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Conserved domains on  [gi|300794763|ref|NP_001178890|]
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peptidoglycan recognition protein 3 precursor [Rattus norvegicus]

Protein Classification

peptidoglycan recognition protein( domain architecture ID 11274790)

peptidoglycan recognition protein (PGRP) is a pattern recognition receptor that binds and may also hydrolyze peptidoglycans (PGNs) of bacterial cell walls

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PGRP smart00701
Animal peptidoglycan recognition proteins homologous to Bacteriophage T3 lysozyme; The ...
 177-317 1.94e-62

Animal peptidoglycan recognition proteins homologous to Bacteriophage T3 lysozyme; The bacteriophage molecule, but not its moth homologue, has been shown to have N-acetylmuramoyl-L-alanine amidase activity. One member of this family, Tag7, is a cytokine.


:

Pssm-ID: 128941  Cd Length: 142  Bit Score: 195.21  E-value: 1.94e-62
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300794763   177 PNIIPRTAW-EARETHCSQMNLPAKFVIIIHTAGESCNESADCLIRVRDTQSFHMDKQDFCDIAYHFLVGQDGVVYEGVG 255
Cdd:smart00701   1 PPIVPRSEWgAKPRGHTPRLTRPVRYVIIHHTATPNCYTDAQCAQILRNIQAYHMEELGWCDIGYNFLVGGDGKVYEGRG 80

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 300794763   256 WTIEGSHTYGYNDIALGIAFMGNFVEKPPNEASLEAAQSLIQCAVAMGYLASNYLLMGHSDV 317
Cdd:smart00701  81 WNVVGAHTGGYNDISLGIAFIGNFTDKLPTDAALDAAQDLLACAVQRGHLSPDYKLVGHRQV 142
PGRP smart00701
Animal peptidoglycan recognition proteins homologous to Bacteriophage T3 lysozyme; The ...
 19-152 2.97e-52

Animal peptidoglycan recognition proteins homologous to Bacteriophage T3 lysozyme; The bacteriophage molecule, but not its moth homologue, has been shown to have N-acetylmuramoyl-L-alanine amidase activity. One member of this family, Tag7, is a cytokine.


:

Pssm-ID: 128941  Cd Length: 142  Bit Score: 169.40  E-value: 2.97e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300794763    19 PTIVSRKVWGASSLTCRVPLSLPVPYLIIEQVTRMQCQDQTSCSQVLRVLHSHYVHNKGWCDVAFNFLVGNDGKVYEGVG 98
Cdd:smart00701   1 PPIVPRSEWGAKPRGHTPRLTRPVRYVIIHHTATPNCYTDAQCAQILRNIQAYHMEELGWCDIGYNFLVGGDGKVYEGRG 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....
gi 300794763    99 WHVQGLHTQGYNNVSLGIAFFGSKIGSSPSPAALSATEDLIFFAILNGYLSPKY 152
Cdd:smart00701  81 WNVVGAHTGGYNDISLGIAFIGNFTDKLPTDAALDAAQDLLACAVQRGHLSPDY 134
 
Name Accession Description Interval E-value
PGRP smart00701
Animal peptidoglycan recognition proteins homologous to Bacteriophage T3 lysozyme; The ...
 177-317 1.94e-62

Animal peptidoglycan recognition proteins homologous to Bacteriophage T3 lysozyme; The bacteriophage molecule, but not its moth homologue, has been shown to have N-acetylmuramoyl-L-alanine amidase activity. One member of this family, Tag7, is a cytokine.


Pssm-ID: 128941  Cd Length: 142  Bit Score: 195.21  E-value: 1.94e-62
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300794763   177 PNIIPRTAW-EARETHCSQMNLPAKFVIIIHTAGESCNESADCLIRVRDTQSFHMDKQDFCDIAYHFLVGQDGVVYEGVG 255
Cdd:smart00701   1 PPIVPRSEWgAKPRGHTPRLTRPVRYVIIHHTATPNCYTDAQCAQILRNIQAYHMEELGWCDIGYNFLVGGDGKVYEGRG 80

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 300794763   256 WTIEGSHTYGYNDIALGIAFMGNFVEKPPNEASLEAAQSLIQCAVAMGYLASNYLLMGHSDV 317
Cdd:smart00701  81 WNVVGAHTGGYNDISLGIAFIGNFTDKLPTDAALDAAQDLLACAVQRGHLSPDYKLVGHRQV 142
PGRP smart00701
Animal peptidoglycan recognition proteins homologous to Bacteriophage T3 lysozyme; The ...
 19-152 2.97e-52

Animal peptidoglycan recognition proteins homologous to Bacteriophage T3 lysozyme; The bacteriophage molecule, but not its moth homologue, has been shown to have N-acetylmuramoyl-L-alanine amidase activity. One member of this family, Tag7, is a cytokine.


Pssm-ID: 128941  Cd Length: 142  Bit Score: 169.40  E-value: 2.97e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300794763    19 PTIVSRKVWGASSLTCRVPLSLPVPYLIIEQVTRMQCQDQTSCSQVLRVLHSHYVHNKGWCDVAFNFLVGNDGKVYEGVG 98
Cdd:smart00701   1 PPIVPRSEWGAKPRGHTPRLTRPVRYVIIHHTATPNCYTDAQCAQILRNIQAYHMEELGWCDIGYNFLVGGDGKVYEGRG 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....
gi 300794763    99 WHVQGLHTQGYNNVSLGIAFFGSKIGSSPSPAALSATEDLIFFAILNGYLSPKY 152
Cdd:smart00701  81 WNVVGAHTGGYNDISLGIAFIGNFTDKLPTDAALDAAQDLLACAVQRGHLSPDY 134
PGRP cd06583
Peptidoglycan recognition proteins (PGRPs) are pattern recognition receptors that bind, and in ...
 198-326 2.96e-38

Peptidoglycan recognition proteins (PGRPs) are pattern recognition receptors that bind, and in certain cases, hydrolyze peptidoglycans (PGNs) of bacterial cell walls. PGRPs have been divided into three classes: short PGRPs (PGRP-S), that are small (20 kDa) extracellular proteins; intermediate PGRPs (PGRP-I) that are 40-45 kDa and are predicted to be transmembrane proteins; and long PGRPs (PGRP-L), up to 90 kDa, which may be either intracellular or transmembrane. Several structures of PGRPs are known in insects and mammals, some bound with substrates like Muramyl Tripeptide (MTP) or Tracheal Cytotoxin (TCT). The substrate binding site is conserved in PGRP-LCx, PGRP-LE, and PGRP-Ialpha proteins. This family includes Zn-dependent N-Acetylmuramoyl-L-alanine Amidase, EC:3.5.1.28. This enzyme cleaves the amide bond between N-acetylmuramoyl and L-amino acids, preferentially D-lactyl-L-Ala, in bacterial cell walls. The structure for the bacteriophage T7 lysozyme shows that two of the conserved histidines and a cysteine are zinc binding residues. Site-directed mutagenesis of T7 lysozyme indicates that two conserved residues, a Tyr and a Lys, are important for amidase activity.


Pssm-ID: 133475 [Multi-domain]  Cd Length: 126  Bit Score: 132.41  E-value: 2.96e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300794763 198 PAKFVIIIHTAGESCNESADClirVRDTQSFHMdkQDFCDIAYHFLVGQDGVVYEGVGWTIEGSHTYG-YNDIALGIAFM 276
Cdd:cd06583    1 PVKYVVIHHTANPNCYTAAAA---VRYLQNYHM--RGWSDISYHFLVGGDGRIYQGRGWNYVGWHAGGnYNSYSIGIELI 75

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 300794763 277 GNFVEKPPNEASLEAAQSLIQCAVAMGYLASNYLLMGHSDVSNI-LSPGQA 326
Cdd:cd06583   76 GNFDGGPPTAAQLEALAELLAYLVKRYGIPPDYRIVGHRDVSPGtECPGDA 126
Amidase_2 pfam01510
N-acetylmuramoyl-L-alanine amidase; This family includes zinc amidases that have ...
 198-325 1.14e-24

N-acetylmuramoyl-L-alanine amidase; This family includes zinc amidases that have N-acetylmuramoyl-L-alanine amidase activity EC:3.5.1.28. This enzyme domain cleaves the amide bond between N-acetylmuramoyl and L-amino acids in bacterial cell walls (preferentially: D-lactyl-L-Ala). The structure is known for the bacteriophage T7 structure and shows that two of the conserved histidines are zinc binding.


Pssm-ID: 460236 [Multi-domain]  Cd Length: 122  Bit Score: 96.66  E-value: 1.14e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300794763  198 PAKFVIIIHTAGEScneSADCLIRVRDTQSfhmdkQDFCDIAYHFLVGQDGVVYEGVGWTIEGSHT--YGYNDIALGIAF 275
Cdd:pfam01510   1 PIRYIVIHHTAGPS---FAGALLPYAACIA-----RGWSDVSYHYLIDRDGTIYQLVPENGRAWHAgnGGGNDRSIGIEL 72

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 300794763  276 MGNFVEKPPNEASLEAAQSLIQCAVAMGYLASNYLLMGHSDVSNILSPGQ 325
Cdd:pfam01510  73 EGNFGGDPPTDAQYEALARLLADLCKRYGIPPDRRIVGHRDVGRKTDPGP 122
PGRP cd06583
Peptidoglycan recognition proteins (PGRPs) are pattern recognition receptors that bind, and in ...
 59-177 1.54e-22

Peptidoglycan recognition proteins (PGRPs) are pattern recognition receptors that bind, and in certain cases, hydrolyze peptidoglycans (PGNs) of bacterial cell walls. PGRPs have been divided into three classes: short PGRPs (PGRP-S), that are small (20 kDa) extracellular proteins; intermediate PGRPs (PGRP-I) that are 40-45 kDa and are predicted to be transmembrane proteins; and long PGRPs (PGRP-L), up to 90 kDa, which may be either intracellular or transmembrane. Several structures of PGRPs are known in insects and mammals, some bound with substrates like Muramyl Tripeptide (MTP) or Tracheal Cytotoxin (TCT). The substrate binding site is conserved in PGRP-LCx, PGRP-LE, and PGRP-Ialpha proteins. This family includes Zn-dependent N-Acetylmuramoyl-L-alanine Amidase, EC:3.5.1.28. This enzyme cleaves the amide bond between N-acetylmuramoyl and L-amino acids, preferentially D-lactyl-L-Ala, in bacterial cell walls. The structure for the bacteriophage T7 lysozyme shows that two of the conserved histidines and a cysteine are zinc binding residues. Site-directed mutagenesis of T7 lysozyme indicates that two conserved residues, a Tyr and a Lys, are important for amidase activity.


Pssm-ID: 133475 [Multi-domain]  Cd Length: 126  Bit Score: 91.20  E-value: 1.54e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300794763  59 TSCSQVLRVLHSHyvHNKGWCDVAFNFLVGNDGKVYEGVGWHVQGLHTQG-YNNVSLGIAFFGSKIGSSPSPAALSATED 137
Cdd:cd06583   16 YTAAAAVRYLQNY--HMRGWSDISYHFLVGGDGRIYQGRGWNYVGWHAGGnYNSYSIGIELIGNFDGGPPTAAQLEALAE 93

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 300794763 138 LIFFAILNGYLSPKYiqpfllkeetCLVPqHSEI-PKKACP 177
Cdd:cd06583   94 LLAYLVKRYGIPPDY----------RIVG-HRDVsPGTECP 123
Amidase_2 pfam01510
N-acetylmuramoyl-L-alanine amidase; This family includes zinc amidases that have ...
 74-177 9.99e-13

N-acetylmuramoyl-L-alanine amidase; This family includes zinc amidases that have N-acetylmuramoyl-L-alanine amidase activity EC:3.5.1.28. This enzyme domain cleaves the amide bond between N-acetylmuramoyl and L-amino acids in bacterial cell walls (preferentially: D-lactyl-L-Ala). The structure is known for the bacteriophage T7 structure and shows that two of the conserved histidines are zinc binding.


Pssm-ID: 460236 [Multi-domain]  Cd Length: 122  Bit Score: 64.30  E-value: 9.99e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300794763   74 HNKGWCDVAFNFLVGNDGKVYE-----GVGWHVQGlhtQGYNNVSLGIAFFGSKIGSSPSPAALSATEDLIFFAILNGYL 148
Cdd:pfam01510  26 IARGWSDVSYHYLIDRDGTIYQlvpenGRAWHAGN---GGGNDRSIGIELEGNFGGDPPTDAQYEALARLLADLCKRYGI 102

                          90       100
                  ....*....|....*....|....*....
gi 300794763  149 SPKYiqpfllkeetcLVPQHSEIPKKACP 177
Cdd:pfam01510 103 PPDR-----------RIVGHRDVGRKTDP 120
PHA00447 PHA00447
lysozyme
 203-324 4.89e-11

lysozyme


Pssm-ID: 177282 [Multi-domain]  Cd Length: 142  Bit Score: 59.79  E-value: 4.89e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300794763 203 IIIHTAGESCNESadclIRVRDTQSFHMDkQDFCDIAYHFLVGQDGVVYEG--VGWTieGSHTYGYNDIALGIAFMGNFV 280
Cdd:PHA00447  13 IFVHCSATKPSMD----VGVREIRQWHKE-QGWLDVGYHFIIRRDGTVEEGrpEDVV--GSHVKGYNSNSVGVCLVGGID 85

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 300794763 281 EKPPNEASLEAAQ--SLIQCAVAMGYLASNYLLMGHSDVSNILSPG 324
Cdd:PHA00447  86 DKGKFDANFTPAQmqSLKSLLVTLKAKYPGAEIKAHHDVAPKACPS 131
PHA00447 PHA00447
lysozyme
 76-177 4.24e-06

lysozyme


Pssm-ID: 177282 [Multi-domain]  Cd Length: 142  Bit Score: 45.92  E-value: 4.24e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300794763  76 KGWCDVAFNFLVGNDGKVYEGVGWHVQGLHTQGYNNVSLGIAFFG-----SKIGSSPSPAALSATEDLIffailnGYLSP 150
Cdd:PHA00447  38 QGWLDVGYHFIIRRDGTVEEGRPEDVVGSHVKGYNSNSVGVCLVGgiddkGKFDANFTPAQMQSLKSLL------VTLKA 111

                         90       100
                 ....*....|....*....|....*..
gi 300794763 151 KYIQPFLLKeetclvpqHSEIPKKACP 177
Cdd:PHA00447 112 KYPGAEIKA--------HHDVAPKACP 130
 
Name Accession Description Interval E-value
PGRP smart00701
Animal peptidoglycan recognition proteins homologous to Bacteriophage T3 lysozyme; The ...
 177-317 1.94e-62

Animal peptidoglycan recognition proteins homologous to Bacteriophage T3 lysozyme; The bacteriophage molecule, but not its moth homologue, has been shown to have N-acetylmuramoyl-L-alanine amidase activity. One member of this family, Tag7, is a cytokine.


Pssm-ID: 128941  Cd Length: 142  Bit Score: 195.21  E-value: 1.94e-62
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300794763   177 PNIIPRTAW-EARETHCSQMNLPAKFVIIIHTAGESCNESADCLIRVRDTQSFHMDKQDFCDIAYHFLVGQDGVVYEGVG 255
Cdd:smart00701   1 PPIVPRSEWgAKPRGHTPRLTRPVRYVIIHHTATPNCYTDAQCAQILRNIQAYHMEELGWCDIGYNFLVGGDGKVYEGRG 80

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 300794763   256 WTIEGSHTYGYNDIALGIAFMGNFVEKPPNEASLEAAQSLIQCAVAMGYLASNYLLMGHSDV 317
Cdd:smart00701  81 WNVVGAHTGGYNDISLGIAFIGNFTDKLPTDAALDAAQDLLACAVQRGHLSPDYKLVGHRQV 142
PGRP smart00701
Animal peptidoglycan recognition proteins homologous to Bacteriophage T3 lysozyme; The ...
 19-152 2.97e-52

Animal peptidoglycan recognition proteins homologous to Bacteriophage T3 lysozyme; The bacteriophage molecule, but not its moth homologue, has been shown to have N-acetylmuramoyl-L-alanine amidase activity. One member of this family, Tag7, is a cytokine.


Pssm-ID: 128941  Cd Length: 142  Bit Score: 169.40  E-value: 2.97e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300794763    19 PTIVSRKVWGASSLTCRVPLSLPVPYLIIEQVTRMQCQDQTSCSQVLRVLHSHYVHNKGWCDVAFNFLVGNDGKVYEGVG 98
Cdd:smart00701   1 PPIVPRSEWGAKPRGHTPRLTRPVRYVIIHHTATPNCYTDAQCAQILRNIQAYHMEELGWCDIGYNFLVGGDGKVYEGRG 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....
gi 300794763    99 WHVQGLHTQGYNNVSLGIAFFGSKIGSSPSPAALSATEDLIFFAILNGYLSPKY 152
Cdd:smart00701  81 WNVVGAHTGGYNDISLGIAFIGNFTDKLPTDAALDAAQDLLACAVQRGHLSPDY 134
PGRP cd06583
Peptidoglycan recognition proteins (PGRPs) are pattern recognition receptors that bind, and in ...
 198-326 2.96e-38

Peptidoglycan recognition proteins (PGRPs) are pattern recognition receptors that bind, and in certain cases, hydrolyze peptidoglycans (PGNs) of bacterial cell walls. PGRPs have been divided into three classes: short PGRPs (PGRP-S), that are small (20 kDa) extracellular proteins; intermediate PGRPs (PGRP-I) that are 40-45 kDa and are predicted to be transmembrane proteins; and long PGRPs (PGRP-L), up to 90 kDa, which may be either intracellular or transmembrane. Several structures of PGRPs are known in insects and mammals, some bound with substrates like Muramyl Tripeptide (MTP) or Tracheal Cytotoxin (TCT). The substrate binding site is conserved in PGRP-LCx, PGRP-LE, and PGRP-Ialpha proteins. This family includes Zn-dependent N-Acetylmuramoyl-L-alanine Amidase, EC:3.5.1.28. This enzyme cleaves the amide bond between N-acetylmuramoyl and L-amino acids, preferentially D-lactyl-L-Ala, in bacterial cell walls. The structure for the bacteriophage T7 lysozyme shows that two of the conserved histidines and a cysteine are zinc binding residues. Site-directed mutagenesis of T7 lysozyme indicates that two conserved residues, a Tyr and a Lys, are important for amidase activity.


Pssm-ID: 133475 [Multi-domain]  Cd Length: 126  Bit Score: 132.41  E-value: 2.96e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300794763 198 PAKFVIIIHTAGESCNESADClirVRDTQSFHMdkQDFCDIAYHFLVGQDGVVYEGVGWTIEGSHTYG-YNDIALGIAFM 276
Cdd:cd06583    1 PVKYVVIHHTANPNCYTAAAA---VRYLQNYHM--RGWSDISYHFLVGGDGRIYQGRGWNYVGWHAGGnYNSYSIGIELI 75

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 300794763 277 GNFVEKPPNEASLEAAQSLIQCAVAMGYLASNYLLMGHSDVSNI-LSPGQA 326
Cdd:cd06583   76 GNFDGGPPTAAQLEALAELLAYLVKRYGIPPDYRIVGHRDVSPGtECPGDA 126
Ami_2 smart00644
Ami_2 domain;
202-323 6.52e-28

Ami_2 domain;


Pssm-ID: 214760 [Multi-domain]  Cd Length: 126  Bit Score: 105.52  E-value: 6.52e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300794763   202 VIIIHTAGESCnesADCLIRVRDTQSFHMDkqdfcDIAYHFLVGQDGVVYEGVG-----WTIEGSHTYGYNDIALGIAFM 276
Cdd:smart00644   5 GIVIHHTANSN---ASCANEARYMQNNHMN-----DIGYHFLVGGDGRVYQGVGwnyvaWHAGGAHTPGYNDISIGIEFI 76

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 300794763   277 GNFVE-KPPNEASLEAAQSLIQCAVAMGYL--ASNYLLMGHSDVSNILSP 323
Cdd:smart00644  77 GSFDSdDEPFAEALYAALDLLAKLLKGAGLppDGRYRIVGHRDVAPTEDP 126
Amidase_2 pfam01510
N-acetylmuramoyl-L-alanine amidase; This family includes zinc amidases that have ...
 198-325 1.14e-24

N-acetylmuramoyl-L-alanine amidase; This family includes zinc amidases that have N-acetylmuramoyl-L-alanine amidase activity EC:3.5.1.28. This enzyme domain cleaves the amide bond between N-acetylmuramoyl and L-amino acids in bacterial cell walls (preferentially: D-lactyl-L-Ala). The structure is known for the bacteriophage T7 structure and shows that two of the conserved histidines are zinc binding.


Pssm-ID: 460236 [Multi-domain]  Cd Length: 122  Bit Score: 96.66  E-value: 1.14e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300794763  198 PAKFVIIIHTAGEScneSADCLIRVRDTQSfhmdkQDFCDIAYHFLVGQDGVVYEGVGWTIEGSHT--YGYNDIALGIAF 275
Cdd:pfam01510   1 PIRYIVIHHTAGPS---FAGALLPYAACIA-----RGWSDVSYHYLIDRDGTIYQLVPENGRAWHAgnGGGNDRSIGIEL 72

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 300794763  276 MGNFVEKPPNEASLEAAQSLIQCAVAMGYLASNYLLMGHSDVSNILSPGQ 325
Cdd:pfam01510  73 EGNFGGDPPTDAQYEALARLLADLCKRYGIPPDRRIVGHRDVGRKTDPGP 122
PGRP cd06583
Peptidoglycan recognition proteins (PGRPs) are pattern recognition receptors that bind, and in ...
 59-177 1.54e-22

Peptidoglycan recognition proteins (PGRPs) are pattern recognition receptors that bind, and in certain cases, hydrolyze peptidoglycans (PGNs) of bacterial cell walls. PGRPs have been divided into three classes: short PGRPs (PGRP-S), that are small (20 kDa) extracellular proteins; intermediate PGRPs (PGRP-I) that are 40-45 kDa and are predicted to be transmembrane proteins; and long PGRPs (PGRP-L), up to 90 kDa, which may be either intracellular or transmembrane. Several structures of PGRPs are known in insects and mammals, some bound with substrates like Muramyl Tripeptide (MTP) or Tracheal Cytotoxin (TCT). The substrate binding site is conserved in PGRP-LCx, PGRP-LE, and PGRP-Ialpha proteins. This family includes Zn-dependent N-Acetylmuramoyl-L-alanine Amidase, EC:3.5.1.28. This enzyme cleaves the amide bond between N-acetylmuramoyl and L-amino acids, preferentially D-lactyl-L-Ala, in bacterial cell walls. The structure for the bacteriophage T7 lysozyme shows that two of the conserved histidines and a cysteine are zinc binding residues. Site-directed mutagenesis of T7 lysozyme indicates that two conserved residues, a Tyr and a Lys, are important for amidase activity.


Pssm-ID: 133475 [Multi-domain]  Cd Length: 126  Bit Score: 91.20  E-value: 1.54e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300794763  59 TSCSQVLRVLHSHyvHNKGWCDVAFNFLVGNDGKVYEGVGWHVQGLHTQG-YNNVSLGIAFFGSKIGSSPSPAALSATED 137
Cdd:cd06583   16 YTAAAAVRYLQNY--HMRGWSDISYHFLVGGDGRIYQGRGWNYVGWHAGGnYNSYSIGIELIGNFDGGPPTAAQLEALAE 93

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 300794763 138 LIFFAILNGYLSPKYiqpfllkeetCLVPqHSEI-PKKACP 177
Cdd:cd06583   94 LLAYLVKRYGIPPDY----------RIVG-HRDVsPGTECP 123
Ami_2 smart00644
Ami_2 domain;
41-177 2.37e-18

Ami_2 domain;


Pssm-ID: 214760 [Multi-domain]  Cd Length: 126  Bit Score: 79.71  E-value: 2.37e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300794763    41 PVPYLIIEQVTRMQCqdqTSCSQVLRVLHSHYVHnkgwcDVAFNFLVGNDGKVYEGVG-----WHVQGLHTQGYNNVSLG 115
Cdd:smart00644   1 PPPRGIVIHHTANSN---ASCANEARYMQNNHMN-----DIGYHFLVGGDGRVYQGVGwnyvaWHAGGAHTPGYNDISIG 72

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 300794763   116 IAFFGSKIGS-SPSPAALSATEDLIFFAILNGYLSPKYIQpfllkeetcLVPQHSEIPKKACP 177
Cdd:smart00644  73 IEFIGSFDSDdEPFAEALYAALDLLAKLLKGAGLPPDGRY---------RIVGHRDVAPTEDP 126
Amidase_2 pfam01510
N-acetylmuramoyl-L-alanine amidase; This family includes zinc amidases that have ...
 74-177 9.99e-13

N-acetylmuramoyl-L-alanine amidase; This family includes zinc amidases that have N-acetylmuramoyl-L-alanine amidase activity EC:3.5.1.28. This enzyme domain cleaves the amide bond between N-acetylmuramoyl and L-amino acids in bacterial cell walls (preferentially: D-lactyl-L-Ala). The structure is known for the bacteriophage T7 structure and shows that two of the conserved histidines are zinc binding.


Pssm-ID: 460236 [Multi-domain]  Cd Length: 122  Bit Score: 64.30  E-value: 9.99e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300794763   74 HNKGWCDVAFNFLVGNDGKVYE-----GVGWHVQGlhtQGYNNVSLGIAFFGSKIGSSPSPAALSATEDLIFFAILNGYL 148
Cdd:pfam01510  26 IARGWSDVSYHYLIDRDGTIYQlvpenGRAWHAGN---GGGNDRSIGIELEGNFGGDPPTDAQYEALARLLADLCKRYGI 102

                          90       100
                  ....*....|....*....|....*....
gi 300794763  149 SPKYiqpfllkeetcLVPQHSEIPKKACP 177
Cdd:pfam01510 103 PPDR-----------RIVGHRDVGRKTDP 120
PHA00447 PHA00447
lysozyme
 203-324 4.89e-11

lysozyme


Pssm-ID: 177282 [Multi-domain]  Cd Length: 142  Bit Score: 59.79  E-value: 4.89e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300794763 203 IIIHTAGESCNESadclIRVRDTQSFHMDkQDFCDIAYHFLVGQDGVVYEG--VGWTieGSHTYGYNDIALGIAFMGNFV 280
Cdd:PHA00447  13 IFVHCSATKPSMD----VGVREIRQWHKE-QGWLDVGYHFIIRRDGTVEEGrpEDVV--GSHVKGYNSNSVGVCLVGGID 85

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 300794763 281 EKPPNEASLEAAQ--SLIQCAVAMGYLASNYLLMGHSDVSNILSPG 324
Cdd:PHA00447  86 DKGKFDANFTPAQmqSLKSLLVTLKAKYPGAEIKAHHDVAPKACPS 131
PHA00447 PHA00447
lysozyme
 76-177 4.24e-06

lysozyme


Pssm-ID: 177282 [Multi-domain]  Cd Length: 142  Bit Score: 45.92  E-value: 4.24e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300794763  76 KGWCDVAFNFLVGNDGKVYEGVGWHVQGLHTQGYNNVSLGIAFFG-----SKIGSSPSPAALSATEDLIffailnGYLSP 150
Cdd:PHA00447  38 QGWLDVGYHFIIRRDGTVEEGRPEDVVGSHVKGYNSNSVGVCLVGgiddkGKFDANFTPAQMQSLKSLL------VTLKA 111

                         90       100
                 ....*....|....*....|....*..
gi 300794763 151 KYIQPFLLKeetclvpqHSEIPKKACP 177
Cdd:PHA00447 112 KYPGAEIKA--------HHDVAPKACP 130
 
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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