| Species | UMGS1572 sp900553045 | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Lineage | Bacteria; Firmicutes; Bacilli; RF39; UBA660; UMGS1572; UMGS1572 sp900553045 | |||||||||||
| CAZyme ID | MGYG000002167_00231 | |||||||||||
| CAZy Family | GT2 | |||||||||||
| CAZyme Description | hypothetical protein | |||||||||||
| CAZyme Property |
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| Genome Property |
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| Gene Location | Start: 6102; End: 7187 Strand: + | |||||||||||
| Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
|---|---|---|---|---|---|---|---|
| cd02511 | Beta4Glucosyltransferase | 6.95e-13 | 7 | 173 | 1 | 165 | UDP-glucose LOS-beta-1,4 glucosyltransferase is required for biosynthesis of lipooligosaccharide. UDP-glucose: lipooligosaccharide (LOS) beta-1-4-glucosyltransferase catalyzes the addition of the first residue, glucose, of the lacto-N-neotetrase structure to HepI of the LOS inner core. LOS is the major constituent of the outer leaflet of the outer membrane of gram-positive bacteria. It consists of a short oligosaccharide chain of variable composition (alpha chain) attached to a branched inner core which is lined in turn to lipid A. Beta 1,4 glucosyltransferase is required to attach the alpha chain to the inner core. |
| sd00006 | TPR | 2.49e-09 | 236 | 343 | 1 | 97 | Tetratricopeptide repeat. The Tetratricopeptide repeat (TPR) typically contains 34 amino acids and is found in a variety of organisms including bacteria, cyanobacteria, yeast, fungi, plants, and humans. It is present in a variety of proteins including those involved in chaperone, cell-cycle, transcription, and protein transport complexes. The number of TPR motifs varies among proteins. Those containing 5-6 tandem repeats generate a right-handed helical structure with an amphipathic channel that is thought to accommodate an alpha-helix of a target protein. It has been proposed that TPR proteins preferentially interact with WD-40 repeat proteins, but in many instances several TPR-proteins seem to aggregate to multi-protein complexes. |
| sd00006 | TPR | 1.17e-08 | 200 | 298 | 4 | 97 | Tetratricopeptide repeat. The Tetratricopeptide repeat (TPR) typically contains 34 amino acids and is found in a variety of organisms including bacteria, cyanobacteria, yeast, fungi, plants, and humans. It is present in a variety of proteins including those involved in chaperone, cell-cycle, transcription, and protein transport complexes. The number of TPR motifs varies among proteins. Those containing 5-6 tandem repeats generate a right-handed helical structure with an amphipathic channel that is thought to accommodate an alpha-helix of a target protein. It has been proposed that TPR proteins preferentially interact with WD-40 repeat proteins, but in many instances several TPR-proteins seem to aggregate to multi-protein complexes. |
| sd00006 | TPR | 4.48e-06 | 273 | 355 | 4 | 75 | Tetratricopeptide repeat. The Tetratricopeptide repeat (TPR) typically contains 34 amino acids and is found in a variety of organisms including bacteria, cyanobacteria, yeast, fungi, plants, and humans. It is present in a variety of proteins including those involved in chaperone, cell-cycle, transcription, and protein transport complexes. The number of TPR motifs varies among proteins. Those containing 5-6 tandem repeats generate a right-handed helical structure with an amphipathic channel that is thought to accommodate an alpha-helix of a target protein. It has been proposed that TPR proteins preferentially interact with WD-40 repeat proteins, but in many instances several TPR-proteins seem to aggregate to multi-protein complexes. |
| sd00006 | TPR | 2.83e-05 | 183 | 263 | 21 | 96 | Tetratricopeptide repeat. The Tetratricopeptide repeat (TPR) typically contains 34 amino acids and is found in a variety of organisms including bacteria, cyanobacteria, yeast, fungi, plants, and humans. It is present in a variety of proteins including those involved in chaperone, cell-cycle, transcription, and protein transport complexes. The number of TPR motifs varies among proteins. Those containing 5-6 tandem repeats generate a right-handed helical structure with an amphipathic channel that is thought to accommodate an alpha-helix of a target protein. It has been proposed that TPR proteins preferentially interact with WD-40 repeat proteins, but in many instances several TPR-proteins seem to aggregate to multi-protein complexes. |
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
|---|---|---|---|---|---|
| QOX65321.1 | 1.45e-120 | 7 | 358 | 5 | 356 |
| CAB1239995.1 | 2.63e-120 | 8 | 358 | 6 | 356 |
| QAT50106.1 | 2.07e-118 | 7 | 360 | 5 | 358 |
| AQS58818.1 | 7.96e-118 | 6 | 358 | 4 | 356 |
| AOK89619.1 | 8.55e-117 | 7 | 358 | 8 | 359 |
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| 7MSN_A | 4.22e-07 | 16 | 360 | 64 | 408 | ChainA, SPbeta prophage-derived glycosyltransferase SunS [Bacillus subtilis subsp. subtilis str. 168],7MSN_B Chain B, SPbeta prophage-derived glycosyltransferase SunS [Bacillus subtilis subsp. subtilis str. 168] |
| 7MSP_A | 8.04e-07 | 16 | 270 | 64 | 323 | ChainA, SPbeta prophage-derived glycosyltransferase SunS [Bacillus subtilis subsp. subtilis str. 168],7MSP_B Chain B, SPbeta prophage-derived glycosyltransferase SunS [Bacillus subtilis subsp. subtilis str. 168] |
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| O31986 | 2.31e-06 | 16 | 360 | 64 | 408 | SPbeta prophage-derived glycosyltransferase SunS OS=Bacillus subtilis (strain 168) OX=224308 GN=sunS PE=1 SV=1 |
| O64036 | 2.31e-06 | 16 | 360 | 64 | 408 | Glycosyltransferase SunS OS=Bacillus phage SPbeta OX=66797 GN=sunS PE=3 SV=1 |
| Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
|---|---|---|---|---|---|
| 1.000056 | 0.000000 | 0.000000 | 0.000000 | 0.000000 | 0.000000 |
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