Species | Virgibacillus kapii | |||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|
Lineage | Bacteria; Firmicutes; Bacilli; Bacillales_D; Amphibacillaceae; Virgibacillus; Virgibacillus kapii | |||||||||||
CAZyme ID | MGYG000001470_00657 | |||||||||||
CAZy Family | GH125 | |||||||||||
CAZyme Description | hypothetical protein | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location | Start: 687565; End: 688866 Strand: + |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
GH125 | 23 | 419 | 9.8e-179 | 0.9975124378109452 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
COG3538 | COG3538 | 0.0 | 1 | 433 | 2 | 434 | Meiotically up-regulated gene 157 (Mug157) protein (function unknown) [Function unknown]. |
pfam06824 | Glyco_hydro_125 | 0.0 | 23 | 419 | 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. |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
QNF27513.1 | 1.06e-241 | 1 | 433 | 1 | 433 |
ASN07283.1 | 9.68e-236 | 9 | 433 | 1 | 425 |
ASK62216.1 | 5.48e-235 | 1 | 433 | 1 | 433 |
AVR01162.1 | 2.37e-231 | 1 | 433 | 1 | 433 |
QRZ20032.1 | 4.06e-231 | 16 | 433 | 2 | 419 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
3QT3_A | 5.44e-168 | 9 | 422 | 8 | 423 | 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 | 7.18e-168 | 9 | 422 | 8 | 423 | 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 | 4.12e-167 | 9 | 422 | 8 | 423 | 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] |
2NVP_A | 2.93e-162 | 9 | 422 | 8 | 423 | X-RayCrystal Structure of Protein CPF_0428 from Clostridium perfringens. Northeast Structural Genomics Consortium Target CpR63. [Clostridium perfringens] |
3QPF_A | 6.15e-147 | 13 | 422 | 12 | 423 | Analysisof a New Family of Widely Distributed Metal-independent alpha-Mannosidases Provides Unique Insight into the Processing of N-linked Glycans, Streptococcus pneumoniae SP_2144 apo-structure [Streptococcus pneumoniae],3QPF_B Analysis of a New Family of Widely Distributed Metal-independent alpha-Mannosidases Provides Unique Insight into the Processing of N-linked Glycans, Streptococcus pneumoniae SP_2144 apo-structure [Streptococcus pneumoniae],3QRY_A Analysis of a new family of widely distributed metal-independent alpha mannosidases provides unique insight into the processing of N-linked glycans, Streptococcus pneumoniae SP_2144 1-deoxymannojirimycin complex [Streptococcus pneumoniae],3QRY_B Analysis of a new family of widely distributed metal-independent alpha mannosidases provides unique insight into the processing of N-linked glycans, Streptococcus pneumoniae SP_2144 1-deoxymannojirimycin complex [Streptococcus pneumoniae],3QSP_A Analysis of a new family of widely distributed metal-independent alpha mannosidases provides unique insight into the processing of N-linked glycans, Streptococcus pneumoniae SP_2144 non-productive substrate complex with alpha-1,6-mannobiose [Streptococcus pneumoniae],3QSP_B Analysis of a new family of widely distributed metal-independent alpha mannosidases provides unique insight into the processing of N-linked glycans, Streptococcus pneumoniae SP_2144 non-productive substrate complex with alpha-1,6-mannobiose [Streptococcus pneumoniae] |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
Q10449 | 5.15e-97 | 8 | 422 | 63 | 497 | 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 |
---|---|---|---|---|---|
1.000074 | 0.000000 | 0.000000 | 0.000000 | 0.000000 | 0.000000 |
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