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Conserved domains on  [gi|1622895099|ref|XP_001111934|]
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N-acetylmuramoyl-L-alanine amidase [Macaca mulatta]

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 ...
380-525 9.26e-63

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: 202.91  E-value: 9.26e-63
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622895099  380 PAIHPRCRWGAAPyQGRPTPLQLPLGFLYVHHTYVPAppCTDFARCAANMRSMQRYHQDTQGWEDIGYSFVVGSDGYVYE 459
Cdd:smart00701   1 PPIVPRSEWGAKP-RGHTPRLTRPVRYVIIHHTATPN--CYTDAQCAQILRNIQAYHMEELGWCDIGYNFLVGGDGKVYE 77
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622895099  460 GRGWHWVGAHTLGHNSRGFGVAIVGNYTAALPTEAALRTVRDTLPsCAVRAGLLRPDYALLGHRQL 525
Cdd:smart00701  78 GRGWNVVGAHTGGYNDISLGIAFIGNFTDKLPTDAALDAAQDLLA-CAVQRGHLSPDYKLVGHRQV 142
 
Name Accession Description Interval E-value
PGRP smart00701
Animal peptidoglycan recognition proteins homologous to Bacteriophage T3 lysozyme; The ...
380-525 9.26e-63

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: 202.91  E-value: 9.26e-63
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622895099  380 PAIHPRCRWGAAPyQGRPTPLQLPLGFLYVHHTYVPAppCTDFARCAANMRSMQRYHQDTQGWEDIGYSFVVGSDGYVYE 459
Cdd:smart00701   1 PPIVPRSEWGAKP-RGHTPRLTRPVRYVIIHHTATPN--CYTDAQCAQILRNIQAYHMEELGWCDIGYNFLVGGDGKVYE 77
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622895099  460 GRGWHWVGAHTLGHNSRGFGVAIVGNYTAALPTEAALRTVRDTLPsCAVRAGLLRPDYALLGHRQL 525
Cdd:smart00701  78 GRGWNVVGAHTGGYNDISLGIAFIGNFTDKLPTDAALDAAQDLLA-CAVQRGHLSPDYKLVGHRQV 142
PGRP cd06583
Peptidoglycan recognition proteins (PGRPs) are pattern recognition receptors that bind, and in ...
406-534 1.43e-37

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: 135.11  E-value: 1.43e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622895099 406 FLYVHHTYVPAPPctdfaRCAANMRSMQRYHQdtQGWEDIGYSFVVGSDGYVYEGRGWHWVGAHTLG-HNSRGFGVAIVG 484
Cdd:cd06583     4 YVVIHHTANPNCY-----TAAAAVRYLQNYHM--RGWSDISYHFLVGGDGRIYQGRGWNYVGWHAGGnYNSYSIGIELIG 76
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1622895099 485 NYTAALPTEAALRTVRDtLPSCAVRAGLLRPDYALLGHRQLVR-TDCPGDA 534
Cdd:cd06583    77 NFDGGPPTAAQLEALAE-LLAYLVKRYGIPPDYRIVGHRDVSPgTECPGDA 126
Amidase_2 pfam01510
N-acetylmuramoyl-L-alanine amidase; This family includes zinc amidases that have ...
406-533 1.78e-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: 92.80  E-value: 1.78e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622895099 406 FLYVHHTYVPappctDFARCAANMRSMQRyhqdtQGWEDIGYSFVVGSDGYVYE-----GRGWHwvgAHTLGHNSRGFGV 480
Cdd:pfam01510   4 YIVIHHTAGP-----SFAGALLPYAACIA-----RGWSDVSYHYLIDRDGTIYQlvpenGRAWH---AGNGGGNDRSIGI 70
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1622895099 481 AIVGNYTAALPTEAALRTVRDtLPSCAVRAGLLRPDYALLGHRQLVRTDCPGD 533
Cdd:pfam01510  71 ELEGNFGGDPPTDAQYEALAR-LLADLCKRYGIPPDRRIVGHRDVGRKTDPGP 122
PHA00447 PHA00447
lysozyme
422-542 1.26e-15

lysozyme


Pssm-ID: 177282 [Multi-domain]  Cd Length: 142  Bit Score: 74.04  E-value: 1.26e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622895099 422 FARCAAN-------MRSMQRYHQDtQGWEDIGYSFVVGSDGYVYEGRGWHWVGAHTLGHNSRGFGVAIVG---------- 484
Cdd:PHA00447   14 FVHCSATkpsmdvgVREIRQWHKE-QGWLDVGYHFIIRRDGTVEEGRPEDVVGSHVKGYNSNSVGVCLVGgiddkgkfda 92
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1622895099 485 NYTAAlpTEAALRTVRDTLpscavraGLLRPDYALLGHRQLVRTDCPGdalFHLLRTW 542
Cdd:PHA00447   93 NFTPA--QMQSLKSLLVTL-------KAKYPGAEIKAHHDVAPKACPS---FDLQRWL 138
 
Name Accession Description Interval E-value
PGRP smart00701
Animal peptidoglycan recognition proteins homologous to Bacteriophage T3 lysozyme; The ...
380-525 9.26e-63

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: 202.91  E-value: 9.26e-63
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622895099  380 PAIHPRCRWGAAPyQGRPTPLQLPLGFLYVHHTYVPAppCTDFARCAANMRSMQRYHQDTQGWEDIGYSFVVGSDGYVYE 459
Cdd:smart00701   1 PPIVPRSEWGAKP-RGHTPRLTRPVRYVIIHHTATPN--CYTDAQCAQILRNIQAYHMEELGWCDIGYNFLVGGDGKVYE 77
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622895099  460 GRGWHWVGAHTLGHNSRGFGVAIVGNYTAALPTEAALRTVRDTLPsCAVRAGLLRPDYALLGHRQL 525
Cdd:smart00701  78 GRGWNVVGAHTGGYNDISLGIAFIGNFTDKLPTDAALDAAQDLLA-CAVQRGHLSPDYKLVGHRQV 142
PGRP cd06583
Peptidoglycan recognition proteins (PGRPs) are pattern recognition receptors that bind, and in ...
406-534 1.43e-37

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: 135.11  E-value: 1.43e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622895099 406 FLYVHHTYVPAPPctdfaRCAANMRSMQRYHQdtQGWEDIGYSFVVGSDGYVYEGRGWHWVGAHTLG-HNSRGFGVAIVG 484
Cdd:cd06583     4 YVVIHHTANPNCY-----TAAAAVRYLQNYHM--RGWSDISYHFLVGGDGRIYQGRGWNYVGWHAGGnYNSYSIGIELIG 76
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1622895099 485 NYTAALPTEAALRTVRDtLPSCAVRAGLLRPDYALLGHRQLVR-TDCPGDA 534
Cdd:cd06583    77 NFDGGPPTAAQLEALAE-LLAYLVKRYGIPPDYRIVGHRDVSPgTECPGDA 126
Ami_2 smart00644
Ami_2 domain;
406-531 2.01e-30

Ami_2 domain;


Pssm-ID: 214760 [Multi-domain]  Cd Length: 126  Bit Score: 115.53  E-value: 2.01e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622895099  406 FLYVHHTYvpappcTDFARCAANMRSMQRYHQDtqgweDIGYSFVVGSDGYVYEGRG-----WHWVGAHTLGHNSRGFGV 480
Cdd:smart00644   5 GIVIHHTA------NSNASCANEARYMQNNHMN-----DIGYHFLVGGDGRVYQGVGwnyvaWHAGGAHTPGYNDISIGI 73
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1622895099  481 AIVGNYTA-ALPTEAALRTVRDTLpSCAVRAGLLRP--DYALLGHRQLVRTDCP 531
Cdd:smart00644  74 EFIGSFDSdDEPFAEALYAALDLL-AKLLKGAGLPPdgRYRIVGHRDVAPTEDP 126
Amidase_2 pfam01510
N-acetylmuramoyl-L-alanine amidase; This family includes zinc amidases that have ...
406-533 1.78e-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: 92.80  E-value: 1.78e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622895099 406 FLYVHHTYVPappctDFARCAANMRSMQRyhqdtQGWEDIGYSFVVGSDGYVYE-----GRGWHwvgAHTLGHNSRGFGV 480
Cdd:pfam01510   4 YIVIHHTAGP-----SFAGALLPYAACIA-----RGWSDVSYHYLIDRDGTIYQlvpenGRAWH---AGNGGGNDRSIGI 70
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1622895099 481 AIVGNYTAALPTEAALRTVRDtLPSCAVRAGLLRPDYALLGHRQLVRTDCPGD 533
Cdd:pfam01510  71 ELEGNFGGDPPTDAQYEALAR-LLADLCKRYGIPPDRRIVGHRDVGRKTDPGP 122
PHA00447 PHA00447
lysozyme
422-542 1.26e-15

lysozyme


Pssm-ID: 177282 [Multi-domain]  Cd Length: 142  Bit Score: 74.04  E-value: 1.26e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622895099 422 FARCAAN-------MRSMQRYHQDtQGWEDIGYSFVVGSDGYVYEGRGWHWVGAHTLGHNSRGFGVAIVG---------- 484
Cdd:PHA00447   14 FVHCSATkpsmdvgVREIRQWHKE-QGWLDVGYHFIIRRDGTVEEGRPEDVVGSHVKGYNSNSVGVCLVGgiddkgkfda 92
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1622895099 485 NYTAAlpTEAALRTVRDTLpscavraGLLRPDYALLGHRQLVRTDCPGdalFHLLRTW 542
Cdd:PHA00447   93 NFTPA--QMQSLKSLLVTL-------KAKYPGAEIKAHHDVAPKACPS---FDLQRWL 138
 
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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