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Conserved domains on  [gi|767909948|ref|XP_011508093|]
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peptidoglycan recognition protein 4 isoform X2 [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

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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 ...
 207-347 1.13e-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: 209.84  E-value: 1.13e-67
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767909948   207 PGVVPRSVWGAR-ETHCPRMTLPAKYGIIIHTAGRTCNISDECRLLVRDIQSFYIDRLKSCDIGYNFLVGQDGAIYEGVG 285
Cdd:smart00701   1 PPIVPRSEWGAKpRGHTPRLTRPVRYVIIHHTATPNCYTDAQCAQILRNIQAYHMEELGWCDIGYNFLVGGDGKVYEGRG 80

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767909948   286 WNVQGSSTPGYDDIALGITFMGTFTGIPPNAAALEAAQDLIQCAMVKGYLTPNYLLVGHSDV 347
Cdd:smart00701  81 WNVVGAHTGGYNDISLGIAFIGNFTDKLPTDAALDAAQDLLACAVQRGHLSPDYKLVGHRQV 142
PGRP smart00701
Animal peptidoglycan recognition proteins homologous to Bacteriophage T3 lysozyme; The ...
 49-190 2.04e-64

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: 201.37  E-value: 2.04e-64
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767909948    49 STTVSRKAWGAEAVGCSIQLTTPVNVLVIHHVPGLECHDQTVCSQRLRELQAHHVHNNSGCDVAYNFLVGDDGRVYEGVG 128
Cdd:smart00701   1 PPIVPRSEWGAKPRGHTPRLTRPVRYVIIHHTATPNCYTDAQCAQILRNIQAYHMEELGWCDIGYNFLVGGDGKVYEGRG 80

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767909948   129 WNIQGVHTQGYNNISLGFAFFGTKKGHSPSPAALSAMENLITYAVQKGHLSSSYVQPLLGKG 190
Cdd:smart00701  81 WNVVGAHTGGYNDISLGIAFIGNFTDKLPTDAALDAAQDLLACAVQRGHLSPDYKLVGHRQV 142
 
Name Accession Description Interval E-value
PGRP smart00701
Animal peptidoglycan recognition proteins homologous to Bacteriophage T3 lysozyme; The ...
 207-347 1.13e-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: 209.84  E-value: 1.13e-67
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767909948   207 PGVVPRSVWGAR-ETHCPRMTLPAKYGIIIHTAGRTCNISDECRLLVRDIQSFYIDRLKSCDIGYNFLVGQDGAIYEGVG 285
Cdd:smart00701   1 PPIVPRSEWGAKpRGHTPRLTRPVRYVIIHHTATPNCYTDAQCAQILRNIQAYHMEELGWCDIGYNFLVGGDGKVYEGRG 80

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767909948   286 WNVQGSSTPGYDDIALGITFMGTFTGIPPNAAALEAAQDLIQCAMVKGYLTPNYLLVGHSDV 347
Cdd:smart00701  81 WNVVGAHTGGYNDISLGIAFIGNFTDKLPTDAALDAAQDLLACAVQRGHLSPDYKLVGHRQV 142
PGRP smart00701
Animal peptidoglycan recognition proteins homologous to Bacteriophage T3 lysozyme; The ...
 49-190 2.04e-64

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: 201.37  E-value: 2.04e-64
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767909948    49 STTVSRKAWGAEAVGCSIQLTTPVNVLVIHHVPGLECHDQTVCSQRLRELQAHHVHNNSGCDVAYNFLVGDDGRVYEGVG 128
Cdd:smart00701   1 PPIVPRSEWGAKPRGHTPRLTRPVRYVIIHHTATPNCYTDAQCAQILRNIQAYHMEELGWCDIGYNFLVGGDGKVYEGRG 80

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767909948   129 WNIQGVHTQGYNNISLGFAFFGTKKGHSPSPAALSAMENLITYAVQKGHLSSSYVQPLLGKG 190
Cdd:smart00701  81 WNVVGAHTGGYNDISLGIAFIGNFTDKLPTDAALDAAQDLLACAVQRGHLSPDYKLVGHRQV 142
PGRP cd06583
Peptidoglycan recognition proteins (PGRPs) are pattern recognition receptors that bind, and in ...
 228-356 1.79e-35

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: 125.86  E-value: 1.79e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767909948 228 PAKYGIIIHTAGRTCNisdECRLLVRDIQSFYIdrLKSCDIGYNFLVGQDGAIYEGVGWNVQGSSTPG-YDDIALGITFM 306
Cdd:cd06583    1 PVKYVVIHHTANPNCY---TAAAAVRYLQNYHM--RGWSDISYHFLVGGDGRIYQGRGWNYVGWHAGGnYNSYSIGIELI 75

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 767909948 307 GTFTGIPPNAAALEAAQDLIQCAMVKGYLTPNYLLVGHSDVAR-TLSPGQA 356
Cdd:cd06583   76 GNFDGGPPTAAQLEALAELLAYLVKRYGIPPDYRIVGHRDVSPgTECPGDA 126
PGRP cd06583
Peptidoglycan recognition proteins (PGRPs) are pattern recognition receptors that bind, and in ...
 71-208 1.71e-28

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: 107.76  E-value: 1.71e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767909948  71 PVNVLVIHHVPGLECHDqtvCSQRLRELQAHHVHNNSgcDVAYNFLVGDDGRVYEGVGWNIQGVHTQG-YNNISLGFAFF 149
Cdd:cd06583    1 PVKYVVIHHTANPNCYT---AAAAVRYLQNYHMRGWS--DISYHFLVGGDGRIYQGRGWNYVGWHAGGnYNSYSIGIELI 75

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 767909948 150 GTKKGHSPSPAALSAMENLITYAVQKGHLSSSYVqpllgkgencLAPRQKTSLKKACPG 208
Cdd:cd06583   76 GNFDGGPPTAAQLEALAELLAYLVKRYGIPPDYR----------IVGHRDVSPGTECPG 124
Amidase_2 pfam01510
N-acetylmuramoyl-L-alanine amidase; This family includes zinc amidases that have ...
 228-355 6.17e-23

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: 92.42  E-value: 6.17e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767909948  228 PAKYGIIIHTAGRTcniSDECRllvrdIQSFYIDRLKSCDIGYNFLVGQDGAIYE-----GVGWNVQGSstpGYDDIALG 302
Cdd:pfam01510   1 PIRYIVIHHTAGPS---FAGAL-----LPYAACIARGWSDVSYHYLIDRDGTIYQlvpenGRAWHAGNG---GGNDRSIG 69

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 767909948  303 ITFMGTFTGIPPNAAALEAAQDLIQCAMVKGYLTPNYLLVGHSDVARTLSPGQ 355
Cdd:pfam01510  70 IELEGNFGGDPPTDAQYEALARLLADLCKRYGIPPDRRIVGHRDVGRKTDPGP 122
Amidase_2 pfam01510
N-acetylmuramoyl-L-alanine amidase; This family includes zinc amidases that have ...
 71-182 4.40e-15

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: 70.85  E-value: 4.40e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767909948   71 PVNVLVIHHvpglechdqTVCSQRL-RELQAHHVHNNSGCDVAYNFLVGDDGRVYEGVGWNIQGVHT--QGYNNISLGFA 147
Cdd:pfam01510   1 PIRYIVIHH---------TAGPSFAgALLPYAACIARGWSDVSYHYLIDRDGTIYQLVPENGRAWHAgnGGGNDRSIGIE 71

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 767909948  148 FFGTKKGHSPSPAALSAMENLITYAVQKGHLSSSY 182
Cdd:pfam01510  72 LEGNFGGDPPTDAQYEALARLLADLCKRYGIPPDR 106
PHA00447 PHA00447
lysozyme
 110-208 3.76e-05

lysozyme


Pssm-ID: 177282 [Multi-domain]  Cd Length: 142  Bit Score: 43.23  E-value: 3.76e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767909948 110 DVAYNFLVGDDGRVYEGVGWNIQGVHTQGYNNISLGFAFFG--TKKGHSP---SPAALSAMENLITyavqkgHLSSSYVQ 184
Cdd:PHA00447  42 DVGYHFIIRRDGTVEEGRPEDVVGSHVKGYNSNSVGVCLVGgiDDKGKFDanfTPAQMQSLKSLLV------TLKAKYPG 115

                         90       100
                 ....*....|....*....|....
gi 767909948 185 PLLgKGENCLAPrqktslkKACPG 208
Cdd:PHA00447 116 AEI-KAHHDVAP-------KACPS 131
PHA00447 PHA00447
lysozyme
 252-354 7.20e-05

lysozyme


Pssm-ID: 177282 [Multi-domain]  Cd Length: 142  Bit Score: 42.46  E-value: 7.20e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767909948 252 VRDIQSFYIDRLKScDIGYNFLVGQDGAIYEGVGWNVQGSSTPGYDDIALGITFMGtftGIPPNAAAlEAAQDLIQCAMV 331
Cdd:PHA00447  28 VREIRQWHKEQGWL-DVGYHFIIRRDGTVEEGRPEDVVGSHVKGYNSNSVGVCLVG---GIDDKGKF-DANFTPAQMQSL 102

                         90       100
                 ....*....|....*....|....*....
gi 767909948 332 KGYLT------PNYLLVGHSDVARTLSPG 354
Cdd:PHA00447 103 KSLLVtlkakyPGAEIKAHHDVAPKACPS 131
 
Name Accession Description Interval E-value
PGRP smart00701
Animal peptidoglycan recognition proteins homologous to Bacteriophage T3 lysozyme; The ...
 207-347 1.13e-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: 209.84  E-value: 1.13e-67
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767909948   207 PGVVPRSVWGAR-ETHCPRMTLPAKYGIIIHTAGRTCNISDECRLLVRDIQSFYIDRLKSCDIGYNFLVGQDGAIYEGVG 285
Cdd:smart00701   1 PPIVPRSEWGAKpRGHTPRLTRPVRYVIIHHTATPNCYTDAQCAQILRNIQAYHMEELGWCDIGYNFLVGGDGKVYEGRG 80

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767909948   286 WNVQGSSTPGYDDIALGITFMGTFTGIPPNAAALEAAQDLIQCAMVKGYLTPNYLLVGHSDV 347
Cdd:smart00701  81 WNVVGAHTGGYNDISLGIAFIGNFTDKLPTDAALDAAQDLLACAVQRGHLSPDYKLVGHRQV 142
PGRP smart00701
Animal peptidoglycan recognition proteins homologous to Bacteriophage T3 lysozyme; The ...
 49-190 2.04e-64

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: 201.37  E-value: 2.04e-64
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767909948    49 STTVSRKAWGAEAVGCSIQLTTPVNVLVIHHVPGLECHDQTVCSQRLRELQAHHVHNNSGCDVAYNFLVGDDGRVYEGVG 128
Cdd:smart00701   1 PPIVPRSEWGAKPRGHTPRLTRPVRYVIIHHTATPNCYTDAQCAQILRNIQAYHMEELGWCDIGYNFLVGGDGKVYEGRG 80

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767909948   129 WNIQGVHTQGYNNISLGFAFFGTKKGHSPSPAALSAMENLITYAVQKGHLSSSYVQPLLGKG 190
Cdd:smart00701  81 WNVVGAHTGGYNDISLGIAFIGNFTDKLPTDAALDAAQDLLACAVQRGHLSPDYKLVGHRQV 142
PGRP cd06583
Peptidoglycan recognition proteins (PGRPs) are pattern recognition receptors that bind, and in ...
 228-356 1.79e-35

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: 125.86  E-value: 1.79e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767909948 228 PAKYGIIIHTAGRTCNisdECRLLVRDIQSFYIdrLKSCDIGYNFLVGQDGAIYEGVGWNVQGSSTPG-YDDIALGITFM 306
Cdd:cd06583    1 PVKYVVIHHTANPNCY---TAAAAVRYLQNYHM--RGWSDISYHFLVGGDGRIYQGRGWNYVGWHAGGnYNSYSIGIELI 75

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 767909948 307 GTFTGIPPNAAALEAAQDLIQCAMVKGYLTPNYLLVGHSDVAR-TLSPGQA 356
Cdd:cd06583   76 GNFDGGPPTAAQLEALAELLAYLVKRYGIPPDYRIVGHRDVSPgTECPGDA 126
Ami_2 smart00644
Ami_2 domain;
228-353 6.04e-30

Ami_2 domain;


Pssm-ID: 214760 [Multi-domain]  Cd Length: 126  Bit Score: 111.30  E-value: 6.04e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767909948   228 PAKYGIIIHTAGRTCnisDECRLLVRDIQSFYIDrlkscDIGYNFLVGQDGAIYEGVGWN-----VQGSSTPGYDDIALG 302
Cdd:smart00644   1 PPPRGIVIHHTANSN---ASCANEARYMQNNHMN-----DIGYHFLVGGDGRVYQGVGWNyvawhAGGAHTPGYNDISIG 72

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....
gi 767909948   303 ITFMGTFTGI-PPNAAALEAAQDLIQCAMVKGYLTP--NYLLVGHSDVARTLSP 353
Cdd:smart00644  73 IEFIGSFDSDdEPFAEALYAALDLLAKLLKGAGLPPdgRYRIVGHRDVAPTEDP 126
PGRP cd06583
Peptidoglycan recognition proteins (PGRPs) are pattern recognition receptors that bind, and in ...
 71-208 1.71e-28

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: 107.76  E-value: 1.71e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767909948  71 PVNVLVIHHVPGLECHDqtvCSQRLRELQAHHVHNNSgcDVAYNFLVGDDGRVYEGVGWNIQGVHTQG-YNNISLGFAFF 149
Cdd:cd06583    1 PVKYVVIHHTANPNCYT---AAAAVRYLQNYHMRGWS--DISYHFLVGGDGRIYQGRGWNYVGWHAGGnYNSYSIGIELI 75

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 767909948 150 GTKKGHSPSPAALSAMENLITYAVQKGHLSSSYVqpllgkgencLAPRQKTSLKKACPG 208
Cdd:cd06583   76 GNFDGGPPTAAQLEALAELLAYLVKRYGIPPDYR----------IVGHRDVSPGTECPG 124
Amidase_2 pfam01510
N-acetylmuramoyl-L-alanine amidase; This family includes zinc amidases that have ...
 228-355 6.17e-23

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: 92.42  E-value: 6.17e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767909948  228 PAKYGIIIHTAGRTcniSDECRllvrdIQSFYIDRLKSCDIGYNFLVGQDGAIYE-----GVGWNVQGSstpGYDDIALG 302
Cdd:pfam01510   1 PIRYIVIHHTAGPS---FAGAL-----LPYAACIARGWSDVSYHYLIDRDGTIYQlvpenGRAWHAGNG---GGNDRSIG 69

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 767909948  303 ITFMGTFTGIPPNAAALEAAQDLIQCAMVKGYLTPNYLLVGHSDVARTLSPGQ 355
Cdd:pfam01510  70 IELEGNFGGDPPTDAQYEALARLLADLCKRYGIPPDRRIVGHRDVGRKTDPGP 122
Ami_2 smart00644
Ami_2 domain;
71-188 2.21e-21

Ami_2 domain;


Pssm-ID: 214760 [Multi-domain]  Cd Length: 126  Bit Score: 88.57  E-value: 2.21e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767909948    71 PVNVLVIHHVPGLEChdqTVCSQRLRELQAHHVHnnsgcDVAYNFLVGDDGRVYEGVGWN-----IQGVHTQGYNNISLG 145
Cdd:smart00644   1 PPPRGIVIHHTANSN---ASCANEARYMQNNHMN-----DIGYHFLVGGDGRVYQGVGWNyvawhAGGAHTPGYNDISIG 72

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 767909948   146 FAFFGTK-KGHSPSPAALSAMENLITYAVQKGHLSSSYVQPLLG 188
Cdd:smart00644  73 IEFIGSFdSDDEPFAEALYAALDLLAKLLKGAGLPPDGRYRIVG 116
Amidase_2 pfam01510
N-acetylmuramoyl-L-alanine amidase; This family includes zinc amidases that have ...
 71-182 4.40e-15

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: 70.85  E-value: 4.40e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767909948   71 PVNVLVIHHvpglechdqTVCSQRL-RELQAHHVHNNSGCDVAYNFLVGDDGRVYEGVGWNIQGVHT--QGYNNISLGFA 147
Cdd:pfam01510   1 PIRYIVIHH---------TAGPSFAgALLPYAACIARGWSDVSYHYLIDRDGTIYQLVPENGRAWHAgnGGGNDRSIGIE 71

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 767909948  148 FFGTKKGHSPSPAALSAMENLITYAVQKGHLSSSY 182
Cdd:pfam01510  72 LEGNFGGDPPTDAQYEALARLLADLCKRYGIPPDR 106
PHA00447 PHA00447
lysozyme
 110-208 3.76e-05

lysozyme


Pssm-ID: 177282 [Multi-domain]  Cd Length: 142  Bit Score: 43.23  E-value: 3.76e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767909948 110 DVAYNFLVGDDGRVYEGVGWNIQGVHTQGYNNISLGFAFFG--TKKGHSP---SPAALSAMENLITyavqkgHLSSSYVQ 184
Cdd:PHA00447  42 DVGYHFIIRRDGTVEEGRPEDVVGSHVKGYNSNSVGVCLVGgiDDKGKFDanfTPAQMQSLKSLLV------TLKAKYPG 115

                         90       100
                 ....*....|....*....|....
gi 767909948 185 PLLgKGENCLAPrqktslkKACPG 208
Cdd:PHA00447 116 AEI-KAHHDVAP-------KACPS 131
PHA00447 PHA00447
lysozyme
 252-354 7.20e-05

lysozyme


Pssm-ID: 177282 [Multi-domain]  Cd Length: 142  Bit Score: 42.46  E-value: 7.20e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767909948 252 VRDIQSFYIDRLKScDIGYNFLVGQDGAIYEGVGWNVQGSSTPGYDDIALGITFMGtftGIPPNAAAlEAAQDLIQCAMV 331
Cdd:PHA00447  28 VREIRQWHKEQGWL-DVGYHFIIRRDGTVEEGRPEDVVGSHVKGYNSNSVGVCLVG---GIDDKGKF-DANFTPAQMQSL 102

                         90       100
                 ....*....|....*....|....*....
gi 767909948 332 KGYLT------PNYLLVGHSDVARTLSPG 354
Cdd:PHA00447 103 KSLLVtlkakyPGAEIKAHHDVAPKACPS 131
 
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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