Species | ||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|
Lineage | Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Muribaculaceae; UBA7173; | |||||||||||
CAZyme ID | MGYG000001885_00544 | |||||||||||
CAZy Family | GH125 | |||||||||||
CAZyme Description | hypothetical protein | |||||||||||
CAZyme Property |
|
|||||||||||
Genome Property |
|
|||||||||||
Gene Location | Start: 3992; End: 5458 Strand: - |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
GH125 | 73 | 471 | 9.2e-183 | 0.9925373134328358 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
COG3538 | COG3538 | 0.0 | 50 | 471 | 1 | 419 | Meiotically up-regulated gene 157 (Mug157) protein (function unknown) [Function unknown]. |
pfam06824 | Glyco_hydro_125 | 0.0 | 72 | 471 | 1 | 415 | 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 |
---|---|---|---|---|---|
QBJ18501.1 | 1.27e-265 | 46 | 486 | 48 | 487 |
QUU01220.1 | 1.27e-265 | 46 | 486 | 48 | 487 |
QUT61519.1 | 1.27e-265 | 46 | 486 | 48 | 487 |
QQA30009.1 | 1.27e-265 | 46 | 486 | 48 | 487 |
QUT65776.1 | 1.27e-265 | 46 | 486 | 48 | 487 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
3P2C_A | 1.90e-246 | 46 | 487 | 21 | 463 | 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 | 5.86e-245 | 43 | 487 | 20 | 461 | 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 | 1.55e-242 | 43 | 487 | 40 | 481 | 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 | 1.25e-134 | 59 | 481 | 12 | 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] |
3QT3_A | 2.73e-134 | 59 | 471 | 12 | 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] |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
Q10449 | 2.08e-112 | 46 | 474 | 51 | 496 | 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 |
---|---|---|---|---|---|
0.000270 | 0.999003 | 0.000161 | 0.000205 | 0.000173 | 0.000153 |
Copyright 2022 © YIN LAB, UNL. All rights reserved. Designed by Jinfang Zheng and Boyang Hu. Maintained by Yanbin Yin.