| Species | CAG-56 sp900762665 | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Lineage | Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; CAG-56; CAG-56 sp900762665 | |||||||||||
| CAZyme ID | MGYG000001748_00818 | |||||||||||
| CAZy Family | GH0 | |||||||||||
| CAZyme Description | hypothetical protein | |||||||||||
| CAZyme Property |
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| Genome Property |
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| Gene Location | Start: 35757; End: 38291 Strand: + | |||||||||||
| Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
|---|---|---|---|---|---|---|---|
| cd10791 | GH38N_AMII_like_1 | 7.98e-71 | 8 | 287 | 1 | 254 | N-terminal catalytic domain of mainly uncharacterized eukaryotic proteins similar to alpha-mannosidases; glycoside hydrolase family 38 (GH38). The subfamily of mainly uncharacterized eukaryotic proteins shows sequence homology with class II alpha-mannosidases (AlphaAMIIs). AlphaAMIIs possess a-1,3, a-1,6, and a-1,2 hydrolytic activity, and catalyze the degradation of N-linked oligosaccharides. The N-terminal catalytic domain of alphaMII adopts a structure consisting of parallel 7-stranded beta/alpha barrel. This subfamily belongs to the GH38 family of retaining glycosyl hydrolases, which employ a two-step mechanism involving the formation of a covalent glycosyl enzyme complex; two carboxylic acids positioned within the active site act in concert: one as a catalytic nucleophile and the other as a general acid/base catalyst. |
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
|---|---|---|---|---|---|
| SET75050.1 | 0.0 | 1 | 836 | 1 | 816 |
| ANS75706.1 | 2.87e-309 | 1 | 837 | 1 | 818 |
| AUS96542.1 | 1.49e-291 | 5 | 837 | 16 | 828 |
| SQI58910.1 | 5.24e-250 | 5 | 842 | 3 | 814 |
| ASN05648.1 | 8.02e-244 | 5 | 842 | 3 | 814 |
| Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
|---|---|---|---|---|---|
| 1.000033 | 0.000001 | 0.000000 | 0.000000 | 0.000000 | 0.000000 |
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