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Conserved domains on  [gi|56550073|ref|NP_065126|]
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peptidoglycan recognition protein 4 precursor [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 ...
 211-351 1.19e-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: 1.19e-67
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56550073    211 PGVVPRSVWGAR-ETHCPRMTLPAKYGIIIHTAGRTCNISDECRLLVRDIQSFYIDRLKSCDIGYNFLVGQDGAIYEGVG 289
Cdd:smart00701   1 PPIVPRSEWGAKpRGHTPRLTRPVRYVIIHHTATPNCYTDAQCAQILRNIQAYHMEELGWCDIGYNFLVGGDGKVYEGRG 80

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 56550073    290 WNVQGSSTPGYDDIALGITFMGTFTGIPPNAAALEAAQDLIQCAMVKGYLTPNYLLVGHSDV 351
Cdd:smart00701  81 WNVVGAHTGGYNDISLGIAFIGNFTDKLPTDAALDAAQDLLACAVQRGHLSPDYKLVGHRQV 142
PGRP smart00701
Animal peptidoglycan recognition proteins homologous to Bacteriophage T3 lysozyme; The ...
 53-194 2.17e-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: 2.17e-64
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56550073     53 STTVSRKAWGAEAVGCSIQLTTPVNVLVIHHVPGLECHDQTVCSQRLRELQAHHVHNNSGCDVAYNFLVGDDGRVYEGVG 132
Cdd:smart00701   1 PPIVPRSEWGAKPRGHTPRLTRPVRYVIIHHTATPNCYTDAQCAQILRNIQAYHMEELGWCDIGYNFLVGGDGKVYEGRG 80

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 56550073    133 WNIQGVHTQGYNNISLGFAFFGTKKGHSPSPAALSAMENLITYAVQKGHLSSSYVQPLLGKG 194
Cdd:smart00701  81 WNVVGAHTGGYNDISLGIAFIGNFTDKLPTDAALDAAQDLLACAVQRGHLSPDYKLVGHRQV 142
 
Name Accession Description Interval E-value
PGRP smart00701
Animal peptidoglycan recognition proteins homologous to Bacteriophage T3 lysozyme; The ...
 211-351 1.19e-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: 1.19e-67
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56550073    211 PGVVPRSVWGAR-ETHCPRMTLPAKYGIIIHTAGRTCNISDECRLLVRDIQSFYIDRLKSCDIGYNFLVGQDGAIYEGVG 289
Cdd:smart00701   1 PPIVPRSEWGAKpRGHTPRLTRPVRYVIIHHTATPNCYTDAQCAQILRNIQAYHMEELGWCDIGYNFLVGGDGKVYEGRG 80

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 56550073    290 WNVQGSSTPGYDDIALGITFMGTFTGIPPNAAALEAAQDLIQCAMVKGYLTPNYLLVGHSDV 351
Cdd:smart00701  81 WNVVGAHTGGYNDISLGIAFIGNFTDKLPTDAALDAAQDLLACAVQRGHLSPDYKLVGHRQV 142
PGRP smart00701
Animal peptidoglycan recognition proteins homologous to Bacteriophage T3 lysozyme; The ...
 53-194 2.17e-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: 2.17e-64
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56550073     53 STTVSRKAWGAEAVGCSIQLTTPVNVLVIHHVPGLECHDQTVCSQRLRELQAHHVHNNSGCDVAYNFLVGDDGRVYEGVG 132
Cdd:smart00701   1 PPIVPRSEWGAKPRGHTPRLTRPVRYVIIHHTATPNCYTDAQCAQILRNIQAYHMEELGWCDIGYNFLVGGDGKVYEGRG 80

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 56550073    133 WNIQGVHTQGYNNISLGFAFFGTKKGHSPSPAALSAMENLITYAVQKGHLSSSYVQPLLGKG 194
Cdd:smart00701  81 WNVVGAHTGGYNDISLGIAFIGNFTDKLPTDAALDAAQDLLACAVQRGHLSPDYKLVGHRQV 142
PGRP cd06583
Peptidoglycan recognition proteins (PGRPs) are pattern recognition receptors that bind, and in ...
 232-360 1.49e-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: 126.25  E-value: 1.49e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56550073 232 PAKYGIIIHTAGRTCNisdECRLLVRDIQSFYIdrLKSCDIGYNFLVGQDGAIYEGVGWNVQGSSTPG-YDDIALGITFM 310
Cdd:cd06583   1 PVKYVVIHHTANPNCY---TAAAAVRYLQNYHM--RGWSDISYHFLVGGDGRIYQGRGWNYVGWHAGGnYNSYSIGIELI 75

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|.
gi 56550073 311 GTFTGIPPNAAALEAAQDLIQCAMVKGYLTPNYLLVGHSDVAR-TLSPGQA 360
Cdd:cd06583  76 GNFDGGPPTAAQLEALAELLAYLVKRYGIPPDYRIVGHRDVSPgTECPGDA 126
PGRP cd06583
Peptidoglycan recognition proteins (PGRPs) are pattern recognition receptors that bind, and in ...
 75-212 1.39e-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: 1.39e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56550073  75 PVNVLVIHHVPGLECHDqtvCSQRLRELQAHHVHNNSgcDVAYNFLVGDDGRVYEGVGWNIQGVHTQG-YNNISLGFAFF 153
Cdd:cd06583   1 PVKYVVIHHTANPNCYT---AAAAVRYLQNYHMRGWS--DISYHFLVGGDGRIYQGRGWNYVGWHAGGnYNSYSIGIELI 75

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 56550073 154 GTKKGHSPSPAALSAMENLITYAVQKGHLSSSYVqpllgkgencLAPRQKTSLKKACPG 212
Cdd:cd06583  76 GNFDGGPPTAAQLEALAELLAYLVKRYGIPPDYR----------IVGHRDVSPGTECPG 124
Amidase_2 pfam01510
N-acetylmuramoyl-L-alanine amidase; This family includes zinc amidases that have ...
 232-359 5.85e-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: 92.80  E-value: 5.85e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56550073   232 PAKYGIIIHTAGRTcniSDECRllvrdIQSFYIDRLKSCDIGYNFLVGQDGAIYE-----GVGWNVQGSstpGYDDIALG 306
Cdd:pfam01510   1 PIRYIVIHHTAGPS---FAGAL-----LPYAACIARGWSDVSYHYLIDRDGTIYQlvpenGRAWHAGNG---GGNDRSIG 69

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 56550073   307 ITFMGTFTGIPPNAAALEAAQDLIQCAMVKGYLTPNYLLVGHSDVARTLSPGQ 359
Cdd:pfam01510  70 IELEGNFGGDPPTDAQYEALARLLADLCKRYGIPPDRRIVGHRDVGRKTDPGP 122
Amidase_2 pfam01510
N-acetylmuramoyl-L-alanine amidase; This family includes zinc amidases that have ...
 75-186 4.17e-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: 71.23  E-value: 4.17e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56550073    75 PVNVLVIHHvpglechdqTVCSQRL-RELQAHHVHNNSGCDVAYNFLVGDDGRVYEGVGWNIQGVHT--QGYNNISLGFA 151
Cdd:pfam01510   1 PIRYIVIHH---------TAGPSFAgALLPYAACIARGWSDVSYHYLIDRDGTIYQLVPENGRAWHAgnGGGNDRSIGIE 71

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 56550073   152 FFGTKKGHSPSPAALSAMENLITYAVQKGHLSSSY 186
Cdd:pfam01510  72 LEGNFGGDPPTDAQYEALARLLADLCKRYGIPPDR 106
PHA00447 PHA00447
lysozyme
 114-212 3.81e-05

lysozyme


Pssm-ID: 177282 [Multi-domain]  Cd Length: 142  Bit Score: 43.23  E-value: 3.81e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56550073  114 DVAYNFLVGDDGRVYEGVGWNIQGVHTQGYNNISLGFAFFG--TKKGHSP---SPAALSAMENLITyavqkgHLSSSYVQ 188
Cdd:PHA00447  42 DVGYHFIIRRDGTVEEGRPEDVVGSHVKGYNSNSVGVCLVGgiDDKGKFDanfTPAQMQSLKSLLV------TLKAKYPG 115

                         90       100
                 ....*....|....*....|....
gi 56550073  189 PLLgKGENCLAPrqktslkKACPG 212
Cdd:PHA00447 116 AEI-KAHHDVAP-------KACPS 131
PHA00447 PHA00447
lysozyme
 256-358 6.89e-05

lysozyme


Pssm-ID: 177282 [Multi-domain]  Cd Length: 142  Bit Score: 42.46  E-value: 6.89e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56550073  256 VRDIQSFYIDRLKScDIGYNFLVGQDGAIYEGVGWNVQGSSTPGYDDIALGITFMGtftGIPPNAAAlEAAQDLIQCAMV 335
Cdd:PHA00447  28 VREIRQWHKEQGWL-DVGYHFIIRRDGTVEEGRPEDVVGSHVKGYNSNSVGVCLVG---GIDDKGKF-DANFTPAQMQSL 102

                         90       100
                 ....*....|....*....|....*....
gi 56550073  336 KGYLT------PNYLLVGHSDVARTLSPG 358
Cdd:PHA00447 103 KSLLVtlkakyPGAEIKAHHDVAPKACPS 131
 
Name Accession Description Interval E-value
PGRP smart00701
Animal peptidoglycan recognition proteins homologous to Bacteriophage T3 lysozyme; The ...
 211-351 1.19e-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: 1.19e-67
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56550073    211 PGVVPRSVWGAR-ETHCPRMTLPAKYGIIIHTAGRTCNISDECRLLVRDIQSFYIDRLKSCDIGYNFLVGQDGAIYEGVG 289
Cdd:smart00701   1 PPIVPRSEWGAKpRGHTPRLTRPVRYVIIHHTATPNCYTDAQCAQILRNIQAYHMEELGWCDIGYNFLVGGDGKVYEGRG 80

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 56550073    290 WNVQGSSTPGYDDIALGITFMGTFTGIPPNAAALEAAQDLIQCAMVKGYLTPNYLLVGHSDV 351
Cdd:smart00701  81 WNVVGAHTGGYNDISLGIAFIGNFTDKLPTDAALDAAQDLLACAVQRGHLSPDYKLVGHRQV 142
PGRP smart00701
Animal peptidoglycan recognition proteins homologous to Bacteriophage T3 lysozyme; The ...
 53-194 2.17e-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: 2.17e-64
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56550073     53 STTVSRKAWGAEAVGCSIQLTTPVNVLVIHHVPGLECHDQTVCSQRLRELQAHHVHNNSGCDVAYNFLVGDDGRVYEGVG 132
Cdd:smart00701   1 PPIVPRSEWGAKPRGHTPRLTRPVRYVIIHHTATPNCYTDAQCAQILRNIQAYHMEELGWCDIGYNFLVGGDGKVYEGRG 80

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 56550073    133 WNIQGVHTQGYNNISLGFAFFGTKKGHSPSPAALSAMENLITYAVQKGHLSSSYVQPLLGKG 194
Cdd:smart00701  81 WNVVGAHTGGYNDISLGIAFIGNFTDKLPTDAALDAAQDLLACAVQRGHLSPDYKLVGHRQV 142
PGRP cd06583
Peptidoglycan recognition proteins (PGRPs) are pattern recognition receptors that bind, and in ...
 232-360 1.49e-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: 126.25  E-value: 1.49e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56550073 232 PAKYGIIIHTAGRTCNisdECRLLVRDIQSFYIdrLKSCDIGYNFLVGQDGAIYEGVGWNVQGSSTPG-YDDIALGITFM 310
Cdd:cd06583   1 PVKYVVIHHTANPNCY---TAAAAVRYLQNYHM--RGWSDISYHFLVGGDGRIYQGRGWNYVGWHAGGnYNSYSIGIELI 75

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|.
gi 56550073 311 GTFTGIPPNAAALEAAQDLIQCAMVKGYLTPNYLLVGHSDVAR-TLSPGQA 360
Cdd:cd06583  76 GNFDGGPPTAAQLEALAELLAYLVKRYGIPPDYRIVGHRDVSPgTECPGDA 126
Ami_2 smart00644
Ami_2 domain;
232-357 5.03e-30

Ami_2 domain;


Pssm-ID: 214760 [Multi-domain]  Cd Length: 126  Bit Score: 111.68  E-value: 5.03e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56550073    232 PAKYGIIIHTAGRTCnisDECRLLVRDIQSFYIDrlkscDIGYNFLVGQDGAIYEGVGWN-----VQGSSTPGYDDIALG 306
Cdd:smart00644   1 PPPRGIVIHHTANSN---ASCANEARYMQNNHMN-----DIGYHFLVGGDGRVYQGVGWNyvawhAGGAHTPGYNDISIG 72

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....
gi 56550073    307 ITFMGTFTGI-PPNAAALEAAQDLIQCAMVKGYLTP--NYLLVGHSDVARTLSP 357
Cdd:smart00644  73 IEFIGSFDSDdEPFAEALYAALDLLAKLLKGAGLPPdgRYRIVGHRDVAPTEDP 126
PGRP cd06583
Peptidoglycan recognition proteins (PGRPs) are pattern recognition receptors that bind, and in ...
 75-212 1.39e-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: 1.39e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56550073  75 PVNVLVIHHVPGLECHDqtvCSQRLRELQAHHVHNNSgcDVAYNFLVGDDGRVYEGVGWNIQGVHTQG-YNNISLGFAFF 153
Cdd:cd06583   1 PVKYVVIHHTANPNCYT---AAAAVRYLQNYHMRGWS--DISYHFLVGGDGRIYQGRGWNYVGWHAGGnYNSYSIGIELI 75

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 56550073 154 GTKKGHSPSPAALSAMENLITYAVQKGHLSSSYVqpllgkgencLAPRQKTSLKKACPG 212
Cdd:cd06583  76 GNFDGGPPTAAQLEALAELLAYLVKRYGIPPDYR----------IVGHRDVSPGTECPG 124
Amidase_2 pfam01510
N-acetylmuramoyl-L-alanine amidase; This family includes zinc amidases that have ...
 232-359 5.85e-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: 92.80  E-value: 5.85e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56550073   232 PAKYGIIIHTAGRTcniSDECRllvrdIQSFYIDRLKSCDIGYNFLVGQDGAIYE-----GVGWNVQGSstpGYDDIALG 306
Cdd:pfam01510   1 PIRYIVIHHTAGPS---FAGAL-----LPYAACIARGWSDVSYHYLIDRDGTIYQlvpenGRAWHAGNG---GGNDRSIG 69

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 56550073   307 ITFMGTFTGIPPNAAALEAAQDLIQCAMVKGYLTPNYLLVGHSDVARTLSPGQ 359
Cdd:pfam01510  70 IELEGNFGGDPPTDAQYEALARLLADLCKRYGIPPDRRIVGHRDVGRKTDPGP 122
Ami_2 smart00644
Ami_2 domain;
75-192 1.93e-21

Ami_2 domain;


Pssm-ID: 214760 [Multi-domain]  Cd Length: 126  Bit Score: 88.57  E-value: 1.93e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56550073     75 PVNVLVIHHVPGLEChdqTVCSQRLRELQAHHVHnnsgcDVAYNFLVGDDGRVYEGVGWN-----IQGVHTQGYNNISLG 149
Cdd:smart00644   1 PPPRGIVIHHTANSN---ASCANEARYMQNNHMN-----DIGYHFLVGGDGRVYQGVGWNyvawhAGGAHTPGYNDISIG 72

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 56550073    150 FAFFGTK-KGHSPSPAALSAMENLITYAVQKGHLSSSYVQPLLG 192
Cdd:smart00644  73 IEFIGSFdSDDEPFAEALYAALDLLAKLLKGAGLPPDGRYRIVG 116
Amidase_2 pfam01510
N-acetylmuramoyl-L-alanine amidase; This family includes zinc amidases that have ...
 75-186 4.17e-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: 71.23  E-value: 4.17e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56550073    75 PVNVLVIHHvpglechdqTVCSQRL-RELQAHHVHNNSGCDVAYNFLVGDDGRVYEGVGWNIQGVHT--QGYNNISLGFA 151
Cdd:pfam01510   1 PIRYIVIHH---------TAGPSFAgALLPYAACIARGWSDVSYHYLIDRDGTIYQLVPENGRAWHAgnGGGNDRSIGIE 71

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 56550073   152 FFGTKKGHSPSPAALSAMENLITYAVQKGHLSSSY 186
Cdd:pfam01510  72 LEGNFGGDPPTDAQYEALARLLADLCKRYGIPPDR 106
PHA00447 PHA00447
lysozyme
 114-212 3.81e-05

lysozyme


Pssm-ID: 177282 [Multi-domain]  Cd Length: 142  Bit Score: 43.23  E-value: 3.81e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56550073  114 DVAYNFLVGDDGRVYEGVGWNIQGVHTQGYNNISLGFAFFG--TKKGHSP---SPAALSAMENLITyavqkgHLSSSYVQ 188
Cdd:PHA00447  42 DVGYHFIIRRDGTVEEGRPEDVVGSHVKGYNSNSVGVCLVGgiDDKGKFDanfTPAQMQSLKSLLV------TLKAKYPG 115

                         90       100
                 ....*....|....*....|....
gi 56550073  189 PLLgKGENCLAPrqktslkKACPG 212
Cdd:PHA00447 116 AEI-KAHHDVAP-------KACPS 131
PHA00447 PHA00447
lysozyme
 256-358 6.89e-05

lysozyme


Pssm-ID: 177282 [Multi-domain]  Cd Length: 142  Bit Score: 42.46  E-value: 6.89e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56550073  256 VRDIQSFYIDRLKScDIGYNFLVGQDGAIYEGVGWNVQGSSTPGYDDIALGITFMGtftGIPPNAAAlEAAQDLIQCAMV 335
Cdd:PHA00447  28 VREIRQWHKEQGWL-DVGYHFIIRRDGTVEEGRPEDVVGSHVKGYNSNSVGVCLVG---GIDDKGKF-DANFTPAQMQSL 102

                         90       100
                 ....*....|....*....|....*....
gi 56550073  336 KGYLT------PNYLLVGHSDVARTLSPG 358
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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