Species | ||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|
Lineage | Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; Bacteroides; | |||||||||||
CAZyme ID | MGYG000002585_01177 | |||||||||||
CAZy Family | GH125 | |||||||||||
CAZyme Description | hypothetical protein | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location | Start: 28166; End: 29617 Strand: - |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
GH125 | 69 | 469 | 8e-182 | 0.9975124378109452 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
COG3538 | COG3538 | 0.0 | 49 | 479 | 3 | 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 | 0.001 | 4 | 22 | 1 | 19 | TAT (twin-arginine translocation) pathway signal sequence. |
TIGR01409 | TAT_signal_seq | 0.007 | 5 | 33 | 1 | 29 | Tat (twin-arginine translocation) pathway signal sequence. Proteins assembled with various cofactors or by means of cytosolic molecular chaperones are poor candidates for translocation across the bacterial inner membrane by the standard general secretory (Sec) pathway. This model describes a family of predicted long, non-Sec signal sequences and signal-anchor sequences (uncleaved signal sequences). All contain an absolutely conserved pair of arginine residues, in a motif approximated by (S/T)-R-R-X-F-L-K, followed by a membrane-spanning hydrophobic region. Members with small amino acid side chains at the -1 and -3 positions from the C-terminus of the model should be predicted to be cleaved as are Sec pathway signal sequences. Members are almost exclusively bacterial, although archaeal sequences are also found. A large fraction of the members of this family may have bound redox-active cofactors. [Protein fate, Protein and peptide secretion and trafficking] |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
CUA18275.1 | 0.0 | 1 | 483 | 1 | 483 |
QRP90519.1 | 0.0 | 1 | 483 | 1 | 483 |
AKA51568.1 | 0.0 | 1 | 483 | 1 | 483 |
QMI79243.1 | 0.0 | 1 | 483 | 1 | 483 |
QBJ17751.1 | 0.0 | 1 | 483 | 1 | 483 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
2P0V_A | 1.29e-194 | 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] |
3ON6_A | 7.40e-192 | 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] |
3P2C_A | 5.26e-190 | 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] |
6RQK_A | 2.41e-133 | 61 | 472 | 17 | 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 | 1.37e-132 | 61 | 472 | 17 | 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] |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
Q10449 | 1.77e-115 | 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 | 0.000001 | 0.000000 | 0.999902 | 0.000081 | 0.000000 |
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