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Conserved domains on  [gi|1891217698|gb|QNF93710|]
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peptidoglycan recognition protein [Janibacter sp. YB324]

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 ...
 195-351 5.26e-43

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: 148.98  E-value: 5.26e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891217698  195 PTIHSRAEWGAdESIRKGDPDYGEVRGAVLHHTAGVNGYSREEVPAIMRGIYEFHVNGRGWNDIGYNVLVDRFGRLWEGR 274
Cdd:smart00701   1 PPIVPRSEWGA-KPRGHTPRLTRPVRYVIIHHTATPNCYTDAQCAQILRNIQAYHMEELGWCDIGYNFLVGGDGKVYEGR 79

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1891217698  275 AGGvdkaVVGAHAQGVNSQTFGISAMGDYDQTAAPDAMTTSIERLMAWKLARHHVDPTAKatiggewlptVVGHRSV 351
Cdd:smart00701  80 GWN----VVGAHTGGYNDISLGIAFIGNFTDKLPTDAALDAAQDLLACAVQRGHLSPDYK----------LVGHRQV 142
 
Name Accession Description Interval E-value
PGRP smart00701
Animal peptidoglycan recognition proteins homologous to Bacteriophage T3 lysozyme; The ...
 195-351 5.26e-43

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: 148.98  E-value: 5.26e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891217698  195 PTIHSRAEWGAdESIRKGDPDYGEVRGAVLHHTAGVNGYSREEVPAIMRGIYEFHVNGRGWNDIGYNVLVDRFGRLWEGR 274
Cdd:smart00701   1 PPIVPRSEWGA-KPRGHTPRLTRPVRYVIIHHTATPNCYTDAQCAQILRNIQAYHMEELGWCDIGYNFLVGGDGKVYEGR 79

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1891217698  275 AGGvdkaVVGAHAQGVNSQTFGISAMGDYDQTAAPDAMTTSIERLMAWKLARHHVDPTAKatiggewlptVVGHRSV 351
Cdd:smart00701  80 GWN----VVGAHTGGYNDISLGIAFIGNFTDKLPTDAALDAAQDLLACAVQRGHLSPDYK----------LVGHRQV 142
PGRP cd06583
Peptidoglycan recognition proteins (PGRPs) are pattern recognition receptors that bind, and in ...
 219-360 4.45e-30

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: 113.54  E-value: 4.45e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891217698 219 VRGAVLHHTAGVNGYSreeVPAIMRGIYEFHVngRGWNDIGYNVLVDRFGRLWEGRaggvDKAVVGAHAQG-VNSQTFGI 297
Cdd:cd06583     2 VKYVVIHHTANPNCYT---AAAAVRYLQNYHM--RGWSDISYHFLVGGDGRIYQGR----GWNYVGWHAGGnYNSYSIGI 72

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1891217698 298 SAMGDYDQTAAPDAMTTSIERLMAWKLARHHVDPtakatiggewLPTVVGHRSV-GQTTCPGQY 360
Cdd:cd06583    73 ELIGNFDGGPPTAAQLEALAELLAYLVKRYGIPP----------DYRIVGHRDVsPGTECPGDA 126
Amidase_2 pfam01510
N-acetylmuramoyl-L-alanine amidase; This family includes zinc amidases that have ...
 219-359 2.91e-22

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: 91.65  E-value: 2.91e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891217698 219 VRGAVLHHTAGVNGYSREevpaimrgIYEFHVNGRGWNDIGYNVLVDRFGRLWE-----GRAGGvdkavvgAHAQGVNSQ 293
Cdd:pfam01510   2 IRYIVIHHTAGPSFAGAL--------LPYAACIARGWSDVSYHYLIDRDGTIYQlvpenGRAWH-------AGNGGGNDR 66

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1891217698 294 TFGISAMGDYDQTAAPDAMTTSIERLMAWKLARHHVDPTakatiggewlPTVVGHRSVGQTTCPGQ 359
Cdd:pfam01510  67 SIGIELEGNFGGDPPTDAQYEALARLLADLCKRYGIPPD----------RRIVGHRDVGRKTDPGP 122
PHA00447 PHA00447
lysozyme
 243-358 8.83e-10

lysozyme


Pssm-ID: 177282 [Multi-domain]  Cd Length: 142  Bit Score: 57.10  E-value: 8.83e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891217698 243 RGIYEFHVNgRGWNDIGYNVLVDRFGRLWEGRaggvDKAVVGAHAQGVNSQTFGISAMGDYDQTAAPDAMTT-----SIE 317
Cdd:PHA00447   29 REIRQWHKE-QGWLDVGYHFIIRRDGTVEEGR----PEDVVGSHVKGYNSNSVGVCLVGGIDDKGKFDANFTpaqmqSLK 103

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1891217698 318 RLMAWKLARHhvdPTAKatiggewlptVVGHRSVGQTTCPG 358
Cdd:PHA00447  104 SLLVTLKAKY---PGAE----------IKAHHDVAPKACPS 131
Psp3 COG5479
LGFP repeat-containing protein, may be involved in cell wall binding [Cell wall/membrane ...
 199-287 1.99e-04

LGFP repeat-containing protein, may be involved in cell wall binding [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 444230 [Multi-domain]  Cd Length: 246  Bit Score: 42.80  E-value: 1.99e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891217698 199 SRAEWGAD--ESIRKGDPDYGEVR-----------GAVLHHTAGVNGYSreeVPAIMRGIYEFHvngrGWND--IGYNVL 263
Cdd:COG5479    88 IRAKWGALgwESGPLGYPTTDEVPtpgggryqtfqGGSVYWTAGTGAHA---VHGAIRGKYAYH----GWEDgpLGYPTS 160

                          90       100       110
                  ....*....|....*....|....*....|
gi 1891217698 264 VDRFGRLWEGR-----AGGVD-KAVVGAHA 287
Cdd:COG5479   161 DEKATPDGGGRyqifeGGGIYwSPATGAHA 190
 
Name Accession Description Interval E-value
PGRP smart00701
Animal peptidoglycan recognition proteins homologous to Bacteriophage T3 lysozyme; The ...
 195-351 5.26e-43

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: 148.98  E-value: 5.26e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891217698  195 PTIHSRAEWGAdESIRKGDPDYGEVRGAVLHHTAGVNGYSREEVPAIMRGIYEFHVNGRGWNDIGYNVLVDRFGRLWEGR 274
Cdd:smart00701   1 PPIVPRSEWGA-KPRGHTPRLTRPVRYVIIHHTATPNCYTDAQCAQILRNIQAYHMEELGWCDIGYNFLVGGDGKVYEGR 79

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1891217698  275 AGGvdkaVVGAHAQGVNSQTFGISAMGDYDQTAAPDAMTTSIERLMAWKLARHHVDPTAKatiggewlptVVGHRSV 351
Cdd:smart00701  80 GWN----VVGAHTGGYNDISLGIAFIGNFTDKLPTDAALDAAQDLLACAVQRGHLSPDYK----------LVGHRQV 142
PGRP cd06583
Peptidoglycan recognition proteins (PGRPs) are pattern recognition receptors that bind, and in ...
 219-360 4.45e-30

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: 113.54  E-value: 4.45e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891217698 219 VRGAVLHHTAGVNGYSreeVPAIMRGIYEFHVngRGWNDIGYNVLVDRFGRLWEGRaggvDKAVVGAHAQG-VNSQTFGI 297
Cdd:cd06583     2 VKYVVIHHTANPNCYT---AAAAVRYLQNYHM--RGWSDISYHFLVGGDGRIYQGR----GWNYVGWHAGGnYNSYSIGI 72

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1891217698 298 SAMGDYDQTAAPDAMTTSIERLMAWKLARHHVDPtakatiggewLPTVVGHRSV-GQTTCPGQY 360
Cdd:cd06583    73 ELIGNFDGGPPTAAQLEALAELLAYLVKRYGIPP----------DYRIVGHRDVsPGTECPGDA 126
Amidase_2 pfam01510
N-acetylmuramoyl-L-alanine amidase; This family includes zinc amidases that have ...
 219-359 2.91e-22

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: 91.65  E-value: 2.91e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891217698 219 VRGAVLHHTAGVNGYSREevpaimrgIYEFHVNGRGWNDIGYNVLVDRFGRLWE-----GRAGGvdkavvgAHAQGVNSQ 293
Cdd:pfam01510   2 IRYIVIHHTAGPSFAGAL--------LPYAACIARGWSDVSYHYLIDRDGTIYQlvpenGRAWH-------AGNGGGNDR 66

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1891217698 294 TFGISAMGDYDQTAAPDAMTTSIERLMAWKLARHHVDPTakatiggewlPTVVGHRSVGQTTCPGQ 359
Cdd:pfam01510  67 SIGIELEGNFGGDPPTDAQYEALARLLADLCKRYGIPPD----------RRIVGHRDVGRKTDPGP 122
Ami_2 smart00644
Ami_2 domain;
217-357 1.87e-17

Ami_2 domain;


Pssm-ID: 214760 [Multi-domain]  Cd Length: 126  Bit Score: 78.55  E-value: 1.87e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891217698  217 GEVRGAVLHHTAGvngySREEVPAIMRGIYEFHvngrgWNDIGYNVLVDRFGRLWEGRAGG-VDKAVVGAHAQGVNSQTF 295
Cdd:smart00644   1 PPPRGIVIHHTAN----SNASCANEARYMQNNH-----MNDIGYHFLVGGDGRVYQGVGWNyVAWHAGGAHTPGYNDISI 71

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1891217698  296 GISAMGDYDQTAAP--DAMTTSIERLmaWKLARHHVDPTAkatiggeWLPTVVGHRSVGQTTCP 357
Cdd:smart00644  72 GIEFIGSFDSDDEPfaEALYAALDLL--AKLLKGAGLPPD-------GRYRIVGHRDVAPTEDP 126
PHA00447 PHA00447
lysozyme
 243-358 8.83e-10

lysozyme


Pssm-ID: 177282 [Multi-domain]  Cd Length: 142  Bit Score: 57.10  E-value: 8.83e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891217698 243 RGIYEFHVNgRGWNDIGYNVLVDRFGRLWEGRaggvDKAVVGAHAQGVNSQTFGISAMGDYDQTAAPDAMTT-----SIE 317
Cdd:PHA00447   29 REIRQWHKE-QGWLDVGYHFIIRRDGTVEEGR----PEDVVGSHVKGYNSNSVGVCLVGGIDDKGKFDANFTpaqmqSLK 103

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1891217698 318 RLMAWKLARHhvdPTAKatiggewlptVVGHRSVGQTTCPG 358
Cdd:PHA00447  104 SLLVTLKAKY---PGAE----------IKAHHDVAPKACPS 131
Psp3 COG5479
LGFP repeat-containing protein, may be involved in cell wall binding [Cell wall/membrane ...
 199-287 1.99e-04

LGFP repeat-containing protein, may be involved in cell wall binding [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 444230 [Multi-domain]  Cd Length: 246  Bit Score: 42.80  E-value: 1.99e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891217698 199 SRAEWGAD--ESIRKGDPDYGEVR-----------GAVLHHTAGVNGYSreeVPAIMRGIYEFHvngrGWND--IGYNVL 263
Cdd:COG5479    88 IRAKWGALgwESGPLGYPTTDEVPtpgggryqtfqGGSVYWTAGTGAHA---VHGAIRGKYAYH----GWEDgpLGYPTS 160

                          90       100       110
                  ....*....|....*....|....*....|
gi 1891217698 264 VDRFGRLWEGR-----AGGVD-KAVVGAHA 287
Cdd:COG5479   161 DEKATPDGGGRyqifeGGGIYwSPATGAHA 190
 
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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