NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|767908235|ref|XP_011507420|]
View 

peptidoglycan recognition protein 3 isoform X1 [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

 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 ...
 215-355 7.25e-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: 205.22  E-value: 7.25e-66
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767908235   215 PNIIKRSAW-EARETHCPKMNLPAKYVIIIHTAGTSCTVSTDCQTVVRNIQSFHMDTRNFCDIGYHFLVGQDGGVYEGVG 293
Cdd:smart00701   1 PPIVPRSEWgAKPRGHTPRLTRPVRYVIIHHTATPNCYTDAQCAQILRNIQAYHMEELGWCDIGYNFLVGGDGKVYEGRG 80

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767908235   294 WHIQGSHTYGFNDIALGIAFIGYFVEKPPNAAALEAAQDLIQCAVVEGYLTPNYLLMGHSDV 355
Cdd:smart00701  81 WNVVGAHTGGYNDISLGIAFIGNFTDKLPTDAALDAAQDLLACAVQRGHLSPDYKLVGHRQV 142
PGRP smart00701
Animal peptidoglycan recognition proteins homologous to Bacteriophage T3 lysozyme; The ...
 57-195 3.10e-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: 162.46  E-value: 3.10e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767908235    57 PTIVSRKEWGARPLACRALLTLPVAYIITDQLPGMQCQQQSVCSQMLRGLQSHSVYTIGWCDVAYNFLVGDDGRVYEGVG 136
Cdd:smart00701   1 PPIVPRSEWGAKPRGHTPRLTRPVRYVIIHHTATPNCYTDAQCAQILRNIQAYHMEELGWCDIGYNFLVGGDGKVYEGRG 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 767908235   137 WNIQGLHTQGYNNISLGIAFFGNKIGSSPSPAALSAAEGLISYAIQKGHLSPRYIQPLL 195
Cdd:smart00701  81 WNVVGAHTGGYNDISLGIAFIGNFTDKLPTDAALDAAQDLLACAVQRGHLSPDYKLVGH 139
 
Name Accession Description Interval E-value
PGRP smart00701
Animal peptidoglycan recognition proteins homologous to Bacteriophage T3 lysozyme; The ...
 215-355 7.25e-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: 205.22  E-value: 7.25e-66
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767908235   215 PNIIKRSAW-EARETHCPKMNLPAKYVIIIHTAGTSCTVSTDCQTVVRNIQSFHMDTRNFCDIGYHFLVGQDGGVYEGVG 293
Cdd:smart00701   1 PPIVPRSEWgAKPRGHTPRLTRPVRYVIIHHTATPNCYTDAQCAQILRNIQAYHMEELGWCDIGYNFLVGGDGKVYEGRG 80

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767908235   294 WHIQGSHTYGFNDIALGIAFIGYFVEKPPNAAALEAAQDLIQCAVVEGYLTPNYLLMGHSDV 355
Cdd:smart00701  81 WNVVGAHTGGYNDISLGIAFIGNFTDKLPTDAALDAAQDLLACAVQRGHLSPDYKLVGHRQV 142
PGRP smart00701
Animal peptidoglycan recognition proteins homologous to Bacteriophage T3 lysozyme; The ...
 57-195 3.10e-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: 162.46  E-value: 3.10e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767908235    57 PTIVSRKEWGARPLACRALLTLPVAYIITDQLPGMQCQQQSVCSQMLRGLQSHSVYTIGWCDVAYNFLVGDDGRVYEGVG 136
Cdd:smart00701   1 PPIVPRSEWGAKPRGHTPRLTRPVRYVIIHHTATPNCYTDAQCAQILRNIQAYHMEELGWCDIGYNFLVGGDGKVYEGRG 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 767908235   137 WNIQGLHTQGYNNISLGIAFFGNKIGSSPSPAALSAAEGLISYAIQKGHLSPRYIQPLL 195
Cdd:smart00701  81 WNVVGAHTGGYNDISLGIAFIGNFTDKLPTDAALDAAQDLLACAVQRGHLSPDYKLVGH 139
PGRP cd06583
Peptidoglycan recognition proteins (PGRPs) are pattern recognition receptors that bind, and in ...
 236-364 2.63e-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: 141.66  E-value: 2.63e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767908235 236 PAKYVIIIHTAGTSCTvstDCQTVVRNIQSFHMdtRNFCDIGYHFLVGQDGGVYEGVGWHIQGSHTYG-FNDIALGIAFI 314
Cdd:cd06583    1 PVKYVVIHHTANPNCY---TAAAAVRYLQNYHM--RGWSDISYHFLVGGDGRIYQGRGWNYVGWHAGGnYNSYSIGIELI 75

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 767908235 315 GYFVEKPPNAAALEAAQDLIQCAVVEGYLTPNYLLMGHSDVVNI-LSPGQA 364
Cdd:cd06583   76 GNFDGGPPTAAQLEALAELLAYLVKRYGIPPDYRIVGHRDVSPGtECPGDA 126
Amidase_2 pfam01510
N-acetylmuramoyl-L-alanine amidase; This family includes zinc amidases that have ...
 236-363 3.49e-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: 98.58  E-value: 3.49e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767908235  236 PAKYVIIIHTAGTSCTVSTDCQtvvrniqsFHMDTRNFCDIGYHFLVGQDGGVYEGVGWHIQGSHT--YGFNDIALGIAF 313
Cdd:pfam01510   1 PIRYIVIHHTAGPSFAGALLPY--------AACIARGWSDVSYHYLIDRDGTIYQLVPENGRAWHAgnGGGNDRSIGIEL 72

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 767908235  314 IGYFVEKPPNAAALEAAQDLIQCAVVEGYLTPNYLLMGHSDVVNILSPGQ 363
Cdd:pfam01510  73 EGNFGGDPPTDAQYEALARLLADLCKRYGIPPDRRIVGHRDVGRKTDPGP 122
PGRP cd06583
Peptidoglycan recognition proteins (PGRPs) are pattern recognition receptors that bind, and in ...
 102-190 4.39e-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: 95.82  E-value: 4.39e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767908235 102 MLRGLQSHsvYTIGWCDVAYNFLVGDDGRVYEGVGWNIQGLHTQG-YNNISLGIAFFGNKIGSSPSPAALSAAEGLISYA 180
Cdd:cd06583   21 AVRYLQNY--HMRGWSDISYHFLVGGDGRIYQGRGWNYVGWHAGGnYNSYSIGIELIGNFDGGPPTAAQLEALAELLAYL 98

                         90
                 ....*....|
gi 767908235 181 IQKGHLSPRY 190
Cdd:cd06583   99 VKRYGIPPDY 108
Amidase_2 pfam01510
N-acetylmuramoyl-L-alanine amidase; This family includes zinc amidases that have ...
 115-190 7.62e-16

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: 73.16  E-value: 7.62e-16
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767908235  115 GWCDVAYNFLVGDDGRVYEGVGWNIQGLHT--QGYNNISLGIAFFGNKIGSSPSPAALSAAEGLISYAIQKGHLSPRY 190
Cdd:pfam01510  29 GWSDVSYHYLIDRDGTIYQLVPENGRAWHAgnGGGNDRSIGIELEGNFGGDPPTDAQYEALARLLADLCKRYGIPPDR 106
PHA00447 PHA00447
lysozyme
 241-362 1.45e-09

lysozyme


Pssm-ID: 177282 [Multi-domain]  Cd Length: 142  Bit Score: 55.94  E-value: 1.45e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767908235 241 IIIHtagtsCTVSTDCQTV-VRNIQSFHMDtRNFCDIGYHFLVGQDGGVYEGVGWHIQGSHTYGFNDIALGIAFIGYFVE 319
Cdd:PHA00447  13 IFVH-----CSATKPSMDVgVREIRQWHKE-QGWLDVGYHFIIRRDGTVEEGRPEDVVGSHVKGYNSNSVGVCLVGGIDD 86

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 767908235 320 KppnaAALEAAQDLIQCAVVEGYLT------PNYLLMGHSDVVNILSPG 362
Cdd:PHA00447  87 K----GKFDANFTPAQMQSLKSLLVtlkakyPGAEIKAHHDVAPKACPS 131
PHA00447 PHA00447
lysozyme
 115-158 3.51e-05

lysozyme


Pssm-ID: 177282 [Multi-domain]  Cd Length: 142  Bit Score: 43.23  E-value: 3.51e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 767908235 115 GWCDVAYNFLVGDDGRVYEGVGWNIQGLHTQGYNNISLGIAFFG 158
Cdd:PHA00447  39 GWLDVGYHFIIRRDGTVEEGRPEDVVGSHVKGYNSNSVGVCLVG 82
 
Name Accession Description Interval E-value
PGRP smart00701
Animal peptidoglycan recognition proteins homologous to Bacteriophage T3 lysozyme; The ...
 215-355 7.25e-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: 205.22  E-value: 7.25e-66
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767908235   215 PNIIKRSAW-EARETHCPKMNLPAKYVIIIHTAGTSCTVSTDCQTVVRNIQSFHMDTRNFCDIGYHFLVGQDGGVYEGVG 293
Cdd:smart00701   1 PPIVPRSEWgAKPRGHTPRLTRPVRYVIIHHTATPNCYTDAQCAQILRNIQAYHMEELGWCDIGYNFLVGGDGKVYEGRG 80

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767908235   294 WHIQGSHTYGFNDIALGIAFIGYFVEKPPNAAALEAAQDLIQCAVVEGYLTPNYLLMGHSDV 355
Cdd:smart00701  81 WNVVGAHTGGYNDISLGIAFIGNFTDKLPTDAALDAAQDLLACAVQRGHLSPDYKLVGHRQV 142
PGRP smart00701
Animal peptidoglycan recognition proteins homologous to Bacteriophage T3 lysozyme; The ...
 57-195 3.10e-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: 162.46  E-value: 3.10e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767908235    57 PTIVSRKEWGARPLACRALLTLPVAYIITDQLPGMQCQQQSVCSQMLRGLQSHSVYTIGWCDVAYNFLVGDDGRVYEGVG 136
Cdd:smart00701   1 PPIVPRSEWGAKPRGHTPRLTRPVRYVIIHHTATPNCYTDAQCAQILRNIQAYHMEELGWCDIGYNFLVGGDGKVYEGRG 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 767908235   137 WNIQGLHTQGYNNISLGIAFFGNKIGSSPSPAALSAAEGLISYAIQKGHLSPRYIQPLL 195
Cdd:smart00701  81 WNVVGAHTGGYNDISLGIAFIGNFTDKLPTDAALDAAQDLLACAVQRGHLSPDYKLVGH 139
PGRP cd06583
Peptidoglycan recognition proteins (PGRPs) are pattern recognition receptors that bind, and in ...
 236-364 2.63e-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: 141.66  E-value: 2.63e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767908235 236 PAKYVIIIHTAGTSCTvstDCQTVVRNIQSFHMdtRNFCDIGYHFLVGQDGGVYEGVGWHIQGSHTYG-FNDIALGIAFI 314
Cdd:cd06583    1 PVKYVVIHHTANPNCY---TAAAAVRYLQNYHM--RGWSDISYHFLVGGDGRIYQGRGWNYVGWHAGGnYNSYSIGIELI 75

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 767908235 315 GYFVEKPPNAAALEAAQDLIQCAVVEGYLTPNYLLMGHSDVVNI-LSPGQA 364
Cdd:cd06583   76 GNFDGGPPTAAQLEALAELLAYLVKRYGIPPDYRIVGHRDVSPGtECPGDA 126
Ami_2 smart00644
Ami_2 domain;
236-361 9.33e-32

Ami_2 domain;


Pssm-ID: 214760 [Multi-domain]  Cd Length: 126  Bit Score: 116.30  E-value: 9.33e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767908235   236 PAKYVIIIHTAGTSCTVstdCQTVVRNIQSFHMDtrnfcDIGYHFLVGQDGGVYEGVG-----WHIQGSHTYGFNDIALG 310
Cdd:smart00644   1 PPPRGIVIHHTANSNAS---CANEARYMQNNHMN-----DIGYHFLVGGDGRVYQGVGwnyvaWHAGGAHTPGYNDISIG 72

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....
gi 767908235   311 IAFIGYFVE-KPPNAAALEAAQDLIQCAVVEGYLTP--NYLLMGHSDVVNILSP 361
Cdd:smart00644  73 IEFIGSFDSdDEPFAEALYAALDLLAKLLKGAGLPPdgRYRIVGHRDVAPTEDP 126
Amidase_2 pfam01510
N-acetylmuramoyl-L-alanine amidase; This family includes zinc amidases that have ...
 236-363 3.49e-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: 98.58  E-value: 3.49e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767908235  236 PAKYVIIIHTAGTSCTVSTDCQtvvrniqsFHMDTRNFCDIGYHFLVGQDGGVYEGVGWHIQGSHT--YGFNDIALGIAF 313
Cdd:pfam01510   1 PIRYIVIHHTAGPSFAGALLPY--------AACIARGWSDVSYHYLIDRDGTIYQLVPENGRAWHAgnGGGNDRSIGIEL 72

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 767908235  314 IGYFVEKPPNAAALEAAQDLIQCAVVEGYLTPNYLLMGHSDVVNILSPGQ 363
Cdd:pfam01510  73 EGNFGGDPPTDAQYEALARLLADLCKRYGIPPDRRIVGHRDVGRKTDPGP 122
PGRP cd06583
Peptidoglycan recognition proteins (PGRPs) are pattern recognition receptors that bind, and in ...
 102-190 4.39e-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: 95.82  E-value: 4.39e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767908235 102 MLRGLQSHsvYTIGWCDVAYNFLVGDDGRVYEGVGWNIQGLHTQG-YNNISLGIAFFGNKIGSSPSPAALSAAEGLISYA 180
Cdd:cd06583   21 AVRYLQNY--HMRGWSDISYHFLVGGDGRIYQGRGWNYVGWHAGGnYNSYSIGIELIGNFDGGPPTAAQLEALAELLAYL 98

                         90
                 ....*....|
gi 767908235 181 IQKGHLSPRY 190
Cdd:cd06583   99 VKRYGIPPDY 108
Ami_2 smart00644
Ami_2 domain;
118-188 5.99e-17

Ami_2 domain;


Pssm-ID: 214760 [Multi-domain]  Cd Length: 126  Bit Score: 76.24  E-value: 5.99e-17
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767908235   118 DVAYNFLVGDDGRVYEGVGWN-----IQGLHTQGYNNISLGIAFFGNKIGS-SPSPAALSAAEGLISYAIQKGHLSP 188
Cdd:smart00644  32 DIGYHFLVGGDGRVYQGVGWNyvawhAGGAHTPGYNDISIGIEFIGSFDSDdEPFAEALYAALDLLAKLLKGAGLPP 108
Amidase_2 pfam01510
N-acetylmuramoyl-L-alanine amidase; This family includes zinc amidases that have ...
 115-190 7.62e-16

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: 73.16  E-value: 7.62e-16
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767908235  115 GWCDVAYNFLVGDDGRVYEGVGWNIQGLHT--QGYNNISLGIAFFGNKIGSSPSPAALSAAEGLISYAIQKGHLSPRY 190
Cdd:pfam01510  29 GWSDVSYHYLIDRDGTIYQLVPENGRAWHAgnGGGNDRSIGIELEGNFGGDPPTDAQYEALARLLADLCKRYGIPPDR 106
PHA00447 PHA00447
lysozyme
 241-362 1.45e-09

lysozyme


Pssm-ID: 177282 [Multi-domain]  Cd Length: 142  Bit Score: 55.94  E-value: 1.45e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767908235 241 IIIHtagtsCTVSTDCQTV-VRNIQSFHMDtRNFCDIGYHFLVGQDGGVYEGVGWHIQGSHTYGFNDIALGIAFIGYFVE 319
Cdd:PHA00447  13 IFVH-----CSATKPSMDVgVREIRQWHKE-QGWLDVGYHFIIRRDGTVEEGRPEDVVGSHVKGYNSNSVGVCLVGGIDD 86

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 767908235 320 KppnaAALEAAQDLIQCAVVEGYLT------PNYLLMGHSDVVNILSPG 362
Cdd:PHA00447  87 K----GKFDANFTPAQMQSLKSLLVtlkakyPGAEIKAHHDVAPKACPS 131
PHA00447 PHA00447
lysozyme
 115-158 3.51e-05

lysozyme


Pssm-ID: 177282 [Multi-domain]  Cd Length: 142  Bit Score: 43.23  E-value: 3.51e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 767908235 115 GWCDVAYNFLVGDDGRVYEGVGWNIQGLHTQGYNNISLGIAFFG 158
Cdd:PHA00447  39 GWLDVGYHFIIRRDGTVEEGRPEDVVGSHVKGYNSNSVGVCLVG 82
PBP2_XBP1_like cd14749
The periplasmic-binding component of ABC transport systems specific for xylo-oligosaccharides; ...
 278-372 6.11e-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: 6.11e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767908235 278 YHFLVGQDGGVYegvgWHIQGSHTYGFNDialgiafigyfvekPPNAAALEAAQDLiqcaVVEGYLTPNYLLMGHSDVVN 357
Cdd:cd14749  171 FQYLVRQAGGGP----LSDDGSGKATFND--------------PAFVQALQKLQDL----VKAGAFQEGFEGIDYDDAGQ 228

                         90
                 ....*....|....*
gi 767908235 358 ILSPGQALYNIISTW 372
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH