Species | CAG-288 sp000437395 | |||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|
Lineage | Bacteria; Firmicutes; Bacilli; RFN20; CAG-288; CAG-288; CAG-288 sp000437395 | |||||||||||
CAZyme ID | MGYG000000431_00836 | |||||||||||
CAZy Family | GH125 | |||||||||||
CAZyme Description | hypothetical protein | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location | Start: 76245; End: 77519 Strand: - |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
GH125 | 20 | 413 | 1.4e-154 | 0.9925373134328358 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
COG3538 | COG3538 | 0.0 | 3 | 413 | 15 | 420 | Meiotically up-regulated gene 157 (Mug157) protein (function unknown) [Function unknown]. |
pfam06824 | Glyco_hydro_125 | 0.0 | 20 | 413 | 3 | 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. |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
AUS97899.1 | 5.25e-157 | 6 | 414 | 10 | 419 |
BBI31258.1 | 2.68e-148 | 20 | 415 | 36 | 433 |
AGF57854.1 | 1.07e-147 | 22 | 414 | 23 | 416 |
AIQ43219.1 | 1.38e-147 | 16 | 412 | 33 | 430 |
SYX82123.1 | 1.53e-147 | 20 | 415 | 36 | 433 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
6RQK_A | 6.43e-144 | 16 | 424 | 23 | 429 | 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 | 3.67e-143 | 16 | 424 | 23 | 429 | 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] |
3QT3_A | 3.98e-143 | 16 | 412 | 23 | 419 | 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] |
2NVP_A | 1.27e-138 | 16 | 424 | 23 | 429 | X-RayCrystal Structure of Protein CPF_0428 from Clostridium perfringens. Northeast Structural Genomics Consortium Target CpR63. [Clostridium perfringens] |
3ON6_A | 1.04e-114 | 5 | 417 | 36 | 450 | 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] |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
Q10449 | 3.30e-85 | 5 | 413 | 64 | 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 |
---|---|---|---|---|---|
1.000050 | 0.000001 | 0.000000 | 0.000000 | 0.000000 | 0.000000 |
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