Species | UMGS1976 sp900556765 | |||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|
Lineage | Bacteria; Firmicutes_A; Clostridia; Oscillospirales; Acutalibacteraceae; UMGS1976; UMGS1976 sp900556765 | |||||||||||
CAZyme ID | MGYG000001766_01100 | |||||||||||
CAZy Family | CBM50 | |||||||||||
CAZyme Description | Autolysin | |||||||||||
CAZyme Property |
|
|||||||||||
Genome Property |
|
|||||||||||
Gene Location | Start: 394; End: 693 Strand: - |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
CBM50 | 5 | 48 | 1.2e-17 | 0.975 |
CBM50 | 56 | 98 | 1.1e-16 | 0.95 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
smart00257 | LysM | 2.31e-18 | 4 | 47 | 1 | 44 | Lysin motif. |
cd00118 | LysM | 2.13e-17 | 3 | 47 | 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. |
smart00257 | LysM | 2.48e-17 | 55 | 98 | 1 | 44 | Lysin motif. |
pfam01476 | LysM | 4.58e-17 | 5 | 48 | 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. |
cd00118 | LysM | 6.37e-17 | 55 | 98 | 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. |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
QEK16471.1 | 3.28e-24 | 2 | 98 | 226 | 325 |
ADL13349.1 | 5.54e-24 | 5 | 98 | 72 | 171 |
QEG13524.1 | 3.05e-23 | 5 | 99 | 222 | 317 |
ALP93086.1 | 5.14e-23 | 5 | 99 | 236 | 330 |
AYD80952.1 | 5.71e-23 | 5 | 99 | 219 | 314 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
4UZ2_A | 9.96e-08 | 5 | 48 | 5 | 47 | Crystalstructure of the N-terminal LysM domains from the putative NlpC/P60 D,L endopeptidase from T. thermophilus [Thermus thermophilus HB8],4UZ2_B Crystal structure of the N-terminal LysM domains from the putative NlpC/P60 D,L endopeptidase from T. thermophilus [Thermus thermophilus HB8],4UZ2_C Crystal structure of the N-terminal LysM domains from the putative NlpC/P60 D,L endopeptidase from T. thermophilus [Thermus thermophilus HB8],4UZ2_D Crystal structure of the N-terminal LysM domains from the putative NlpC/P60 D,L endopeptidase from T. thermophilus [Thermus thermophilus HB8],4UZ3_A Crystal structure of the N-terminal LysM domains from the putative NlpC/P60 D,L endopeptidase from T. thermophilus bound to N-acetyl-chitohexaose [Thermus thermophilus HB8],4UZ3_B Crystal structure of the N-terminal LysM domains from the putative NlpC/P60 D,L endopeptidase from T. thermophilus bound to N-acetyl-chitohexaose [Thermus thermophilus HB8],4UZ3_C Crystal structure of the N-terminal LysM domains from the putative NlpC/P60 D,L endopeptidase from T. thermophilus bound to N-acetyl-chitohexaose [Thermus thermophilus HB8] |
5JCD_A | 2.74e-07 | 4 | 98 | 84 | 191 | Crystalstructure of OsCEBiP [Oryza sativa Japonica Group],5JCD_B Crystal structure of OsCEBiP [Oryza sativa Japonica Group],5JCD_C Crystal structure of OsCEBiP [Oryza sativa Japonica Group] |
5JCE_A | 4.08e-07 | 4 | 98 | 84 | 191 | Crystalstructure of OsCEBiP complex [Oryza sativa Japonica Group],5JCE_B Crystal structure of OsCEBiP complex [Oryza sativa Japonica Group] |
4XCM_A | 4.98e-07 | 5 | 48 | 5 | 47 | Crystalstructure of the putative NlpC/P60 D,L endopeptidase from T. thermophilus [Thermus thermophilus HB8],4XCM_B Crystal structure of the putative NlpC/P60 D,L endopeptidase from T. thermophilus [Thermus thermophilus HB8] |
4S3K_A | 5.99e-07 | 4 | 52 | 6 | 54 | ChainA, Spore germination protein YaaH [Priestia megaterium QM B1551] |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
P37710 | 2.30e-13 | 5 | 99 | 363 | 473 | Autolysin OS=Enterococcus faecalis (strain ATCC 700802 / V583) OX=226185 GN=EF_0799 PE=1 SV=2 |
Q5HRU2 | 8.34e-13 | 4 | 98 | 85 | 190 | N-acetylmuramoyl-L-alanine amidase sle1 OS=Staphylococcus epidermidis (strain ATCC 35984 / RP62A) OX=176279 GN=sle1 PE=3 SV=1 |
Q8CMN2 | 8.34e-13 | 4 | 98 | 85 | 190 | N-acetylmuramoyl-L-alanine amidase sle1 OS=Staphylococcus epidermidis (strain ATCC 12228 / FDA PCI 1200) OX=176280 GN=sle1 PE=3 SV=1 |
Q4L3C1 | 8.51e-13 | 5 | 98 | 30 | 131 | N-acetylmuramoyl-L-alanine amidase sle1 OS=Staphylococcus haemolyticus (strain JCSC1435) OX=279808 GN=sle1 PE=3 SV=1 |
O34669 | 1.80e-12 | 6 | 99 | 29 | 122 | Cell wall-binding protein YocH OS=Bacillus subtilis (strain 168) OX=224308 GN=yocH PE=1 SV=1 |
Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
---|---|---|---|---|---|
1.000054 | 0.000000 | 0.000000 | 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.