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CAZyme Information: MGYG000000741_01937
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Basic Information |
Genomic context |
Full Sequence |
Enzyme annotations |
CAZy signature domains |
CDD domains |
CAZyme hits |
PDB hits |
Swiss-Prot hits |
SignalP and Lipop annotations |
TMHMM annotations
Basic Information help
| Species | CAG-170 sp900548625 | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Lineage | Bacteria; Firmicutes_A; Clostridia; Oscillospirales; Oscillospiraceae; CAG-170; CAG-170 sp900548625 | |||||||||||
| CAZyme ID | MGYG000000741_01937 | |||||||||||
| CAZy Family | GH125 | |||||||||||
| CAZyme Description | hypothetical protein | |||||||||||
| CAZyme Property |
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| Genome Property |
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| Gene Location | Start: 8283; End: 10082 Strand: + | |||||||||||
CAZyme Signature Domains help
| Family | Start | End | Evalue | family coverage |
|---|---|---|---|---|
| GH125 | 389 | 586 | 4.5e-16 | 0.5223880597014925 |
CDD Domains download full data without filtering help
| Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
|---|---|---|---|---|---|---|---|
| COG3538 | COG3538 | 7.25e-17 | 287 | 532 | 60 | 363 | Meiotically up-regulated gene 157 (Mug157) protein (function unknown) [Function unknown]. |
| pfam06824 | Glyco_hydro_125 | 5.13e-14 | 340 | 533 | 122 | 358 | 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. |
CAZyme Hits help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
|---|---|---|---|---|---|
| QEY34932.1 | 1.31e-233 | 2 | 593 | 3 | 593 |
| QKN24824.1 | 2.38e-230 | 5 | 593 | 1 | 588 |
| ARP51233.1 | 2.38e-230 | 5 | 593 | 1 | 588 |
| QKO31192.1 | 2.38e-230 | 5 | 593 | 1 | 588 |
| QIA31705.1 | 1.03e-227 | 2 | 586 | 3 | 588 |
PDB Hits download full data without filtering help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| 3QPF_A | 6.18e-08 | 389 | 565 | 207 | 398 | 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] |
| 3P2C_A | 1.54e-07 | 287 | 529 | 87 | 384 | 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] |
| 6RQK_A | 2.56e-07 | 337 | 548 | 129 | 377 | 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] |
| 2NVP_A | 3.38e-07 | 337 | 548 | 129 | 377 | X-RayCrystal Structure of Protein CPF_0428 from Clostridium perfringens. Northeast Structural Genomics Consortium Target CpR63. [Clostridium perfringens] |
| 3QT3_A | 7.69e-07 | 337 | 548 | 129 | 377 | 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] |
Swiss-Prot Hits help
SignalP and Lipop Annotations help
This protein is predicted as OTHER
| Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
|---|---|---|---|---|---|
| 1.000047 | 0.000000 | 0.000000 | 0.000000 | 0.000000 | 0.000000 |