NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|260166616|ref|NP_997130|]
View 

peptidoglycan recognition protein 3 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

 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 ...
 185-325 5.16e-64

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: 199.83  E-value: 5.16e-64
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260166616   185 PNITPRSAW-EARETHCPQMNLPAKFVIIIHTAGKSCNESADCLVRVRDTQSFHIDNQDFCDIAYHFLVGQDGEVYEGVG 263
Cdd:smart00701   1 PPIVPRSEWgAKPRGHTPRLTRPVRYVIIHHTATPNCYTDAQCAQILRNIQAYHMEELGWCDIGYNFLVGGDGKVYEGRG 80

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 260166616   264 WNIEGSHTYGYNDIALGIAFMGNFVEKPPNEASLKAAQSLIQCAVAKGYLTSNYLLMGHSDV 325
Cdd:smart00701  81 WNVVGAHTGGYNDISLGIAFIGNFTDKLPTDAALDAAQDLLACAVQRGHLSPDYKLVGHRQV 142
PGRP smart00701
Animal peptidoglycan recognition proteins homologous to Bacteriophage T3 lysozyme; The ...
 28-160 1.39e-50

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: 165.16  E-value: 1.39e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260166616    28 PTIVSRKEWGASSLTCRVPLSLPVPYLIIEQVTRMQCQDQITCSQVVRVLQSQYVHNKGWCDIAFNFLVGDDGKVYEGVG 107
Cdd:smart00701   1 PPIVPRSEWGAKPRGHTPRLTRPVRYVIIHHTATPNCYTDAQCAQILRNIQAYHMEELGWCDIGYNFLVGGDGKVYEGRG 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....
gi 260166616   108 WYVQGLHTQGYNNVSLGIAFFGSKIGS-PSPAALSATEDLIFFAIQNGYLSPKY 160
Cdd:smart00701  81 WNVVGAHTGGYNDISLGIAFIGNFTDKlPTDAALDAAQDLLACAVQRGHLSPDY 134
 
Name Accession Description Interval E-value
PGRP smart00701
Animal peptidoglycan recognition proteins homologous to Bacteriophage T3 lysozyme; The ...
 185-325 5.16e-64

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: 199.83  E-value: 5.16e-64
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260166616   185 PNITPRSAW-EARETHCPQMNLPAKFVIIIHTAGKSCNESADCLVRVRDTQSFHIDNQDFCDIAYHFLVGQDGEVYEGVG 263
Cdd:smart00701   1 PPIVPRSEWgAKPRGHTPRLTRPVRYVIIHHTATPNCYTDAQCAQILRNIQAYHMEELGWCDIGYNFLVGGDGKVYEGRG 80

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 260166616   264 WNIEGSHTYGYNDIALGIAFMGNFVEKPPNEASLKAAQSLIQCAVAKGYLTSNYLLMGHSDV 325
Cdd:smart00701  81 WNVVGAHTGGYNDISLGIAFIGNFTDKLPTDAALDAAQDLLACAVQRGHLSPDYKLVGHRQV 142
PGRP smart00701
Animal peptidoglycan recognition proteins homologous to Bacteriophage T3 lysozyme; The ...
 28-160 1.39e-50

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: 165.16  E-value: 1.39e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260166616    28 PTIVSRKEWGASSLTCRVPLSLPVPYLIIEQVTRMQCQDQITCSQVVRVLQSQYVHNKGWCDIAFNFLVGDDGKVYEGVG 107
Cdd:smart00701   1 PPIVPRSEWGAKPRGHTPRLTRPVRYVIIHHTATPNCYTDAQCAQILRNIQAYHMEELGWCDIGYNFLVGGDGKVYEGRG 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....
gi 260166616   108 WYVQGLHTQGYNNVSLGIAFFGSKIGS-PSPAALSATEDLIFFAIQNGYLSPKY 160
Cdd:smart00701  81 WNVVGAHTGGYNDISLGIAFIGNFTDKlPTDAALDAAQDLLACAVQRGHLSPDY 134
PGRP cd06583
Peptidoglycan recognition proteins (PGRPs) are pattern recognition receptors that bind, and in ...
 206-334 5.34e-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: 134.72  E-value: 5.34e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260166616 206 PAKFVIIIHTAGKSCNESADClvrVRDTQSFHIDNqdFCDIAYHFLVGQDGEVYEGVGWNIEGSHTYG-YNDIALGIAFM 284
Cdd:cd06583    1 PVKYVVIHHTANPNCYTAAAA---VRYLQNYHMRG--WSDISYHFLVGGDGRIYQGRGWNYVGWHAGGnYNSYSIGIELI 75

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 260166616 285 GNFVEKPPNEASLKAAQSLIQCAVAKGYLTSNYLLMGHSDVSNI-LSPGQA 334
Cdd:cd06583   76 GNFDGGPPTAAQLEALAELLAYLVKRYGIPPDYRIVGHRDVSPGtECPGDA 126
Amidase_2 pfam01510
N-acetylmuramoyl-L-alanine amidase; This family includes zinc amidases that have ...
 206-333 6.61e-26

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: 100.12  E-value: 6.61e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260166616  206 PAKFVIIIHTAGKScneSADCLVRVRDTQsfhidNQDFCDIAYHFLVGQDGEVYEGVGWNIEGSHT--YGYNDIALGIAF 283
Cdd:pfam01510   1 PIRYIVIHHTAGPS---FAGALLPYAACI-----ARGWSDVSYHYLIDRDGTIYQLVPENGRAWHAgnGGGNDRSIGIEL 72

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 260166616  284 MGNFVEKPPNEASLKAAQSLIQCAVAKGYLTSNYLLMGHSDVSNILSPGQ 333
Cdd:pfam01510  73 EGNFGGDPPTDAQYEALARLLADLCKRYGIPPDRRIVGHRDVGRKTDPGP 122
PGRP cd06583
Peptidoglycan recognition proteins (PGRPs) are pattern recognition receptors that bind, and in ...
 69-185 1.02e-21

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: 88.88  E-value: 1.02e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260166616  69 TCSQVVRVLQSQyvHNKGWCDIAFNFLVGDDGKVYEGVGWYVQGLHTQG-YNNVSLGIAFFGSKIG-SPSPAALSATEDL 146
Cdd:cd06583   17 TAAAAVRYLQNY--HMRGWSDISYHFLVGGDGRIYQGRGWNYVGWHAGGnYNSYSIGIELIGNFDGgPPTAAQLEALAEL 94

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 260166616 147 IFFAIQNGYLSPKYiqpfllkeetCLVPqHSEI-PKKACP 185
Cdd:cd06583   95 LAYLVKRYGIPPDY----------RIVG-HRDVsPGTECP 123
Amidase_2 pfam01510
N-acetylmuramoyl-L-alanine amidase; This family includes zinc amidases that have ...
 83-185 2.75e-12

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: 63.14  E-value: 2.75e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260166616   83 HNKGWCDIAFNFLVGDDGKVYEGVGWYVQGLHT--QGYNNVSLGIAFFGSKIGSP-SPAALSATEDLIFFAIQNGYLSPK 159
Cdd:pfam01510  26 IARGWSDVSYHYLIDRDGTIYQLVPENGRAWHAgnGGGNDRSIGIELEGNFGGDPpTDAQYEALARLLADLCKRYGIPPD 105

                          90       100
                  ....*....|....*....|....*.
gi 260166616  160 YiqpfllkeetcLVPQHSEIPKKACP 185
Cdd:pfam01510 106 R-----------RIVGHRDVGRKTDP 120
PHA00447 PHA00447
lysozyme
 186-332 9.08e-10

lysozyme


Pssm-ID: 177282 [Multi-domain]  Cd Length: 142  Bit Score: 56.32  E-value: 9.08e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260166616 186 NITPRSAWEARETHC----PQMNlpakfviiihtagkscnesadclVRVRDTQSFHIDnQDFCDIAYHFLVGQDGEVYEG 261
Cdd:PHA00447   3 QFKPRSSTKAIFVHCsatkPSMD-----------------------VGVREIRQWHKE-QGWLDVGYHFIIRRDGTVEEG 58

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 260166616 262 VGWNIEGSHTYGYNDIALGIAFMGNFVEKPPNEASLKAAQ--SLIQCAVAKGYLTSNYLLMGHSDVSNILSPG 332
Cdd:PHA00447  59 RPEDVVGSHVKGYNSNSVGVCLVGGIDDKGKFDANFTPAQmqSLKSLLVTLKAKYPGAEIKAHHDVAPKACPS 131
PHA00447 PHA00447
lysozyme
 80-197 1.23e-06

lysozyme


Pssm-ID: 177282 [Multi-domain]  Cd Length: 142  Bit Score: 47.47  E-value: 1.23e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260166616  80 QYVHNKGWCDIAFNFLVGDDGKVYEGVGWYVQGLHTQGYNNVSLGIAFFG--SKIGSP----SPAALSATEDLIffaiqn 153
Cdd:PHA00447  33 QWHKEQGWLDVGYHFIIRRDGTVEEGRPEDVVGSHVKGYNSNSVGVCLVGgiDDKGKFdanfTPAQMQSLKSLL------ 106

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 260166616 154 GYLSPKYIQPFLLKeetclvpqHSEIPKKACPNITPRSAWEARE 197
Cdd:PHA00447 107 VTLKAKYPGAEIKA--------HHDVAPKACPSFDLQRWLKKNE 142
 
Name Accession Description Interval E-value
PGRP smart00701
Animal peptidoglycan recognition proteins homologous to Bacteriophage T3 lysozyme; The ...
 185-325 5.16e-64

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: 199.83  E-value: 5.16e-64
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260166616   185 PNITPRSAW-EARETHCPQMNLPAKFVIIIHTAGKSCNESADCLVRVRDTQSFHIDNQDFCDIAYHFLVGQDGEVYEGVG 263
Cdd:smart00701   1 PPIVPRSEWgAKPRGHTPRLTRPVRYVIIHHTATPNCYTDAQCAQILRNIQAYHMEELGWCDIGYNFLVGGDGKVYEGRG 80

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 260166616   264 WNIEGSHTYGYNDIALGIAFMGNFVEKPPNEASLKAAQSLIQCAVAKGYLTSNYLLMGHSDV 325
Cdd:smart00701  81 WNVVGAHTGGYNDISLGIAFIGNFTDKLPTDAALDAAQDLLACAVQRGHLSPDYKLVGHRQV 142
PGRP smart00701
Animal peptidoglycan recognition proteins homologous to Bacteriophage T3 lysozyme; The ...
 28-160 1.39e-50

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: 165.16  E-value: 1.39e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260166616    28 PTIVSRKEWGASSLTCRVPLSLPVPYLIIEQVTRMQCQDQITCSQVVRVLQSQYVHNKGWCDIAFNFLVGDDGKVYEGVG 107
Cdd:smart00701   1 PPIVPRSEWGAKPRGHTPRLTRPVRYVIIHHTATPNCYTDAQCAQILRNIQAYHMEELGWCDIGYNFLVGGDGKVYEGRG 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....
gi 260166616   108 WYVQGLHTQGYNNVSLGIAFFGSKIGS-PSPAALSATEDLIFFAIQNGYLSPKY 160
Cdd:smart00701  81 WNVVGAHTGGYNDISLGIAFIGNFTDKlPTDAALDAAQDLLACAVQRGHLSPDY 134
PGRP cd06583
Peptidoglycan recognition proteins (PGRPs) are pattern recognition receptors that bind, and in ...
 206-334 5.34e-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: 134.72  E-value: 5.34e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260166616 206 PAKFVIIIHTAGKSCNESADClvrVRDTQSFHIDNqdFCDIAYHFLVGQDGEVYEGVGWNIEGSHTYG-YNDIALGIAFM 284
Cdd:cd06583    1 PVKYVVIHHTANPNCYTAAAA---VRYLQNYHMRG--WSDISYHFLVGGDGRIYQGRGWNYVGWHAGGnYNSYSIGIELI 75

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 260166616 285 GNFVEKPPNEASLKAAQSLIQCAVAKGYLTSNYLLMGHSDVSNI-LSPGQA 334
Cdd:cd06583   76 GNFDGGPPTAAQLEALAELLAYLVKRYGIPPDYRIVGHRDVSPGtECPGDA 126
Ami_2 smart00644
Ami_2 domain;
210-331 1.18e-28

Ami_2 domain;


Pssm-ID: 214760 [Multi-domain]  Cd Length: 126  Bit Score: 107.44  E-value: 1.18e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260166616   210 VIIIHTAGkscNESADCLVRVRDTQSFHIDnqdfcDIAYHFLVGQDGEVYEGVGWN-----IEGSHTYGYNDIALGIAFM 284
Cdd:smart00644   5 GIVIHHTA---NSNASCANEARYMQNNHMN-----DIGYHFLVGGDGRVYQGVGWNyvawhAGGAHTPGYNDISIGIEFI 76

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 260166616   285 GNFVE-KPPNEASLKAAQSLIQCAVAKGYL--TSNYLLMGHSDVSNILSP 331
Cdd:smart00644  77 GSFDSdDEPFAEALYAALDLLAKLLKGAGLppDGRYRIVGHRDVAPTEDP 126
Amidase_2 pfam01510
N-acetylmuramoyl-L-alanine amidase; This family includes zinc amidases that have ...
 206-333 6.61e-26

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: 100.12  E-value: 6.61e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260166616  206 PAKFVIIIHTAGKScneSADCLVRVRDTQsfhidNQDFCDIAYHFLVGQDGEVYEGVGWNIEGSHT--YGYNDIALGIAF 283
Cdd:pfam01510   1 PIRYIVIHHTAGPS---FAGALLPYAACI-----ARGWSDVSYHYLIDRDGTIYQLVPENGRAWHAgnGGGNDRSIGIEL 72

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 260166616  284 MGNFVEKPPNEASLKAAQSLIQCAVAKGYLTSNYLLMGHSDVSNILSPGQ 333
Cdd:pfam01510  73 EGNFGGDPPTDAQYEALARLLADLCKRYGIPPDRRIVGHRDVGRKTDPGP 122
PGRP cd06583
Peptidoglycan recognition proteins (PGRPs) are pattern recognition receptors that bind, and in ...
 69-185 1.02e-21

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: 88.88  E-value: 1.02e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260166616  69 TCSQVVRVLQSQyvHNKGWCDIAFNFLVGDDGKVYEGVGWYVQGLHTQG-YNNVSLGIAFFGSKIG-SPSPAALSATEDL 146
Cdd:cd06583   17 TAAAAVRYLQNY--HMRGWSDISYHFLVGGDGRIYQGRGWNYVGWHAGGnYNSYSIGIELIGNFDGgPPTAAQLEALAEL 94

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 260166616 147 IFFAIQNGYLSPKYiqpfllkeetCLVPqHSEI-PKKACP 185
Cdd:cd06583   95 LAYLVKRYGIPPDY----------RIVG-HRDVsPGTECP 123
Ami_2 smart00644
Ami_2 domain;
50-185 2.56e-17

Ami_2 domain;


Pssm-ID: 214760 [Multi-domain]  Cd Length: 126  Bit Score: 77.01  E-value: 2.56e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260166616    50 PVPYLIIEQVTRMQCQdqiTCSQVVRVLQSQYVHnkgwcDIAFNFLVGDDGKVYEGVG-----WYVQGLHTQGYNNVSLG 124
Cdd:smart00644   1 PPPRGIVIHHTANSNA---SCANEARYMQNNHMN-----DIGYHFLVGGDGRVYQGVGwnyvaWHAGGAHTPGYNDISIG 72

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 260166616   125 IAFFGSKIGS--PSPAALSATEDLIFFAIQNGYLSPKYIQpfllkeetcLVPQHSEIPKKACP 185
Cdd:smart00644  73 IEFIGSFDSDdePFAEALYAALDLLAKLLKGAGLPPDGRY---------RIVGHRDVAPTEDP 126
Amidase_2 pfam01510
N-acetylmuramoyl-L-alanine amidase; This family includes zinc amidases that have ...
 83-185 2.75e-12

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: 63.14  E-value: 2.75e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260166616   83 HNKGWCDIAFNFLVGDDGKVYEGVGWYVQGLHT--QGYNNVSLGIAFFGSKIGSP-SPAALSATEDLIFFAIQNGYLSPK 159
Cdd:pfam01510  26 IARGWSDVSYHYLIDRDGTIYQLVPENGRAWHAgnGGGNDRSIGIELEGNFGGDPpTDAQYEALARLLADLCKRYGIPPD 105

                          90       100
                  ....*....|....*....|....*.
gi 260166616  160 YiqpfllkeetcLVPQHSEIPKKACP 185
Cdd:pfam01510 106 R-----------RIVGHRDVGRKTDP 120
PHA00447 PHA00447
lysozyme
 186-332 9.08e-10

lysozyme


Pssm-ID: 177282 [Multi-domain]  Cd Length: 142  Bit Score: 56.32  E-value: 9.08e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260166616 186 NITPRSAWEARETHC----PQMNlpakfviiihtagkscnesadclVRVRDTQSFHIDnQDFCDIAYHFLVGQDGEVYEG 261
Cdd:PHA00447   3 QFKPRSSTKAIFVHCsatkPSMD-----------------------VGVREIRQWHKE-QGWLDVGYHFIIRRDGTVEEG 58

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 260166616 262 VGWNIEGSHTYGYNDIALGIAFMGNFVEKPPNEASLKAAQ--SLIQCAVAKGYLTSNYLLMGHSDVSNILSPG 332
Cdd:PHA00447  59 RPEDVVGSHVKGYNSNSVGVCLVGGIDDKGKFDANFTPAQmqSLKSLLVTLKAKYPGAEIKAHHDVAPKACPS 131
PHA00447 PHA00447
lysozyme
 80-197 1.23e-06

lysozyme


Pssm-ID: 177282 [Multi-domain]  Cd Length: 142  Bit Score: 47.47  E-value: 1.23e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260166616  80 QYVHNKGWCDIAFNFLVGDDGKVYEGVGWYVQGLHTQGYNNVSLGIAFFG--SKIGSP----SPAALSATEDLIffaiqn 153
Cdd:PHA00447  33 QWHKEQGWLDVGYHFIIRRDGTVEEGRPEDVVGSHVKGYNSNSVGVCLVGgiDDKGKFdanfTPAQMQSLKSLL------ 106

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 260166616 154 GYLSPKYIQPFLLKeetclvpqHSEIPKKACPNITPRSAWEARE 197
Cdd:PHA00447 107 VTLKAKYPGAEIKA--------HHDVAPKACPSFDLQRWLKKNE 142
 
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