Species | GCA-900066755 sp902363085 | |||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|
Lineage | Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; GCA-900066755; GCA-900066755 sp902363085 | |||||||||||
CAZyme ID | MGYG000000095_02424 | |||||||||||
CAZy Family | GH151 | |||||||||||
CAZyme Description | hypothetical protein | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location | Start: 27318; End: 29327 Strand: - |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
GH151 | 26 | 158 | 6.2e-49 | 0.9923664122137404 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
pfam14871 | GHL6 | 4.41e-23 | 26 | 158 | 1 | 135 | Hypothetical glycosyl hydrolase 6. GHL6 is a family of hypothetical glycoside hydrolases. |
cd03143 | A4_beta-galactosidase_middle_domain | 5.74e-07 | 382 | 428 | 44 | 90 | A4 beta-galactosidase middle domain: a type 1 glutamine amidotransferase (GATase1)-like domain. A4 beta-galactosidase middle domain: a type 1 glutamine amidotransferase (GATase1)-like domain. This group includes proteins similar to beta-galactosidase from Thermus thermophilus. Beta-Galactosidase hydrolyzes the beta-1,4-D-galactosidic linkage of lactose, as well as those of related chromogens, o-nitrophenyl-beta-D-galactopyranoside (ONP-Gal) and 5-bromo-4-chloro-3-indolyl-beta-D-galactoside (X-gal). This A4 beta-galactosidase middle domain lacks the catalytic triad of typical GATase1 domains. The reactive Cys residue found in the sharp turn between a beta strand and an alpha helix termed the nucleophile elbow in typical GATase1 domains is not conserved in this group. |
pfam08532 | Glyco_hydro_42M | 2.98e-06 | 382 | 435 | 48 | 100 | Beta-galactosidase trimerisation domain. This is non catalytic domain B of beta-galactosidase enzymes belong to the glycosyl hydrolase 42 family. This domain is related to glutamine amidotransferase enzymes, but the catalytic residues are replaced by non functional amino acids. This domain is involved in trimerisation. |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
BCJ98360.1 | 1.18e-254 | 3 | 665 | 1 | 657 |
BCJ93865.1 | 3.89e-251 | 3 | 665 | 1 | 659 |
AFH63272.1 | 3.51e-249 | 3 | 666 | 1 | 659 |
QUH32064.1 | 4.48e-247 | 3 | 665 | 1 | 656 |
AEI43293.1 | 9.32e-247 | 3 | 666 | 1 | 659 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
6TVK_AAA | 2.42e-225 | 3 | 665 | 30 | 686 | ChainAAA, Alpha-L-fucosidase [Paenibacillus thiaminolyticus] |
Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
---|---|---|---|---|---|
1.000058 | 0.000000 | 0.000000 | 0.000000 | 0.000000 | 0.000000 |
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