Species | Trichophyton rubrum | |||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|
Lineage | Ascomycota; Eurotiomycetes; ; Arthrodermataceae; Trichophyton; Trichophyton rubrum | |||||||||||
CAZyme ID | KFL62339.1 | |||||||||||
CAZy Family | GT59 | |||||||||||
CAZyme Description | hypothetical protein | |||||||||||
CAZyme Property |
|
|||||||||||
Genome Property |
|
|||||||||||
Gene Location |
EC | 2.4.1.109:13 |
---|
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
GT39 | 68 | 306 | 5.6e-77 | 0.9910313901345291 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
224839 | PMT1 | 0.0 | 59 | 529 | 21 | 483 | Dolichyl-phosphate-mannose--protein O-mannosyl transferase [Posttranslational modification, protein turnover, chaperones]. |
396786 | PMT | 1.77e-89 | 67 | 309 | 2 | 244 | 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. |
397103 | MIR | 2.27e-41 | 357 | 518 | 11 | 183 | MIR domain. The MIR (protein mannosyltransferase, IP3R and RyR) domain is a domain that may have a ligand transferase function. |
197746 | MIR | 1.84e-11 | 405 | 459 | 3 | 57 | Domain in ryanodine and inositol trisphosphate receptors and protein O-mannosyltransferases. |
197746 | MIR | 2.46e-10 | 340 | 391 | 4 | 57 | Domain in ryanodine and inositol trisphosphate receptors and protein O-mannosyltransferases. |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
0.0 | 1 | 529 | 1 | 531 | |
0.0 | 1 | 529 | 1 | 531 | |
1.21e-308 | 3 | 529 | 2 | 525 | |
2.43e-308 | 1 | 529 | 1 | 525 | |
9.60e-307 | 1 | 529 | 1 | 528 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
3.48e-183 | 39 | 529 | 42 | 533 | Structure of S. cerevisiae protein O-mannosyltransferase Pmt1-Pmt2 complex bound to the sugar donor and a peptide acceptor [Saccharomyces cerevisiae W303],6P2R_B Structure of S. cerevisiae protein O-mannosyltransferase Pmt1-Pmt2 complex bound to the sugar donor [Saccharomyces cerevisiae W303] |
|
2.93e-84 | 66 | 527 | 51 | 516 | Structure of S. cerevisiae protein O-mannosyltransferase Pmt1-Pmt2 complex bound to the sugar donor and a peptide acceptor [Saccharomyces cerevisiae W303],6P2R_A Structure of S. cerevisiae protein O-mannosyltransferase Pmt1-Pmt2 complex bound to the sugar donor [Saccharomyces cerevisiae W303] |
|
4.06e-64 | 337 | 529 | 20 | 214 | Structure of the Pmt2-MIR domain with bound ligands [Saccharomyces cerevisiae] |
|
1.24e-63 | 337 | 528 | 3 | 196 | Crystal structure of the MIR domain (aa 337-532) of the S. cerevisiae mannosyltransferase Pmt2 [Saccharomyces cerevisiae] |
|
1.97e-59 | 337 | 529 | 12 | 207 | Structure of the Pmt3-MIR domain with bound ligands [Saccharomyces cerevisiae],6ZQQ_B Structure of the Pmt3-MIR domain with bound ligands [Saccharomyces cerevisiae],6ZQQ_C Structure of the Pmt3-MIR domain with bound ligands [Saccharomyces cerevisiae],6ZQQ_D Structure of the Pmt3-MIR domain with bound ligands [Saccharomyces cerevisiae] |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
3.35e-185 | 47 | 527 | 51 | 536 | Dolichyl-phosphate-mannose--protein mannosyltransferase 2 OS=Candida albicans (strain SC5314 / ATCC MYA-2876) OX=237561 GN=PMT2 PE=1 SV=1 |
|
1.79e-182 | 39 | 529 | 42 | 533 | Dolichyl-phosphate-mannose--protein mannosyltransferase 2 OS=Saccharomyces cerevisiae (strain ATCC 204508 / S288c) OX=559292 GN=PMT2 PE=1 SV=2 |
|
3.93e-177 | 59 | 529 | 55 | 527 | Dolichyl-phosphate-mannose--protein mannosyltransferase 3 OS=Saccharomyces cerevisiae (strain ATCC 204508 / S288c) OX=559292 GN=PMT3 PE=1 SV=2 |
|
3.10e-167 | 59 | 529 | 55 | 525 | Dolichyl-phosphate-mannose--protein mannosyltransferase 2 OS=Schizosaccharomyces pombe (strain 972 / ATCC 24843) OX=284812 GN=ogm2 PE=3 SV=1 |
|
8.17e-152 | 3 | 527 | 4 | 542 | Dolichyl-phosphate-mannose--protein mannosyltransferase 6 OS=Saccharomyces cerevisiae (strain ATCC 204508 / S288c) OX=559292 GN=PMT6 PE=1 SV=1 |
Other | SP_Sec_SPI | CS Position |
---|---|---|
0.999796 | 0.000225 |
Start | End |
---|---|
109 | 131 |
146 | 165 |
177 | 199 |
229 | 251 |
287 | 309 |
Copyright 2022 © YIN LAB, UNL. All rights reserved. Designed by Jinfang Zheng and Boyang Hu. Maintained by Yanbin Yin.