785 [Multi-domain]  Cd Length: 1315  Bit Score: 65.96  E-value: 3.66e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557896  135 YEDIIDRTSRTYGIPKSLIQKMIEVESDFNPKTVSHAGAKGLMQLMPANVKEMGIKNP----FSPAESIEGGVKELSGYL 210
Cdd:PHA00368   11 YDGLFQKAADAHGVSYDLLRKVGWDESRFNPTAKSPTGPKGLMQFTKATAKALGLIVDdddrLDPELAIDAGARYLADLV 90

                          90
                  ....*....|....*....
gi 446557896  211 KKNNGDLVLALASYNAGPG 229
Cdd:PHA00368   91 GKYDGDELKAALAYNQGEG 109
mltC PRK11671
membrane-bound lytic murein transglycosylase MltC;
134-231 1.77e-11

membrane-bound lytic murein transglycosylase MltC;


Pssm-ID: 183271 [Multi-domain]  Cd Length: 359  Bit Score: 63.15  E-value: 1.77e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557896 134 KYEDIIDRTSRTYGIPKSLIQKMIEVESDFNPKTVSHAGAKGLMQLMPA----NVKEMGIKN--P-----FSPAESIEGG 202
Cdd:PRK11671 191 KYLPMVRKASRKYGVDESLILAIMQTESSFNPYAVSRSDALGLMQVVQHtagkDVFRMKGKSgqPsrsylFDPANNIDTG 270

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 446557896 203 VKELS----GYLK--KNNGDLVLALAS-YNAGPGNV 231
Cdd:PRK11671 271 TAYLAilqnVYLGgiTNPTSRRYAVITaYNGGAGSV 306
PRK10859 PRK10859
membrane-bound lytic murein transglycosylase MltF;
160-232 7.28e-11

membrane-bound lytic murein transglycosylase MltF;


Pssm-ID: 236778 [Multi-domain]  Cd Length: 482  Bit Score: 61.81  E-value: 7.28e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557896 160 ESDFNPKTVSHAGAKGLMQLMPANVKEMGIKNPFSPAESIEGGVKelsgYLKknngDLV--------------LALASYN 225
Cdd:PRK10859 313 ESHWNPQATSPTGVRGLMMLTRNTAQSMGVTDRLDPEQSIRGGAR----YLQ----DLMerlpesipeperiwFALAAYN 384


                 ....*..
gi 446557896 226 AGPGNVR 232
Cdd:PRK10859 385 IGYGHML 391
GEWL cd01021
Goose egg-white lysozyme; Eukaryotic goose-type or G-type lysozyme (goose egg-white lysozyme; ...
 134-237 9.99e-08

Goose egg-white lysozyme; Eukaryotic goose-type or G-type lysozyme (goose egg-white lysozyme; GEWL) catalyzes the cleavage of the beta-1,4-glycosidic bond between N-acetylmuramic acid (MurNAc) and N-acetylglucosamine (GlcNAc). Mammals have two lysozymes. This family corresponds to human and mouse lysozyme G-like protein 2.


Pssm-ID: 381601 [Multi-domain]  Cd Length: 174  Bit Score: 50.68  E-value: 9.99e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557896 134 KYEDIIDRTSRTYGIPKSLIQKMIEVESdfnpktvsHAGAK-------------GLMQLmpaNVKEMGIKNPFSPAESIE 200
Cdd:cd01021   36 KYKDCIKQVGKKLCIDPALIAAIISRES--------RAGAAldkngwgdhgngfGLMQV---DKRYHPPKGAWDSEEHIE 104

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 446557896 201 GGVKELSGYLK--KNNGD-------LVLALASYNAGPGNVRKYGGV 237
Cdd:cd01021  105 QATGILIDFIKtvQRKHPswspeqqLKGGIAAYNAGVGNVQSYAGM 150
CwlT-like cd16891
CwlT-like N-terminal lysozyme domain and similar domains; CwlT is a bifunctional cell wall ...
 135-237 1.36e-05

CwlT-like N-terminal lysozyme domain and similar domains; CwlT is a bifunctional cell wall hydrolase containing an N-terminal lysozyme domain and a C-terminal NlpC/P60 endopeptidase domain (gamma-d-D-glutamyl-L-diamino acid endopeptidase), and has been implicated in the spread of transposons. 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: 381612 [Multi-domain]  Cd Length: 151  Bit Score: 44.13  E-value: 1.36e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557896 135 YEDIIDRTSRTYGIPK--SLIQKMIEVESdfnpktvshaGAKG--LMQL-----MPANvkemGIKNPfspAESIEGGVKE 205
Cdd:cd16891    1 YRPLVEKEAKKYGIPEyvPLILAIIMQES----------GGKGpdIMQSsesagLPPN----TITDP---EESIEQGVKY 63

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 446557896 206 LSGYLKK---NNGDLVLALASYNAGPG---NVRKYGGV 237
Cdd:cd16891   64 FADVLKKakgKGVDIWTAVQAYNFGGGyidYVAKNGGK 101
LT_IagB-like cd13400
Escherichia coli invasion protein IagB and similar proteins; Lytic transglycosylase-like ...
 146-253 1.50e-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: 40.20  E-value: 1.50e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557896 146 YGIPKSLIQKMIEVESDFNPKTVSHAGAK----GLMQ--------LmpanvKEMGIKNP---FSPAESIEGGVKELSGYL 210
Cdd:cd13400    1 YGVPPRLLRAIAKVESGFNPNAINRNKNGsydiGLMQinsiwlpeL-----ARYGITREellNDPCTNIYVGAWILARNI 75

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 446557896 211 KKnNGDLVLALASYNAGPGNVRkyggvppfketQGYIKKILNI 253
Cdd:cd13400   76 KR-YGNTWKAVGAYNSGTPKKN-----------DKYARKVYRI 106
emtA PRK15470
membrane-bound lytic murein transglycosylase EmtA;
138-182 8.47e-04

membrane-bound lytic murein transglycosylase EmtA;


Pssm-ID: 185367 [Multi-domain]  Cd Length: 203  Bit Score: 39.56  E-value: 8.47e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 446557896 138 IIDRTSRTYGIPKSLIQKMIEVESDFNPKTVSHAGAKGLMQLMPA 182
Cdd:PRK15470  42 ISQKAGAAWGVDPQLITAIIAIESGGNPNAVSKSNAIGLMQLKAS 86
Lyz-like cd00442
lysozyme-like domains; This family contains several members, including soluble lytic ...
 156-205 6.25e-03

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: 34.31  E-value: 6.25e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 446557896 156 MIEVESDFNPKT--VSHAGAKGLMQLMPANVKEMGIKNP---FSPAESIEGGVKE 205
Cdd:cd00442    5 IIGQESGGNKPAnaGSGSGAAGLFQFMPGTWKAYGKNSSsdlNDPEASIEAAAKY 59
 
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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