NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|18860051|ref|NP_573078|]
View 

peptidoglycan recognition protein LE, isoform A [Drosophila melanogaster]

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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
PGRP smart00701
Animal peptidoglycan recognition proteins homologous to Bacteriophage T3 lysozyme; The ...
 175-317 9.24e-74

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: 224.48  E-value: 9.24e-74
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18860051    175 SAIIPRSSWLAqKPMDEPLPLQLPVKYVVILHTATESSEKRAINVRLIRDMQCFHIESRGWNDIAYNFLVGCDGNIYEGR 254
Cdd:smart00701   1 PPIVPRSEWGA-KPRGHTPRLTRPVRYVIIHHTATPNCYTDAQCAQILRNIQAYHMEELGWCDIGYNFLVGGDGKVYEGR 79

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 18860051    255 GWKTVGAHTLGYNRISLGISFIGCFMKELPTADALNMCRNLLARGVEDGHISTDYRLICHCQC 317
Cdd:smart00701  80 GWNVVGAHTGGYNDISLGIAFIGNFTDKLPTDAALDAAQDLLACAVQRGHLSPDYKLVGHRQV 142
 
Name Accession Description Interval E-value
PGRP smart00701
Animal peptidoglycan recognition proteins homologous to Bacteriophage T3 lysozyme; The ...
 175-317 9.24e-74

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: 224.48  E-value: 9.24e-74
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18860051    175 SAIIPRSSWLAqKPMDEPLPLQLPVKYVVILHTATESSEKRAINVRLIRDMQCFHIESRGWNDIAYNFLVGCDGNIYEGR 254
Cdd:smart00701   1 PPIVPRSEWGA-KPRGHTPRLTRPVRYVIIHHTATPNCYTDAQCAQILRNIQAYHMEELGWCDIGYNFLVGGDGKVYEGR 79

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 18860051    255 GWKTVGAHTLGYNRISLGISFIGCFMKELPTADALNMCRNLLARGVEDGHISTDYRLICHCQC 317
Cdd:smart00701  80 GWNVVGAHTGGYNDISLGIAFIGNFTDKLPTDAALDAAQDLLACAVQRGHLSPDYKLVGHRQV 142
PGRP cd06583
Peptidoglycan recognition proteins (PGRPs) are pattern recognition receptors that bind, and in ...
 198-326 7.91e-43

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: 144.74  E-value: 7.91e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18860051 198 PVKYVVILHTATESSEKRAINVRlirDMQCFHIesRGWNDIAYNFLVGCDGNIYEGRGWKTVGAHTLG-YNRISLGISFI 276
Cdd:cd06583   1 PVKYVVIHHTANPNCYTAAAAVR---YLQNYHM--RGWSDISYHFLVGGDGRIYQGRGWNYVGWHAGGnYNSYSIGIELI 75

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|.
gi 18860051 277 GCFMKELPTADALNMCRNLLARGVEDGHISTDYRLICHCQC-NSTESPGRR 326
Cdd:cd06583  76 GNFDGGPPTAAQLEALAELLAYLVKRYGIPPDYRIVGHRDVsPGTECPGDA 126
Amidase_2 pfam01510
N-acetylmuramoyl-L-alanine amidase; This family includes zinc amidases that have ...
 198-325 2.01e-25

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: 98.97  E-value: 2.01e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18860051   198 PVKYVVILHTATESSEKRAINVrlirdmqcFHIESRGWNDIAYNFLVGCDGNIYE-----GRGWktvGAHTLGYNRISLG 272
Cdd:pfam01510   1 PIRYIVIHHTAGPSFAGALLPY--------AACIARGWSDVSYHYLIDRDGTIYQlvpenGRAW---HAGNGGGNDRSIG 69

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 18860051   273 ISFIGCFMKELPTADALNMCRNLLARGVEDGHISTDYRLICHCQCNSTESPGR 325
Cdd:pfam01510  70 IELEGNFGGDPPTDAQYEALARLLADLCKRYGIPPDRRIVGHRDVGRKTDPGP 122
PHA00447 PHA00447
lysozyme
 200-277 1.36e-10

lysozyme


Pssm-ID: 177282 [Multi-domain]  Cd Length: 142  Bit Score: 58.64  E-value: 1.36e-10
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 18860051  200 KYVVILHTATESSEKraINVRLIRDmqcFHIEsRGWNDIAYNFLVGCDGNIYEGRGWKTVGAHTLGYNRISLGISFIG 277
Cdd:PHA00447  11 KAIFVHCSATKPSMD--VGVREIRQ---WHKE-QGWLDVGYHFIIRRDGTVEEGRPEDVVGSHVKGYNSNSVGVCLVG 82
 
Name Accession Description Interval E-value
PGRP smart00701
Animal peptidoglycan recognition proteins homologous to Bacteriophage T3 lysozyme; The ...
 175-317 9.24e-74

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: 224.48  E-value: 9.24e-74
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18860051    175 SAIIPRSSWLAqKPMDEPLPLQLPVKYVVILHTATESSEKRAINVRLIRDMQCFHIESRGWNDIAYNFLVGCDGNIYEGR 254
Cdd:smart00701   1 PPIVPRSEWGA-KPRGHTPRLTRPVRYVIIHHTATPNCYTDAQCAQILRNIQAYHMEELGWCDIGYNFLVGGDGKVYEGR 79

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 18860051    255 GWKTVGAHTLGYNRISLGISFIGCFMKELPTADALNMCRNLLARGVEDGHISTDYRLICHCQC 317
Cdd:smart00701  80 GWNVVGAHTGGYNDISLGIAFIGNFTDKLPTDAALDAAQDLLACAVQRGHLSPDYKLVGHRQV 142
PGRP cd06583
Peptidoglycan recognition proteins (PGRPs) are pattern recognition receptors that bind, and in ...
 198-326 7.91e-43

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: 144.74  E-value: 7.91e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18860051 198 PVKYVVILHTATESSEKRAINVRlirDMQCFHIesRGWNDIAYNFLVGCDGNIYEGRGWKTVGAHTLG-YNRISLGISFI 276
Cdd:cd06583   1 PVKYVVIHHTANPNCYTAAAAVR---YLQNYHM--RGWSDISYHFLVGGDGRIYQGRGWNYVGWHAGGnYNSYSIGIELI 75

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|.
gi 18860051 277 GCFMKELPTADALNMCRNLLARGVEDGHISTDYRLICHCQC-NSTESPGRR 326
Cdd:cd06583  76 GNFDGGPPTAAQLEALAELLAYLVKRYGIPPDYRIVGHRDVsPGTECPGDA 126
Ami_2 smart00644
Ami_2 domain;
198-323 6.62e-31

Ami_2 domain;


Pssm-ID: 214760 [Multi-domain]  Cd Length: 126  Bit Score: 113.61  E-value: 6.62e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18860051    198 PVKYVVILHTATESSEKRAInvrlIRDMQCFHiesrgWNDIAYNFLVGCDGNIYEGRGWKTV-----GAHTLGYNRISLG 272
Cdd:smart00644   2 PPRGIVIHHTANSNASCANE----ARYMQNNH-----MNDIGYHFLVGGDGRVYQGVGWNYVawhagGAHTPGYNDISIG 72

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 18860051    273 ISFIGCFMK-ELPTADALNMCRNLLARgVEDGH---ISTDYRLICHCQCNSTESP 323
Cdd:smart00644  73 IEFIGSFDSdDEPFAEALYAALDLLAK-LLKGAglpPDGRYRIVGHRDVAPTEDP 126
Amidase_2 pfam01510
N-acetylmuramoyl-L-alanine amidase; This family includes zinc amidases that have ...
 198-325 2.01e-25

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: 98.97  E-value: 2.01e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18860051   198 PVKYVVILHTATESSEKRAINVrlirdmqcFHIESRGWNDIAYNFLVGCDGNIYE-----GRGWktvGAHTLGYNRISLG 272
Cdd:pfam01510   1 PIRYIVIHHTAGPSFAGALLPY--------AACIARGWSDVSYHYLIDRDGTIYQlvpenGRAW---HAGNGGGNDRSIG 69

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 18860051   273 ISFIGCFMKELPTADALNMCRNLLARGVEDGHISTDYRLICHCQCNSTESPGR 325
Cdd:pfam01510  70 IELEGNFGGDPPTDAQYEALARLLADLCKRYGIPPDRRIVGHRDVGRKTDPGP 122
PHA00447 PHA00447
lysozyme
 200-277 1.36e-10

lysozyme


Pssm-ID: 177282 [Multi-domain]  Cd Length: 142  Bit Score: 58.64  E-value: 1.36e-10
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 18860051  200 KYVVILHTATESSEKraINVRLIRDmqcFHIEsRGWNDIAYNFLVGCDGNIYEGRGWKTVGAHTLGYNRISLGISFIG 277
Cdd:PHA00447  11 KAIFVHCSATKPSMD--VGVREIRQ---WHKE-QGWLDVGYHFIIRRDGTVEEGRPEDVVGSHVKGYNSNSVGVCLVG 82
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH