Species | TF01-11 sp000436755 | |||||||||||
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Lineage | Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; TF01-11; TF01-11 sp000436755 | |||||||||||
CAZyme ID | MGYG000001831_01138 | |||||||||||
CAZy Family | GH73 | |||||||||||
CAZyme Description | hypothetical protein | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location | Start: 18335; End: 20545 Strand: - |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
COG4193 | LytD | 8.93e-17 | 401 | 631 | 45 | 244 | Beta- N-acetylglucosaminidase [Carbohydrate transport and metabolism]. |
pfam08239 | SH3_3 | 3.45e-06 | 43 | 104 | 1 | 54 | Bacterial SH3 domain. |
pfam12733 | Cadherin-like | 5.31e-06 | 670 | 735 | 11 | 88 | 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. |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
QHQ61172.1 | 2.34e-159 | 10 | 731 | 10 | 762 |
BCN29841.1 | 3.92e-153 | 45 | 735 | 42 | 888 |
BCJ97942.1 | 2.01e-135 | 36 | 735 | 152 | 906 |
BCJ93456.1 | 7.39e-135 | 45 | 735 | 151 | 894 |
ABX43817.1 | 9.02e-133 | 82 | 735 | 582 | 1278 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
4PI8_A | 1.52e-06 | 448 | 601 | 59 | 198 | ChainA, Autolysin E [Staphylococcus aureus subsp. aureus Mu50] |
4PI7_A | 2.74e-06 | 448 | 601 | 59 | 198 | 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 |
---|---|---|---|---|---|---|
P39848 | 3.49e-08 | 404 | 631 | 679 | 879 | Beta-N-acetylglucosaminidase OS=Bacillus subtilis (strain 168) OX=224308 GN=lytD PE=1 SV=1 |
Q8CPQ1 | 1.17e-07 | 356 | 632 | 1086 | 1335 | Bifunctional autolysin OS=Staphylococcus epidermidis (strain ATCC 12228 / FDA PCI 1200) OX=176280 GN=atl PE=3 SV=1 |
O33635 | 2.65e-07 | 356 | 632 | 1086 | 1335 | Bifunctional autolysin OS=Staphylococcus epidermidis OX=1282 GN=atl PE=1 SV=1 |
Q5HQB9 | 2.65e-07 | 356 | 632 | 1086 | 1335 | Bifunctional autolysin OS=Staphylococcus epidermidis (strain ATCC 35984 / RP62A) OX=176279 GN=atl PE=3 SV=1 |
Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
---|---|---|---|---|---|
0.008112 | 0.816915 | 0.174028 | 0.000358 | 0.000292 | 0.000285 |
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