Species | Acetatifactor sp900066565 | |||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|
Lineage | Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; Acetatifactor; Acetatifactor sp900066565 | |||||||||||
CAZyme ID | MGYG000000217_02804 | |||||||||||
CAZy Family | GH106 | |||||||||||
CAZyme Description | hypothetical protein | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location | Start: 23170; End: 24426 Strand: + |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
GH106 | 11 | 418 | 1.8e-49 | 0.42961165048543687 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
pfam17132 | Glyco_hydro_106 | 1.19e-07 | 197 | 408 | 401 | 609 | alpha-L-rhamnosidase. |
pfam17132 | Glyco_hydro_106 | 1.38e-04 | 15 | 86 | 1 | 80 | alpha-L-rhamnosidase. |
cd01299 | Met_dep_hydrolase_A | 0.002 | 34 | 86 | 118 | 174 | Metallo-dependent hydrolases, subgroup A is part of the superfamily of metallo-dependent hydrolases, a large group of proteins that show conservation in their 3-dimensional fold (TIM barrel) and in details of their active site. The vast majority of the members have a conserved metal binding site, involving four histidines and one aspartic acid residue. In the common reaction mechanism, the metal ion (or ions) deprotonate a water molecule for a nucleophilic attack on the substrate. The function of this subgroup is unknown. |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
AUO20156.1 | 2.72e-160 | 7 | 418 | 3 | 402 |
QJD85865.1 | 1.41e-156 | 14 | 418 | 21 | 429 |
ACX65274.1 | 3.07e-151 | 10 | 418 | 7 | 412 |
AEI43260.1 | 1.09e-146 | 13 | 418 | 10 | 436 |
AFC30916.1 | 6.27e-146 | 13 | 418 | 10 | 438 |
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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