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Conserved domains on  [gi|24651867|ref|NP_610410|]
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peptidoglycan recognition protein SC2 [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 ...
21-162 1.59e-67

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: 202.53  E-value: 1.59e-67
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24651867     21 VTIISKSEWGGRSATSKTSLANYLSYAVIHHTAGNYCSTKAACITQLQNIQAYHMDSLGWADIGYNFLIGGDGNVYEGRG 100
Cdd:smart00701   1 PPIVPRSEWGAKPRGHTPRLTRPVRYVIIHHTATPNCYTDAQCAQILRNIQAYHMEELGWCDIGYNFLVGGDGKVYEGRG 80
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 24651867    101 WNVMGAHATNWNSKSIGISFLGNYNTNTLTSAQITAAKGLLSDAVSRGQIVSGYILYGHRQV 162
Cdd:smart00701  81 WNVVGAHTGGYNDISLGIAFIGNFTDKLPTDAALDAAQDLLACAVQRGHLSPDYKLVGHRQV 142
 
Name Accession Description Interval E-value
PGRP smart00701
Animal peptidoglycan recognition proteins homologous to Bacteriophage T3 lysozyme; The ...
21-162 1.59e-67

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: 202.53  E-value: 1.59e-67
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24651867     21 VTIISKSEWGGRSATSKTSLANYLSYAVIHHTAGNYCSTKAACITQLQNIQAYHMDSLGWADIGYNFLIGGDGNVYEGRG 100
Cdd:smart00701   1 PPIVPRSEWGAKPRGHTPRLTRPVRYVIIHHTATPNCYTDAQCAQILRNIQAYHMEELGWCDIGYNFLVGGDGKVYEGRG 80
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 24651867    101 WNVMGAHATNWNSKSIGISFLGNYNTNTLTSAQITAAKGLLSDAVSRGQIVSGYILYGHRQV 162
Cdd:smart00701  81 WNVVGAHTGGYNDISLGIAFIGNFTDKLPTDAALDAAQDLLACAVQRGHLSPDYKLVGHRQV 142
PGRP cd06583
Peptidoglycan recognition proteins (PGRPs) are pattern recognition receptors that bind, and in ...
45-169 3.41e-45

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: 145.12  E-value: 3.41e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24651867  45 SYAVIHHTAGNYCSTKAACItqlQNIQAYHMdsLGWADIGYNFLIGGDGNVYEGRGWNVMGAHATNW-NSKSIGISFLGN 123
Cdd:cd06583   3 KYVVIHHTANPNCYTAAAAV---RYLQNYHM--RGWSDISYHFLVGGDGRIYQGRGWNYVGWHAGGNyNSYSIGIELIGN 77
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
gi 24651867 124 YNTNTLTSAQITAAKGLLSDAVSRGQIVSGYILYGHRQV-GSTECPG 169
Cdd:cd06583  78 FDGGPPTAAQLEALAELLAYLVKRYGIPPDYRIVGHRDVsPGTECPG 124
Amidase_2 pfam01510
N-acetylmuramoyl-L-alanine amidase; This family includes zinc amidases that have ...
45-169 4.31e-29

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: 103.97  E-value: 4.31e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24651867    45 SYAVIHHTAGNYCSTKAACITQLQNiqayhmdsLGWADIGYNFLIGGDGNVYE-----GRGWnvmGAHATNWNSKSIGIS 119
Cdd:pfam01510   3 RYIVIHHTAGPSFAGALLPYAACIA--------RGWSDVSYHYLIDRDGTIYQlvpenGRAW---HAGNGGGNDRSIGIE 71
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 24651867   120 FLGNYNTNTLTSAQITAAKGLLSDAVSRGQIVSGYILYGHRQVGSTECPG 169
Cdd:pfam01510  72 LEGNFGGDPPTDAQYEALARLLADLCKRYGIPPDRRIVGHRDVGRKTDPG 121
PHA00447 PHA00447
lysozyme
56-172 3.11e-19

lysozyme


Pssm-ID: 177282 [Multi-domain]  Cd Length: 142  Bit Score: 79.44  E-value: 3.11e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24651867   56 YCS-TKAACITQLQNIQAYHMDSlGWADIGYNFLIGGDGNVYEGRGWNVMGAHATNWNSKSIGISFLGNYN-----TNTL 129
Cdd:PHA00447  16 HCSaTKPSMDVGVREIRQWHKEQ-GWLDVGYHFIIRRDGTVEEGRPEDVVGSHVKGYNSNSVGVCLVGGIDdkgkfDANF 94
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 24651867  130 TSAQITAAKGLLSDAVSRgqiVSGYILYGHRQVGSTECPGTNI 172
Cdd:PHA00447  95 TPAQMQSLKSLLVTLKAK---YPGAEIKAHHDVAPKACPSFDL 134
AmpD COG3023
N-acetyl-anhydromuramyl-L-alanine amidase AmpD [Cell wall/membrane/envelope biogenesis];
45-169 2.10e-08

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


Pssm-ID: 442259  Cd Length: 167  Bit Score: 51.02  E-value: 2.10e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24651867  45 SYAVIHHTAGNYCstkAACITQLQNIQA---YHmdslgwadigynFLIGGDGNVY-----EGRGWnvmgaHA-------- 108
Cdd:COG3023  28 DLIVIHYTAGPPG---GGALDWLTDPALrvsAH------------YLIDRDGEIYqlvpeDDRAW-----HAgvsswrgr 87
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 24651867 109 TNWNSKSIGISFLGN-YNTNTLTSAQITAAKGLLSDAVSRGQIVSGYILyGHRQV--GSTECPG 169
Cdd:COG3023  88 TNLNDFSIGIELENPgHGWAPFTEAQYEALAALLRDLCARYGIPPDHIV-GHSDIapGRKTDPG 150
 
Name Accession Description Interval E-value
PGRP smart00701
Animal peptidoglycan recognition proteins homologous to Bacteriophage T3 lysozyme; The ...
21-162 1.59e-67

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: 202.53  E-value: 1.59e-67
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24651867     21 VTIISKSEWGGRSATSKTSLANYLSYAVIHHTAGNYCSTKAACITQLQNIQAYHMDSLGWADIGYNFLIGGDGNVYEGRG 100
Cdd:smart00701   1 PPIVPRSEWGAKPRGHTPRLTRPVRYVIIHHTATPNCYTDAQCAQILRNIQAYHMEELGWCDIGYNFLVGGDGKVYEGRG 80
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 24651867    101 WNVMGAHATNWNSKSIGISFLGNYNTNTLTSAQITAAKGLLSDAVSRGQIVSGYILYGHRQV 162
Cdd:smart00701  81 WNVVGAHTGGYNDISLGIAFIGNFTDKLPTDAALDAAQDLLACAVQRGHLSPDYKLVGHRQV 142
PGRP cd06583
Peptidoglycan recognition proteins (PGRPs) are pattern recognition receptors that bind, and in ...
45-169 3.41e-45

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: 145.12  E-value: 3.41e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24651867  45 SYAVIHHTAGNYCSTKAACItqlQNIQAYHMdsLGWADIGYNFLIGGDGNVYEGRGWNVMGAHATNW-NSKSIGISFLGN 123
Cdd:cd06583   3 KYVVIHHTANPNCYTAAAAV---RYLQNYHM--RGWSDISYHFLVGGDGRIYQGRGWNYVGWHAGGNyNSYSIGIELIGN 77
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
gi 24651867 124 YNTNTLTSAQITAAKGLLSDAVSRGQIVSGYILYGHRQV-GSTECPG 169
Cdd:cd06583  78 FDGGPPTAAQLEALAELLAYLVKRYGIPPDYRIVGHRDVsPGTECPG 124
Ami_2 smart00644
Ami_2 domain;
45-168 1.62e-30

Ami_2 domain;


Pssm-ID: 214760 [Multi-domain]  Cd Length: 126  Bit Score: 107.83  E-value: 1.62e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24651867     45 SYAVIHHTAGNYcstkAACITQLQNIQAYHMDslgwaDIGYNFLIGGDGNVYEGRGWN-----VMGAHATNWNSKSIGIS 119
Cdd:smart00644   4 RGIVIHHTANSN----ASCANEARYMQNNHMN-----DIGYHFLVGGDGRVYQGVGWNyvawhAGGAHTPGYNDISIGIE 74
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 24651867    120 FLGNYNTNTLTSAQ-ITAAKGLLSDAVSR--GQIVSGYILYGHRQVGSTECP 168
Cdd:smart00644  75 FIGSFDSDDEPFAEaLYAALDLLAKLLKGagLPPDGRYRIVGHRDVAPTEDP 126
Amidase_2 pfam01510
N-acetylmuramoyl-L-alanine amidase; This family includes zinc amidases that have ...
45-169 4.31e-29

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: 103.97  E-value: 4.31e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24651867    45 SYAVIHHTAGNYCSTKAACITQLQNiqayhmdsLGWADIGYNFLIGGDGNVYE-----GRGWnvmGAHATNWNSKSIGIS 119
Cdd:pfam01510   3 RYIVIHHTAGPSFAGALLPYAACIA--------RGWSDVSYHYLIDRDGTIYQlvpenGRAW---HAGNGGGNDRSIGIE 71
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 24651867   120 FLGNYNTNTLTSAQITAAKGLLSDAVSRGQIVSGYILYGHRQVGSTECPG 169
Cdd:pfam01510  72 LEGNFGGDPPTDAQYEALARLLADLCKRYGIPPDRRIVGHRDVGRKTDPG 121
PHA00447 PHA00447
lysozyme
56-172 3.11e-19

lysozyme


Pssm-ID: 177282 [Multi-domain]  Cd Length: 142  Bit Score: 79.44  E-value: 3.11e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24651867   56 YCS-TKAACITQLQNIQAYHMDSlGWADIGYNFLIGGDGNVYEGRGWNVMGAHATNWNSKSIGISFLGNYN-----TNTL 129
Cdd:PHA00447  16 HCSaTKPSMDVGVREIRQWHKEQ-GWLDVGYHFIIRRDGTVEEGRPEDVVGSHVKGYNSNSVGVCLVGGIDdkgkfDANF 94
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 24651867  130 TSAQITAAKGLLSDAVSRgqiVSGYILYGHRQVGSTECPGTNI 172
Cdd:PHA00447  95 TPAQMQSLKSLLVTLKAK---YPGAEIKAHHDVAPKACPSFDL 134
AmpD COG3023
N-acetyl-anhydromuramyl-L-alanine amidase AmpD [Cell wall/membrane/envelope biogenesis];
45-169 2.10e-08

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


Pssm-ID: 442259  Cd Length: 167  Bit Score: 51.02  E-value: 2.10e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24651867  45 SYAVIHHTAGNYCstkAACITQLQNIQA---YHmdslgwadigynFLIGGDGNVY-----EGRGWnvmgaHA-------- 108
Cdd:COG3023  28 DLIVIHYTAGPPG---GGALDWLTDPALrvsAH------------YLIDRDGEIYqlvpeDDRAW-----HAgvsswrgr 87
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 24651867 109 TNWNSKSIGISFLGN-YNTNTLTSAQITAAKGLLSDAVSRGQIVSGYILyGHRQV--GSTECPG 169
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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