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Conserved domains on  [gi|1176239922|gb|OQY48385|]
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hypothetical protein B6242_02480 [Anaerolineaceae bacterium 4572_78]

Protein Classification

peptidoglycan recognition family protein( domain architecture ID 10159278)

peptidoglycan recognition protein (PGRP) family protein is a pattern recognition receptor that binds, and in certain cases, hydrolyzes peptidoglycans (PGNs) of bacterial cell walls

CATH:  3.40.80.10
Gene Ontology:  GO:0042834|GO:0046872
PubMed:  16930467
SCOP:  4001915

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Amidase_2 pfam01510
N-acetylmuramoyl-L-alanine amidase; This family includes zinc amidases that have ...
 571-691 8.30e-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: 91.26  E-value: 8.30e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176239922 571 IKRIIIHHTATSSMTTiERIAQYQVTNRGVYGITYHYCVMADGHIFQTEPLESVSLHAA--DFSQDSVGVALIGNFTQQL 648
Cdd:pfam01510   2 IRYIVIHHTAGPSFAG-ALLPYAACIARGWSDVSYHYLIDRDGTIYQLVPENGRAWHAGngGGNDRSIGIELEGNFGGDP 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1176239922 649 PPQKQMRATAQLIAMLSAQLNIlISDENVIGCREVIRTSSPGN 691
Cdd:pfam01510  81 PTDAQYEALARLLADLCKRYGI-PPDRRIVGHRDVGRKTDPGP 122
PGRP cd06583
Peptidoglycan recognition proteins (PGRPs) are pattern recognition receptors that bind, and in ...
 386-504 7.73e-13

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: 65.77  E-value: 7.73e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176239922 386 IKRLILYHSVSGATITPKALANYHVNS--RNFAGIRYHYCVTNEGKVYQTQPLMIVSPHAG-SYSQESIIICLIGNFSDN 462
Cdd:cd06583     2 VKYVVIHHTANPNCYTAAAAVRYLQNYhmRGWSDISYHFLVGGDGRIYQGRGWNYVGWHAGgNYNSYSIGIELIGNFDGG 81

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1176239922 463 PPPTKQLGGTASLLAYLRSELHLGEGS-VFAYRELSHV-ASPGD 504
Cdd:cd06583    82 PPTAAQLEALAELLAYLVKRYGIPPDYrIVGHRDVSPGtECPGD 125
 
Name Accession Description Interval E-value
Amidase_2 pfam01510
N-acetylmuramoyl-L-alanine amidase; This family includes zinc amidases that have ...
 571-691 8.30e-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: 91.26  E-value: 8.30e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176239922 571 IKRIIIHHTATSSMTTiERIAQYQVTNRGVYGITYHYCVMADGHIFQTEPLESVSLHAA--DFSQDSVGVALIGNFTQQL 648
Cdd:pfam01510   2 IRYIVIHHTAGPSFAG-ALLPYAACIARGWSDVSYHYLIDRDGTIYQLVPENGRAWHAGngGGNDRSIGIELEGNFGGDP 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1176239922 649 PPQKQMRATAQLIAMLSAQLNIlISDENVIGCREVIRTSSPGN 691
Cdd:pfam01510  81 PTDAQYEALARLLADLCKRYGI-PPDRRIVGHRDVGRKTDPGP 122
PGRP cd06583
Peptidoglycan recognition proteins (PGRPs) are pattern recognition receptors that bind, and in ...
 571-691 4.18e-19

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: 83.88  E-value: 4.18e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176239922 571 IKRIIIHHTATSSMTTIERIAQY--QVTNRGVYGITYHYCVMADGHIFQTEPLESVSLHAADFSQD-SVGVALIGNFTQQ 647
Cdd:cd06583     2 VKYVVIHHTANPNCYTAAAAVRYlqNYHMRGWSDISYHFLVGGDGRIYQGRGWNYVGWHAGGNYNSySIGIELIGNFDGG 81

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1176239922 648 LPPQKQMRATAQLIAMLSAQLNIlISDENVIGCREVIR-TSSPGN 691
Cdd:cd06583    82 PPTAAQLEALAELLAYLVKRYGI-PPDYRIVGHRDVSPgTECPGD 125
PGRP smart00701
Animal peptidoglycan recognition proteins homologous to Bacteriophage T3 lysozyme; The ...
 568-662 2.39e-13

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: 67.71  E-value: 2.39e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176239922  568 RRAIKRIIIHHTATSSMTTIER-------IAQYQVTNRGVYGITYHYCVMADGHIFQTEPLESVSLHAADFSQDSVGVAL 640
Cdd:smart00701  21 TRPVRYVIIHHTATPNCYTDAQcaqilrnIQAYHMEELGWCDIGYNFLVGGDGKVYEGRGWNVVGAHTGGYNDISLGIAF 100

                           90       100
                   ....*....|....*....|..
gi 1176239922  641 IGNFTQQLPPQKQMRATAQLIA 662
Cdd:smart00701 101 IGNFTDKLPTDAALDAAQDLLA 122
PGRP cd06583
Peptidoglycan recognition proteins (PGRPs) are pattern recognition receptors that bind, and in ...
 386-504 7.73e-13

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: 65.77  E-value: 7.73e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176239922 386 IKRLILYHSVSGATITPKALANYHVNS--RNFAGIRYHYCVTNEGKVYQTQPLMIVSPHAG-SYSQESIIICLIGNFSDN 462
Cdd:cd06583     2 VKYVVIHHTANPNCYTAAAAVRYLQNYhmRGWSDISYHFLVGGDGRIYQGRGWNYVGWHAGgNYNSYSIGIELIGNFDGG 81

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1176239922 463 PPPTKQLGGTASLLAYLRSELHLGEGS-VFAYRELSHV-ASPGD 504
Cdd:cd06583    82 PPTAAQLEALAELLAYLVKRYGIPPDYrIVGHRDVSPGtECPGD 125
PGRP smart00701
Animal peptidoglycan recognition proteins homologous to Bacteriophage T3 lysozyme; The ...
 375-478 1.50e-11

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: 62.70  E-value: 1.50e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176239922  375 TTPYQSRdisAIKRLILYHSVSGATITP-------KALANYHVNSRNFAGIRYHYCVTNEGKVYQTQPLMIVSPHAGSYS 447
Cdd:smart00701  16 HTPRLTR---PVRYVIIHHTATPNCYTDaqcaqilRNIQAYHMEELGWCDIGYNFLVGGDGKVYEGRGWNVVGAHTGGYN 92

                           90       100       110
                   ....*....|....*....|....*....|.
gi 1176239922  448 QESIIICLIGNFSDNPPPTKQLGGTASLLAY 478
Cdd:smart00701  93 DISLGIAFIGNFTDKLPTDAALDAAQDLLAC 123
Amidase_2 pfam01510
N-acetylmuramoyl-L-alanine amidase; This family includes zinc amidases that have ...
 386-504 3.25e-09

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: 55.44  E-value: 3.25e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176239922 386 IKRLILYHSVSGATiTPKALANYHVNSRNFAGIRYHYCVTNEGKVYQTQPLMIVSPHAG--SYSQESIIICLIGNFSDNP 463
Cdd:pfam01510   2 IRYIVIHHTAGPSF-AGALLPYAACIARGWSDVSYHYLIDRDGTIYQLVPENGRAWHAGngGGNDRSIGIELEGNFGGDP 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1176239922 464 PPTKQLGGTASLLAYLRSELHL-GEGSVFAYRELSHVASPGD 504
Cdd:pfam01510  81 PTDAQYEALARLLADLCKRYGIpPDRRIVGHRDVGRKTDPGP 122
PHA00447 PHA00447
lysozyme
 568-667 2.23e-08

lysozyme


Pssm-ID: 177282 [Multi-domain]  Cd Length: 142  Bit Score: 53.63  E-value: 2.23e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176239922 568 RRAIKRIIIHHTAT-SSM-TTIERIAQYQVtNRGVYGITYHYCVMADGHIFQTEPLESVSLHAADFSQDSVGVALIGNFT 645
Cdd:PHA00447    7 RSSTKAIFVHCSATkPSMdVGVREIRQWHK-EQGWLDVGYHFIIRRDGTVEEGRPEDVVGSHVKGYNSNSVGVCLVGGID 85

                          90       100
                  ....*....|....*....|....*..
gi 1176239922 646 QQLPPQ-----KQMRATAQLIAMLSAQ 667
Cdd:PHA00447   86 DKGKFDanftpAQMQSLKSLLVTLKAK 112
AmpD COG3023
N-acetyl-anhydromuramyl-L-alanine amidase AmpD [Cell wall/membrane/envelope biogenesis];
565-679 6.79e-08

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


Pssm-ID: 442259  Cd Length: 167  Bit Score: 52.56  E-value: 6.79e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176239922 565 RRNRRAIKRIIIHHTATSSMT-TIERIAQyqvTNRGVygiTYHYCVMADGHIFQTEPLESVSLHAA-----------DFs 632
Cdd:COG3023    21 RPAGAEIDLIVIHYTAGPPGGgALDWLTD---PALRV---SAHYLIDRDGEIYQLVPEDDRAWHAGvsswrgrtnlnDF- 93

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1176239922 633 qdSVGVALIGNFTQQLP-PQKQMRATAQLIAMLSAQLNILIsdENVIG 679
Cdd:COG3023    94 --SIGIELENPGHGWAPfTEAQYEALAALLRDLCARYGIPP--DHIVG 137
PHA00447 PHA00447
lysozyme
 400-509 7.74e-05

lysozyme


Pssm-ID: 177282 [Multi-domain]  Cd Length: 142  Bit Score: 43.23  E-value: 7.74e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176239922 400 ITPKALANYHVNsRNFAGIRYHYCVTNEGKVYQTQPLMIVSPHAGSYSQESIIICLIGNFSDNPPPT-----KQLGGTAS 474
Cdd:PHA00447   26 VGVREIRQWHKE-QGWLDVGYHFIIRRDGTVEEGRPEDVVGSHVKGYNSNSVGVCLVGGIDDKGKFDanftpAQMQSLKS 104

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1176239922 475 LLAYLRSELHlgEGSVFAYRELSHVASPGDTWTEW 509
Cdd:PHA00447  105 LLVTLKAKYP--GAEIKAHHDVAPKACPSFDLQRW 137
 
Name Accession Description Interval E-value
Amidase_2 pfam01510
N-acetylmuramoyl-L-alanine amidase; This family includes zinc amidases that have ...
 571-691 8.30e-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: 91.26  E-value: 8.30e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176239922 571 IKRIIIHHTATSSMTTiERIAQYQVTNRGVYGITYHYCVMADGHIFQTEPLESVSLHAA--DFSQDSVGVALIGNFTQQL 648
Cdd:pfam01510   2 IRYIVIHHTAGPSFAG-ALLPYAACIARGWSDVSYHYLIDRDGTIYQLVPENGRAWHAGngGGNDRSIGIELEGNFGGDP 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1176239922 649 PPQKQMRATAQLIAMLSAQLNIlISDENVIGCREVIRTSSPGN 691
Cdd:pfam01510  81 PTDAQYEALARLLADLCKRYGI-PPDRRIVGHRDVGRKTDPGP 122
PGRP cd06583
Peptidoglycan recognition proteins (PGRPs) are pattern recognition receptors that bind, and in ...
 571-691 4.18e-19

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: 83.88  E-value: 4.18e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176239922 571 IKRIIIHHTATSSMTTIERIAQY--QVTNRGVYGITYHYCVMADGHIFQTEPLESVSLHAADFSQD-SVGVALIGNFTQQ 647
Cdd:cd06583     2 VKYVVIHHTANPNCYTAAAAVRYlqNYHMRGWSDISYHFLVGGDGRIYQGRGWNYVGWHAGGNYNSySIGIELIGNFDGG 81

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1176239922 648 LPPQKQMRATAQLIAMLSAQLNIlISDENVIGCREVIR-TSSPGN 691
Cdd:cd06583    82 PPTAAQLEALAELLAYLVKRYGI-PPDYRIVGHRDVSPgTECPGD 125
PGRP smart00701
Animal peptidoglycan recognition proteins homologous to Bacteriophage T3 lysozyme; The ...
 568-662 2.39e-13

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: 67.71  E-value: 2.39e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176239922  568 RRAIKRIIIHHTATSSMTTIER-------IAQYQVTNRGVYGITYHYCVMADGHIFQTEPLESVSLHAADFSQDSVGVAL 640
Cdd:smart00701  21 TRPVRYVIIHHTATPNCYTDAQcaqilrnIQAYHMEELGWCDIGYNFLVGGDGKVYEGRGWNVVGAHTGGYNDISLGIAF 100

                           90       100
                   ....*....|....*....|..
gi 1176239922  641 IGNFTQQLPPQKQMRATAQLIA 662
Cdd:smart00701 101 IGNFTDKLPTDAALDAAQDLLA 122
PGRP cd06583
Peptidoglycan recognition proteins (PGRPs) are pattern recognition receptors that bind, and in ...
 386-504 7.73e-13

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: 65.77  E-value: 7.73e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176239922 386 IKRLILYHSVSGATITPKALANYHVNS--RNFAGIRYHYCVTNEGKVYQTQPLMIVSPHAG-SYSQESIIICLIGNFSDN 462
Cdd:cd06583     2 VKYVVIHHTANPNCYTAAAAVRYLQNYhmRGWSDISYHFLVGGDGRIYQGRGWNYVGWHAGgNYNSYSIGIELIGNFDGG 81

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1176239922 463 PPPTKQLGGTASLLAYLRSELHLGEGS-VFAYRELSHV-ASPGD 504
Cdd:cd06583    82 PPTAAQLEALAELLAYLVKRYGIPPDYrIVGHRDVSPGtECPGD 125
Ami_2 smart00644
Ami_2 domain;
569-689 6.15e-12

Ami_2 domain;


Pssm-ID: 214760 [Multi-domain]  Cd Length: 126  Bit Score: 63.15  E-value: 6.15e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176239922  569 RAIKRIIIHHTATSSMTTIERIAQYQvtNRGVYGITYHYCVMADGHIFQTEPLESVSLHAADFSQD-----SVGVALIGN 643
Cdd:smart00644   1 PPPRGIVIHHTANSNASCANEARYMQ--NNHMNDIGYHFLVGGDGRVYQGVGWNYVAWHAGGAHTPgyndiSIGIEFIGS 78

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 1176239922  644 FT-QQLPPQKQMRATAQLIA-MLSAQLNILISDENVIGCREVIRTSSP 689
Cdd:smart00644  79 FDsDDEPFAEALYAALDLLAkLLKGAGLPPDGRYRIVGHRDVAPTEDP 126
PGRP smart00701
Animal peptidoglycan recognition proteins homologous to Bacteriophage T3 lysozyme; The ...
 375-478 1.50e-11

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: 62.70  E-value: 1.50e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176239922  375 TTPYQSRdisAIKRLILYHSVSGATITP-------KALANYHVNSRNFAGIRYHYCVTNEGKVYQTQPLMIVSPHAGSYS 447
Cdd:smart00701  16 HTPRLTR---PVRYVIIHHTATPNCYTDaqcaqilRNIQAYHMEELGWCDIGYNFLVGGDGKVYEGRGWNVVGAHTGGYN 92

                           90       100       110
                   ....*....|....*....|....*....|.
gi 1176239922  448 QESIIICLIGNFSDNPPPTKQLGGTASLLAY 478
Cdd:smart00701  93 DISLGIAFIGNFTDKLPTDAALDAAQDLLAC 123
Amidase_2 pfam01510
N-acetylmuramoyl-L-alanine amidase; This family includes zinc amidases that have ...
 386-504 3.25e-09

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: 55.44  E-value: 3.25e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176239922 386 IKRLILYHSVSGATiTPKALANYHVNSRNFAGIRYHYCVTNEGKVYQTQPLMIVSPHAG--SYSQESIIICLIGNFSDNP 463
Cdd:pfam01510   2 IRYIVIHHTAGPSF-AGALLPYAACIARGWSDVSYHYLIDRDGTIYQLVPENGRAWHAGngGGNDRSIGIELEGNFGGDP 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1176239922 464 PPTKQLGGTASLLAYLRSELHL-GEGSVFAYRELSHVASPGD 504
Cdd:pfam01510  81 PTDAQYEALARLLADLCKRYGIpPDRRIVGHRDVGRKTDPGP 122
PHA00447 PHA00447
lysozyme
 568-667 2.23e-08

lysozyme


Pssm-ID: 177282 [Multi-domain]  Cd Length: 142  Bit Score: 53.63  E-value: 2.23e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176239922 568 RRAIKRIIIHHTAT-SSM-TTIERIAQYQVtNRGVYGITYHYCVMADGHIFQTEPLESVSLHAADFSQDSVGVALIGNFT 645
Cdd:PHA00447    7 RSSTKAIFVHCSATkPSMdVGVREIRQWHK-EQGWLDVGYHFIIRRDGTVEEGRPEDVVGSHVKGYNSNSVGVCLVGGID 85

                          90       100
                  ....*....|....*....|....*..
gi 1176239922 646 QQLPPQ-----KQMRATAQLIAMLSAQ 667
Cdd:PHA00447   86 DKGKFDanftpAQMQSLKSLLVTLKAK 112
AmpD COG3023
N-acetyl-anhydromuramyl-L-alanine amidase AmpD [Cell wall/membrane/envelope biogenesis];
565-679 6.79e-08

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


Pssm-ID: 442259  Cd Length: 167  Bit Score: 52.56  E-value: 6.79e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176239922 565 RRNRRAIKRIIIHHTATSSMT-TIERIAQyqvTNRGVygiTYHYCVMADGHIFQTEPLESVSLHAA-----------DFs 632
Cdd:COG3023    21 RPAGAEIDLIVIHYTAGPPGGgALDWLTD---PALRV---SAHYLIDRDGEIYQLVPEDDRAWHAGvsswrgrtnlnDF- 93

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1176239922 633 qdSVGVALIGNFTQQLP-PQKQMRATAQLIAMLSAQLNILIsdENVIG 679
Cdd:COG3023    94 --SIGIELENPGHGWAPfTEAQYEALAALLRDLCARYGIPP--DHIVG 137
CwlA COG5632
N-acetylmuramoyl-L-alanine amidase CwlA [Cell wall/membrane/envelope biogenesis];
558-698 4.87e-05

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


Pssm-ID: 444359  Cd Length: 177  Bit Score: 44.58  E-value: 4.87e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176239922 558 SSNPSYLRRNRRAIKRIIIHHTATSSmTTIERIAQYQVTN-RGVYgitYHYCVmADGHIFQTEPLESVSLHAADFS---- 632
Cdd:COG5632    11 PKNNSYRPGYKMKPKGIVIHNTANPG-ATAENHANYFNNNnRSAS---WHYFV-DDKEIIQHIPLNENAWHAGDGTgpgn 85

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1176239922 633 QDSVGVALIGNFTQQlpPQKQMRATAQLIAMLSAQLNILISdeNVIGCREVIRTSSPGNTWLNWKH 698
Cdd:COG5632    86 RRSIGIEICENKDGD--FAKAYENAAELIAYLMKKYGIPID--NVVRHYDWSGKNCPHGLLANGGY 147
PHA00447 PHA00447
lysozyme
 400-509 7.74e-05

lysozyme


Pssm-ID: 177282 [Multi-domain]  Cd Length: 142  Bit Score: 43.23  E-value: 7.74e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176239922 400 ITPKALANYHVNsRNFAGIRYHYCVTNEGKVYQTQPLMIVSPHAGSYSQESIIICLIGNFSDNPPPT-----KQLGGTAS 474
Cdd:PHA00447   26 VGVREIRQWHKE-QGWLDVGYHFIIRRDGTVEEGRPEDVVGSHVKGYNSNSVGVCLVGGIDDKGKFDanftpAQMQSLKS 104

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1176239922 475 LLAYLRSELHlgEGSVFAYRELSHVASPGDTWTEW 509
Cdd:PHA00447  105 LLVTLKAKYP--GAEIKAHHDVAPKACPSFDLQRW 137
Ami_2 smart00644
Ami_2 domain;
403-468 4.62e-03

Ami_2 domain;


Pssm-ID: 214760 [Multi-domain]  Cd Length: 126  Bit Score: 37.72  E-value: 4.62e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1176239922  403 KALANYHVNsrnfaGIRYHYCVTNEGKVYQTQPLMIVSPHAGSYSQE-----SIIICLIGNFSDNPPPTKQ 468
Cdd:smart00644  23 RYMQNNHMN-----DIGYHFLVGGDGRVYQGVGWNYVAWHAGGAHTPgyndiSIGIEFIGSFDSDDEPFAE 88
 
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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