| Species | CAG-1435 sp003537755 | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Lineage | Bacteria; Firmicutes_A; Clostridia_A; Christensenellales; CAG-314; CAG-1435; CAG-1435 sp003537755 | |||||||||||
| CAZyme ID | MGYG000003504_01104 | |||||||||||
| CAZy Family | CBM38 | |||||||||||
| CAZyme Description | hypothetical protein | |||||||||||
| CAZyme Property |
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| Genome Property |
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| Gene Location | Start: 60238; End: 62646 Strand: - | |||||||||||
| Family | Start | End | Evalue | family coverage |
|---|---|---|---|---|
| GH125 | 389 | 790 | 5.5e-115 | 0.9950248756218906 |
| CBM38 | 46 | 168 | 5.1e-20 | 0.9844961240310077 |
| Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
|---|---|---|---|---|---|---|---|
| pfam06824 | Glyco_hydro_125 | 5.89e-165 | 388 | 790 | 1 | 416 | Metal-independent alpha-mannosidase (GH125). This family, which contains bacterial and fungal glycoside hydrolases, is also known as GH125. They function as metal-independent alpha-mannosidases, with specificity for alpha-1,6-linked non-reducing terminal mannose residues. Structurally this family is part of the 6 hairpin glycosidase superfamily. |
| COG3538 | COG3538 | 7.08e-139 | 375 | 790 | 2 | 420 | Meiotically up-regulated gene 157 (Mug157) protein (function unknown) [Function unknown]. |
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
|---|---|---|---|---|---|
| ANE45239.1 | 1.75e-102 | 391 | 787 | 30 | 420 |
| AZN43553.1 | 2.50e-99 | 395 | 802 | 2 | 405 |
| AGF57854.1 | 3.75e-99 | 387 | 790 | 18 | 415 |
| QDM44646.1 | 1.29e-98 | 391 | 789 | 25 | 419 |
| AZI44065.1 | 1.61e-97 | 391 | 790 | 23 | 417 |
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| 3QT3_A | 1.07e-91 | 373 | 795 | 10 | 425 | Analysisof a New Family of Widely Distributed Metal-independent alpha-Mannosidases Provides Unique Insight into the Processing of N-linked Glycans, Clostridium perfringens CPE0426 apo-structure [Clostridium perfringens],3QT9_A Analysis of a new family of widely distributed metal-independent alpha mannosidases provides unique insight into the processing of N-linked glycans, Clostridium perfringens CPE0426 complexed with alpha-1,6-linked 1-thio-alpha-mannobiose [Clostridium perfringens] |
| 6RQK_A | 2.67e-91 | 373 | 795 | 10 | 425 | Crystalstructure of GH125 1,6-alpha-mannosidase from Clostridium perfringens in complex with mannoimidazole [Clostridium perfringens str. 13],6RQK_B Crystal structure of GH125 1,6-alpha-mannosidase from Clostridium perfringens in complex with mannoimidazole [Clostridium perfringens str. 13] |
| 5M7I_A | 1.44e-90 | 373 | 795 | 10 | 425 | Crystalstructure of GH125 1,6-alpha-mannosidase mutant from Clostridium perfringens in complex with 1,6-alpha-mannobiose [Clostridium perfringens str. 13],5M7Y_A Crystal structure of GH125 1,6-alpha-mannosidase mutant from Clostridium perfringens in complex with 1,6-alpha-mannotriose [Clostridium perfringens str. 13] |
| 3ON6_A | 4.93e-87 | 373 | 798 | 34 | 454 | Crystalstructure of an exo-alpha-1,6-mannosidase (bacova_03626) from bacteroides ovatus at 1.70 a resolution [Bacteroides ovatus ATCC 8483],3ON6_B Crystal structure of an exo-alpha-1,6-mannosidase (bacova_03626) from bacteroides ovatus at 1.70 a resolution [Bacteroides ovatus ATCC 8483] |
| 3P2C_A | 2.78e-86 | 395 | 798 | 54 | 456 | Crystalstructure of an exo-alpha-1,6-mannosidase (bacova_03347) from bacteroides ovatus at 1.60 a resolution [Bacteroides ovatus ATCC 8483],3P2C_B Crystal structure of an exo-alpha-1,6-mannosidase (bacova_03347) from bacteroides ovatus at 1.60 a resolution [Bacteroides ovatus ATCC 8483] |
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| Q10449 | 1.09e-63 | 359 | 790 | 53 | 494 | Meiotically up-regulated gene 157 protein OS=Schizosaccharomyces pombe (strain 972 / ATCC 24843) OX=284812 GN=mug157 PE=1 SV=1 |
| Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
|---|---|---|---|---|---|
| 0.000001 | 0.000333 | 0.999698 | 0.000000 | 0.000000 | 0.000000 |
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