Species | Prevotellamassilia sp900541575 | |||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|
Lineage | Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; Prevotellamassilia; Prevotellamassilia sp900541575 | |||||||||||
CAZyme ID | MGYG000001918_01639 | |||||||||||
CAZy Family | CBM32 | |||||||||||
CAZyme Description | hypothetical protein | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location | Start: 6392; End: 9808 Strand: - |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
CBM32 | 48 | 179 | 1.4e-17 | 0.8629032258064516 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
pfam00754 | F5_F8_type_C | 1.21e-17 | 52 | 181 | 12 | 127 | F5/8 type C domain. This domain is also known as the discoidin (DS) domain family. |
cd14791 | GH36 | 7.76e-11 | 395 | 498 | 1 | 87 | 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. |
COG3345 | GalA | 3.55e-05 | 399 | 498 | 290 | 377 | Alpha-galactosidase [Carbohydrate transport and metabolism]. |
cd14792 | GH27 | 1.33e-04 | 404 | 572 | 5 | 138 | glycosyl hydrolase family 27 (GH27). GH27 enzymes occur in eukaryotes, prokaryotes, and archaea with a wide range of hydrolytic activities, including alpha-glucosidase (glucoamylase and sucrase-isomaltase), alpha-N-acetylgalactosaminidase, and 3-alpha-isomalto-dextranase. All GH27 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. GH27 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. |
cd00057 | FA58C | 3.64e-04 | 58 | 181 | 29 | 139 | Substituted updates: Jan 31, 2002 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
QUT26415.1 | 1.61e-219 | 190 | 1069 | 86 | 913 |
QDO70357.1 | 1.48e-218 | 190 | 1074 | 86 | 918 |
AZU64122.1 | 2.30e-185 | 1 | 1099 | 68 | 1188 |
AQW23840.1 | 2.85e-185 | 3 | 1074 | 73 | 1171 |
SQI04569.1 | 3.98e-185 | 3 | 1074 | 73 | 1171 |
Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
---|---|---|---|---|---|
0.999219 | 0.000821 | 0.000007 | 0.000002 | 0.000001 | 0.000002 |
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