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Conserved domains on  [gi|16418405|ref|NP_443123|]
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peptidoglycan recognition protein 3 precursor [Homo sapiens]

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 ...
 179-319 5.44e-66

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: 204.45  E-value: 5.44e-66
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16418405    179 PNIIKRSAW-EARETHCPKMNLPAKYVIIIHTAGTSCTVSTDCQTVVRNIQSFHMDTRNFCDIGYHFLVGQDGGVYEGVG 257
Cdd:smart00701   1 PPIVPRSEWgAKPRGHTPRLTRPVRYVIIHHTATPNCYTDAQCAQILRNIQAYHMEELGWCDIGYNFLVGGDGKVYEGRG 80

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16418405    258 WHIQGSHTYGFNDIALGIAFIGYFVEKPPNAAALEAAQDLIQCAVVEGYLTPNYLLMGHSDV 319
Cdd:smart00701  81 WNVVGAHTGGYNDISLGIAFIGNFTDKLPTDAALDAAQDLLACAVQRGHLSPDYKLVGHRQV 142
PGRP smart00701
Animal peptidoglycan recognition proteins homologous to Bacteriophage T3 lysozyme; The ...
 21-159 1.95e-49

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: 162.08  E-value: 1.95e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16418405     21 PTIVSRKEWGARPLACRALLTLPVAYIITDQLPGMQCQQQSVCSQMLRGLQSHSVYTIGWCDVAYNFLVGDDGRVYEGVG 100
Cdd:smart00701   1 PPIVPRSEWGAKPRGHTPRLTRPVRYVIIHHTATPNCYTDAQCAQILRNIQAYHMEELGWCDIGYNFLVGGDGKVYEGRG 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 16418405    101 WNIQGLHTQGYNNISLGIAFFGNKIGSSPSPAALSAAEGLISYAIQKGHLSPRYIQPLL 159
Cdd:smart00701  81 WNVVGAHTGGYNDISLGIAFIGNFTDKLPTDAALDAAQDLLACAVQRGHLSPDYKLVGH 139
 
Name Accession Description Interval E-value
PGRP smart00701
Animal peptidoglycan recognition proteins homologous to Bacteriophage T3 lysozyme; The ...
 179-319 5.44e-66

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: 204.45  E-value: 5.44e-66
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16418405    179 PNIIKRSAW-EARETHCPKMNLPAKYVIIIHTAGTSCTVSTDCQTVVRNIQSFHMDTRNFCDIGYHFLVGQDGGVYEGVG 257
Cdd:smart00701   1 PPIVPRSEWgAKPRGHTPRLTRPVRYVIIHHTATPNCYTDAQCAQILRNIQAYHMEELGWCDIGYNFLVGGDGKVYEGRG 80

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16418405    258 WHIQGSHTYGFNDIALGIAFIGYFVEKPPNAAALEAAQDLIQCAVVEGYLTPNYLLMGHSDV 319
Cdd:smart00701  81 WNVVGAHTGGYNDISLGIAFIGNFTDKLPTDAALDAAQDLLACAVQRGHLSPDYKLVGHRQV 142
PGRP smart00701
Animal peptidoglycan recognition proteins homologous to Bacteriophage T3 lysozyme; The ...
 21-159 1.95e-49

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: 162.08  E-value: 1.95e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16418405     21 PTIVSRKEWGARPLACRALLTLPVAYIITDQLPGMQCQQQSVCSQMLRGLQSHSVYTIGWCDVAYNFLVGDDGRVYEGVG 100
Cdd:smart00701   1 PPIVPRSEWGAKPRGHTPRLTRPVRYVIIHHTATPNCYTDAQCAQILRNIQAYHMEELGWCDIGYNFLVGGDGKVYEGRG 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 16418405    101 WNIQGLHTQGYNNISLGIAFFGNKIGSSPSPAALSAAEGLISYAIQKGHLSPRYIQPLL 159
Cdd:smart00701  81 WNVVGAHTGGYNDISLGIAFIGNFTDKLPTDAALDAAQDLLACAVQRGHLSPDYKLVGH 139
PGRP cd06583
Peptidoglycan recognition proteins (PGRPs) are pattern recognition receptors that bind, and in ...
 200-328 4.46e-41

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: 140.12  E-value: 4.46e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16418405 200 PAKYVIIIHTAGTSCTvstDCQTVVRNIQSFHMdtRNFCDIGYHFLVGQDGGVYEGVGWHIQGSHTYG-FNDIALGIAFI 278
Cdd:cd06583   1 PVKYVVIHHTANPNCY---TAAAAVRYLQNYHM--RGWSDISYHFLVGGDGRIYQGRGWNYVGWHAGGnYNSYSIGIELI 75

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|.
gi 16418405 279 GYFVEKPPNAAALEAAQDLIQCAVVEGYLTPNYLLMGHSDVVNI-LSPGQA 328
Cdd:cd06583  76 GNFDGGPPTAAQLEALAELLAYLVKRYGIPPDYRIVGHRDVSPGtECPGDA 126
Amidase_2 pfam01510
N-acetylmuramoyl-L-alanine amidase; This family includes zinc amidases that have ...
 200-327 5.12e-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: 97.81  E-value: 5.12e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16418405   200 PAKYVIIIHTAGTSCTVSTDCQtvvrniqsFHMDTRNFCDIGYHFLVGQDGGVYEGVGWHIQGSHT--YGFNDIALGIAF 277
Cdd:pfam01510   1 PIRYIVIHHTAGPSFAGALLPY--------AACIARGWSDVSYHYLIDRDGTIYQLVPENGRAWHAgnGGGNDRSIGIEL 72

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 16418405   278 IGYFVEKPPNAAALEAAQDLIQCAVVEGYLTPNYLLMGHSDVVNILSPGQ 327
Cdd:pfam01510  73 EGNFGGDPPTDAQYEALARLLADLCKRYGIPPDRRIVGHRDVGRKTDPGP 122
PGRP cd06583
Peptidoglycan recognition proteins (PGRPs) are pattern recognition receptors that bind, and in ...
 66-154 6.45e-24

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: 95.05  E-value: 6.45e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16418405  66 MLRGLQSHsvYTIGWCDVAYNFLVGDDGRVYEGVGWNIQGLHTQG-YNNISLGIAFFGNKIGSSPSPAALSAAEGLISYA 144
Cdd:cd06583  21 AVRYLQNY--HMRGWSDISYHFLVGGDGRIYQGRGWNYVGWHAGGnYNSYSIGIELIGNFDGGPPTAAQLEALAELLAYL 98

                        90
                ....*....|
gi 16418405 145 IQKGHLSPRY 154
Cdd:cd06583  99 VKRYGIPPDY 108
Amidase_2 pfam01510
N-acetylmuramoyl-L-alanine amidase; This family includes zinc amidases that have ...
 79-154 1.03e-15

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: 72.39  E-value: 1.03e-15
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16418405    79 GWCDVAYNFLVGDDGRVYEGVGWNIQGLHT--QGYNNISLGIAFFGNKIGSSPSPAALSAAEGLISYAIQKGHLSPRY 154
Cdd:pfam01510  29 GWSDVSYHYLIDRDGTIYQLVPENGRAWHAgnGGGNDRSIGIELEGNFGGDPPTDAQYEALARLLADLCKRYGIPPDR 106
PHA00447 PHA00447
lysozyme
 205-326 1.25e-09

lysozyme


Pssm-ID: 177282 [Multi-domain]  Cd Length: 142  Bit Score: 55.94  E-value: 1.25e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16418405  205 IIIHtagtsCTVSTDCQTV-VRNIQSFHMDtRNFCDIGYHFLVGQDGGVYEGVGWHIQGSHTYGFNDIALGIAFIGYFVE 283
Cdd:PHA00447  13 IFVH-----CSATKPSMDVgVREIRQWHKE-QGWLDVGYHFIIRRDGTVEEGRPEDVVGSHVKGYNSNSVGVCLVGGIDD 86

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 16418405  284 KppnaAALEAAQDLIQCAVVEGYLT------PNYLLMGHSDVVNILSPG 326
Cdd:PHA00447  87 K----GKFDANFTPAQMQSLKSLLVtlkakyPGAEIKAHHDVAPKACPS 131
PHA00447 PHA00447
lysozyme
 79-122 3.08e-05

lysozyme


Pssm-ID: 177282 [Multi-domain]  Cd Length: 142  Bit Score: 43.23  E-value: 3.08e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 16418405   79 GWCDVAYNFLVGDDGRVYEGVGWNIQGLHTQGYNNISLGIAFFG 122
Cdd:PHA00447  39 GWLDVGYHFIIRRDGTVEEGRPEDVVGSHVKGYNSNSVGVCLVG 82
 
Name Accession Description Interval E-value
PGRP smart00701
Animal peptidoglycan recognition proteins homologous to Bacteriophage T3 lysozyme; The ...
 179-319 5.44e-66

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: 204.45  E-value: 5.44e-66
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16418405    179 PNIIKRSAW-EARETHCPKMNLPAKYVIIIHTAGTSCTVSTDCQTVVRNIQSFHMDTRNFCDIGYHFLVGQDGGVYEGVG 257
Cdd:smart00701   1 PPIVPRSEWgAKPRGHTPRLTRPVRYVIIHHTATPNCYTDAQCAQILRNIQAYHMEELGWCDIGYNFLVGGDGKVYEGRG 80

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16418405    258 WHIQGSHTYGFNDIALGIAFIGYFVEKPPNAAALEAAQDLIQCAVVEGYLTPNYLLMGHSDV 319
Cdd:smart00701  81 WNVVGAHTGGYNDISLGIAFIGNFTDKLPTDAALDAAQDLLACAVQRGHLSPDYKLVGHRQV 142
PGRP smart00701
Animal peptidoglycan recognition proteins homologous to Bacteriophage T3 lysozyme; The ...
 21-159 1.95e-49

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: 162.08  E-value: 1.95e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16418405     21 PTIVSRKEWGARPLACRALLTLPVAYIITDQLPGMQCQQQSVCSQMLRGLQSHSVYTIGWCDVAYNFLVGDDGRVYEGVG 100
Cdd:smart00701   1 PPIVPRSEWGAKPRGHTPRLTRPVRYVIIHHTATPNCYTDAQCAQILRNIQAYHMEELGWCDIGYNFLVGGDGKVYEGRG 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 16418405    101 WNIQGLHTQGYNNISLGIAFFGNKIGSSPSPAALSAAEGLISYAIQKGHLSPRYIQPLL 159
Cdd:smart00701  81 WNVVGAHTGGYNDISLGIAFIGNFTDKLPTDAALDAAQDLLACAVQRGHLSPDYKLVGH 139
PGRP cd06583
Peptidoglycan recognition proteins (PGRPs) are pattern recognition receptors that bind, and in ...
 200-328 4.46e-41

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: 140.12  E-value: 4.46e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16418405 200 PAKYVIIIHTAGTSCTvstDCQTVVRNIQSFHMdtRNFCDIGYHFLVGQDGGVYEGVGWHIQGSHTYG-FNDIALGIAFI 278
Cdd:cd06583   1 PVKYVVIHHTANPNCY---TAAAAVRYLQNYHM--RGWSDISYHFLVGGDGRIYQGRGWNYVGWHAGGnYNSYSIGIELI 75

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|.
gi 16418405 279 GYFVEKPPNAAALEAAQDLIQCAVVEGYLTPNYLLMGHSDVVNI-LSPGQA 328
Cdd:cd06583  76 GNFDGGPPTAAQLEALAELLAYLVKRYGIPPDYRIVGHRDVSPGtECPGDA 126
Ami_2 smart00644
Ami_2 domain;
200-325 1.26e-31

Ami_2 domain;


Pssm-ID: 214760 [Multi-domain]  Cd Length: 126  Bit Score: 115.15  E-value: 1.26e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16418405    200 PAKYVIIIHTAGTSCTVstdCQTVVRNIQSFHMDtrnfcDIGYHFLVGQDGGVYEGVG-----WHIQGSHTYGFNDIALG 274
Cdd:smart00644   1 PPPRGIVIHHTANSNAS---CANEARYMQNNHMN-----DIGYHFLVGGDGRVYQGVGwnyvaWHAGGAHTPGYNDISIG 72

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....
gi 16418405    275 IAFIGYFVE-KPPNAAALEAAQDLIQCAVVEGYLTP--NYLLMGHSDVVNILSP 325
Cdd:smart00644  73 IEFIGSFDSdDEPFAEALYAALDLLAKLLKGAGLPPdgRYRIVGHRDVAPTEDP 126
Amidase_2 pfam01510
N-acetylmuramoyl-L-alanine amidase; This family includes zinc amidases that have ...
 200-327 5.12e-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: 97.81  E-value: 5.12e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16418405   200 PAKYVIIIHTAGTSCTVSTDCQtvvrniqsFHMDTRNFCDIGYHFLVGQDGGVYEGVGWHIQGSHT--YGFNDIALGIAF 277
Cdd:pfam01510   1 PIRYIVIHHTAGPSFAGALLPY--------AACIARGWSDVSYHYLIDRDGTIYQLVPENGRAWHAgnGGGNDRSIGIEL 72

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 16418405   278 IGYFVEKPPNAAALEAAQDLIQCAVVEGYLTPNYLLMGHSDVVNILSPGQ 327
Cdd:pfam01510  73 EGNFGGDPPTDAQYEALARLLADLCKRYGIPPDRRIVGHRDVGRKTDPGP 122
PGRP cd06583
Peptidoglycan recognition proteins (PGRPs) are pattern recognition receptors that bind, and in ...
 66-154 6.45e-24

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: 95.05  E-value: 6.45e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16418405  66 MLRGLQSHsvYTIGWCDVAYNFLVGDDGRVYEGVGWNIQGLHTQG-YNNISLGIAFFGNKIGSSPSPAALSAAEGLISYA 144
Cdd:cd06583  21 AVRYLQNY--HMRGWSDISYHFLVGGDGRIYQGRGWNYVGWHAGGnYNSYSIGIELIGNFDGGPPTAAQLEALAELLAYL 98

                        90
                ....*....|
gi 16418405 145 IQKGHLSPRY 154
Cdd:cd06583  99 VKRYGIPPDY 108
Ami_2 smart00644
Ami_2 domain;
82-152 7.70e-17

Ami_2 domain;


Pssm-ID: 214760 [Multi-domain]  Cd Length: 126  Bit Score: 75.86  E-value: 7.70e-17
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16418405     82 DVAYNFLVGDDGRVYEGVGWN-----IQGLHTQGYNNISLGIAFFGNKIGS-SPSPAALSAAEGLISYAIQKGHLSP 152
Cdd:smart00644  32 DIGYHFLVGGDGRVYQGVGWNyvawhAGGAHTPGYNDISIGIEFIGSFDSDdEPFAEALYAALDLLAKLLKGAGLPP 108
Amidase_2 pfam01510
N-acetylmuramoyl-L-alanine amidase; This family includes zinc amidases that have ...
 79-154 1.03e-15

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: 72.39  E-value: 1.03e-15
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16418405    79 GWCDVAYNFLVGDDGRVYEGVGWNIQGLHT--QGYNNISLGIAFFGNKIGSSPSPAALSAAEGLISYAIQKGHLSPRY 154
Cdd:pfam01510  29 GWSDVSYHYLIDRDGTIYQLVPENGRAWHAgnGGGNDRSIGIELEGNFGGDPPTDAQYEALARLLADLCKRYGIPPDR 106
PHA00447 PHA00447
lysozyme
 205-326 1.25e-09

lysozyme


Pssm-ID: 177282 [Multi-domain]  Cd Length: 142  Bit Score: 55.94  E-value: 1.25e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16418405  205 IIIHtagtsCTVSTDCQTV-VRNIQSFHMDtRNFCDIGYHFLVGQDGGVYEGVGWHIQGSHTYGFNDIALGIAFIGYFVE 283
Cdd:PHA00447  13 IFVH-----CSATKPSMDVgVREIRQWHKE-QGWLDVGYHFIIRRDGTVEEGRPEDVVGSHVKGYNSNSVGVCLVGGIDD 86

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 16418405  284 KppnaAALEAAQDLIQCAVVEGYLT------PNYLLMGHSDVVNILSPG 326
Cdd:PHA00447  87 K----GKFDANFTPAQMQSLKSLLVtlkakyPGAEIKAHHDVAPKACPS 131
PHA00447 PHA00447
lysozyme
 79-122 3.08e-05

lysozyme


Pssm-ID: 177282 [Multi-domain]  Cd Length: 142  Bit Score: 43.23  E-value: 3.08e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 16418405   79 GWCDVAYNFLVGDDGRVYEGVGWNIQGLHTQGYNNISLGIAFFG 122
Cdd:PHA00447  39 GWLDVGYHFIIRRDGTVEEGRPEDVVGSHVKGYNSNSVGVCLVG 82
PBP2_XBP1_like cd14749
The periplasmic-binding component of ABC transport systems specific for xylo-oligosaccharides; ...
 242-336 5.16e-04

The periplasmic-binding component of ABC transport systems specific for xylo-oligosaccharides; possesses type 2 periplasmic binding fold; This group represents the periplasmic component of an ABC transport system XBP1 that shows preference for xylo-oligosaccharides in the order of xylotriose > xylobiose > xylotetraose. Members of this group belong to the type 2 periplasmic-binding fold superfamily. PBP2 proteins are comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. The majority of PBP2 proteins function in the uptake of small soluble substrates in eubacteria and archaea. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis.


Pssm-ID: 270452 [Multi-domain]  Cd Length: 388  Bit Score: 41.60  E-value: 5.16e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16418405 242 YHFLVGQDGGVYegvgWHIQGSHTYGFNDialgiafigyfvekPPNAAALEAAQDLiqcaVVEGYLTPNYLLMGHSDVVN 321
Cdd:cd14749 171 FQYLVRQAGGGP----LSDDGSGKATFND--------------PAFVQALQKLQDL----VKAGAFQEGFEGIDYDDAGQ 228

                        90
                ....*....|....*
gi 16418405 322 ILSPGQALYNIISTW 336
Cdd:cd14749 229 AFAQGKAAMNIGGSW 243
 
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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