Species | Bacteroides sp900556215 | |||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|
Lineage | Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; Bacteroides; Bacteroides sp900556215 | |||||||||||
CAZyme ID | MGYG000000211_01916 | |||||||||||
CAZy Family | GH125 | |||||||||||
CAZyme Description | hypothetical protein | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location | Start: 219103; End: 220554 Strand: + |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
GH125 | 69 | 469 | 7.2e-181 | 0.9975124378109452 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
COG3538 | COG3538 | 0.0 | 47 | 479 | 1 | 430 | Meiotically up-regulated gene 157 (Mug157) protein (function unknown) [Function unknown]. |
pfam06824 | Glyco_hydro_125 | 0.0 | 69 | 469 | 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. |
pfam10518 | TAT_signal | 0.002 | 4 | 22 | 1 | 19 | TAT (twin-arginine translocation) pathway signal sequence. |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
QMI79243.1 | 0.0 | 1 | 483 | 1 | 483 |
QBJ17751.1 | 0.0 | 1 | 483 | 1 | 483 |
QPH58103.1 | 0.0 | 1 | 483 | 1 | 483 |
QUT33873.1 | 0.0 | 1 | 483 | 1 | 483 |
QUU00423.1 | 0.0 | 1 | 483 | 1 | 483 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
3P2C_A | 9.00e-196 | 43 | 474 | 21 | 453 | 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] |
3ON6_A | 5.56e-194 | 39 | 474 | 19 | 451 | 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] |
2P0V_A | 2.11e-193 | 39 | 474 | 39 | 471 | Crystalstructure of BT3781 protein from Bacteroides thetaiotaomicron, Northeast Structural Genomics Target BtR58 [Bacteroides thetaiotaomicron VPI-5482],2P0V_B Crystal structure of BT3781 protein from Bacteroides thetaiotaomicron, Northeast Structural Genomics Target BtR58 [Bacteroides thetaiotaomicron VPI-5482] |
6RQK_A | 2.02e-137 | 66 | 472 | 22 | 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] |
3QT3_A | 2.20e-137 | 66 | 472 | 22 | 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] |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
Q10449 | 2.23e-113 | 43 | 481 | 51 | 506 | 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 |
---|---|---|---|---|---|
0.000000 | 0.000000 | 0.000000 | 0.999926 | 0.000062 | 0.000000 |
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