| Species | Clostridium_B tyrobutyricum | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Lineage | Bacteria; Firmicutes_A; Clostridia; Clostridiales; Clostridiaceae; Clostridium_B; Clostridium_B tyrobutyricum | |||||||||||
| CAZyme ID | MGYG000000125_01843 | |||||||||||
| CAZy Family | GT83 | |||||||||||
| CAZyme Description | Undecaprenyl phosphate-alpha-4-amino-4-deoxy-L-arabinose arabinosyl transferase | |||||||||||
| CAZyme Property |
|
|||||||||||
| Genome Property |
|
|||||||||||
| Gene Location | Start: 74251; End: 76506 Strand: - | |||||||||||
| Family | Start | End | Evalue | family coverage |
|---|---|---|---|---|
| GT83 | 13 | 231 | 6.7e-36 | 0.39444444444444443 |
| Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
|---|---|---|---|---|---|---|---|
| COG1807 | ArnT | 1.25e-60 | 5 | 695 | 2 | 531 | 4-amino-4-deoxy-L-arabinose transferase or related glycosyltransferase of PMT family [Cell wall/membrane/envelope biogenesis]. |
| pfam13231 | PMT_2 | 1.12e-44 | 66 | 224 | 1 | 160 | Dolichyl-phosphate-mannose-protein mannosyltransferase. This family contains members that are not captured by pfam02366. |
| COG1928 | PMT1 | 1.25e-10 | 1 | 220 | 15 | 255 | Dolichyl-phosphate-mannose--protein O-mannosyl transferase [Posttranslational modification, protein turnover, chaperones]. |
| pfam02366 | PMT | 7.58e-09 | 67 | 225 | 62 | 233 | Dolichyl-phosphate-mannose-protein mannosyltransferase. This is a family of Dolichyl-phosphate-mannose-protein mannosyltransferase proteins EC:2.4.1.109. These proteins are responsible for O-linked glycosylation of proteins, they catalyze the reaction:- Dolichyl phosphate D-mannose + protein <=> dolichyl phosphate + O-D-mannosyl-protein. Also in this family is Drosophila rotated abdomen protein which is a putative mannosyltransferase. This family appears to be distantly related to pfam02516 (A Bateman pers. obs.). This family also contains sequences from ArnTs (4-amino-4-deoxy-L-arabinose lipid A transferase). They catalyze the addition of 4-amino-4-deoxy-l-arabinose (l-Ara4N) to the lipid A moiety of the lipopolysaccharide. This is a critical modification enabling bacteria (e.g. Escherichia coli and Salmonella typhimurium) to resist killing by antimicrobial peptides such as polymyxins. Members such as undecaprenyl phosphate-alpha-4-amino-4-deoxy-L-arabinose arabinosyl transferase are predicted to have 12 trans-membrane regions. The N-terminal portion of these proteins is hypothesized to have a conserved glycosylation activity which is shared between distantly related oligosaccharyltransferases ArnT and PglB families. |
| COG4745 | COG4745 | 6.34e-07 | 69 | 233 | 67 | 234 | Predicted membrane-bound mannosyltransferase [General function prediction only]. |
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
|---|---|---|---|---|---|
| QHU89858.1 | 1.38e-71 | 9 | 690 | 271 | 889 |
| QUB37647.1 | 8.87e-69 | 16 | 690 | 210 | 780 |
| QHU90800.1 | 1.96e-68 | 9 | 690 | 271 | 886 |
| QJU10517.1 | 1.02e-64 | 9 | 690 | 271 | 892 |
| QHU92512.1 | 1.31e-64 | 16 | 690 | 276 | 886 |
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| 5EZM_A | 8.33e-08 | 66 | 229 | 87 | 255 | CrystalStructure of ArnT from Cupriavidus metallidurans in the apo state [Cupriavidus metallidurans CH34],5F15_A Crystal Structure of ArnT from Cupriavidus metallidurans bound to Undecaprenyl phosphate [Cupriavidus metallidurans CH34] |
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| O34575 | 1.58e-123 | 8 | 699 | 5 | 673 | Putative mannosyltransferase YkcB OS=Bacillus subtilis (strain 168) OX=224308 GN=ykcB PE=3 SV=2 |
| P37483 | 1.44e-113 | 12 | 703 | 9 | 664 | Putative mannosyltransferase YycA OS=Bacillus subtilis (strain 168) OX=224308 GN=yycA PE=3 SV=2 |
| Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
|---|---|---|---|---|---|
| 0.979074 | 0.009868 | 0.000766 | 0.000068 | 0.000043 | 0.010215 |
| start | end |
|---|---|
| 13 | 30 |
| 52 | 74 |
| 86 | 108 |
| 112 | 134 |
| 141 | 158 |
| 181 | 203 |
| 210 | 232 |
| 384 | 401 |
| 414 | 433 |
| 443 | 465 |
| 472 | 494 |
| 499 | 521 |
| 534 | 556 |
Copyright 2022 © YIN LAB, UNL. All rights reserved. Designed by Jinfang Zheng and Boyang Hu. Maintained by Yanbin Yin.