Species | Bariatricus massiliensis | |||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|
Lineage | Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; Bariatricus; Bariatricus massiliensis | |||||||||||
CAZyme ID | MGYG000002945_01945 | |||||||||||
CAZy Family | GH146 | |||||||||||
CAZyme Description | hypothetical protein | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location | Start: 119236; End: 121506 Strand: + |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
GH146 | 203 | 713 | 6.1e-179 | 0.9880715705765407 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
pfam07944 | Glyco_hydro_127 | 1.13e-129 | 204 | 713 | 7 | 503 | Beta-L-arabinofuranosidase, GH127. One member of this family, from Bidobacterium longicum, UniProtKB:E8MGH8, has been characterized as an unusual beta-L-arabinofuranosidase enzyme, EC:3.2.1.185. It rleases l-arabinose from the l-arabinofuranose (Araf)-beta1,2-Araf disaccharide and also transglycosylates 1-alkanols with retention of the anomeric configuration. Terminal beta-l-arabinofuranosyl residues have been found in arabinogalactan proteins from a mumber of different plantt species. beta-l-Arabinofuranosyl linkages with 1-4 arabinofuranosides are also found in the sugar chains of extensin and solanaceous lectins, hydroxyproline (Hyp)2-rich glycoproteins that are widely observed in plant cell wall fractions. The critical residue for catalytic activity is Glu-338, in a ET/SCAS sequence context. |
COG3533 | COG3533 | 1.94e-79 | 204 | 714 | 17 | 502 | Uncharacterized conserved protein, DUF1680 family [Function unknown]. |
pfam07532 | Big_4 | 1.80e-05 | 103 | 160 | 1 | 58 | Bacterial Ig-like domain (group 4). This family consists of bacterial domains with an Ig-like fold. Members of this family are found in a variety of bacterial surface proteins. |
cd04791 | LanC_SerThrkinase | 2.60e-04 | 336 | 411 | 91 | 169 | Lanthionine synthetase C-like domain associated with serine/threonine kinases. Some members of this subgroup lack the zinc binding site and the active site residues, and therefore are most likely inactive. The function of this domain is unknown. |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
AWY98728.1 | 3.98e-267 | 2 | 751 | 4 | 753 |
ASR48105.1 | 1.16e-262 | 1 | 751 | 1 | 757 |
QNM13425.1 | 1.46e-257 | 7 | 751 | 5 | 754 |
QOS77131.1 | 2.11e-255 | 7 | 753 | 7 | 765 |
ASA23792.1 | 2.57e-251 | 1 | 751 | 1 | 757 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
6YQH_AAA | 3.61e-75 | 204 | 732 | 38 | 579 | ChainAAA, Acetyl-CoA carboxylase, biotin carboxylase [Bacteroides thetaiotaomicron VPI-5482] |
5OPJ_A | 4.07e-71 | 204 | 732 | 38 | 579 | Beta-L-arabinofuranosidase[Bacteroides thetaiotaomicron] |
5HO9_A | 8.91e-08 | 6 | 92 | 551 | 637 | Structureof truncated AbnA (domains 1-3), a GH43 arabinanase from Geobacilllus stearothermophilus, in complex with arabinooctaose [Geobacillus stearothermophilus],5HO9_B Structure of truncated AbnA (domains 1-3), a GH43 arabinanase from Geobacilllus stearothermophilus, in complex with arabinooctaose [Geobacillus stearothermophilus] |
5HO0_A | 1.01e-07 | 6 | 92 | 551 | 637 | Crystalstructure of AbnA (closed conformation), a GH43 extracellular arabinanase from Geobacillus stearothermophilus [Geobacillus stearothermophilus],5HO2_A Crystal structure of AbnA (open conformation), a GH43 extracellular arabinanase from Geobacillus stearothermophilus [Geobacillus stearothermophilus],5HOF_A Crystal structure of AbnA, a GH43 extracellular arabinanase from Geobacillus stearothermophilus, in complex with arabinopentaose [Geobacillus stearothermophilus],5HP6_A Structure of AbnA, a GH43 extracellular arabinanase from Geobacillus stearothermophilus (a new conformational state) [Geobacillus stearothermophilus] |
Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
---|---|---|---|---|---|
1.000055 | 0.000000 | 0.000000 | 0.000000 | 0.000000 | 0.000000 |
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