Species | Victivallis sp002998355 | |||||||||||
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Lineage | Bacteria; Verrucomicrobiota; Lentisphaeria; Victivallales; Victivallaceae; Victivallis; Victivallis sp002998355 | |||||||||||
CAZyme ID | MGYG000003237_00348 | |||||||||||
CAZy Family | GH163 | |||||||||||
CAZyme Description | hypothetical protein | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location | Start: 882; End: 3137 Strand: + |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
GH163 | 206 | 471 | 2e-82 | 0.9960159362549801 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
pfam16126 | DUF4838 | 7.41e-93 | 199 | 471 | 1 | 263 | Domain of unknown function (DUF4838). This family consists of several uncharacterized proteins found in various Bacteroides and Chloroflexus species. The function of this family is unknown. |
pfam03648 | Glyco_hydro_67N | 3.04e-05 | 22 | 124 | 7 | 119 | Glycosyl hydrolase family 67 N-terminus. Alpha-glucuronidases, components of an ensemble of enzymes central to the recycling of photosynthetic biomass, remove the alpha-1,2 linked 4-O-methyl glucuronic acid from xylans. This family represents the N-terminal region of alpha-glucuronidase. The N-terminal domain forms a two-layer sandwich, each layer being formed by a beta sheet of five strands. A further two helices form part of the interface with the central, catalytic, module (pfam07488). |
cd14791 | GH36 | 0.003 | 205 | 323 | 88 | 195 | glycosyl hydrolase family 36 (GH36). GH36 enzymes occur in prokaryotes, eukaryotes, and archaea with a wide range of hydrolytic activities, including alpha-galactosidase, alpha-N-acetylgalactosaminidase, stachyose synthase, and raffinose synthase. All GH36 enzymes cleave a terminal carbohydrate moiety from a substrate that varies considerably in size, depending on the enzyme, and may be either a starch or a glycoprotein. GH36 members are retaining enzymes that cleave their substrates via an acid/base-catalyzed, double-displacement mechanism involving a covalent glycosyl-enzyme intermediate. Two aspartic acid residues have been identified as the catalytic nucleophile and the acid/base, respectively. |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
AVM44733.1 | 0.0 | 1 | 751 | 9 | 759 |
ASV73444.1 | 3.53e-95 | 3 | 542 | 6 | 550 |
QQL44163.1 | 1.32e-93 | 29 | 538 | 19 | 528 |
AIE83908.1 | 8.63e-93 | 29 | 472 | 19 | 452 |
AIF26900.1 | 1.78e-86 | 23 | 479 | 6 | 484 |
Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
---|---|---|---|---|---|
0.000727 | 0.998027 | 0.000528 | 0.000215 | 0.000237 | 0.000251 |
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