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Conserved domains on  [gi|37665277|emb|CAD89155|]
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peptidoglycan recognition protein SC1A [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 ...
22-163 1.83e-71

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: 212.54  E-value: 1.83e-71
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37665277     22 VYVVSKAEWGGRGAKWTVGLGNYLSYAIIHHTAGSYCETRAQCNAVLQSVQNYHMDSLGWPDIGYNFLIGGDGNVYEGRG 101
Cdd:smart00701   1 PPIVPRSEWGAKPRGHTPRLTRPVRYVIIHHTATPNCYTDAQCAQILRNIQAYHMEELGWCDIGYNFLVGGDGKVYEGRG 80
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 37665277    102 WNNMGAHAAEWNPYSIGISFLGNYNWDTLEPNMISAAQQLLNDAVNRGQLSSGYILYGHRQV 163
Cdd:smart00701  81 WNVVGAHTGGYNDISLGIAFIGNFTDKLPTDAALDAAQDLLACAVQRGHLSPDYKLVGHRQV 142
 
Name Accession Description Interval E-value
PGRP smart00701
Animal peptidoglycan recognition proteins homologous to Bacteriophage T3 lysozyme; The ...
22-163 1.83e-71

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: 212.54  E-value: 1.83e-71
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37665277     22 VYVVSKAEWGGRGAKWTVGLGNYLSYAIIHHTAGSYCETRAQCNAVLQSVQNYHMDSLGWPDIGYNFLIGGDGNVYEGRG 101
Cdd:smart00701   1 PPIVPRSEWGAKPRGHTPRLTRPVRYVIIHHTATPNCYTDAQCAQILRNIQAYHMEELGWCDIGYNFLVGGDGKVYEGRG 80
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 37665277    102 WNNMGAHAAEWNPYSIGISFLGNYNWDTLEPNMISAAQQLLNDAVNRGQLSSGYILYGHRQV 163
Cdd:smart00701  81 WNVVGAHTGGYNDISLGIAFIGNFTDKLPTDAALDAAQDLLACAVQRGHLSPDYKLVGHRQV 142
PGRP cd06583
Peptidoglycan recognition proteins (PGRPs) are pattern recognition receptors that bind, and in ...
46-170 2.64e-40

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: 132.80  E-value: 2.64e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37665277  46 SYAIIHHTAGSYCETraqCNAVLQSVQNYHMdsLGWPDIGYNFLIGGDGNVYEGRGWNNMGAHA-AEWNPYSIGISFLGN 124
Cdd:cd06583   3 KYVVIHHTANPNCYT---AAAAVRYLQNYHM--RGWSDISYHFLVGGDGRIYQGRGWNYVGWHAgGNYNSYSIGIELIGN 77
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
gi 37665277 125 YNWDTLEPNMISAAQQLLNDAVNRGQLSSGYILYGHRQVSA-TECPG 170
Cdd:cd06583  78 FDGGPPTAAQLEALAELLAYLVKRYGIPPDYRIVGHRDVSPgTECPG 124
Amidase_2 pfam01510
N-acetylmuramoyl-L-alanine amidase; This family includes zinc amidases that have ...
46-170 4.35e-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: 96.66  E-value: 4.35e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37665277    46 SYAIIHHTAGSYCETRAQCNAVLQSVqnyhmdslGWPDIGYNFLIGGDGNVYEGRGWNNMGAHAAEW--NPYSIGISFLG 123
Cdd:pfam01510   3 RYIVIHHTAGPSFAGALLPYAACIAR--------GWSDVSYHYLIDRDGTIYQLVPENGRAWHAGNGggNDRSIGIELEG 74
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 37665277   124 NYNWDTLEPNMISAAQQLLNDAVNRGQLSSGYILYGHRQVSATECPG 170
Cdd:pfam01510  75 NFGGDPPTDAQYEALARLLADLCKRYGIPPDRRIVGHRDVGRKTDPG 121
PHA00447 PHA00447
lysozyme
46-173 5.60e-13

lysozyme


Pssm-ID: 177282 [Multi-domain]  Cd Length: 142  Bit Score: 62.87  E-value: 5.60e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37665277   46 SYAIIHHTAgsyceTRAQCNAVLQSVQNYHMDSlGWPDIGYNFLIGGDGNVYEGRGWNNMGAHAAEWNPYSIGISFLGNY 125
Cdd:PHA00447  11 KAIFVHCSA-----TKPSMDVGVREIRQWHKEQ-GWLDVGYHFIIRRDGTVEEGRPEDVVGSHVKGYNSNSVGVCLVGGI 84
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 37665277  126 NW-----DTLEPNMISAAQQLLNDavnrgqLSSGYI---LYGHRQVSATECPGTHI 173
Cdd:PHA00447  85 DDkgkfdANFTPAQMQSLKSLLVT------LKAKYPgaeIKAHHDVAPKACPSFDL 134
AmpD COG3023
N-acetyl-anhydromuramyl-L-alanine amidase AmpD [Cell wall/membrane/envelope biogenesis];
46-170 3.69e-04

N-acetyl-anhydromuramyl-L-alanine amidase AmpD [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442259  Cd Length: 167  Bit Score: 39.08  E-value: 3.69e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37665277  46 SYAIIHHTAGSYCETRAQ--CNAVLQ-SvqnYHmdslgwpdigynFLIGGDGNVY-----EGRGWnnmgaHAAEW----- 112
Cdd:COG3023  28 DLIVIHYTAGPPGGGALDwlTDPALRvS---AH------------YLIDRDGEIYqlvpeDDRAW-----HAGVSswrgr 87
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 37665277 113 ---NPYSIGISFLGN-YNWDTLEPNMISAAQQLLNDAVNRGQLSSGYILyGHRQVSAT--ECPG 170
Cdd:COG3023  88 tnlNDFSIGIELENPgHGWAPFTEAQYEALAALLRDLCARYGIPPDHIV-GHSDIAPGrkTDPG 150
 
Name Accession Description Interval E-value
PGRP smart00701
Animal peptidoglycan recognition proteins homologous to Bacteriophage T3 lysozyme; The ...
22-163 1.83e-71

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: 212.54  E-value: 1.83e-71
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37665277     22 VYVVSKAEWGGRGAKWTVGLGNYLSYAIIHHTAGSYCETRAQCNAVLQSVQNYHMDSLGWPDIGYNFLIGGDGNVYEGRG 101
Cdd:smart00701   1 PPIVPRSEWGAKPRGHTPRLTRPVRYVIIHHTATPNCYTDAQCAQILRNIQAYHMEELGWCDIGYNFLVGGDGKVYEGRG 80
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 37665277    102 WNNMGAHAAEWNPYSIGISFLGNYNWDTLEPNMISAAQQLLNDAVNRGQLSSGYILYGHRQV 163
Cdd:smart00701  81 WNVVGAHTGGYNDISLGIAFIGNFTDKLPTDAALDAAQDLLACAVQRGHLSPDYKLVGHRQV 142
PGRP cd06583
Peptidoglycan recognition proteins (PGRPs) are pattern recognition receptors that bind, and in ...
46-170 2.64e-40

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: 132.80  E-value: 2.64e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37665277  46 SYAIIHHTAGSYCETraqCNAVLQSVQNYHMdsLGWPDIGYNFLIGGDGNVYEGRGWNNMGAHA-AEWNPYSIGISFLGN 124
Cdd:cd06583   3 KYVVIHHTANPNCYT---AAAAVRYLQNYHM--RGWSDISYHFLVGGDGRIYQGRGWNYVGWHAgGNYNSYSIGIELIGN 77
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
gi 37665277 125 YNWDTLEPNMISAAQQLLNDAVNRGQLSSGYILYGHRQVSA-TECPG 170
Cdd:cd06583  78 FDGGPPTAAQLEALAELLAYLVKRYGIPPDYRIVGHRDVSPgTECPG 124
Ami_2 smart00644
Ami_2 domain;
46-169 5.20e-31

Ami_2 domain;


Pssm-ID: 214760 [Multi-domain]  Cd Length: 126  Bit Score: 109.37  E-value: 5.20e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37665277     46 SYAIIHHTAGSYcetrAQCNAVLQSVQNYHMDslgwpDIGYNFLIGGDGNVYEGRGWNN-----MGAHAAEWNPYSIGIS 120
Cdd:smart00644   4 RGIVIHHTANSN----ASCANEARYMQNNHMN-----DIGYHFLVGGDGRVYQGVGWNYvawhaGGAHTPGYNDISIGIE 74
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 37665277    121 FLGNYNWDTLE-PNMISAAQQLLNDAVNRGQLSS--GYILYGHRQVSATECP 169
Cdd:smart00644  75 FIGSFDSDDEPfAEALYAALDLLAKLLKGAGLPPdgRYRIVGHRDVAPTEDP 126
Amidase_2 pfam01510
N-acetylmuramoyl-L-alanine amidase; This family includes zinc amidases that have ...
46-170 4.35e-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: 96.66  E-value: 4.35e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37665277    46 SYAIIHHTAGSYCETRAQCNAVLQSVqnyhmdslGWPDIGYNFLIGGDGNVYEGRGWNNMGAHAAEW--NPYSIGISFLG 123
Cdd:pfam01510   3 RYIVIHHTAGPSFAGALLPYAACIAR--------GWSDVSYHYLIDRDGTIYQLVPENGRAWHAGNGggNDRSIGIELEG 74
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 37665277   124 NYNWDTLEPNMISAAQQLLNDAVNRGQLSSGYILYGHRQVSATECPG 170
Cdd:pfam01510  75 NFGGDPPTDAQYEALARLLADLCKRYGIPPDRRIVGHRDVGRKTDPG 121
PHA00447 PHA00447
lysozyme
46-173 5.60e-13

lysozyme


Pssm-ID: 177282 [Multi-domain]  Cd Length: 142  Bit Score: 62.87  E-value: 5.60e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37665277   46 SYAIIHHTAgsyceTRAQCNAVLQSVQNYHMDSlGWPDIGYNFLIGGDGNVYEGRGWNNMGAHAAEWNPYSIGISFLGNY 125
Cdd:PHA00447  11 KAIFVHCSA-----TKPSMDVGVREIRQWHKEQ-GWLDVGYHFIIRRDGTVEEGRPEDVVGSHVKGYNSNSVGVCLVGGI 84
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 37665277  126 NW-----DTLEPNMISAAQQLLNDavnrgqLSSGYI---LYGHRQVSATECPGTHI 173
Cdd:PHA00447  85 DDkgkfdANFTPAQMQSLKSLLVT------LKAKYPgaeIKAHHDVAPKACPSFDL 134
AmpD COG3023
N-acetyl-anhydromuramyl-L-alanine amidase AmpD [Cell wall/membrane/envelope biogenesis];
46-170 3.69e-04

N-acetyl-anhydromuramyl-L-alanine amidase AmpD [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442259  Cd Length: 167  Bit Score: 39.08  E-value: 3.69e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37665277  46 SYAIIHHTAGSYCETRAQ--CNAVLQ-SvqnYHmdslgwpdigynFLIGGDGNVY-----EGRGWnnmgaHAAEW----- 112
Cdd:COG3023  28 DLIVIHYTAGPPGGGALDwlTDPALRvS---AH------------YLIDRDGEIYqlvpeDDRAW-----HAGVSswrgr 87
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 37665277 113 ---NPYSIGISFLGN-YNWDTLEPNMISAAQQLLNDAVNRGQLSSGYILyGHRQVSAT--ECPG 170
Cdd:COG3023  88 tnlNDFSIGIELENPgHGWAPFTEAQYEALAALLRDLCARYGIPPDHIV-GHSDIAPGrkTDPG 150
 
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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