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Conserved domains on  [gi|6679293|ref|NP_033428|]
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peptidoglycan recognition protein 1 precursor [Mus musculus]

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 ...
 20-160 5.12e-69

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: 206.38  E-value: 5.12e-69
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679293      20 IVPRSEWRALPSECSSRLGHPVRYVVISHTAGSFCNSPDSCEQQARNVQHYHKNELGWCDVAYNFLIGEDGHVYEGRGWN 99
Cdd:smart00701   3 IVPRSEWGAKPRGHTPRLTRPVRYVIIHHTATPNCYTDAQCAQILRNIQAYHMEELGWCDIGYNFLVGGDGKVYEGRGWN 82

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6679293     100 IKGDHTGPiWNPMSIGITFMGNFMDRVPAKRALRAALNLLECGVSRGFLRSNYEVKGHRDV 160
Cdd:smart00701  83 VVGAHTGG-YNDISLGIAFIGNFTDKLPTDAALDAAQDLLACAVQRGHLSPDYKLVGHRQV 142
 
Name Accession Description Interval E-value
PGRP smart00701
Animal peptidoglycan recognition proteins homologous to Bacteriophage T3 lysozyme; The ...
 20-160 5.12e-69

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: 206.38  E-value: 5.12e-69
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679293      20 IVPRSEWRALPSECSSRLGHPVRYVVISHTAGSFCNSPDSCEQQARNVQHYHKNELGWCDVAYNFLIGEDGHVYEGRGWN 99
Cdd:smart00701   3 IVPRSEWGAKPRGHTPRLTRPVRYVIIHHTATPNCYTDAQCAQILRNIQAYHMEELGWCDIGYNFLVGGDGKVYEGRGWN 82

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6679293     100 IKGDHTGPiWNPMSIGITFMGNFMDRVPAKRALRAALNLLECGVSRGFLRSNYEVKGHRDV 160
Cdd:smart00701  83 VVGAHTGG-YNDISLGIAFIGNFTDKLPTDAALDAAQDLLACAVQRGHLSPDYKLVGHRQV 142
PGRP cd06583
Peptidoglycan recognition proteins (PGRPs) are pattern recognition receptors that bind, and in ...
 40-168 1.14e-45

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: 146.28  E-value: 1.14e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679293   40 PVRYVVISHTAGSFCNSpdsCEQQARNVQHYHKNelGWCDVAYNFLIGEDGHVYEGRGWNIKGDHTGPIWNPMSIGITFM 119
Cdd:cd06583   1 PVKYVVIHHTANPNCYT---AAAAVRYLQNYHMR--GWSDISYHFLVGGDGRIYQGRGWNYVGWHAGGNYNSYSIGIELI 75

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|
gi 6679293  120 GNFMDRVPAKRALRAALNLLECGVSRGFLRSNYEVKGHRDV-QSTLSPGD 168
Cdd:cd06583  76 GNFDGGPPTAAQLEALAELLAYLVKRYGIPPDYRIVGHRDVsPGTECPGD 125
Amidase_2 pfam01510
N-acetylmuramoyl-L-alanine amidase; This family includes zinc amidases that have ...
 40-168 3.17e-30

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: 107.06  E-value: 3.17e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679293     40 PVRYVVISHTAGSFCnspdsceqQARNVQHYHKNELGWCDVAYNFLIGEDGHVYE-----GRGWnikgdHTGP-IWNPMS 113
Cdd:pfam01510   1 PIRYIVIHHTAGPSF--------AGALLPYAACIARGWSDVSYHYLIDRDGTIYQlvpenGRAW-----HAGNgGGNDRS 67

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 6679293    114 IGITFMGNFMDRVPAKRALRAALNLLECGVSRGFLRSNYEVKGHRDVQSTLSPGD 168
Cdd:pfam01510  68 IGIELEGNFGGDPPTDAQYEALARLLADLCKRYGIPPDRRIVGHRDVGRKTDPGP 122
PHA00447 PHA00447
lysozyme
 64-167 3.20e-08

lysozyme


Pssm-ID: 177282 [Multi-domain]  Cd Length: 142  Bit Score: 50.16  E-value: 3.20e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679293    64 ARNVQHYHKnELGWCDVAYNFLIGEDGHVYEGRGWNIKGDHTGPiWNPMSIGITFMGNFMDR-------VPAK-RALRAA 135
Cdd:PHA00447  28 VREIRQWHK-EQGWLDVGYHFIIRRDGTVEEGRPEDVVGSHVKG-YNSNSVGVCLVGGIDDKgkfdanfTPAQmQSLKSL 105

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 6679293   136 LNLlecgvsrgfLRSNY---EVKGHRDVQSTLSPG 167
Cdd:PHA00447 106 LVT---------LKAKYpgaEIKAHHDVAPKACPS 131
AmpD COG3023
N-acetyl-anhydromuramyl-L-alanine amidase AmpD [Cell wall/membrane/envelope biogenesis];
20-116 4.54e-03

N-acetyl-anhydromuramyl-L-alanine amidase AmpD [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442259  Cd Length: 167  Bit Score: 36.00  E-value: 4.54e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679293   20 IVPRSEWRALPSeCSSRL-GHPVRYVVISHTAGSFCnspdsceqqARNVQHYHKNELGwcdVAYNFLIGEDGHVY----- 93
Cdd:COG3023   6 IDTGARFVPSPN-FDERPaGAEIDLIVIHYTAGPPG---------GGALDWLTDPALR---VSAHYLIDRDGEIYqlvpe 72

                        90       100       110
                ....*....|....*....|....*....|
gi 6679293   94 EGRGWnikgdHTGPIW-------NPMSIGI 116
Cdd:COG3023  73 DDRAW-----HAGVSSwrgrtnlNDFSIGI 97
 
Name Accession Description Interval E-value
PGRP smart00701
Animal peptidoglycan recognition proteins homologous to Bacteriophage T3 lysozyme; The ...
 20-160 5.12e-69

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: 206.38  E-value: 5.12e-69
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679293      20 IVPRSEWRALPSECSSRLGHPVRYVVISHTAGSFCNSPDSCEQQARNVQHYHKNELGWCDVAYNFLIGEDGHVYEGRGWN 99
Cdd:smart00701   3 IVPRSEWGAKPRGHTPRLTRPVRYVIIHHTATPNCYTDAQCAQILRNIQAYHMEELGWCDIGYNFLVGGDGKVYEGRGWN 82

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6679293     100 IKGDHTGPiWNPMSIGITFMGNFMDRVPAKRALRAALNLLECGVSRGFLRSNYEVKGHRDV 160
Cdd:smart00701  83 VVGAHTGG-YNDISLGIAFIGNFTDKLPTDAALDAAQDLLACAVQRGHLSPDYKLVGHRQV 142
PGRP cd06583
Peptidoglycan recognition proteins (PGRPs) are pattern recognition receptors that bind, and in ...
 40-168 1.14e-45

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: 146.28  E-value: 1.14e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679293   40 PVRYVVISHTAGSFCNSpdsCEQQARNVQHYHKNelGWCDVAYNFLIGEDGHVYEGRGWNIKGDHTGPIWNPMSIGITFM 119
Cdd:cd06583   1 PVKYVVIHHTANPNCYT---AAAAVRYLQNYHMR--GWSDISYHFLVGGDGRIYQGRGWNYVGWHAGGNYNSYSIGIELI 75

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|
gi 6679293  120 GNFMDRVPAKRALRAALNLLECGVSRGFLRSNYEVKGHRDV-QSTLSPGD 168
Cdd:cd06583  76 GNFDGGPPTAAQLEALAELLAYLVKRYGIPPDYRIVGHRDVsPGTECPGD 125
Ami_2 smart00644
Ami_2 domain;
39-166 3.50e-36

Ami_2 domain;


Pssm-ID: 214760 [Multi-domain]  Cd Length: 126  Bit Score: 122.47  E-value: 3.50e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679293      39 HPVRYVVISHTAgsfcNSPDSCEQQARNVQHYHKNelgwcDVAYNFLIGEDGHVYEGRGWNIKGDHTG----PIWNPMSI 114
Cdd:smart00644   1 PPPRGIVIHHTA----NSNASCANEARYMQNNHMN-----DIGYHFLVGGDGRVYQGVGWNYVAWHAGgahtPGYNDISI 71

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 6679293     115 GITFMGNFM-DRVPAKRALRAALNLLECGVSRGFLRS--NYEVKGHRDVQSTLSP 166
Cdd:smart00644  72 GIEFIGSFDsDDEPFAEALYAALDLLAKLLKGAGLPPdgRYRIVGHRDVAPTEDP 126
Amidase_2 pfam01510
N-acetylmuramoyl-L-alanine amidase; This family includes zinc amidases that have ...
 40-168 3.17e-30

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: 107.06  E-value: 3.17e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679293     40 PVRYVVISHTAGSFCnspdsceqQARNVQHYHKNELGWCDVAYNFLIGEDGHVYE-----GRGWnikgdHTGP-IWNPMS 113
Cdd:pfam01510   1 PIRYIVIHHTAGPSF--------AGALLPYAACIARGWSDVSYHYLIDRDGTIYQlvpenGRAW-----HAGNgGGNDRS 67

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 6679293    114 IGITFMGNFMDRVPAKRALRAALNLLECGVSRGFLRSNYEVKGHRDVQSTLSPGD 168
Cdd:pfam01510  68 IGIELEGNFGGDPPTDAQYEALARLLADLCKRYGIPPDRRIVGHRDVGRKTDPGP 122
PHA00447 PHA00447
lysozyme
 64-167 3.20e-08

lysozyme


Pssm-ID: 177282 [Multi-domain]  Cd Length: 142  Bit Score: 50.16  E-value: 3.20e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679293    64 ARNVQHYHKnELGWCDVAYNFLIGEDGHVYEGRGWNIKGDHTGPiWNPMSIGITFMGNFMDR-------VPAK-RALRAA 135
Cdd:PHA00447  28 VREIRQWHK-EQGWLDVGYHFIIRRDGTVEEGRPEDVVGSHVKG-YNSNSVGVCLVGGIDDKgkfdanfTPAQmQSLKSL 105

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 6679293   136 LNLlecgvsrgfLRSNY---EVKGHRDVQSTLSPG 167
Cdd:PHA00447 106 LVT---------LKAKYpgaEIKAHHDVAPKACPS 131
AmpD COG3023
N-acetyl-anhydromuramyl-L-alanine amidase AmpD [Cell wall/membrane/envelope biogenesis];
20-116 4.54e-03

N-acetyl-anhydromuramyl-L-alanine amidase AmpD [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442259  Cd Length: 167  Bit Score: 36.00  E-value: 4.54e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679293   20 IVPRSEWRALPSeCSSRL-GHPVRYVVISHTAGSFCnspdsceqqARNVQHYHKNELGwcdVAYNFLIGEDGHVY----- 93
Cdd:COG3023   6 IDTGARFVPSPN-FDERPaGAEIDLIVIHYTAGPPG---------GGALDWLTDPALR---VSAHYLIDRDGEIYqlvpe 72

                        90       100       110
                ....*....|....*....|....*....|
gi 6679293   94 EGRGWnikgdHTGPIW-------NPMSIGI 116
Cdd:COG3023  73 DDRAW-----HAGVSSwrgrtnlNDFSIGI 97
 
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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