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Conserved domains on  [gi|45553005|ref|NP_996030|]
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peptidoglycan recognition protein LC, isoform C [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

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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 ...
 337-476 1.65e-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: 174.41  E-value: 1.65e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553005    337 VVSIKGWGGMPtRGNLKPFKLPVSKVIISETPPEICTTQDSCSYWTRVTQSRHMDTFNWSQVGYNFLVGGDGRIYEGRGW 416
Cdd:smart00701   3 IVPRSEWGAKP-RGHTPRLTRPVRYVIIHHTATPNCYTDAQCAQILRNIQAYHMEELGWCDIGYNFLVGGDGKVYEGRGW 81

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553005    417 NYMGDHTRDNNNNSIGITFLGTFRRQEPTPKSLEACQLLIAQGVRLKKLKPDYQLLGHRQ 476
Cdd:smart00701  82 NVVGAHTGGYNDISLGIAFIGNFTDKLPTDAALDAAQDLLACAVQRGHLSPDYKLVGHRQ 141
 
Name Accession Description Interval E-value
PGRP smart00701
Animal peptidoglycan recognition proteins homologous to Bacteriophage T3 lysozyme; The ...
 337-476 1.65e-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: 174.41  E-value: 1.65e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553005    337 VVSIKGWGGMPtRGNLKPFKLPVSKVIISETPPEICTTQDSCSYWTRVTQSRHMDTFNWSQVGYNFLVGGDGRIYEGRGW 416
Cdd:smart00701   3 IVPRSEWGAKP-RGHTPRLTRPVRYVIIHHTATPNCYTDAQCAQILRNIQAYHMEELGWCDIGYNFLVGGDGKVYEGRGW 81

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553005    417 NYMGDHTRDNNNNSIGITFLGTFRRQEPTPKSLEACQLLIAQGVRLKKLKPDYQLLGHRQ 476
Cdd:smart00701  82 NVVGAHTGGYNDISLGIAFIGNFTDKLPTDAALDAAQDLLACAVQRGHLSPDYKLVGHRQ 141
PGRP cd06583
Peptidoglycan recognition proteins (PGRPs) are pattern recognition receptors that bind, and in ...
 358-485 7.57e-39

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: 137.81  E-value: 7.57e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553005 358 PVSKVIISETPPEICTTqdsCSYWTRVTQSRHMDtfNWSQVGYNFLVGGDGRIYEGRGWNYMGDHTRDN-NNNSIGITFL 436
Cdd:cd06583   1 PVKYVVIHHTANPNCYT---AAAAVRYLQNYHMR--GWSDISYHFLVGGDGRIYQGRGWNYVGWHAGGNyNSYSIGIELI 75

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|
gi 45553005 437 GTFRRQEPTPKSLEACQLLIAQGVRLKKLKPDYQLLGHRQITG-TLMPGE 485
Cdd:cd06583  76 GNFDGGPPTAAQLEALAELLAYLVKRYGIPPDYRIVGHRDVSPgTECPGD 125
Amidase_2 pfam01510
N-acetylmuramoyl-L-alanine amidase; This family includes zinc amidases that have ...
 358-485 5.89e-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: 5.89e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553005   358 PVSKVIISETppeICTTQDSCSYWTRVTQSRhmdtfNWSQVGYNFLVGGDGRIYEGRGWNYMGDHTRDN--NNNSIGITF 435
Cdd:pfam01510   1 PIRYIVIHHT---AGPSFAGALLPYAACIAR-----GWSDVSYHYLIDRDGTIYQLVPENGRAWHAGNGggNDRSIGIEL 72

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 45553005   436 LGTFRRQEPTPKSLEACQLLIAQGVRLKKLKPDYQLLGHRQITGTLMPGE 485
Cdd:pfam01510  73 EGNFGGDPPTDAQYEALARLLADLCKRYGIPPDRRIVGHRDVGRKTDPGP 122
PHA00447 PHA00447
lysozyme
 395-493 1.11e-08

lysozyme


Pssm-ID: 177282 [Multi-domain]  Cd Length: 142  Bit Score: 54.01  E-value: 1.11e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553005  395 WSQVGYNFLVGGDGRIYEGRGWNYMGDHTRDNNNNSIGITFLGTFRRQEP-----TPKSLEACQLLIaqgVRLKKLKPDY 469
Cdd:PHA00447  40 WLDVGYHFIIRRDGTVEEGRPEDVVGSHVKGYNSNSVGVCLVGGIDDKGKfdanfTPAQMQSLKSLL---VTLKAKYPGA 116

                         90       100
                 ....*....|....*....|....
gi 45553005  470 QLLGHRQITGTLMPGEELYRIIQT 493
Cdd:PHA00447 117 EIKAHHDVAPKACPSFDLQRWLKK 140
CwlA COG5632
N-acetylmuramoyl-L-alanine amidase CwlA [Cell wall/membrane/envelope biogenesis];
394-503 1.07e-03

N-acetylmuramoyl-L-alanine amidase CwlA [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 444359  Cd Length: 177  Bit Score: 39.95  E-value: 1.07e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553005 394 NWSQVGYNFLVGgDGRIYEGRGWNYM----GDHTRDNNNNSIGI----TFLGTFrrqeptPKSLEACQLLIAQGVRLKKL 465
Cdd:COG5632  49 NNRSASWHYFVD-DKEIIQHIPLNENawhaGDGTGPGNRRSIGIeiceNKDGDF------AKAYENAAELIAYLMKKYGI 121

                        90       100       110
                ....*....|....*....|....*....|....*...
gi 45553005 466 KPDyQLLGHRQITGTLMPGEELYRIIQTWNNWYNLTKT 503
Cdd:COG5632 122 PID-NVVRHYDWSGKNCPHGLLANGGYRWDQFKADVKS 158
 
Name Accession Description Interval E-value
PGRP smart00701
Animal peptidoglycan recognition proteins homologous to Bacteriophage T3 lysozyme; The ...
 337-476 1.65e-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: 174.41  E-value: 1.65e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553005    337 VVSIKGWGGMPtRGNLKPFKLPVSKVIISETPPEICTTQDSCSYWTRVTQSRHMDTFNWSQVGYNFLVGGDGRIYEGRGW 416
Cdd:smart00701   3 IVPRSEWGAKP-RGHTPRLTRPVRYVIIHHTATPNCYTDAQCAQILRNIQAYHMEELGWCDIGYNFLVGGDGKVYEGRGW 81

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553005    417 NYMGDHTRDNNNNSIGITFLGTFRRQEPTPKSLEACQLLIAQGVRLKKLKPDYQLLGHRQ 476
Cdd:smart00701  82 NVVGAHTGGYNDISLGIAFIGNFTDKLPTDAALDAAQDLLACAVQRGHLSPDYKLVGHRQ 141
PGRP cd06583
Peptidoglycan recognition proteins (PGRPs) are pattern recognition receptors that bind, and in ...
 358-485 7.57e-39

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: 137.81  E-value: 7.57e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553005 358 PVSKVIISETPPEICTTqdsCSYWTRVTQSRHMDtfNWSQVGYNFLVGGDGRIYEGRGWNYMGDHTRDN-NNNSIGITFL 436
Cdd:cd06583   1 PVKYVVIHHTANPNCYT---AAAAVRYLQNYHMR--GWSDISYHFLVGGDGRIYQGRGWNYVGWHAGGNyNSYSIGIELI 75

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|
gi 45553005 437 GTFRRQEPTPKSLEACQLLIAQGVRLKKLKPDYQLLGHRQITG-TLMPGE 485
Cdd:cd06583  76 GNFDGGPPTAAQLEALAELLAYLVKRYGIPPDYRIVGHRDVSPgTECPGD 125
Ami_2 smart00644
Ami_2 domain;
358-483 3.91e-27

Ami_2 domain;


Pssm-ID: 214760 [Multi-domain]  Cd Length: 126  Bit Score: 105.90  E-value: 3.91e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553005    358 PVSKVIISETPPeicTTQDSCSYWTRVTQSRHMDtfnwsQVGYNFLVGGDGRIYEGRGWNY-----MGDHTRDNNNNSIG 432
Cdd:smart00644   1 PPPRGIVIHHTA---NSNASCANEARYMQNNHMN-----DIGYHFLVGGDGRVYQGVGWNYvawhaGGAHTPGYNDISIG 72

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....
gi 45553005    433 ITFLGTF-RRQEPTPKSLEACQLLIAQGVRLKKLKP--DYQLLGHRQITGTLMP 483
Cdd:smart00644  73 IEFIGSFdSDDEPFAEALYAALDLLAKLLKGAGLPPdgRYRIVGHRDVAPTEDP 126
Amidase_2 pfam01510
N-acetylmuramoyl-L-alanine amidase; This family includes zinc amidases that have ...
 358-485 5.89e-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: 5.89e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553005   358 PVSKVIISETppeICTTQDSCSYWTRVTQSRhmdtfNWSQVGYNFLVGGDGRIYEGRGWNYMGDHTRDN--NNNSIGITF 435
Cdd:pfam01510   1 PIRYIVIHHT---AGPSFAGALLPYAACIAR-----GWSDVSYHYLIDRDGTIYQLVPENGRAWHAGNGggNDRSIGIEL 72

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 45553005   436 LGTFRRQEPTPKSLEACQLLIAQGVRLKKLKPDYQLLGHRQITGTLMPGE 485
Cdd:pfam01510  73 EGNFGGDPPTDAQYEALARLLADLCKRYGIPPDRRIVGHRDVGRKTDPGP 122
PHA00447 PHA00447
lysozyme
 395-493 1.11e-08

lysozyme


Pssm-ID: 177282 [Multi-domain]  Cd Length: 142  Bit Score: 54.01  E-value: 1.11e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553005  395 WSQVGYNFLVGGDGRIYEGRGWNYMGDHTRDNNNNSIGITFLGTFRRQEP-----TPKSLEACQLLIaqgVRLKKLKPDY 469
Cdd:PHA00447  40 WLDVGYHFIIRRDGTVEEGRPEDVVGSHVKGYNSNSVGVCLVGGIDDKGKfdanfTPAQMQSLKSLL---VTLKAKYPGA 116

                         90       100
                 ....*....|....*....|....
gi 45553005  470 QLLGHRQITGTLMPGEELYRIIQT 493
Cdd:PHA00447 117 EIKAHHDVAPKACPSFDLQRWLKK 140
CwlA COG5632
N-acetylmuramoyl-L-alanine amidase CwlA [Cell wall/membrane/envelope biogenesis];
394-503 1.07e-03

N-acetylmuramoyl-L-alanine amidase CwlA [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 444359  Cd Length: 177  Bit Score: 39.95  E-value: 1.07e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553005 394 NWSQVGYNFLVGgDGRIYEGRGWNYM----GDHTRDNNNNSIGI----TFLGTFrrqeptPKSLEACQLLIAQGVRLKKL 465
Cdd:COG5632  49 NNRSASWHYFVD-DKEIIQHIPLNENawhaGDGTGPGNRRSIGIeiceNKDGDF------AKAYENAAELIAYLMKKYGI 121

                        90       100       110
                ....*....|....*....|....*....|....*...
gi 45553005 466 KPDyQLLGHRQITGTLMPGEELYRIIQTWNNWYNLTKT 503
Cdd:COG5632 122 PID-NVVRHYDWSGKNCPHGLLANGGYRWDQFKADVKS 158
 
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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