Species | Johnsonella sp900766185 | |||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|
Lineage | Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; Johnsonella; Johnsonella sp900766185 | |||||||||||
CAZyme ID | MGYG000003366_01324 | |||||||||||
CAZy Family | GH73 | |||||||||||
CAZyme Description | hypothetical protein | |||||||||||
CAZyme Property |
|
|||||||||||
Genome Property |
|
|||||||||||
Gene Location | Start: 15582; End: 17228 Strand: - |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
COG4193 | LytD | 5.83e-14 | 276 | 426 | 106 | 245 | Beta- N-acetylglucosaminidase [Carbohydrate transport and metabolism]. |
pfam12733 | Cadherin-like | 1.36e-08 | 446 | 524 | 1 | 86 | Cadherin-like beta sandwich domain. This domain is found in several bacterial, metazoan and chlorophyte algal proteins. A profile-profile comparison recovered the cadherin domain and a comparison of the predicted structure of this domain with the crystal structure of the cadherin showed a congruent seven stranded secondary structure. The domain is widespread in bacteria and seen in the firmicutes, actinobacteria, certain proteobacteria, bacteroides and chlamydiae with an expansion in Clostridium. In contrast, it is limited in its distribution in eukaryotes suggesting that it was derived through lateral transfer from bacteria. In prokaryotes, this domain is widely fused to other domains such as FNIII (Fibronectin Type III), TIG, SLH (S-layer homology), discoidin, cell-wall-binding repeat domain and alpha-amylase-like glycohydrolases. These associations are suggestive of a carbohydrate-binding function for this cadherin-like domain. In animal proteins it is associated with an ATP-grasp domain. |
smart00047 | LYZ2 | 0.002 | 276 | 393 | 22 | 124 | Lysozyme subfamily 2. Eubacterial enzymes distantly related to eukaryotic lysozymes. |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
QRV21758.1 | 1.33e-154 | 39 | 527 | 115 | 608 |
ADL03932.1 | 1.33e-154 | 39 | 527 | 115 | 608 |
QIX93811.1 | 3.33e-153 | 29 | 527 | 106 | 678 |
ANU49989.1 | 1.90e-152 | 29 | 527 | 106 | 678 |
QQR01104.1 | 1.90e-152 | 29 | 527 | 106 | 678 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
6FXO_A | 1.26e-10 | 276 | 426 | 98 | 244 | ChainA, Bifunctional autolysin [Staphylococcus aureus subsp. aureus Mu50] |
4PI7_A | 3.41e-06 | 272 | 409 | 86 | 212 | ChainA, Autolysin E [Staphylococcus aureus subsp. aureus Mu50],4PI9_A Chain A, Autolysin E [Staphylococcus aureus subsp. aureus Mu50],4PIA_A Chain A, Autolysin E [Staphylococcus aureus subsp. aureus Mu50] |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
Q5HH31 | 4.59e-09 | 276 | 426 | 1110 | 1256 | Bifunctional autolysin OS=Staphylococcus aureus (strain COL) OX=93062 GN=atl PE=3 SV=1 |
Q6GI31 | 4.59e-09 | 276 | 426 | 1111 | 1257 | Bifunctional autolysin OS=Staphylococcus aureus (strain MRSA252) OX=282458 GN=atl PE=3 SV=1 |
A7X0T9 | 4.59e-09 | 276 | 426 | 1109 | 1255 | Bifunctional autolysin OS=Staphylococcus aureus (strain Mu3 / ATCC 700698) OX=418127 GN=atl PE=3 SV=2 |
Q931U5 | 4.59e-09 | 276 | 426 | 1102 | 1248 | Bifunctional autolysin OS=Staphylococcus aureus (strain Mu50 / ATCC 700699) OX=158878 GN=atl PE=1 SV=2 |
P0C5Z8 | 4.59e-09 | 276 | 426 | 1109 | 1255 | Bifunctional autolysin OS=Staphylococcus aureus OX=1280 GN=atl PE=1 SV=1 |
Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
---|---|---|---|---|---|
0.001091 | 0.998052 | 0.000241 | 0.000241 | 0.000173 | 0.000154 |
Copyright 2022 © YIN LAB, UNL. All rights reserved. Designed by Jinfang Zheng and Boyang Hu. Maintained by Yanbin Yin.