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Conserved domains on  [gi|15231684|ref|NP_190847|]
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peptidoglycan-binding LysM domain-containing protein [Arabidopsis thaliana]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PRK11198 super family cl36007
LysM domain/BON superfamily protein; Provisional
61-107 2.29e-05

LysM domain/BON superfamily protein; Provisional


The actual alignment was detected with superfamily member PRK11198:

Pssm-ID: 236880 [Multi-domain]  Cd Length: 147  Bit Score: 40.67  E-value: 2.29e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 15231684   61 DEIYEVKEGETLQTISEKC-GD----PYIVEGN-PHIHDHDDLFPGLLIRITP 107
Cdd:PRK11198  95 SQFYTVKSGDTLSAIAKKVyGNankyNKIFEANkPMLKSPDKIYPGQVLRIPE 147
 
Name Accession Description Interval E-value
PRK11198 PRK11198
LysM domain/BON superfamily protein; Provisional
61-107 2.29e-05

LysM domain/BON superfamily protein; Provisional


Pssm-ID: 236880 [Multi-domain]  Cd Length: 147  Bit Score: 40.67  E-value: 2.29e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 15231684   61 DEIYEVKEGETLQTISEKC-GD----PYIVEGN-PHIHDHDDLFPGLLIRITP 107
Cdd:PRK11198  95 SQFYTVKSGDTLSAIAKKVyGNankyNKIFEANkPMLKSPDKIYPGQVLRIPE 147
LysM cd00118
Lysin Motif is a small domain involved in binding peptidoglycan; LysM, a small globular domain ...
63-105 2.84e-04

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: 35.54  E-value: 2.84e-04
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*
gi 15231684  63 IYEVKEGETLQTISEKCGDPY--IVEGNPhIHDHDDLFPGLLIRI 105
Cdd:cd00118   2 TYTVKPGDTLWSIAKKYGVTVeeLAAANP-LINPDCIYPGQKLKI 45
LysM pfam01476
LysM domain; The LysM (lysin motif) domain is about 40 residues long. It is found in a variety ...
64-106 1.28e-03

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: 33.91  E-value: 1.28e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 15231684    64 YEVKEGETLQTISEKCGDPY--IVEGNpHIHDhDDLFPGLLIRIT 106
Cdd:pfam01476   1 YTVKKGDTLSSIAKRYGITVeqLAELN-GLSS-PNLYVGQKLKIP 43
 
Name Accession Description Interval E-value
PRK11198 PRK11198
LysM domain/BON superfamily protein; Provisional
61-107 2.29e-05

LysM domain/BON superfamily protein; Provisional


Pssm-ID: 236880 [Multi-domain]  Cd Length: 147  Bit Score: 40.67  E-value: 2.29e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 15231684   61 DEIYEVKEGETLQTISEKC-GD----PYIVEGN-PHIHDHDDLFPGLLIRITP 107
Cdd:PRK11198  95 SQFYTVKSGDTLSAIAKKVyGNankyNKIFEANkPMLKSPDKIYPGQVLRIPE 147
LysM cd00118
Lysin Motif is a small domain involved in binding peptidoglycan; LysM, a small globular domain ...
63-105 2.84e-04

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: 35.54  E-value: 2.84e-04
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*
gi 15231684  63 IYEVKEGETLQTISEKCGDPY--IVEGNPhIHDHDDLFPGLLIRI 105
Cdd:cd00118   2 TYTVKPGDTLWSIAKKYGVTVeeLAAANP-LINPDCIYPGQKLKI 45
LysM pfam01476
LysM domain; The LysM (lysin motif) domain is about 40 residues long. It is found in a variety ...
64-106 1.28e-03

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: 33.91  E-value: 1.28e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 15231684    64 YEVKEGETLQTISEKCGDPY--IVEGNpHIHDhDDLFPGLLIRIT 106
Cdd:pfam01476   1 YTVKKGDTLSSIAKRYGITVeqLAELN-GLSS-PNLYVGQKLKIP 43
 
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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