Species | Porphyromonas sp900539765 | |||||||||||
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Lineage | Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Porphyromonadaceae; Porphyromonas; Porphyromonas sp900539765 | |||||||||||
CAZyme ID | MGYG000000873_00495 | |||||||||||
CAZy Family | CBM50 | |||||||||||
CAZyme Description | hypothetical protein | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location | Start: 36451; End: 37974 Strand: - |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
cd00118 | LysM | 8.66e-12 | 93 | 136 | 2 | 45 | 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. |
COG1388 | LysM | 1.66e-11 | 41 | 148 | 1 | 122 | LysM repeat [Cell wall/membrane/envelope biogenesis]. |
smart00257 | LysM | 2.03e-10 | 93 | 136 | 1 | 44 | Lysin motif. |
pfam13458 | Peripla_BP_6 | 8.45e-10 | 156 | 444 | 1 | 292 | Periplasmic binding protein. This family includes a diverse range of periplasmic binding proteins. |
cd00118 | LysM | 1.43e-09 | 30 | 71 | 3 | 45 | 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. |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
AEE13417.1 | 0.0 | 1 | 507 | 1 | 507 |
ATS00530.1 | 1.22e-78 | 30 | 500 | 37 | 496 |
ATS06910.1 | 1.22e-78 | 30 | 500 | 37 | 496 |
ATR99267.1 | 1.71e-78 | 30 | 500 | 37 | 496 |
ATS02331.1 | 1.71e-78 | 30 | 500 | 37 | 496 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
P54421 | 3.31e-06 | 32 | 125 | 90 | 182 | Probable peptidoglycan endopeptidase LytE OS=Bacillus subtilis (strain 168) OX=224308 GN=lytE PE=1 SV=1 |
Q5HRU2 | 9.93e-06 | 24 | 120 | 23 | 112 | N-acetylmuramoyl-L-alanine amidase sle1 OS=Staphylococcus epidermidis (strain ATCC 35984 / RP62A) OX=176279 GN=sle1 PE=3 SV=1 |
Q8CMN2 | 9.93e-06 | 24 | 120 | 23 | 112 | N-acetylmuramoyl-L-alanine amidase sle1 OS=Staphylococcus epidermidis (strain ATCC 12228 / FDA PCI 1200) OX=176280 GN=sle1 PE=3 SV=1 |
Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
---|---|---|---|---|---|
0.000627 | 0.998577 | 0.000274 | 0.000174 | 0.000160 | 0.000155 |
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