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Conserved domains on  [gi|516017185|ref|WP_017447768|]
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LysM peptidoglycan-binding domain-containing protein [Vibrio parahaemolyticus]

Protein Classification

lytic transglycosylase( domain architecture ID 13298690)

lytic transglycosylase cleaves the glycosidic linkage between N-acetylmuramoyl and N-acetylglucosaminyl residues with the concomitant formation of a 1,6-anydromuramoyl product

CATH:  3.10.350.10
Gene Ontology:  GO:0097367
PubMed:  24652063|18430080
SCOP:  4000905

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
mltD super family cl32574
membrane-bound lytic murein transglycosylase D; Provisional
 11-468 1.41e-127

membrane-bound lytic murein transglycosylase D; Provisional


The actual alignment was detected with superfamily member PRK10783:

Pssm-ID: 182727 [Multi-domain]  Cd Length: 456  Bit Score: 380.23  E-value: 1.41e-127
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516017185  11 LLLSGCQltqpnssttptpeTNKSEQTAKQNATKTKSKNKQSLAK--DSAKDTPKVLSPQEQEDVWQRIAMQLEMDIPNN 88
Cdd:PRK10783  11 VLLVGCQ-------------SSKNDATVQQHAQSLSSAGQGEAGKytSQARWMDDGTSIAPDQDLWAFIGDELKMGIPEN 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516017185  89 KKVDYYRTWYLKHPNHLYTVSKRAAPFLYMITQRIEERGLPMELALLPVVESSFDAFAYSHGSAAGLWQFVPGTGKMMGL 168
Cdd:PRK10783  78 SRIREQKQKYLRNKSYLHDVTLRAEPYMYWIVGQIKKRNMPMELVLLPIVESAFDPHATSGANAAGIWQIIPSTGRNYGL 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516017185 169 EQNYWYDGRRDVAASTDAALDYLVQLNERFDGNWEHAIAAYNSGGGRVSSAIRKNKKLGKPVDFFSLDLPKETSSYVPKL 248
Cdd:PRK10783 158 KQTRWYDARRDVVASTTAALDMMQRLNKMFDGDWLLTVAAYNSGEGRVMKAIKANKAKGKPTDFWSLSLPRETKIYVPKM 237

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516017185 249 LALADVVANQEKYGIDIPSIPNKPVLTLVDPKEQLDLAIAADYAGIGVKELQSYNPAYNQWSTAPEGPHQLLIPVEK--- 325
Cdd:PRK10783 238 LALSDILKNSKRYGVRLPTTDESRALARVDLGQQIELAQAAEMAGMSLTKLKTFNAGYKRSTTAPSGPHYIMVPKKHadq 317

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516017185 326 -KDAFL---------TQVESNRGKgmKVARYKVKSGDSLSMLAKKYGTTSKVIRRANGLSNNNIRIGQYLLIPTSTKdds 395
Cdd:PRK10783 318 lRESLAsgeiaavqsTLVADNTPL--NSRSYKVRSGDTLSGIASRLNVSTKDLQQWNNLRGSKLKVGQTLTIGAGSS--- 392

                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 516017185 396 kyaltAQNRLNKTQSqargqlkLSHVVQSGESLWSIARDNKVSHKSLAKWNGmGPKDPLRVGQKLVIWKKSDQ 468
Cdd:PRK10783 393 -----AQRLANNSDS-------ITYRVRKGDSLSSIAKRHGVNIKDVMRWNS-DTAKNLQPGDKLTLFVKNNS 452
LysM cd00118
Lysin Motif is a small domain involved in binding peptidoglycan; LysM, a small globular domain ...
 475-519 2.17e-10

Lysin Motif is a small domain involved in binding peptidoglycan; LysM, a small globular domain with approximately 40 amino acids, is a widespread protein module involved in binding peptidoglycan in bacteria and chitin in eukaryotes. The domain was originally identified in enzymes that degrade bacterial cell walls, but proteins involved in many other biological functions also contain this domain. It has been reported that the LysM domain functions as a signal for specific plant-bacteria recognition in bacterial pathogenesis. Many of these enzymes are modular and are composed of catalytic units linked to one or several repeats of LysM domains. LysM domains are found in bacteria and eukaryotes.


:

Pssm-ID: 212030 [Multi-domain]  Cd Length: 45  Bit Score: 55.95  E-value: 2.17e-10
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 516017185 475 VFYNVRSGDTISGIASKFKVKSNDIVKWNSLHKQKYLKPGQKLKL 519
Cdd:cd00118    1 KTYTVKPGDTLWSIAKKYGVTVEELAAANPLINPDCIYPGQKLKI 45
 
Name Accession Description Interval E-value
mltD PRK10783
membrane-bound lytic murein transglycosylase D; Provisional
 11-468 1.41e-127

membrane-bound lytic murein transglycosylase D; Provisional


Pssm-ID: 182727 [Multi-domain]  Cd Length: 456  Bit Score: 380.23  E-value: 1.41e-127
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516017185  11 LLLSGCQltqpnssttptpeTNKSEQTAKQNATKTKSKNKQSLAK--DSAKDTPKVLSPQEQEDVWQRIAMQLEMDIPNN 88
Cdd:PRK10783  11 VLLVGCQ-------------SSKNDATVQQHAQSLSSAGQGEAGKytSQARWMDDGTSIAPDQDLWAFIGDELKMGIPEN 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516017185  89 KKVDYYRTWYLKHPNHLYTVSKRAAPFLYMITQRIEERGLPMELALLPVVESSFDAFAYSHGSAAGLWQFVPGTGKMMGL 168
Cdd:PRK10783  78 SRIREQKQKYLRNKSYLHDVTLRAEPYMYWIVGQIKKRNMPMELVLLPIVESAFDPHATSGANAAGIWQIIPSTGRNYGL 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516017185 169 EQNYWYDGRRDVAASTDAALDYLVQLNERFDGNWEHAIAAYNSGGGRVSSAIRKNKKLGKPVDFFSLDLPKETSSYVPKL 248
Cdd:PRK10783 158 KQTRWYDARRDVVASTTAALDMMQRLNKMFDGDWLLTVAAYNSGEGRVMKAIKANKAKGKPTDFWSLSLPRETKIYVPKM 237

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516017185 249 LALADVVANQEKYGIDIPSIPNKPVLTLVDPKEQLDLAIAADYAGIGVKELQSYNPAYNQWSTAPEGPHQLLIPVEK--- 325
Cdd:PRK10783 238 LALSDILKNSKRYGVRLPTTDESRALARVDLGQQIELAQAAEMAGMSLTKLKTFNAGYKRSTTAPSGPHYIMVPKKHadq 317

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516017185 326 -KDAFL---------TQVESNRGKgmKVARYKVKSGDSLSMLAKKYGTTSKVIRRANGLSNNNIRIGQYLLIPTSTKdds 395
Cdd:PRK10783 318 lRESLAsgeiaavqsTLVADNTPL--NSRSYKVRSGDTLSGIASRLNVSTKDLQQWNNLRGSKLKVGQTLTIGAGSS--- 392

                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 516017185 396 kyaltAQNRLNKTQSqargqlkLSHVVQSGESLWSIARDNKVSHKSLAKWNGmGPKDPLRVGQKLVIWKKSDQ 468
Cdd:PRK10783 393 -----AQRLANNSDS-------ITYRVRKGDSLSSIAKRHGVNIKDVMRWNS-DTAKNLQPGDKLTLFVKNNS 452
MltD-like cd16894
Membrane-bound lytic murein transglycosylase D and similar proteins; Lytic transglycosylases ...
 123-253 1.09e-58

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: 190.42  E-value: 1.09e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516017185 123 IEERGLPMELALLPVVESSFDAFAYSHGSAAGLWQFVPGTGKMMGLEQNYWYDGRRDVAASTDAALDYLVQLNERFdGNW 202
Cdd:cd16894    1 LLKEGLPEELKYLALVESGFNPDAVSSAGAAGLWQFMPATAREYGLRVDSWVDERRDPEKSTRAAARYLKDLYKRF-GDW 79

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 516017185 203 EHAIAAYNSGGGRVSSAIRKNkKLGKPVDFFSLDLPKETSSYVPKLLALAD 253
Cdd:cd16894   80 LLALAAYNAGEGRVRRAIKRA-GTDKWEDYYRLYLPAETRRYVPKFLAAKI 129
MltE COG0741
Soluble lytic murein transglycosylase or regulatory protein s ( may contain LysM/invasin ...
 109-254 3.66e-39

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: 142.83  E-value: 3.66e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516017185 109 SKRAAPFLYMITQRIEERGLPMELAL-LPVVESSFDAFAYSHGSAAGLWQFVPGTGKMMGLEQN--YWYDGRRDVAASTD 185
Cdd:COG0741   97 LRRPLPYLPLIEEAAKKYGVDPALVLaLIRQESAFNPNAVSPAGARGLMQLMPATARRLGLKLGlgPSPDDLFDPETNIR 176

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516017185 186 AALDYLVQLNERFDGNWEHAIAAYNSGGGRVSSAIRKNKKLGKPVdffsldLP-KETSSYVPKLLALADV 254
Cdd:COG0741  177 AGAAYLRELLDRFDGDLVLALAAYNAGPGRVRRWLRRNGDRDGEI------IPyAETRNYVKKVLANYAI 240
SLT pfam01464
Transglycosylase SLT domain; This family is distantly related to pfam00062. Members are found ...
 129-228 2.95e-26

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: 103.16  E-value: 2.95e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516017185  129 PMELALLPVVESSFDAFAYSHGSAAGLWQFVPGTGKMMGLEQNYWYDGRRDVAASTDAALDYLVQLNERFDGNWEHAIAA 208
Cdd:pfam01464  12 PSLLLAIAQQESGFNPKAVSKSGAVGLMQIMPSTAKRLGLRVNPGVDDLFDPEKNIKAGTKYLKELYKQYGGDLWLALAA 91

                          90       100
                  ....*....|....*....|
gi 516017185  209 YNSGGGRVSSAIRKNKKLGK 228
Cdd:pfam01464  92 YNAGPGRVRKWIKNAGAKDK 111
LysM cd00118
Lysin Motif is a small domain involved in binding peptidoglycan; LysM, a small globular domain ...
 475-519 2.17e-10

Lysin Motif is a small domain involved in binding peptidoglycan; LysM, a small globular domain with approximately 40 amino acids, is a widespread protein module involved in binding peptidoglycan in bacteria and chitin in eukaryotes. The domain was originally identified in enzymes that degrade bacterial cell walls, but proteins involved in many other biological functions also contain this domain. It has been reported that the LysM domain functions as a signal for specific plant-bacteria recognition in bacterial pathogenesis. Many of these enzymes are modular and are composed of catalytic units linked to one or several repeats of LysM domains. LysM domains are found in bacteria and eukaryotes.


Pssm-ID: 212030 [Multi-domain]  Cd Length: 45  Bit Score: 55.95  E-value: 2.17e-10
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 516017185 475 VFYNVRSGDTISGIASKFKVKSNDIVKWNSLHKQKYLKPGQKLKL 519
Cdd:cd00118    1 KTYTVKPGDTLWSIAKKYGVTVEELAAANPLINPDCIYPGQKLKI 45
LysM smart00257
Lysin motif;
346-387 1.15e-09

Lysin motif;


Pssm-ID: 197609 [Multi-domain]  Cd Length: 44  Bit Score: 53.60  E-value: 1.15e-09
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 516017185   346 YKVKSGDSLSMLAKKYGTTSKVIRRANGLSN-NNIRIGQYLLI 387
Cdd:smart00257   2 YTVKKGDTLSSIARRYGISVSDLLELNNILDpDNLQVGQKLKI 44
LysM smart00257
Lysin motif;
476-519 2.59e-08

Lysin motif;


Pssm-ID: 197609 [Multi-domain]  Cd Length: 44  Bit Score: 49.75  E-value: 2.59e-08
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 516017185   476 FYNVRSGDTISGIASKFKVKSNDIVKWNSLHKQKYLKPGQKLKL 519
Cdd:smart00257   1 TYTVKKGDTLSSIARRYGISVSDLLELNNILDPDNLQVGQKLKI 44
LysM pfam01476
LysM domain; The LysM (lysin motif) domain is about 40 residues long. It is found in a variety ...
 477-519 3.04e-08

LysM domain; The LysM (lysin motif) domain is about 40 residues long. It is found in a variety of enzymes involved in bacterial cell wall degradation. This domain may have a general peptidoglycan binding function. The structure of this domain is known.


Pssm-ID: 396179 [Multi-domain]  Cd Length: 43  Bit Score: 49.70  E-value: 3.04e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 516017185  477 YNVRSGDTISGIASKFKVKSNDIVKWNSLhKQKYLKPGQKLKL 519
Cdd:pfam01476   1 YTVKKGDTLSSIAKRYGITVEQLAELNGL-SSPNLYVGQKLKI 42
 
Name Accession Description Interval E-value
mltD PRK10783
membrane-bound lytic murein transglycosylase D; Provisional
 11-468 1.41e-127

membrane-bound lytic murein transglycosylase D; Provisional


Pssm-ID: 182727 [Multi-domain]  Cd Length: 456  Bit Score: 380.23  E-value: 1.41e-127
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516017185  11 LLLSGCQltqpnssttptpeTNKSEQTAKQNATKTKSKNKQSLAK--DSAKDTPKVLSPQEQEDVWQRIAMQLEMDIPNN 88
Cdd:PRK10783  11 VLLVGCQ-------------SSKNDATVQQHAQSLSSAGQGEAGKytSQARWMDDGTSIAPDQDLWAFIGDELKMGIPEN 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516017185  89 KKVDYYRTWYLKHPNHLYTVSKRAAPFLYMITQRIEERGLPMELALLPVVESSFDAFAYSHGSAAGLWQFVPGTGKMMGL 168
Cdd:PRK10783  78 SRIREQKQKYLRNKSYLHDVTLRAEPYMYWIVGQIKKRNMPMELVLLPIVESAFDPHATSGANAAGIWQIIPSTGRNYGL 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516017185 169 EQNYWYDGRRDVAASTDAALDYLVQLNERFDGNWEHAIAAYNSGGGRVSSAIRKNKKLGKPVDFFSLDLPKETSSYVPKL 248
Cdd:PRK10783 158 KQTRWYDARRDVVASTTAALDMMQRLNKMFDGDWLLTVAAYNSGEGRVMKAIKANKAKGKPTDFWSLSLPRETKIYVPKM 237

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516017185 249 LALADVVANQEKYGIDIPSIPNKPVLTLVDPKEQLDLAIAADYAGIGVKELQSYNPAYNQWSTAPEGPHQLLIPVEK--- 325
Cdd:PRK10783 238 LALSDILKNSKRYGVRLPTTDESRALARVDLGQQIELAQAAEMAGMSLTKLKTFNAGYKRSTTAPSGPHYIMVPKKHadq 317

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516017185 326 -KDAFL---------TQVESNRGKgmKVARYKVKSGDSLSMLAKKYGTTSKVIRRANGLSNNNIRIGQYLLIPTSTKdds 395
Cdd:PRK10783 318 lRESLAsgeiaavqsTLVADNTPL--NSRSYKVRSGDTLSGIASRLNVSTKDLQQWNNLRGSKLKVGQTLTIGAGSS--- 392

                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 516017185 396 kyaltAQNRLNKTQSqargqlkLSHVVQSGESLWSIARDNKVSHKSLAKWNGmGPKDPLRVGQKLVIWKKSDQ 468
Cdd:PRK10783 393 -----AQRLANNSDS-------ITYRVRKGDSLSSIAKRHGVNIKDVMRWNS-DTAKNLQPGDKLTLFVKNNS 452
MltD-like cd16894
Membrane-bound lytic murein transglycosylase D and similar proteins; Lytic transglycosylases ...
 123-253 1.09e-58

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: 190.42  E-value: 1.09e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516017185 123 IEERGLPMELALLPVVESSFDAFAYSHGSAAGLWQFVPGTGKMMGLEQNYWYDGRRDVAASTDAALDYLVQLNERFdGNW 202
Cdd:cd16894    1 LLKEGLPEELKYLALVESGFNPDAVSSAGAAGLWQFMPATAREYGLRVDSWVDERRDPEKSTRAAARYLKDLYKRF-GDW 79

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 516017185 203 EHAIAAYNSGGGRVSSAIRKNkKLGKPVDFFSLDLPKETSSYVPKLLALAD 253
Cdd:cd16894   80 LLALAAYNAGEGRVRRAIKRA-GTDKWEDYYRLYLPAETRRYVPKFLAAKI 129
MltE COG0741
Soluble lytic murein transglycosylase or regulatory protein s ( may contain LysM/invasin ...
 109-254 3.66e-39

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: 142.83  E-value: 3.66e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516017185 109 SKRAAPFLYMITQRIEERGLPMELAL-LPVVESSFDAFAYSHGSAAGLWQFVPGTGKMMGLEQN--YWYDGRRDVAASTD 185
Cdd:COG0741   97 LRRPLPYLPLIEEAAKKYGVDPALVLaLIRQESAFNPNAVSPAGARGLMQLMPATARRLGLKLGlgPSPDDLFDPETNIR 176

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516017185 186 AALDYLVQLNERFDGNWEHAIAAYNSGGGRVSSAIRKNKKLGKPVdffsldLP-KETSSYVPKLLALADV 254
Cdd:COG0741  177 AGAAYLRELLDRFDGDLVLALAAYNAGPGRVRRWLRRNGDRDGEI------IPyAETRNYVKKVLANYAI 240
MltF COG4623
Membrane-bound lytic murein transglycosylase MltF [Cell wall/membrane/envelope biogenesis, ...
 92-254 1.43e-32

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


Pssm-ID: 443662 [Multi-domain]  Cd Length: 421  Bit Score: 129.03  E-value: 1.43e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516017185  92 DYYRTWYLKHPNHLYTVSKRAAPFLYMITQRIEERGLPME-LALLPVVESSFDAFAYSHGSAAGLWQFVPGTGKMMGLeq 170
Cdd:COG4623  241 RYFGHVKRDTRAFLRRIEGRLPPYDPLFEKYAEEYGLDWRlLAALAYQESHWNPRARSPTGARGLMQLMPATAKELGV-- 318

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516017185 171 nywyDGRRDVAASTDAALDYLVQLNERFD------GNWEHAIAAYNSGGGRVSSAIRKNKKLGKPVDFFS---------L 235
Cdd:COG4623  319 ----DDRLDPEQSIRAGAKYLRWLYDRFPeaidepDRWWFALAAYNAGPGHVQDARRLAKKQGLDPDRWFdveksqpkyY 394

                        170       180
                 ....*....|....*....|...
gi 516017185 236 DL----PKETSSYVPKLLALADV 254
Cdd:COG4623  395 DTgyarGRETVNYVPNIRAYYDI 417
SLT pfam01464
Transglycosylase SLT domain; This family is distantly related to pfam00062. Members are found ...
 129-228 2.95e-26

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: 103.16  E-value: 2.95e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516017185  129 PMELALLPVVESSFDAFAYSHGSAAGLWQFVPGTGKMMGLEQNYWYDGRRDVAASTDAALDYLVQLNERFDGNWEHAIAA 208
Cdd:pfam01464  12 PSLLLAIAQQESGFNPKAVSKSGAVGLMQIMPSTAKRLGLRVNPGVDDLFDPEKNIKAGTKYLKELYKQYGGDLWLALAA 91

                          90       100
                  ....*....|....*....|
gi 516017185  209 YNSGGGRVSSAIRKNKKLGK 228
Cdd:pfam01464  92 YNAGPGRVRKWIKNAGAKDK 111
LT-like cd00254
lytic transglycosylase(LT)-like domain; Members include the soluble and insoluble ...
 138-250 2.89e-20

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: 86.11  E-value: 2.89e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516017185 138 VESSFDAFAYSHGSAAGLWQFVPGTGKMMGLEQNywyDGRRDVAASTDAALDYLVQLNERFDGNWEHAIAAYNSGGGRVs 217
Cdd:cd00254   10 VESGFNPRAVSPAGARGLMQLMPGTARDLGRRGV---DDLFDPEENIRAGARYLRELLDRFGGDLELALAAYNAGPGAV- 85

                         90       100       110
                 ....*....|....*....|....*....|...
gi 516017185 218 saiRKNKKLGKPvdffsldLPKETSSYVPKLLA 250
Cdd:cd00254   86 ---DRWGGGEVP-------PYKETRNYVQRVLA 108
Slt70-like cd13401
70kDa soluble lytic transglycosylase (Slt70) and similar proteins; Catalytic domain of the ...
 114-250 1.37e-17

70kDa soluble lytic transglycosylase (Slt70) and similar proteins; Catalytic domain of the 70kda soluble lytic transglycosylase (LT)-like proteins, which also have an N-terminal U-shaped U-domain and a linker L-domain. LTs catalyze the cleavage of the beta-1,4-glycosidic bond between N-acetylmuramic acid (MurNAc) and N-acetyl-D-glucosamine (GlcNAc), as do "goose-type" lysozymes. However, in addition to this, they also make a new glycosidic bond with the C6 hydroxyl group of the same muramic acid residue. Proteins similar to this family include the soluble and insoluble membrane-bound LTs in bacteria and the LTs in bacteriophage lambda.


Pssm-ID: 381604 [Multi-domain]  Cd Length: 152  Bit Score: 79.83  E-value: 1.37e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516017185 114 PFLYMITQRIEERGLPMELaLLPVV--ESSFDAFAYSHGSAAGLWQFVPGTGKMMGLEQNYWYDGRRDVaasTDAAL--- 188
Cdd:cd13401    5 PYRDLVERAAKKNGLDPAL-VYAIIrqESAFDPDAVSPAGALGLMQLMPATAKDVAKKLGLPYYSPRDL---FDPEYnir 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 516017185 189 ---DYLVQLNERFDGNWEHAIAAYNSGGGRVSSAIRKNKKLgkPVDFFSLDLP-KETSSYVPKLLA 250
Cdd:cd13401   81 lgsAYLAELLDRFDGNPVLALAAYNAGPGRVRRWLKRRGDL--DPDLWIETIPfSETRNYVKRVLE 144
LysM COG1388
LysM repeat [Cell wall/membrane/envelope biogenesis];
262-390 1.78e-16

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


Pssm-ID: 440998 [Multi-domain]  Cd Length: 156  Bit Score: 76.67  E-value: 1.78e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516017185 262 GIDIPSIPNKPVLTLVDPKEQLDLAIAADYAGIGVKELQSYNPAYNQWSTAPEGPHQLLIPVEKKDAFLTQVES------ 335
Cdd:COG1388    1 GLLLALSANAALLAAVLTLLAALLLLAAALAAVALLLLAALAPAGLSLAAALNGEALLLLLPAAAAAAKAALAAapeaaa 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 516017185 336 ---------------------NRGKGMKVARYKVKSGDSLSMLAKKYGTTSKVIRRANGLSNNNIRIGQYLLIPTS 390
Cdd:COG1388   81 aaaarytvksgdtlsgiarryGAAAAPSPVTYTVKKGDTLWSIARRYGVSVEELKRWNGLSSDTIRPGQKLKIPAS 156
PRK06347 PRK06347
1,4-beta-N-acetylmuramoylhydrolase;
335-519 9.86e-16

1,4-beta-N-acetylmuramoylhydrolase;


Pssm-ID: 180536 [Multi-domain]  Cd Length: 592  Bit Score: 80.12  E-value: 9.86e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516017185 335 SNRGKGMKVARYKVKSGDSLSMLAKKYGTTSKVIRRANGLSNNNIRIGQYLLIP--TSTKDDSKYALTAQNRLNKTQSQA 412
Cdd:PRK06347 322 SNTGNTSNAKIYTVVKGDSLWRIANNHKVTVANLKAWNNLKSDFIYPGQKLKVSagSTTSDTNTSKPSTGTSTSKPSTGT 401

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516017185 413 RGQLKLSHVVQsGESLWSIARDNKVSHKSLAKWNGMgPKDPLRVGQKLVI------------------WKKSDQGAVIRT 474
Cdd:PRK06347 402 STNAKVYTVVK-GDSLWRIANNNKVTIANLKSWNNL-KSDFIYPGQKLKVsagstsntntskpstntnTSKPSTNTNTNA 479

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 516017185 475 VFYNVRSGDTISGIASKFKVKSNDIVKWNSLhKQKYLKPGQKLKL 519
Cdd:PRK06347 480 KVYTVAKGDSLWRIANNNKVTIANLKSWNNL-KSDFIYPGQKLKV 523
LysM pfam01476
LysM domain; The LysM (lysin motif) domain is about 40 residues long. It is found in a variety ...
 346-388 7.63e-14

LysM domain; The LysM (lysin motif) domain is about 40 residues long. It is found in a variety of enzymes involved in bacterial cell wall degradation. This domain may have a general peptidoglycan binding function. The structure of this domain is known.


Pssm-ID: 396179 [Multi-domain]  Cd Length: 43  Bit Score: 65.50  E-value: 7.63e-14
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 516017185  346 YKVKSGDSLSMLAKKYGTTSKVIRRANGLSNNNIRIGQYLLIP 388
Cdd:pfam01476   1 YTVKKGDTLSSIAKRYGITVEQLAELNGLSSPNLYVGQKLKIP 43
LT_Slt70-like cd16896
uncharacterized lytic transglycosylase subfamily with similarity to Slt70; Uncharacterized ...
 138-249 1.33e-13

uncharacterized lytic transglycosylase subfamily with similarity to Slt70; Uncharacterized lytic transglycosylase (LT) with a conserved sequence pattern suggesting similarity to the Slt70, a 70kda soluble lytic transglycosylase which also has an N-terminal U-shaped U-domain and a linker L-domain. LTs catalyze the cleavage of the beta-1,4-glycosidic bond between N-acetylmuramic acid (MurNAc) and N-acetyl-D-glucosamine (GlcNAc), as do "goose-type" lysozymes. However, in addition to this, they also make a new glycosidic bond with the C6 hydroxyl group of the same muramic acid residue.


Pssm-ID: 381617 [Multi-domain]  Cd Length: 146  Bit Score: 68.31  E-value: 1.33e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516017185 138 VESSFDAFAYSHGSAAGLWQFVPGTG----KMMGLEqNYWYDGRRDVAASTDAALDYLVQLNERFDGNWEHAIAAYNSGG 213
Cdd:cd16896   28 VESNFNPNAVSSKGAIGLMQIMPETAewiaEKLGLE-DFSEDDLYDPETNIRLGTWYLSYLLKEFDGNLVLALAAYNAGP 106

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 516017185 214 GRVSSAIRKNKKLGKPVDffSLDLP-KETSSYVPKLL 249
Cdd:cd16896  107 GNVDKWLKDGGWSGDGKT--LDQIPfPETRHYVKKVL 141
PRK06347 PRK06347
1,4-beta-N-acetylmuramoylhydrolase;
346-519 1.97e-13

1,4-beta-N-acetylmuramoylhydrolase;


Pssm-ID: 180536 [Multi-domain]  Cd Length: 592  Bit Score: 72.81  E-value: 1.97e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516017185 346 YKVKSGDSLSMLAKKYGTTSKVIRRANGLSNNNIRIGQYLLIPTSTKDDSKYALTAQN-RLNKTQSQARGQLKLsHVVQS 424
Cdd:PRK06347 408 YTVVKGDSLWRIANNNKVTIANLKSWNNLKSDFIYPGQKLKVSAGSTSNTNTSKPSTNtNTSKPSTNTNTNAKV-YTVAK 486

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516017185 425 GESLWSIARDNKVSHKSLAKWNGMgPKDPLRVGQKLVIWKKSD--------------QGAVIRTvfYNVRSGDTISGIAS 490
Cdd:PRK06347 487 GDSLWRIANNNKVTIANLKSWNNL-KSDFIYPGQKLKVSAGSTtnntntakpstnkpSNSTVKT--YTVKKGDSLWAISR 563

                        170       180
                 ....*....|....*....|....*....
gi 516017185 491 KFKVKSNDIVKWNSLhKQKYLKPGQKLKL 519
Cdd:PRK06347 564 QYKTTVDNIKAWNKL-TSNMIHVGQKLTI 591
LysM cd00118
Lysin Motif is a small domain involved in binding peptidoglycan; LysM, a small globular domain ...
 419-462 5.73e-12

Lysin Motif is a small domain involved in binding peptidoglycan; LysM, a small globular domain with approximately 40 amino acids, is a widespread protein module involved in binding peptidoglycan in bacteria and chitin in eukaryotes. The domain was originally identified in enzymes that degrade bacterial cell walls, but proteins involved in many other biological functions also contain this domain. It has been reported that the LysM domain functions as a signal for specific plant-bacteria recognition in bacterial pathogenesis. Many of these enzymes are modular and are composed of catalytic units linked to one or several repeats of LysM domains. LysM domains are found in bacteria and eukaryotes.


Pssm-ID: 212030 [Multi-domain]  Cd Length: 45  Bit Score: 60.19  E-value: 5.73e-12
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 516017185 419 SHVVQSGESLWSIARDNKVSHKSLAKWNGMGPKDPLRVGQKLVI 462
Cdd:cd00118    2 TYTVKPGDTLWSIAKKYGVTVEELAAANPLINPDCIYPGQKLKI 45
MLTF-like cd13403
membrane-bound lytic murein transglycosylase F (MLTF) and similar proteins; This subfamily ...
 139-228 6.21e-11

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: 61.01  E-value: 6.21e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516017185 139 ESSFDAFAYSHGSAAGLWQFVPGTGKMMGLEQnywydgRRDVAASTDAALDYLVQLNERFDGN------WEHAIAAYNSG 212
Cdd:cd13403   22 ESRFNPNARSPAGARGLMQLMPSTARELGVND------RLDPEQNIHAGAKYLRYLRDRFPPDidepdrLKFALAAYNAG 95

                         90
                 ....*....|....*.
gi 516017185 213 GGRVSSAIRKNKKLGK 228
Cdd:cd13403   96 PGHVRDARRLAKKYGL 111
LysM cd00118
Lysin Motif is a small domain involved in binding peptidoglycan; LysM, a small globular domain ...
 346-387 6.79e-11

Lysin Motif is a small domain involved in binding peptidoglycan; LysM, a small globular domain with approximately 40 amino acids, is a widespread protein module involved in binding peptidoglycan in bacteria and chitin in eukaryotes. The domain was originally identified in enzymes that degrade bacterial cell walls, but proteins involved in many other biological functions also contain this domain. It has been reported that the LysM domain functions as a signal for specific plant-bacteria recognition in bacterial pathogenesis. Many of these enzymes are modular and are composed of catalytic units linked to one or several repeats of LysM domains. LysM domains are found in bacteria and eukaryotes.


Pssm-ID: 212030 [Multi-domain]  Cd Length: 45  Bit Score: 57.11  E-value: 6.79e-11
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 516017185 346 YKVKSGDSLSMLAKKYGTTSKVIRRANGLSNNN-IRIGQYLLI 387
Cdd:cd00118    3 YTVKPGDTLWSIAKKYGVTVEELAAANPLINPDcIYPGQKLKI 45
LysM cd00118
Lysin Motif is a small domain involved in binding peptidoglycan; LysM, a small globular domain ...
 475-519 2.17e-10

Lysin Motif is a small domain involved in binding peptidoglycan; LysM, a small globular domain with approximately 40 amino acids, is a widespread protein module involved in binding peptidoglycan in bacteria and chitin in eukaryotes. The domain was originally identified in enzymes that degrade bacterial cell walls, but proteins involved in many other biological functions also contain this domain. It has been reported that the LysM domain functions as a signal for specific plant-bacteria recognition in bacterial pathogenesis. Many of these enzymes are modular and are composed of catalytic units linked to one or several repeats of LysM domains. LysM domains are found in bacteria and eukaryotes.


Pssm-ID: 212030 [Multi-domain]  Cd Length: 45  Bit Score: 55.95  E-value: 2.17e-10
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 516017185 475 VFYNVRSGDTISGIASKFKVKSNDIVKWNSLHKQKYLKPGQKLKL 519
Cdd:cd00118    1 KTYTVKPGDTLWSIAKKYGVTVEELAAANPLINPDCIYPGQKLKI 45
LysM COG1388
LysM repeat [Cell wall/membrane/envelope biogenesis];
343-521 2.79e-10

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


Pssm-ID: 440998 [Multi-domain]  Cd Length: 156  Bit Score: 58.95  E-value: 2.79e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516017185 343 VARYKVKSGDSLSMLAKKYGTTSKVIRRANGLSNNNIRIGQYLLIPTSTKDDSKYALTAQNRLNKTQSQARGQlKLSHVV 422
Cdd:COG1388   10 AALLAAVLTLLAALLLLAAALAAVALLLLAALAPAGLSLAAALNGEALLLLLPAAAAAAKAALAAAPEAAAAA-AARYTV 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516017185 423 QSGESLWSIARdnkvshkslakwngmgpkdplrvgqklviwkKSDQGAVIRTVFYNVRSGDTISGIASKFKVKSNDIVKW 502
Cdd:COG1388   89 KSGDTLSGIAR-------------------------------RYGAAAAPSPVTYTVKKGDTLWSIARRYGVSVEELKRW 137

                        170
                 ....*....|....*....
gi 516017185 503 NSLhKQKYLKPGQKLKLYV 521
Cdd:COG1388  138 NGL-SSDTIRPGQKLKIPA 155
LysM pfam01476
LysM domain; The LysM (lysin motif) domain is about 40 residues long. It is found in a variety ...
 420-463 6.55e-10

LysM domain; The LysM (lysin motif) domain is about 40 residues long. It is found in a variety of enzymes involved in bacterial cell wall degradation. This domain may have a general peptidoglycan binding function. The structure of this domain is known.


Pssm-ID: 396179 [Multi-domain]  Cd Length: 43  Bit Score: 54.32  E-value: 6.55e-10
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 516017185  420 HVVQSGESLWSIARDNKVSHKSLAKWNGMGPKDpLRVGQKLVIW 463
Cdd:pfam01476   1 YTVKKGDTLSSIAKRYGITVEQLAELNGLSSPN-LYVGQKLKIP 43
LysM smart00257
Lysin motif;
346-387 1.15e-09

Lysin motif;


Pssm-ID: 197609 [Multi-domain]  Cd Length: 44  Bit Score: 53.60  E-value: 1.15e-09
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 516017185   346 YKVKSGDSLSMLAKKYGTTSKVIRRANGLSN-NNIRIGQYLLI 387
Cdd:smart00257   2 YTVKKGDTLSSIARRYGISVSDLLELNNILDpDNLQVGQKLKI 44
LysM smart00257
Lysin motif;
420-462 3.41e-09

Lysin motif;


Pssm-ID: 197609 [Multi-domain]  Cd Length: 44  Bit Score: 52.45  E-value: 3.41e-09
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 516017185   420 HVVQSGESLWSIARDNKVSHKSLAKWNGMGPKDPLRVGQKLVI 462
Cdd:smart00257   2 YTVKKGDTLSSIARRYGISVSDLLELNNILDPDNLQVGQKLKI 44
LysM smart00257
Lysin motif;
476-519 2.59e-08

Lysin motif;


Pssm-ID: 197609 [Multi-domain]  Cd Length: 44  Bit Score: 49.75  E-value: 2.59e-08
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 516017185   476 FYNVRSGDTISGIASKFKVKSNDIVKWNSLHKQKYLKPGQKLKL 519
Cdd:smart00257   1 TYTVKKGDTLSSIARRYGISVSDLLELNNILDPDNLQVGQKLKI 44
LysM pfam01476
LysM domain; The LysM (lysin motif) domain is about 40 residues long. It is found in a variety ...
 477-519 3.04e-08

LysM domain; The LysM (lysin motif) domain is about 40 residues long. It is found in a variety of enzymes involved in bacterial cell wall degradation. This domain may have a general peptidoglycan binding function. The structure of this domain is known.


Pssm-ID: 396179 [Multi-domain]  Cd Length: 43  Bit Score: 49.70  E-value: 3.04e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 516017185  477 YNVRSGDTISGIASKFKVKSNDIVKWNSLhKQKYLKPGQKLKL 519
Cdd:pfam01476   1 YTVKKGDTLSSIAKRYGITVEQLAELNGL-SSPNLYVGQKLKI 42
mltC PRK11671
membrane-bound lytic murein transglycosylase MltC;
102-216 1.10e-07

membrane-bound lytic murein transglycosylase MltC;


Pssm-ID: 183271 [Multi-domain]  Cd Length: 359  Bit Score: 53.90  E-value: 1.10e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516017185 102 PNHLytvSKRAAPFLYMITQRIEERGLPMELAL-LPVVESSFDAFAYSHGSAAGLWQFVPGTG-----KMMGL----EQN 171
Cdd:PRK11671 182 PNHL---DKRAHKYLPMVRKASRKYGVDESLILaIMQTESSFNPYAVSRSDALGLMQVVQHTAgkdvfRMKGKsgqpSRS 258

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 516017185 172 YWYDGRRDVaastDAALDYLVQLNERFDGNWEHA-------IAAYNSGGGRV 216
Cdd:PRK11671 259 YLFDPANNI----DTGTAYLAILQNVYLGGITNPtsrryavITAYNGGAGSV 306
LT_MltC_MltE cd16893
membrane-bound lytic murein transglycosylases MltC and MltE, and similar proteins; MltC and ...
 138-225 1.38e-06

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: 48.32  E-value: 1.38e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516017185 138 VESSFDAFAYSHGSAAGLWQFVPGTGkmmGLEQNYWYDGrRDVAASTDAALD----------YLVQLNERFDGNWEH--- 204
Cdd:cd16893   23 TESSFNPYAVSHSPAYGLMQIVPSTA---GRDVYRLLGG-KGGLPSKSYLFDpennidigtaYLHILQNRYLKGIKNpks 98

                         90       100
                 ....*....|....*....|....*
gi 516017185 205 ----AIAAYNSGGGRVSSAIRKNKK 225
Cdd:cd16893   99 reycAIAAYNGGAGNVLRTFSSDRK 123
Slt35-like cd13399
Slt35-like lytic transglycosylase; Lytic transglycosylase similar to Escherichia coli lytic ...
 138-212 2.24e-06

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: 46.53  E-value: 2.24e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516017185 138 VESSFDAFAY-SHGSAAGLWQFVPGTGKMMGLEQNywYDGRRDVAASTDA---ALDYLVQ----LNERFDGNWEHAIAAY 209
Cdd:cd13399   14 VESGFGPNAGgSPAGAQGIAQFMPSTWKAYGVDGN--GDGKADPFNPEDAiasAANYLCRhgwdLNAFLGEDNFLALAAY 91


                 ...
gi 516017185 210 NSG 212
Cdd:cd13399   92 NAG 94
PHA00368 PHA00368
internal virion protein D
 138-252 2.19e-05

internal virion protein D


Pssm-ID: 222785 [Multi-domain]  Cd Length: 1315  Bit Score: 47.47  E-value: 2.19e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516017185  138 VESSFDAFAYSHGSAAGLWQFVPGTGKMMGLEQNYwyDGRRDVAASTDAALDYLVQLNERFDGNWEHAIAAYNSGGGRvs 217
Cdd:PHA00368   35 DESRFNPTAKSPTGPKGLMQFTKATAKALGLIVDD--DDRLDPELAIDAGARYLADLVGKYDGDELKAALAYNQGEGR-- 110

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 516017185  218 sairknkkLGKP-------VDFFSLDlpKETSSYVPKLLALA 252
Cdd:PHA00368  111 --------LGAPqleaydkGDFASIS--EEGRNYLRNLLDVA 142
PHA00658 PHA00658
putative lysin
 152-290 1.25e-04

putative lysin


Pssm-ID: 106967 [Multi-domain]  Cd Length: 720  Bit Score: 44.81  E-value: 1.25e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516017185 152 AAGLWQFVPGTG----KMMGL--EQNYWydgRRDVAASTDAALDYLVQLNERFDGNWEHAIAAYNSGGGRVSSAIrKNKK 225
Cdd:PHA00658 330 AVGIAQVMPDTApeaaKLAGLpwDENRY---RNDAAYNRALGMAYFQKQLRDFGGDLPKAYAAYNAGPGALQSAL-KDAK 405

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 516017185 226 LGkpvDFFSLdLPKETSSYvpkllaladVVANQEKYGIDiPSIPNKPVLTLVDPKEQLDLAIAAD 290
Cdd:PHA00658 406 DG---NWLAL-LPKETQDY---------VVKNMQAYNAG-QGRPARPTLADIEAQLQNDPRLAGN 456
Lyz-like cd00442
lysozyme-like domains; This family contains several members, including soluble lytic ...
 131-190 2.18e-04

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: 39.32  E-value: 2.18e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 516017185 131 ELALLPVVESSFD--AFAYSHGSAAGLWQFVPGTGKMMGLEQnywYDGRRDVAASTDAALDY 190
Cdd:cd00442    1 VLAAIIGQESGGNkpANAGSGSGAAGLFQFMPGTWKAYGKNS---SSDLNDPEASIEAAAKY 59
XkdP COG1652
Cytoplasmic potassium-binding protein Kbp/XkdP/YgaU, contains LysM domain [Inorganic ion ...
 419-462 2.71e-04

Cytoplasmic potassium-binding protein Kbp/XkdP/YgaU, contains LysM domain [Inorganic ion transport and metabolism];


Pssm-ID: 441258 [Multi-domain]  Cd Length: 163  Bit Score: 41.92  E-value: 2.71e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 516017185 419 SHVVQSGESLWSIARD---NKVSHKSLAKWNGMGPKDP--LRVGQKLVI 462
Cdd:COG1652  111 TYTVKPGDTLWGIAKRfygDPARWPEIAEANRDQIKNPdlIYPGQVLRI 159
PRK06347 PRK06347
1,4-beta-N-acetylmuramoylhydrolase;
335-387 1.33e-03

1,4-beta-N-acetylmuramoylhydrolase;


Pssm-ID: 180536 [Multi-domain]  Cd Length: 592  Bit Score: 41.60  E-value: 1.33e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 516017185 335 SNRGKGMKVARYKVKSGDSLSMLAKKYGTTSKVIRRANGLSNNNIRIGQYLLI 387
Cdd:PRK06347 539 TNKPSNSTVKTYTVKKGDSLWAISRQYKTTVDNIKAWNKLTSNMIHVGQKLTI 591
 
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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