Species | Puccinia triticina | |||||||||||
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Lineage | Basidiomycota; Pucciniomycetes; ; Pucciniaceae; Puccinia; Puccinia triticina | |||||||||||
CAZyme ID | PTTG_02691-t43_2-p1 | |||||||||||
CAZy Family | GH152 | |||||||||||
CAZyme Description | hypothetical protein, variant | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location |
EC | 2.4.1.109:13 |
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Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
GT39 | 77 | 314 | 1.2e-67 | 0.9865470852017937 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
224839 | PMT1 | 2.12e-155 | 67 | 539 | 21 | 483 | Dolichyl-phosphate-mannose--protein O-mannosyl transferase [Posttranslational modification, protein turnover, chaperones]. |
396786 | PMT | 9.79e-82 | 77 | 318 | 4 | 245 | 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 | 4.29e-28 | 364 | 525 | 11 | 180 | MIR domain. The MIR (protein mannosyltransferase, IP3R and RyR) domain is a domain that may have a ligand transferase function. |
197746 | MIR | 1.06e-11 | 410 | 466 | 1 | 57 | Domain in ryanodine and inositol trisphosphate receptors and protein O-mannosyltransferases. |
197746 | MIR | 1.32e-08 | 347 | 397 | 4 | 56 | Domain in ryanodine and inositol trisphosphate receptors and protein O-mannosyltransferases. |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
8.65e-253 | 62 | 539 | 163 | 641 | |
1.00e-227 | 42 | 539 | 71 | 565 | |
1.00e-227 | 42 | 539 | 71 | 565 | |
1.95e-227 | 42 | 539 | 70 | 564 | |
8.59e-225 | 20 | 539 | 87 | 608 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
1.29e-161 | 67 | 539 | 62 | 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] |
|
4.87e-74 | 51 | 538 | 25 | 517 | 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] |
|
1.85e-57 | 340 | 539 | 16 | 214 | Structure of the Pmt2-MIR domain with bound ligands [Saccharomyces cerevisiae] |
|
5.68e-57 | 342 | 537 | 1 | 195 | Crystal structure of the MIR domain (aa 337-532) of the S. cerevisiae mannosyltransferase Pmt2 [Saccharomyces cerevisiae] |
|
1.16e-52 | 344 | 539 | 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 |
---|---|---|---|---|---|---|
6.65e-161 | 67 | 539 | 62 | 533 | Dolichyl-phosphate-mannose--protein mannosyltransferase 2 OS=Saccharomyces cerevisiae (strain ATCC 204508 / S288c) OX=559292 GN=PMT2 PE=1 SV=2 |
|
3.53e-159 | 65 | 539 | 53 | 527 | Dolichyl-phosphate-mannose--protein mannosyltransferase 3 OS=Saccharomyces cerevisiae (strain ATCC 204508 / S288c) OX=559292 GN=PMT3 PE=1 SV=2 |
|
4.16e-157 | 70 | 539 | 59 | 525 | Dolichyl-phosphate-mannose--protein mannosyltransferase 2 OS=Schizosaccharomyces pombe (strain 972 / ATCC 24843) OX=284812 GN=ogm2 PE=3 SV=1 |
|
2.78e-150 | 59 | 537 | 52 | 536 | Dolichyl-phosphate-mannose--protein mannosyltransferase 2 OS=Candida albicans (strain SC5314 / ATCC MYA-2876) OX=237561 GN=PMT2 PE=1 SV=1 |
|
2.81e-131 | 67 | 537 | 63 | 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 |
---|---|---|
1.000065 | 0.000000 |
Start | End |
---|---|
158 | 180 |
201 | 223 |
238 | 260 |
295 | 317 |
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