| Species | ||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Lineage | Bacteria; Firmicutes_A; Clostridia; Tissierellales; Peptoniphilaceae; Anaerococcus; | |||||||||||
| CAZyme ID | MGYG000002901_00321 | |||||||||||
| CAZy Family | GH125 | |||||||||||
| CAZyme Description | hypothetical protein | |||||||||||
| CAZyme Property |
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| Genome Property |
|
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| Gene Location | Start: 3938; End: 5197 Strand: + | |||||||||||
| Family | Start | End | Evalue | family coverage |
|---|---|---|---|---|
| GH125 | 13 | 408 | 7.3e-146 | 0.9950248756218906 |
| Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
|---|---|---|---|---|---|---|---|
| pfam06824 | Glyco_hydro_125 | 0.0 | 13 | 408 | 2 | 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 | 2.21e-176 | 4 | 412 | 16 | 424 | Meiotically up-regulated gene 157 (Mug157) protein (function unknown) [Function unknown]. |
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
|---|---|---|---|---|---|
| QUY64940.1 | 6.43e-189 | 7 | 417 | 17 | 428 |
| QZO75647.1 | 4.55e-188 | 7 | 417 | 13 | 424 |
| ASN07283.1 | 9.14e-144 | 8 | 408 | 13 | 411 |
| QNF27513.1 | 7.85e-142 | 1 | 408 | 12 | 419 |
| AVR01162.1 | 2.72e-137 | 18 | 417 | 29 | 433 |
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| 6RQK_A | 1.78e-129 | 15 | 403 | 28 | 415 | 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] |
| 3QT3_A | 5.50e-129 | 15 | 403 | 28 | 415 | 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] |
| 5M7I_A | 1.01e-128 | 15 | 403 | 28 | 415 | 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 | 2.43e-124 | 15 | 403 | 28 | 415 | X-RayCrystal Structure of Protein CPF_0428 from Clostridium perfringens. Northeast Structural Genomics Consortium Target CpR63. [Clostridium perfringens] |
| 3QPF_A | 6.35e-106 | 13 | 411 | 23 | 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 | 1.36e-78 | 14 | 408 | 79 | 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 |
|---|---|---|---|---|---|
| 1.000012 | 0.000000 | 0.000000 | 0.000000 | 0.000000 | 0.000000 |
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