Species | ||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|
Lineage | Bacteria; Firmicutes_A; Clostridia; Oscillospirales; Acutalibacteraceae; UMGS1484; | |||||||||||
CAZyme ID | MGYG000004131_00403 | |||||||||||
CAZy Family | GH36 | |||||||||||
CAZyme Description | hypothetical protein | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location | Start: 56400; End: 59501 Strand: - |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
GH36 | 720 | 1015 | 4.1e-19 | 0.40988372093023256 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
pfam16874 | Glyco_hydro_36C | 1.06e-07 | 946 | 1029 | 1 | 78 | Glycosyl hydrolase family 36 C-terminal domain. This domain is found at the C-terminus of many family 36 glycoside hydrolases. It has a beta-sandwich structure with a Greek key motif. |
cd14791 | GH36 | 2.54e-07 | 639 | 860 | 39 | 244 | 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. |
pfam02065 | Melibiase | 1.21e-04 | 632 | 860 | 71 | 285 | Melibiase. Glycoside hydrolase families GH27, GH31 and GH36 form the glycoside hydrolase clan GH-D. Glycoside hydrolase family 36 can be split into 11 families, GH36A to GH36K. This family includes enzymes from GH36A-B and GH36D-K and from GH27. |
cd14256 | Dockerin_I | 1.62e-04 | 273 | 329 | 1 | 57 | Type I dockerin repeat domain. Bacterial cohesin domains bind to a complementary protein domain named dockerin, and this interaction is required for the formation of the cellulosome, a cellulose-degrading complex. The cellulosome consists of scaffoldin, a noncatalytic scaffolding polypeptide, that comprises repeating cohesion modules and a single carbohydrate-binding module (CBM). Specific calcium-dependent interactions between cohesins and dockerins appear to be essential for cellulosome assembly. This subfamily represents type I dockerins, which are responsible for anchoring a variety of enzymatic domains to the complex. |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
QGQ94273.1 | 6.25e-128 | 344 | 1030 | 346 | 1029 |
AEE97820.1 | 9.49e-17 | 568 | 1030 | 245 | 688 |
CED94212.1 | 1.31e-11 | 720 | 1031 | 396 | 695 |
BBH24245.1 | 3.06e-11 | 40 | 172 | 1097 | 1230 |
SCM59591.1 | 1.11e-10 | 722 | 1033 | 87 | 374 |
Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
---|---|---|---|---|---|
0.000832 | 0.665494 | 0.332642 | 0.000378 | 0.000338 | 0.000285 |
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