Species | HGM12814 sp900770165 | |||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|
Lineage | Bacteria; Firmicutes_A; Clostridia; Oscillospirales; Acutalibacteraceae; HGM12814; HGM12814 sp900770165 | |||||||||||
CAZyme ID | MGYG000003581_00057 | |||||||||||
CAZy Family | CBM50 | |||||||||||
CAZyme Description | hypothetical protein | |||||||||||
CAZyme Property |
|
|||||||||||
Genome Property |
|
|||||||||||
Gene Location | Start: 26328; End: 26783 Strand: - |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
CBM50 | 55 | 98 | 3e-16 | 0.975 |
CBM50 | 105 | 150 | 6e-16 | 0.975 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
cd00118 | LysM | 1.89e-16 | 53 | 97 | 1 | 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. |
PRK11198 | PRK11198 | 3.53e-16 | 98 | 150 | 91 | 146 | LysM domain/BON superfamily protein; Provisional |
pfam01476 | LysM | 4.93e-15 | 55 | 98 | 1 | 43 | 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. |
pfam01476 | LysM | 2.14e-14 | 105 | 150 | 1 | 43 | 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. |
smart00257 | LysM | 7.58e-14 | 54 | 97 | 1 | 44 | Lysin motif. |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
CDM70433.1 | 3.45e-29 | 6 | 151 | 175 | 321 |
QEK16471.1 | 6.90e-27 | 5 | 149 | 172 | 325 |
QYX27151.1 | 2.64e-26 | 5 | 149 | 172 | 325 |
QQR02580.1 | 1.09e-25 | 39 | 150 | 455 | 563 |
QHZ46391.1 | 5.13e-23 | 4 | 149 | 162 | 316 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
2MKX_A | 3.76e-08 | 53 | 100 | 5 | 51 | Solutionstructure of LysM the peptidoglycan binding domain of autolysin AtlA from Enterococcus faecalis [Enterococcus faecalis V583] |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
Q8CMN2 | 7.77e-16 | 10 | 150 | 47 | 191 | N-acetylmuramoyl-L-alanine amidase sle1 OS=Staphylococcus epidermidis (strain ATCC 12228 / FDA PCI 1200) OX=176280 GN=sle1 PE=3 SV=1 |
Q5HRU2 | 7.77e-16 | 10 | 150 | 47 | 191 | N-acetylmuramoyl-L-alanine amidase sle1 OS=Staphylococcus epidermidis (strain ATCC 35984 / RP62A) OX=176279 GN=sle1 PE=3 SV=1 |
Q49UX4 | 1.97e-14 | 41 | 149 | 72 | 193 | N-acetylmuramoyl-L-alanine amidase sle1 OS=Staphylococcus saprophyticus subsp. saprophyticus (strain ATCC 15305 / DSM 20229 / NCIMB 8711 / NCTC 7292 / S-41) OX=342451 GN=sle1 PE=3 SV=1 |
Q7A7E0 | 9.31e-13 | 20 | 149 | 56 | 201 | N-acetylmuramoyl-L-alanine amidase sle1 OS=Staphylococcus aureus (strain N315) OX=158879 GN=sle1 PE=1 SV=1 |
P0C1U7 | 9.31e-13 | 20 | 149 | 56 | 201 | N-acetylmuramoyl-L-alanine amidase sle1 OS=Staphylococcus aureus OX=1280 GN=sle1 PE=3 SV=1 |
Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
---|---|---|---|---|---|
1.000008 | 0.000028 | 0.000001 | 0.000000 | 0.000000 | 0.000000 |
Copyright 2022 © YIN LAB, UNL. All rights reserved. Designed by Jinfang Zheng and Boyang Hu. Maintained by Yanbin Yin.