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Conserved domains on  [gi|500205258|ref|WP_011875482|]
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MULTISPECIES: lytic transglycosylase domain-containing protein [Burkholderia]

Protein Classification

lytic transglycosylase domain-containing protein( domain architecture ID 12989917)

lytic transglycosylase domain-containing protein similar to phage exolysin that catalyzes the cleavage of the host peptidoglycans during virus entry

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
LT_IagB-like cd13400
Escherichia coli invasion protein IagB and similar proteins; Lytic transglycosylase-like ...
 30-135 1.35e-57

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: 174.25  E-value: 1.35e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500205258  30 HGVNPQLLRVIAQHESGMRPNAVNRNTNGSEDIGLMQINTSWLPTLARYGI-RREHLFNGCVSAYVGAWILASNVRRFGP 108
Cdd:cd13400    1 YGVPPRLLRAIAKVESGFNPNAINRNKNGSYDIGLMQINSIWLPELARYGItREELLNDPCTNIYVGAWILARNIKRYGN 80

                         90       100
                 ....*....|....*....|....*..
gi 500205258 109 NWKAVGAYNAVTPSKQLVYASAIYRRF 135
Cdd:cd13400   81 TWKAVGAYNSGTPKKNDKYARKVYRIY 107
 
Name Accession Description Interval E-value
LT_IagB-like cd13400
Escherichia coli invasion protein IagB and similar proteins; Lytic transglycosylase-like ...
 30-135 1.35e-57

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: 174.25  E-value: 1.35e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500205258  30 HGVNPQLLRVIAQHESGMRPNAVNRNTNGSEDIGLMQINTSWLPTLARYGI-RREHLFNGCVSAYVGAWILASNVRRFGP 108
Cdd:cd13400    1 YGVPPRLLRAIAKVESGFNPNAINRNKNGSYDIGLMQINSIWLPELARYGItREELLNDPCTNIYVGAWILARNIKRYGN 80

                         90       100
                 ....*....|....*....|....*..
gi 500205258 109 NWKAVGAYNAVTPSKQLVYASAIYRRF 135
Cdd:cd13400   81 TWKAVGAYNSGTPKKNDKYARKVYRIY 107
PRK15328 PRK15328
type III secretion system invasion protein IagB;
1-137 1.13e-34

type III secretion system invasion protein IagB;


Pssm-ID: 185228 [Multi-domain]  Cd Length: 160  Bit Score: 118.04  E-value: 1.13e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500205258   1 MRIVPIVAAVLAFTAlpSRADCLDDAAAFHGVNPQLLRVIAQHESGMRPNAVNRNTNGSEDIGLMQINTSWLPTLARYGI 80
Cdd:PRK15328   2 HYFFIIVIWLLSINT--AWADCWLQAEKMFNIESELLYAIAQQESAMKPGAIGHNRDGSTDLGLMQINSFHMKRLKKMGI 79

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 500205258  81 RREHLF-NGCVSAYVGAWILASNVRRFGPNWKAVGAYNAVTP----SKQLVYASAIYRRFMQ 137
Cdd:PRK15328  80 SEKQLLqDPCISVIVGASILSDMMKIYGYSWEAVGAYNAGTSpkrsDIRKRYAKKIWENYRK 141
SLT pfam01464
Transglycosylase SLT domain; This family is distantly related to pfam00062. Members are found ...
 31-118 2.87e-18

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: 74.65  E-value: 2.87e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500205258   31 GVNPQLLRVIAQHESGMRPNAVNRntngSEDIGLMQINTSwlpTLARYGIRREH----LFNGCVSAYVGAWILASNVRRF 106
Cdd:pfam01464   9 GVDPSLLLAIAQQESGFNPKAVSK----SGAVGLMQIMPS---TAKRLGLRVNPgvddLFDPEKNIKAGTKYLKELYKQY 81

                          90
                  ....*....|...
gi 500205258  107 GPNW-KAVGAYNA 118
Cdd:pfam01464  82 GGDLwLALAAYNA 94
MltE COG0741
Soluble lytic murein transglycosylase or regulatory protein s ( may contain LysM/invasin ...
 24-118 2.02e-07

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: 48.07  E-value: 2.02e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500205258  24 DDAAAFHGVNPQLLRVIAQHESGMRPNAVNRntNGSedIGLMQIntswLP-TLARYGIR------REHLFNGCVSAYVGA 96
Cdd:COG0741  108 EEAAKKYGVDPALVLALIRQESAFNPNAVSP--AGA--RGLMQL----MPaTARRLGLKlglgpsPDDLFDPETNIRAGA 179

                         90       100
                 ....*....|....*....|...
gi 500205258  97 WILASNVRRFGPNW-KAVGAYNA 118
Cdd:COG0741  180 AYLRELLDRFDGDLvLALAAYNA 202
LYZ1 smart00263
Alpha-lactalbumin / lysozyme C;
40-71 8.36e-07

Alpha-lactalbumin / lysozyme C;


Pssm-ID: 197612  Cd Length: 127  Bit Score: 44.97  E-value: 8.36e-07
                           10        20        30
                   ....*....|....*....|....*....|..
gi 500205258    40 IAQHESGMRPNAVNRNTNGSEDIGLMQINTSW 71
Cdd:smart00263  31 LAFHESGYNTQATNYNNGGSTDYGIFQINSKY 62
 
Name Accession Description Interval E-value
LT_IagB-like cd13400
Escherichia coli invasion protein IagB and similar proteins; Lytic transglycosylase-like ...
 30-135 1.35e-57

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: 174.25  E-value: 1.35e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500205258  30 HGVNPQLLRVIAQHESGMRPNAVNRNTNGSEDIGLMQINTSWLPTLARYGI-RREHLFNGCVSAYVGAWILASNVRRFGP 108
Cdd:cd13400    1 YGVPPRLLRAIAKVESGFNPNAINRNKNGSYDIGLMQINSIWLPELARYGItREELLNDPCTNIYVGAWILARNIKRYGN 80

                         90       100
                 ....*....|....*....|....*..
gi 500205258 109 NWKAVGAYNAVTPSKQLVYASAIYRRF 135
Cdd:cd13400   81 TWKAVGAYNSGTPKKNDKYARKVYRIY 107
PRK15328 PRK15328
type III secretion system invasion protein IagB;
1-137 1.13e-34

type III secretion system invasion protein IagB;


Pssm-ID: 185228 [Multi-domain]  Cd Length: 160  Bit Score: 118.04  E-value: 1.13e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500205258   1 MRIVPIVAAVLAFTAlpSRADCLDDAAAFHGVNPQLLRVIAQHESGMRPNAVNRNTNGSEDIGLMQINTSWLPTLARYGI 80
Cdd:PRK15328   2 HYFFIIVIWLLSINT--AWADCWLQAEKMFNIESELLYAIAQQESAMKPGAIGHNRDGSTDLGLMQINSFHMKRLKKMGI 79

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 500205258  81 RREHLF-NGCVSAYVGAWILASNVRRFGPNWKAVGAYNAVTP----SKQLVYASAIYRRFMQ 137
Cdd:PRK15328  80 SEKQLLqDPCISVIVGASILSDMMKIYGYSWEAVGAYNAGTSpkrsDIRKRYAKKIWENYRK 141
PRK13722 PRK13722
lytic transglycosylase; Provisional
 21-133 9.17e-22

lytic transglycosylase; Provisional


Pssm-ID: 184274 [Multi-domain]  Cd Length: 169  Bit Score: 85.13  E-value: 9.17e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500205258  21 DCLDDAAAFHGVNPQLLRVIAQHESGMRPNAVNRNTNGSEDIGLMQINTSWLPTLARYGIRREHL-FNGCVSAYVGAWIL 99
Cdd:PRK13722  21 DCFDLAGRDYKIDPDLLRAISWKESRYRVNAIGINPVTGYGSGLMQVDSQHFNELARYGIKPEHLtTDPCMNIYTGAYYL 100

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 500205258 100 ASNVRRFGPNWKAVGAYNA------VTPSKQLVYASAIYR 133
Cdd:PRK13722 101 AIAFKKWGVSWEAVGAYNAgfrkteRQNQRRLAYASEVYR 140
SLT pfam01464
Transglycosylase SLT domain; This family is distantly related to pfam00062. Members are found ...
 31-118 2.87e-18

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: 74.65  E-value: 2.87e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500205258   31 GVNPQLLRVIAQHESGMRPNAVNRntngSEDIGLMQINTSwlpTLARYGIRREH----LFNGCVSAYVGAWILASNVRRF 106
Cdd:pfam01464   9 GVDPSLLLAIAQQESGFNPKAVSK----SGAVGLMQIMPS---TAKRLGLRVNPgvddLFDPEKNIKAGTKYLKELYKQY 81

                          90
                  ....*....|...
gi 500205258  107 GPNW-KAVGAYNA 118
Cdd:pfam01464  82 GGDLwLALAAYNA 94
PRK13888 PRK13888
conjugal transfer protein TrbN; Provisional
 19-134 3.21e-18

conjugal transfer protein TrbN; Provisional


Pssm-ID: 237545  Cd Length: 206  Bit Score: 76.79  E-value: 3.21e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500205258  19 RADCLDDAAAFHGVNPQLLRVIAQHESGmRPNAVNRNTNGSEDIGLMQINTSWLPTLARYGIRREHLFN-GCVSAYVGAW 97
Cdd:PRK13888  14 RVVCSISAAVKYEVPANIVLAVAEKEGG-KPGQWVRNTNGTHDVGPMQFNTAYLGDLARYGITANDVAAaGCYSFDLAAW 92

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 500205258  98 ILASNVRR-FGPNWKAVGAYNAVTPSKQLVYASAIYRR 134
Cdd:PRK13888  93 RLRMHIRNdKGDLWTKAANYHSRTPQYNAVYRADLMRK 130
LT-like cd00254
lytic transglycosylase(LT)-like domain; Members include the soluble and insoluble ...
 34-118 1.76e-09

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: 51.83  E-value: 1.76e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500205258  34 PQLLRVIAQHESGMRPNAVNRNTngseDIGLMQINTSWLPTLARYGIRRehLFNGCVSAYVGAWILASNVRRFGPNW-KA 112
Cdd:cd00254    1 PALVLAVIRVESGFNPRAVSPAG----ARGLMQLMPGTARDLGRRGVDD--LFDPEENIRAGARYLRELLDRFGGDLeLA 74


                 ....*.
gi 500205258 113 VGAYNA 118
Cdd:cd00254   75 LAAYNA 80
LT_VirB1-like cd16892
VirB1-like subfamily; This subfamily includes VirB1 protein, one of twelve proteins making up ...
 31-105 1.57e-08

VirB1-like subfamily; This subfamily includes VirB1 protein, one of twelve proteins making up type IV secretion systems (T4SS). T4SS are macromolecular assemblies generally composed of VirB1-11 and VirD4 proteins, and are used by bacteria to transport material across their membranes. VirB1 acts as a lytic transglycosylase (LT), and is important with respect to piercing the peptidoglycan layer in the periplasm. 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, the LTs in bacteriophage lambda, as well as the eukaryotic "goose-type" lysozymes (goose egg-white lysozyme; GEWL).


Pssm-ID: 381613 [Multi-domain]  Cd Length: 143  Bit Score: 49.85  E-value: 1.57e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500205258  31 GVNPQLLRVIAQHESGMRPNAVNRNTNG-----------------------SEDIGLMQINTSwlpTLARYGIRREHLFN 87
Cdd:cd16892    8 GVHPETLAAIVQVESGGNPYAIGVNGGKlsrqpktkaeaiatarqliaaghNFDVGLGQINSR---NLARLGLTVEDVFD 84

                         90
                 ....*....|....*...
gi 500205258  88 GCVSAYVGAWILASNVRR 105
Cdd:cd16892   85 PCTNLKAGATILTECYAR 102
MltE COG0741
Soluble lytic murein transglycosylase or regulatory protein s ( may contain LysM/invasin ...
 24-118 2.02e-07

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: 48.07  E-value: 2.02e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500205258  24 DDAAAFHGVNPQLLRVIAQHESGMRPNAVNRntNGSedIGLMQIntswLP-TLARYGIR------REHLFNGCVSAYVGA 96
Cdd:COG0741  108 EEAAKKYGVDPALVLALIRQESAFNPNAVSP--AGA--RGLMQL----MPaTARRLGLKlglgpsPDDLFDPETNIRAGA 179

                         90       100
                 ....*....|....*....|...
gi 500205258  97 WILASNVRRFGPNW-KAVGAYNA 118
Cdd:COG0741  180 AYLRELLDRFDGDLvLALAAYNA 202
LYZ1 smart00263
Alpha-lactalbumin / lysozyme C;
40-71 8.36e-07

Alpha-lactalbumin / lysozyme C;


Pssm-ID: 197612  Cd Length: 127  Bit Score: 44.97  E-value: 8.36e-07
                           10        20        30
                   ....*....|....*....|....*....|..
gi 500205258    40 IAQHESGMRPNAVNRNTNGSEDIGLMQINTSW 71
Cdd:smart00263  31 LAFHESGYNTQATNYNNGGSTDYGIFQINSKY 62
Slt70-like cd13401
70kDa soluble lytic transglycosylase (Slt70) and similar proteins; Catalytic domain of the ...
 24-118 2.55e-06

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: 44.00  E-value: 2.55e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500205258  24 DDAAAFHGVNPQLLRVIAQHESGMRPNAVNRntngSEDIGLMQIntswLPTLAR-----YGIR---REHLFNGCVSAYVG 95
Cdd:cd13401   11 ERAAKKNGLDPALVYAIIRQESAFDPDAVSP----AGALGLMQL----MPATAKdvakkLGLPyysPRDLFDPEYNIRLG 82

                         90       100
                 ....*....|....*....|....
gi 500205258  96 AWILASNVRRFGPNW-KAVGAYNA 118
Cdd:cd13401   83 SAYLAELLDRFDGNPvLALAAYNA 106
LYZ_C cd16897
C-type lysozyme; C-type lysozyme (chicken or conventional type; 1, 4-beta-N-acetylmuramidase). ...
 41-71 5.22e-06

C-type lysozyme; C-type lysozyme (chicken or conventional type; 1, 4-beta-N-acetylmuramidase). In humans, lysozyme is found in a wide variety of tissue types and body fluids. It has bacteriolytic properties through the hydolysis of beta-1,4, glyocosidic linkages between N-acetylmuramic acid and N-acetyl-D-glucosamine residues in a peptidoglycan, as well as between N-acetyl-D-glucosamine residues in chitodextrins. This family also includes digestive stomach lysozyme, which allow ruminants to digest bacteria in the foregut. The mammalian enzyme is related to lysozyme found hen egg-whites and related species.


Pssm-ID: 340383  Cd Length: 126  Bit Score: 43.02  E-value: 5.22e-06
                         10        20        30
                 ....*....|....*....|....*....|.
gi 500205258  41 AQHESGMRPNAVNRNTNGSEDIGLMQINTSW 71
Cdd:cd16897   32 AYYESGFNTRATNENPDGSTDYGIFQINSRY 62
LYZ_C_invert cd16899
C-type invertebrate lysozyme; C-type lysozyme proteins of invertebrates, including digestive ...
 40-68 6.08e-06

C-type invertebrate lysozyme; C-type lysozyme proteins of invertebrates, including digestive lysozymes 1 and 2 from Musca domestica, which aid in the use of bacteria as a food source. These lysozymes have high expression in the gut and optimal lytic activity at a lower pH. Other lysozymes in this subfamily have immunological roles. e.g. Anopheles gambiae has eight lysozymes, most of which seem to have immunological roles, those some may function as digestive enzymes in larvae. C-type lysozyme (chicken or conventional type; 1, 4-beta-N-acetylmuramidase) has bacteriolytic properties through the hydolysis of beta-1,4, glyocosidic linkages between N-acetylmuramic acid and N-acetyl-D-glucosamine residues in a peptidoglycan, as well as between N-acetyl-D-glucosamine residues in chitodextrins.


Pssm-ID: 381618 [Multi-domain]  Cd Length: 121  Bit Score: 42.60  E-value: 6.08e-06
                         10        20        30
                 ....*....|....*....|....*....|
gi 500205258  40 IAQHESGMRPNAVNR-NTNGSEDIGLMQIN 68
Cdd:cd16899   28 LAEHESSFNTTAVGGpNSDGSGDYGLFQIN 57
PRK13864 PRK13864
type IV secretion system lytic transglycosylase VirB1; Provisional
 2-117 3.18e-05

type IV secretion system lytic transglycosylase VirB1; Provisional


Pssm-ID: 237534  Cd Length: 245  Bit Score: 41.77  E-value: 3.18e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500205258   2 RIVPIVAAVLAFTALPSRADCLDDAAAFH-------GVNPQLLRVIAQHESGMRPNAVNRNTNG---------------- 58
Cdd:PRK13864   4 AAGSLSIILLASMCPSSKAAPLSFAEFNQlarecapSVAPSTLAAIAKVESRFDPLAVHDNTTGetlhwqnhaqatqsvr 83

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 500205258  59 -------SEDIGLMQINTSwlpTLARYGIRREHLFNGCVSAYVGAWILASnvRRFGPNW---------KAVGAYN 117
Cdd:PRK13864  84 hrlearhSLDVGLMQINSK---NFSVLGLTPDGALQPCTSLSAAANLLGS--RYAGGDTadekqlalrRAISAYN 153
Lys pfam00062
C-type lysozyme/alpha-lactalbumin family; Alpha-lactalbumin is the regulatory subunit of ...
 40-71 4.21e-05

C-type lysozyme/alpha-lactalbumin family; Alpha-lactalbumin is the regulatory subunit of lactose synthase, changing the substrate specificity of galactosyltransferase from N-acetylglucosamine to glucose. C-type lysozymes are secreted bacteriolytic enzymes that cleave the peptidoglycan of bacterial cell walls. Structure is a multi-domain, mixed alpha and beta fold, containing four conserved disulfide bonds.


Pssm-ID: 395016  Cd Length: 123  Bit Score: 40.48  E-value: 4.21e-05
                          10        20        30
                  ....*....|....*....|....*....|..
gi 500205258   40 IAQHESGMRPNAVNRNtNGSEDIGLMQINTSW 71
Cdd:pfam00062  31 LAFHESGYDTQAIVYN-NGSTDYGIFQINDKY 61
LT_Slt70-like cd16896
uncharacterized lytic transglycosylase subfamily with similarity to Slt70; Uncharacterized ...
 26-118 6.10e-05

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: 40.19  E-value: 6.10e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500205258  26 AAAFHGVNPQLLRVIAQHESGMRPNAVNRntNGSedIGLMQIntswLPTLARY--------GIRREHLFNGCVSAYVGAW 97
Cdd:cd16896   11 YAKEYGVDPLLVAAVIKVESNFNPNAVSS--KGA--IGLMQI----MPETAEWiaeklgleDFSEDDLYDPETNIRLGTW 82

                         90       100
                 ....*....|....*....|..
gi 500205258  98 ILASNVRRFGPNW-KAVGAYNA 118
Cdd:cd16896   83 YLSYLLKEFDGNLvLALAAYNA 104
LYZ cd00119
C-type lysozyme and alpha-lactalbumin; C-type lysozyme (chicken or conventional type, 1, ...
 23-68 2.19e-04

C-type lysozyme and alpha-lactalbumin; C-type lysozyme (chicken or conventional type, 1,4-beta-N-acetylmuramidase) and alpha-lactalbumin (lactose synthase B protein, LA). They have a close evolutionary relationship and similar tertiary structure, however, functionally they are quite different. Lysozymes have primarily bacteriolytic function; hydrolysis of peptidoglycans of prokaryotic cell walls and transglycosylation. LA is a calcium-binding metalloprotein that is expressed exclusively in the mammary gland during lactation. LA is the regulatory subunit of the enzyme lactose synthase. The association of LA with the catalytic component of lactose synthase, galactosyltransferase, alters the acceptor substrate specificity of this glycosyltransferase, facilitating biosynthesis of lactose. Some lysozymes have evolved into digestive enzymes, both in mammals and invertebrates.


Pssm-ID: 340357  Cd Length: 122  Bit Score: 38.32  E-value: 2.19e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 500205258  23 LDDAAAFHGVNPQLLRVIAQHESGMRPNAVNRNTNGSEDIGLMQIN 68
Cdd:cd00119   12 LKDIGGYGGISLPNWVCLMKHESGYDTQATNENNNGSTDYGLFQIN 57
emtA PRK15470
membrane-bound lytic murein transglycosylase EmtA;
26-70 9.98e-04

membrane-bound lytic murein transglycosylase EmtA;


Pssm-ID: 185367 [Multi-domain]  Cd Length: 203  Bit Score: 37.64  E-value: 9.98e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 500205258  26 AAAFHGVNPQLLRVIAQHESGMRPNAVNRntngSEDIGLMQINTS 70
Cdd:PRK15470  46 AGAAWGVDPQLITAIIAIESGGNPNAVSK----SNAIGLMQLKAS 86
MLTF-like cd13403
membrane-bound lytic murein transglycosylase F (MLTF) and similar proteins; This subfamily ...
 25-118 4.01e-03

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: 35.59  E-value: 4.01e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500205258  25 DAAAFHGVNPQLLRVIAQHESGMRPNAVNRntNGSedIGLMQINTSwlpTLARYGIRRehLFNGCVSAYVGAWILASNVR 104
Cdd:cd13403    3 KYAEKYGFDWRLLAAQAYQESRFNPNARSP--AGA--RGLMQLMPS---TARELGVND--RLDPEQNIHAGAKYLRYLRD 73

                         90       100
                 ....*....|....*....|.
gi 500205258 105 RFGP-------NWKAVGAYNA 118
Cdd:cd13403   74 RFPPdidepdrLKFALAAYNA 94
LT_MltC_MltE cd16893
membrane-bound lytic murein transglycosylases MltC and MltE, and similar proteins; MltC and ...
 25-67 5.49e-03

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: 35.23  E-value: 5.49e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 500205258  25 DAAAFHGVNPQLLRVIAQHESGMRPNAVNRntngSEDIGLMQI 67
Cdd:cd16893    5 KYAKKYGVDPALILAIIETESSFNPYAVSH----SPAYGLMQI 43
LT_TF-like cd13402
lytic transglycosylase-like domain of tail fiber-like proteins and similar domains; These tail ...
 34-66 5.59e-03

lytic transglycosylase-like domain of tail fiber-like proteins and similar domains; These tail fiber-like proteins are multi-domain proteins that include a lytic transglycosylase (LT) domain. Members of the LT family include the soluble and insoluble membrane-bound LTs in bacteria, the LTs in bacteriophage lambda, and the eukaryotic "goose-type" lysozymes (goose egg-white lysozyme; GEWL). 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: 381605 [Multi-domain]  Cd Length: 117  Bit Score: 34.48  E-value: 5.59e-03
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 500205258  34 PQLLRVIaQHESGMRPNAVN---RNT-NGSEDIGLMQ 66
Cdd:cd13402    2 NALLRQI-QTESGGNPNAINnwdSNAkAGHPSKGLMQ 37
SLT_3 pfam18896
Lysozyme like domain; This entry represents a lysozyme like domain found in candidate phyla ...
 40-76 8.45e-03

Lysozyme like domain; This entry represents a lysozyme like domain found in candidate phyla radiation bacteria. The domain contains several conserved cysteine and histidine residues suggesting that it may bind to zinc.


Pssm-ID: 436815 [Multi-domain]  Cd Length: 89  Bit Score: 33.53  E-value: 8.45e-03
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 500205258   40 IAQHESGMRPNAVN--RNTNGSEDIGLMQINTSWLPTLA 76
Cdd:pfam18896  20 VAMAESGGDPSAVGdlANTKGSPSRGLWQINSLAHPEVT 58
 
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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