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Conserved domains on  [gi|45552997|ref|NP_996026|]
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peptidoglycan recognition protein LA, isoform E [Drosophila melanogaster]

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 ...
181-322 5.68e-53

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: 172.09  E-value: 5.68e-53
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552997    181 HLVVDREQWGAskNSHGLTIPLKRPIPYVLITHIGVQSlpCDNIYKCSIKMRTIQDSAIAEKGLPDIQSNFYVSEEGNIY 260
Cdd:smart00701   1 PPIVPRSEWGA--KPRGHTPRLTRPVRYVIIHHTATPN--CYTDAQCAQILRNIQAYHMEELGWCDIGYNFLVGGDGKVY 76
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 45552997    261 VGRGWDWANTYA----NQTLAITFMGDYGRFKPGPKQLEGVQFLLAHAVANRNIDVDYKLVAQNQT 322
Cdd:smart00701  77 EGRGWNVVGAHTggynDISLGIAFIGNFTDKLPTDAALDAAQDLLACAVQRGHLSPDYKLVGHRQV 142
 
Name Accession Description Interval E-value
PGRP smart00701
Animal peptidoglycan recognition proteins homologous to Bacteriophage T3 lysozyme; The ...
181-322 5.68e-53

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: 172.09  E-value: 5.68e-53
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552997    181 HLVVDREQWGAskNSHGLTIPLKRPIPYVLITHIGVQSlpCDNIYKCSIKMRTIQDSAIAEKGLPDIQSNFYVSEEGNIY 260
Cdd:smart00701   1 PPIVPRSEWGA--KPRGHTPRLTRPVRYVIIHHTATPN--CYTDAQCAQILRNIQAYHMEELGWCDIGYNFLVGGDGKVY 76
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 45552997    261 VGRGWDWANTYA----NQTLAITFMGDYGRFKPGPKQLEGVQFLLAHAVANRNIDVDYKLVAQNQT 322
Cdd:smart00701  77 EGRGWNVVGAHTggynDISLGIAFIGNFTDKLPTDAALDAAQDLLACAVQRGHLSPDYKLVGHRQV 142
PGRP cd06583
Peptidoglycan recognition proteins (PGRPs) are pattern recognition receptors that bind, and in ...
205-331 7.48e-22

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: 89.66  E-value: 7.48e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552997 205 PIPYVLITHIGvqslpCDNIYKCSIKMRTIQDSAIaeKGLPDIQSNFYVSEEGNIYVGRGWDWA-----NTYANQTLAIT 279
Cdd:cd06583   1 PVKYVVIHHTA-----NPNCYTAAAAVRYLQNYHM--RGWSDISYHFLVGGDGRIYQGRGWNYVgwhagGNYNSYSIGIE 73
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|...
gi 45552997 280 FMGDYGRFKPGPKQLEGVQFLLAHAVANRNIDVDYKLVAQNQ-TKVTRSPGAY 331
Cdd:cd06583  74 LIGNFDGGPPTAAQLEALAELLAYLVKRYGIPPDYRIVGHRDvSPGTECPGDA 126
Amidase_2 pfam01510
N-acetylmuramoyl-L-alanine amidase; This family includes zinc amidases that have ...
246-329 2.29e-07

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: 48.89  E-value: 2.29e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552997   246 DIQSNFYVSEEGNIYV-----GRGWDWANTYANQ-TLAITFMGDYGRFKPGPKQLEGVQFLLAHAVANRNIDVDYKLVAQ 319
Cdd:pfam01510  32 DVSYHYLIDRDGTIYQlvpenGRAWHAGNGGGNDrSIGIELEGNFGGDPPTDAQYEALARLLADLCKRYGIPPDRRIVGH 111
                          90
                  ....*....|
gi 45552997   320 NQTKVTRSPG 329
Cdd:pfam01510 112 RDVGRKTDPG 121
 
Name Accession Description Interval E-value
PGRP smart00701
Animal peptidoglycan recognition proteins homologous to Bacteriophage T3 lysozyme; The ...
181-322 5.68e-53

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: 172.09  E-value: 5.68e-53
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552997    181 HLVVDREQWGAskNSHGLTIPLKRPIPYVLITHIGVQSlpCDNIYKCSIKMRTIQDSAIAEKGLPDIQSNFYVSEEGNIY 260
Cdd:smart00701   1 PPIVPRSEWGA--KPRGHTPRLTRPVRYVIIHHTATPN--CYTDAQCAQILRNIQAYHMEELGWCDIGYNFLVGGDGKVY 76
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 45552997    261 VGRGWDWANTYA----NQTLAITFMGDYGRFKPGPKQLEGVQFLLAHAVANRNIDVDYKLVAQNQT 322
Cdd:smart00701  77 EGRGWNVVGAHTggynDISLGIAFIGNFTDKLPTDAALDAAQDLLACAVQRGHLSPDYKLVGHRQV 142
PGRP cd06583
Peptidoglycan recognition proteins (PGRPs) are pattern recognition receptors that bind, and in ...
205-331 7.48e-22

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: 89.66  E-value: 7.48e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552997 205 PIPYVLITHIGvqslpCDNIYKCSIKMRTIQDSAIaeKGLPDIQSNFYVSEEGNIYVGRGWDWA-----NTYANQTLAIT 279
Cdd:cd06583   1 PVKYVVIHHTA-----NPNCYTAAAAVRYLQNYHM--RGWSDISYHFLVGGDGRIYQGRGWNYVgwhagGNYNSYSIGIE 73
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|...
gi 45552997 280 FMGDYGRFKPGPKQLEGVQFLLAHAVANRNIDVDYKLVAQNQ-TKVTRSPGAY 331
Cdd:cd06583  74 LIGNFDGGPPTAAQLEALAELLAYLVKRYGIPPDYRIVGHRDvSPGTECPGDA 126
Amidase_2 pfam01510
N-acetylmuramoyl-L-alanine amidase; This family includes zinc amidases that have ...
246-329 2.29e-07

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: 48.89  E-value: 2.29e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552997   246 DIQSNFYVSEEGNIYV-----GRGWDWANTYANQ-TLAITFMGDYGRFKPGPKQLEGVQFLLAHAVANRNIDVDYKLVAQ 319
Cdd:pfam01510  32 DVSYHYLIDRDGTIYQlvpenGRAWHAGNGGGNDrSIGIELEGNFGGDPPTDAQYEALARLLADLCKRYGIPPDRRIVGH 111
                          90
                  ....*....|
gi 45552997   320 NQTKVTRSPG 329
Cdd:pfam01510 112 RDVGRKTDPG 121
Ami_2 smart00644
Ami_2 domain;
204-328 8.88e-06

Ami_2 domain;


Pssm-ID: 214760 [Multi-domain]  Cd Length: 126  Bit Score: 44.66  E-value: 8.88e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552997    204 RPIPYVLITHIGvqsLPCDNiykCSIKMRTIQDsaiaeKGLPDIQSNFYVSEEGNIYVGRGWD---------WANTYANQ 274
Cdd:smart00644   1 PPPRGIVIHHTA---NSNAS---CANEARYMQN-----NHMNDIGYHFLVGGDGRVYQGVGWNyvawhaggaHTPGYNDI 69
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 45552997    275 TLAITFMGDYGRFK-PGPKQLEGVQFLLAHAVANRNI--DVDYKLVAQNQTKVTRSP 328
Cdd:smart00644  70 SIGIEFIGSFDSDDePFAEALYAALDLLAKLLKGAGLppDGRYRIVGHRDVAPTEDP 126
 
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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