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Conserved domains on  [gi|148669246|gb|EDL01193|]
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mCG1025408 [Mus musculus]

Protein Classification

LysM peptidoglycan-binding domain-containing protein( domain architecture ID 10061503)

LysM peptidoglycan-binding domain-containing protein may bind N-acetylglucosamine in carbohydrates such as chitin, chitio-oligosaccharides and peptidoglycan

CATH:  3.10.350.10
Gene Ontology:  GO:0097367
PubMed:  18430080|24652063
SCOP:  4000905

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
LysM cd00118
Lysin Motif is a small domain involved in binding peptidoglycan; LysM, a small globular domain ...
42-84 2.00e-09

Lysin Motif is a small domain involved in binding peptidoglycan; LysM, a small globular domain with approximately 40 amino acids, is a widespread protein module involved in binding peptidoglycan in bacteria and chitin in eukaryotes. The domain was originally identified in enzymes that degrade bacterial cell walls, but proteins involved in many other biological functions also contain this domain. It has been reported that the LysM domain functions as a signal for specific plant-bacteria recognition in bacterial pathogenesis. Many of these enzymes are modular and are composed of catalytic units linked to one or several repeats of LysM domains. LysM domains are found in bacteria and eukaryotes.


:

Pssm-ID: 212030 [Multi-domain]  Cd Length: 45  Bit Score: 51.72  E-value: 2.00e-09
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 148669246  42 HQLEPGDTLAGLALKYGVTMEQIKRTNRLYTNDSIFLKKTLYI 84
Cdd:cd00118    3 YTVKPGDTLWSIAKKYGVTVEELAAANPLINPDCIYPGQKLKI 45
 
Name Accession Description Interval E-value
LysM cd00118
Lysin Motif is a small domain involved in binding peptidoglycan; LysM, a small globular domain ...
42-84 2.00e-09

Lysin Motif is a small domain involved in binding peptidoglycan; LysM, a small globular domain with approximately 40 amino acids, is a widespread protein module involved in binding peptidoglycan in bacteria and chitin in eukaryotes. The domain was originally identified in enzymes that degrade bacterial cell walls, but proteins involved in many other biological functions also contain this domain. It has been reported that the LysM domain functions as a signal for specific plant-bacteria recognition in bacterial pathogenesis. Many of these enzymes are modular and are composed of catalytic units linked to one or several repeats of LysM domains. LysM domains are found in bacteria and eukaryotes.


Pssm-ID: 212030 [Multi-domain]  Cd Length: 45  Bit Score: 51.72  E-value: 2.00e-09
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 148669246  42 HQLEPGDTLAGLALKYGVTMEQIKRTNRLYTNDSIFLKKTLYI 84
Cdd:cd00118    3 YTVKPGDTLWSIAKKYGVTVEELAAANPLINPDCIYPGQKLKI 45
LysM COG1388
LysM repeat [Cell wall/membrane/envelope biogenesis];
23-85 2.01e-09

LysM repeat [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440998 [Multi-domain]  Cd Length: 156  Bit Score: 54.71  E-value: 2.01e-09
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 148669246  23 SYGSLVQSSCSPVRERRLEHQLEPGDTLAGLALKYGVTMEQIKRTNRLyTNDSIFLKKTLYIP 85
Cdd:COG1388   93 TLSGIARRYGAAAAPSPVTYTVKKGDTLWSIARRYGVSVEELKRWNGL-SSDTIRPGQKLKIP 154
LysM pfam01476
LysM domain; The LysM (lysin motif) domain is about 40 residues long. It is found in a variety ...
42-85 8.31e-08

LysM domain; The LysM (lysin motif) domain is about 40 residues long. It is found in a variety of enzymes involved in bacterial cell wall degradation. This domain may have a general peptidoglycan binding function. The structure of this domain is known.


Pssm-ID: 396179 [Multi-domain]  Cd Length: 43  Bit Score: 47.01  E-value: 8.31e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 148669246   42 HQLEPGDTLAGLALKYGVTMEQIKRTNRLyTNDSIFLKKTLYIP 85
Cdd:pfam01476   1 YTVKKGDTLSSIAKRYGITVEQLAELNGL-SSPNLYVGQKLKIP 43
LysM smart00257
Lysin motif;
41-84 2.24e-06

Lysin motif;


Pssm-ID: 197609 [Multi-domain]  Cd Length: 44  Bit Score: 43.20  E-value: 2.24e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 148669246    41 EHQLEPGDTLAGLALKYGVTMEQIKRTNRLYTNDSIFLKKTLYI 84
Cdd:smart00257   1 TYTVKKGDTLSSIARRYGISVSDLLELNNILDPDNLQVGQKLKI 44
 
Name Accession Description Interval E-value
LysM cd00118
Lysin Motif is a small domain involved in binding peptidoglycan; LysM, a small globular domain ...
42-84 2.00e-09

Lysin Motif is a small domain involved in binding peptidoglycan; LysM, a small globular domain with approximately 40 amino acids, is a widespread protein module involved in binding peptidoglycan in bacteria and chitin in eukaryotes. The domain was originally identified in enzymes that degrade bacterial cell walls, but proteins involved in many other biological functions also contain this domain. It has been reported that the LysM domain functions as a signal for specific plant-bacteria recognition in bacterial pathogenesis. Many of these enzymes are modular and are composed of catalytic units linked to one or several repeats of LysM domains. LysM domains are found in bacteria and eukaryotes.


Pssm-ID: 212030 [Multi-domain]  Cd Length: 45  Bit Score: 51.72  E-value: 2.00e-09
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 148669246  42 HQLEPGDTLAGLALKYGVTMEQIKRTNRLYTNDSIFLKKTLYI 84
Cdd:cd00118    3 YTVKPGDTLWSIAKKYGVTVEELAAANPLINPDCIYPGQKLKI 45
LysM COG1388
LysM repeat [Cell wall/membrane/envelope biogenesis];
23-85 2.01e-09

LysM repeat [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440998 [Multi-domain]  Cd Length: 156  Bit Score: 54.71  E-value: 2.01e-09
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 148669246  23 SYGSLVQSSCSPVRERRLEHQLEPGDTLAGLALKYGVTMEQIKRTNRLyTNDSIFLKKTLYIP 85
Cdd:COG1388   93 TLSGIARRYGAAAAPSPVTYTVKKGDTLWSIARRYGVSVEELKRWNGL-SSDTIRPGQKLKIP 154
LysM pfam01476
LysM domain; The LysM (lysin motif) domain is about 40 residues long. It is found in a variety ...
42-85 8.31e-08

LysM domain; The LysM (lysin motif) domain is about 40 residues long. It is found in a variety of enzymes involved in bacterial cell wall degradation. This domain may have a general peptidoglycan binding function. The structure of this domain is known.


Pssm-ID: 396179 [Multi-domain]  Cd Length: 43  Bit Score: 47.01  E-value: 8.31e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 148669246   42 HQLEPGDTLAGLALKYGVTMEQIKRTNRLyTNDSIFLKKTLYIP 85
Cdd:pfam01476   1 YTVKKGDTLSSIAKRYGITVEQLAELNGL-SSPNLYVGQKLKIP 43
LysM smart00257
Lysin motif;
41-84 2.24e-06

Lysin motif;


Pssm-ID: 197609 [Multi-domain]  Cd Length: 44  Bit Score: 43.20  E-value: 2.24e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 148669246    41 EHQLEPGDTLAGLALKYGVTMEQIKRTNRLYTNDSIFLKKTLYI 84
Cdd:smart00257   1 TYTVKKGDTLSSIARRYGISVSDLLELNNILDPDNLQVGQKLKI 44
GyrB_insert pfam18053
DNA gyrase B subunit insert domain; This is the insert domain found in DNA gyrase B subunit ...
47-89 3.03e-03

DNA gyrase B subunit insert domain; This is the insert domain found in DNA gyrase B subunit proteins. Studies indicate that the insert has two functions, acting as a steric buttress to pre-configure the primary DNA-binding site, and serving as a relay that may help coordinate communication between different functional domains.


Pssm-ID: 465629  Cd Length: 167  Bit Score: 37.12  E-value: 3.03e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 148669246   47 GDTLAGLALKYGVTMEQIKRTNRLYtnDSIFLKKTLYIPILSE 89
Cdd:pfam18053  14 GEALEELARQYRLAEAIIKRLSRRY--DPAVLEALLYLPPLDA 54
 
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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