NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1259580057|gb|PER59365|]
View 

N-acetylmuramoyl-L-alanine amidase [Bacillus thuringiensis]

Protein Classification

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
CwlA COG5632
N-acetylmuramoyl-L-alanine amidase CwlA [Cell wall/membrane/envelope biogenesis];
1-177 8.94e-60

N-acetylmuramoyl-L-alanine amidase CwlA [Cell wall/membrane/envelope biogenesis];


:

Pssm-ID: 444359  Cd Length: 177  Bit Score: 186.33  E-value: 8.94e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1259580057   1 MEIKQMLVPASRYpVLCPYPMTPTEVTFHNTYND-ASALNERNNVANNSTGTSFHIAVDDKEAIQLISFNRNAWHAGDGv 79
Cdd:COG5632     3 VNIKKKLIPKNNS-YRPGYKMKPKGIVIHNTANPgATAENHANYFNNNNRSASWHYFVDDKEIIQHIPLNENAWHAGDG- 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1259580057  80 NGRGNRHSIGVEICYSKSGgeRYRKAELNAIKVIRQLMDTFNIPISKVKTHQERNGKYCPHRMLDEGRVQW--FKSQLIQ 157
Cdd:COG5632    81 TGPGNRRSIGIEICENKDG--DFAKAYENAAELIAYLMKKYGIPIDNVVRHYDWSGKNCPHGLLANGGYRWdqFKADVKS 158

                         170       180
                  ....*....|....*....|
gi 1259580057 158 TNQKeqgvGIIVNPFNKVVT 177
Cdd:COG5632   159 ALNG----LSTVKPYTKVVK 174
CBD_PlyG super family cl13548
PlyG Cell wall binding domain; This domain is found in bacteria and viruses. This domain is ...
 194-239 4.74e-10

PlyG Cell wall binding domain; This domain is found in bacteria and viruses. This domain is about 50 amino acids in length. This domain is thought to be a cell wall binding domain.


The actual alignment was detected with superfamily member pfam12123:

Pssm-ID: 338253  Cd Length: 44  Bit Score: 53.65  E-value: 4.74e-10
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1259580057 194 ALGFESRVISNGDkqGLVRFETAHRQGNELDRATAWLDAKGLKYFY 239
Cdd:pfam12123   1 SLGMTGKIILQPD--GLTYFITDPTSDTQLDKFTAWLDRKGWWYEY 44
 
Name Accession Description Interval E-value
CwlA COG5632
N-acetylmuramoyl-L-alanine amidase CwlA [Cell wall/membrane/envelope biogenesis];
1-177 8.94e-60

N-acetylmuramoyl-L-alanine amidase CwlA [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 444359  Cd Length: 177  Bit Score: 186.33  E-value: 8.94e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1259580057   1 MEIKQMLVPASRYpVLCPYPMTPTEVTFHNTYND-ASALNERNNVANNSTGTSFHIAVDDKEAIQLISFNRNAWHAGDGv 79
Cdd:COG5632     3 VNIKKKLIPKNNS-YRPGYKMKPKGIVIHNTANPgATAENHANYFNNNNRSASWHYFVDDKEIIQHIPLNENAWHAGDG- 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1259580057  80 NGRGNRHSIGVEICYSKSGgeRYRKAELNAIKVIRQLMDTFNIPISKVKTHQERNGKYCPHRMLDEGRVQW--FKSQLIQ 157
Cdd:COG5632    81 TGPGNRRSIGIEICENKDG--DFAKAYENAAELIAYLMKKYGIPIDNVVRHYDWSGKNCPHGLLANGGYRWdqFKADVKS 158

                         170       180
                  ....*....|....*....|
gi 1259580057 158 TNQKeqgvGIIVNPFNKVVT 177
Cdd:COG5632   159 ALNG----LSTVKPYTKVVK 174
Ami_2 smart00644
Ami_2 domain;
21-139 1.07e-23

Ami_2 domain;


Pssm-ID: 214760 [Multi-domain]  Cd Length: 126  Bit Score: 92.04  E-value: 1.07e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1259580057   21 MTPTEVTFHNTYND-ASALNERNNVANNST-GTSFHIAVD-DKEAIQLISFNRNAWHAGDGVNGRGNRHSIGVEICYSKS 97
Cdd:smart00644   1 PPPRGIVIHHTANSnASCANEARYMQNNHMnDIGYHFLVGgDGRVYQGVGWNYVAWHAGGAHTPGYNDISIGIEFIGSFD 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 1259580057   98 G-GERYRKAELNAIKVIRQLMDTFNIPIS---KVKTHQERNGKYCP 139
Cdd:smart00644  81 SdDEPFAEALYAALDLLAKLLKGAGLPPDgryRIVGHRDVAPTEDP 126
Amidase_2 pfam01510
N-acetylmuramoyl-L-alanine amidase; This family includes zinc amidases that have ...
 26-141 1.71e-22

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: 88.95  E-value: 1.71e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1259580057  26 VTFHNTYN---DASALNERNNVANNSTGTSFHIAVDDKEAI-QLISFNRNAWHAGdgvNGRGNRHSIGVEICYSKSGGER 101
Cdd:pfam01510   5 IVIHHTAGpsfAGALLPYAACIARGWSDVSYHYLIDRDGTIyQLVPENGRAWHAG---NGGGNDRSIGIELEGNFGGDPP 81

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1259580057 102 YRKAELNAIKVIRQLMDTFNIPI-SKVKTHQERNGKYCPHR 141
Cdd:pfam01510  82 TDAQYEALARLLADLCKRYGIPPdRRIVGHRDVGRKTDPGP 122
PGRP cd06583
Peptidoglycan recognition proteins (PGRPs) are pattern recognition receptors that bind, and in ...
 23-142 2.11e-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: 88.88  E-value: 2.11e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1259580057  23 PTEVTFHNTYNDASALNE------RNNVANNSTGTSFHIAVD-DKEAIQLISFNRNAWHAGdgvnGRGNRHSIGVEICYS 95
Cdd:cd06583     2 VKYVVIHHTANPNCYTAAaavrylQNYHMRGWSDISYHFLVGgDGRIYQGRGWNYVGWHAG----GNYNSYSIGIELIGN 77

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1259580057  96 KSGGERYRKAELNAIKVIRQLMDTFNIP-ISKVKTHQE-RNGKYCPHRM 142
Cdd:cd06583    78 FDGGPPTAAQLEALAELLAYLVKRYGIPpDYRIVGHRDvSPGTECPGDA 126
CBD_PlyG pfam12123
PlyG Cell wall binding domain; This domain is found in bacteria and viruses. This domain is ...
 194-239 4.74e-10

PlyG Cell wall binding domain; This domain is found in bacteria and viruses. This domain is about 50 amino acids in length. This domain is thought to be a cell wall binding domain.


Pssm-ID: 338253  Cd Length: 44  Bit Score: 53.65  E-value: 4.74e-10
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1259580057 194 ALGFESRVISNGDkqGLVRFETAHRQGNELDRATAWLDAKGLKYFY 239
Cdd:pfam12123   1 SLGMTGKIILQPD--GLTYFITDPTSDTQLDKFTAWLDRKGWWYEY 44
PRK11789 PRK11789
1,6-anhydro-N-acetylmuramyl-L-alanine amidase AmpD;
59-131 1.11e-03

1,6-anhydro-N-acetylmuramyl-L-alanine amidase AmpD;


Pssm-ID: 236984  Cd Length: 185  Bit Score: 38.63  E-value: 1.11e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1259580057  59 DKEAIQLISFNRNAWHAGDGV-NGRG--NRHSIGVEIcySKSGGERYRKAELNA-IKVIRQLMDTFNIPISKVKTHQ 131
Cdd:PRK11789   83 DGEIVQFVSFDDRAWHAGVSSfQGRErcNDFSIGIEL--EGTDTLPFTDAQYQAlAALTRALRAAYPIIAERITGHS 157
 
Name Accession Description Interval E-value
CwlA COG5632
N-acetylmuramoyl-L-alanine amidase CwlA [Cell wall/membrane/envelope biogenesis];
1-177 8.94e-60

N-acetylmuramoyl-L-alanine amidase CwlA [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 444359  Cd Length: 177  Bit Score: 186.33  E-value: 8.94e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1259580057   1 MEIKQMLVPASRYpVLCPYPMTPTEVTFHNTYND-ASALNERNNVANNSTGTSFHIAVDDKEAIQLISFNRNAWHAGDGv 79
Cdd:COG5632     3 VNIKKKLIPKNNS-YRPGYKMKPKGIVIHNTANPgATAENHANYFNNNNRSASWHYFVDDKEIIQHIPLNENAWHAGDG- 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1259580057  80 NGRGNRHSIGVEICYSKSGgeRYRKAELNAIKVIRQLMDTFNIPISKVKTHQERNGKYCPHRMLDEGRVQW--FKSQLIQ 157
Cdd:COG5632    81 TGPGNRRSIGIEICENKDG--DFAKAYENAAELIAYLMKKYGIPIDNVVRHYDWSGKNCPHGLLANGGYRWdqFKADVKS 158

                         170       180
                  ....*....|....*....|
gi 1259580057 158 TNQKeqgvGIIVNPFNKVVT 177
Cdd:COG5632   159 ALNG----LSTVKPYTKVVK 174
Ami_2 smart00644
Ami_2 domain;
21-139 1.07e-23

Ami_2 domain;


Pssm-ID: 214760 [Multi-domain]  Cd Length: 126  Bit Score: 92.04  E-value: 1.07e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1259580057   21 MTPTEVTFHNTYND-ASALNERNNVANNST-GTSFHIAVD-DKEAIQLISFNRNAWHAGDGVNGRGNRHSIGVEICYSKS 97
Cdd:smart00644   1 PPPRGIVIHHTANSnASCANEARYMQNNHMnDIGYHFLVGgDGRVYQGVGWNYVAWHAGGAHTPGYNDISIGIEFIGSFD 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 1259580057   98 G-GERYRKAELNAIKVIRQLMDTFNIPIS---KVKTHQERNGKYCP 139
Cdd:smart00644  81 SdDEPFAEALYAALDLLAKLLKGAGLPPDgryRIVGHRDVAPTEDP 126
Amidase_2 pfam01510
N-acetylmuramoyl-L-alanine amidase; This family includes zinc amidases that have ...
 26-141 1.71e-22

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: 88.95  E-value: 1.71e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1259580057  26 VTFHNTYN---DASALNERNNVANNSTGTSFHIAVDDKEAI-QLISFNRNAWHAGdgvNGRGNRHSIGVEICYSKSGGER 101
Cdd:pfam01510   5 IVIHHTAGpsfAGALLPYAACIARGWSDVSYHYLIDRDGTIyQLVPENGRAWHAG---NGGGNDRSIGIELEGNFGGDPP 81

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1259580057 102 YRKAELNAIKVIRQLMDTFNIPI-SKVKTHQERNGKYCPHR 141
Cdd:pfam01510  82 TDAQYEALARLLADLCKRYGIPPdRRIVGHRDVGRKTDPGP 122
PGRP cd06583
Peptidoglycan recognition proteins (PGRPs) are pattern recognition receptors that bind, and in ...
 23-142 2.11e-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: 88.88  E-value: 2.11e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1259580057  23 PTEVTFHNTYNDASALNE------RNNVANNSTGTSFHIAVD-DKEAIQLISFNRNAWHAGdgvnGRGNRHSIGVEICYS 95
Cdd:cd06583     2 VKYVVIHHTANPNCYTAAaavrylQNYHMRGWSDISYHFLVGgDGRIYQGRGWNYVGWHAG----GNYNSYSIGIELIGN 77

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1259580057  96 KSGGERYRKAELNAIKVIRQLMDTFNIP-ISKVKTHQE-RNGKYCPHRM 142
Cdd:cd06583    78 FDGGPPTAAQLEALAELLAYLVKRYGIPpDYRIVGHRDvSPGTECPGDA 126
AmpD COG3023
N-acetyl-anhydromuramyl-L-alanine amidase AmpD [Cell wall/membrane/envelope biogenesis];
18-132 6.05e-13

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


Pssm-ID: 442259  Cd Length: 167  Bit Score: 64.50  E-value: 6.05e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1259580057  18 PYPMTPTEVTFHNT--YNDASALNErnnVANNSTGTSFHIAVD-DKEAIQLISFNRNAWHAGDGV-NGRG--NRHSIGVE 91
Cdd:COG3023    22 PAGAEIDLIVIHYTagPPGGGALDW---LTDPALRVSAHYLIDrDGEIYQLVPEDDRAWHAGVSSwRGRTnlNDFSIGIE 98

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1259580057  92 ICYSKSGGERYRKAELNA-IKVIRQLMDTFNIPISKVKTHQE 132
Cdd:COG3023    99 LENPGHGWAPFTEAQYEAlAALLRDLCARYGIPPDHIVGHSD 140
CBD_PlyG pfam12123
PlyG Cell wall binding domain; This domain is found in bacteria and viruses. This domain is ...
 194-239 4.74e-10

PlyG Cell wall binding domain; This domain is found in bacteria and viruses. This domain is about 50 amino acids in length. This domain is thought to be a cell wall binding domain.


Pssm-ID: 338253  Cd Length: 44  Bit Score: 53.65  E-value: 4.74e-10
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1259580057 194 ALGFESRVISNGDkqGLVRFETAHRQGNELDRATAWLDAKGLKYFY 239
Cdd:pfam12123   1 SLGMTGKIILQPD--GLTYFITDPTSDTQLDKFTAWLDRKGWWYEY 44
PRK11789 PRK11789
1,6-anhydro-N-acetylmuramyl-L-alanine amidase AmpD;
59-131 1.11e-03

1,6-anhydro-N-acetylmuramyl-L-alanine amidase AmpD;


Pssm-ID: 236984  Cd Length: 185  Bit Score: 38.63  E-value: 1.11e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1259580057  59 DKEAIQLISFNRNAWHAGDGV-NGRG--NRHSIGVEIcySKSGGERYRKAELNA-IKVIRQLMDTFNIPISKVKTHQ 131
Cdd:PRK11789   83 DGEIVQFVSFDDRAWHAGVSSfQGRErcNDFSIGIEL--EGTDTLPFTDAQYQAlAALTRALRAAYPIIAERITGHS 157
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH