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CAZyme Information: PTTG_26926-t43_1-p1

You are here: Home > Sequence: PTTG_26926-t43_1-p1

Basic Information | Genomic context | Full Sequence | Enzyme annotations |  CAZy signature domains |  CDD domains | CAZyme hits | PDB hits | Swiss-Prot hits | SignalP and Lipop annotations | TMHMM annotations

Basic Information help

Species Puccinia triticina
Lineage Basidiomycota; Pucciniomycetes; ; Pucciniaceae; Puccinia; Puccinia triticina
CAZyme ID PTTG_26926-t43_1-p1
CAZy Family GT39
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
860 98663.50 8.5587
Genome Property
Genome Version/Assembly ID Genes Strain NCBI Taxon ID Non Protein Coding Genes Protein Coding Genes
FungiDB-61_Ptriticina1-1BBBDRace1 15692 630390 814 14878
Gene Location

Full Sequence      Download help

Enzyme Prediction      help

EC 2.4.1.109:12

CAZyme Signature Domains help

Family Start End Evalue family coverage
GT39 66 306 1.2e-71 0.9910313901345291

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
224839 PMT1 0.0 72 755 36 697
Dolichyl-phosphate-mannose--protein O-mannosyl transferase [Posttranslational modification, protein turnover, chaperones].
406576 PMT_4TMC 5.21e-71 561 749 1 198
C-terminal four TMM region of protein-O-mannosyltransferase. PMT_4TMC is the C-terminal four membrane-pass region of protein-O-mannosyltransferases and similar enzymes.
396786 PMT 1.70e-64 72 310 9 245
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 2.99e-32 358 533 13 183
MIR domain. The MIR (protein mannosyltransferase, IP3R and RyR) domain is a domain that may have a ligand transferase function.
197746 MIR 2.36e-13 490 538 8 57
Domain in ryanodine and inositol trisphosphate receptors and protein O-mannosyltransferases.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
6.26e-298 40 765 101 824
2.12e-284 30 765 45 755
1.21e-283 30 765 45 755
1.21e-283 30 765 45 755
1.75e-281 1 849 1 851

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
3.32e-171 59 765 49 741
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]
2.29e-123 67 754 72 754
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]
2.10e-30 338 538 5 193
Crystal structure of the MIR domain (aa 337-532) of the S. cerevisiae mannosyltransferase Pmt2 [Saccharomyces cerevisiae]
3.43e-30 338 538 22 210
Structure of the Pmt2-MIR domain with bound ligands [Saccharomyces cerevisiae]
2.06e-29 338 545 14 210
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]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
8.03e-189 56 766 62 760
Dolichyl-phosphate-mannose--protein mannosyltransferase 1 OS=Candida albicans (strain SC5314 / ATCC MYA-2876) OX=237561 GN=PMT1 PE=2 SV=1
1.71e-170 59 765 49 741
Dolichyl-phosphate-mannose--protein mannosyltransferase 1 OS=Saccharomyces cerevisiae (strain ATCC 204508 / S288c) OX=559292 GN=PMT1 PE=1 SV=1
5.00e-154 59 756 45 728
Dolichyl-phosphate-mannose--protein mannosyltransferase 5 OS=Saccharomyces cerevisiae (strain ATCC 204508 / S288c) OX=559292 GN=PMT5 PE=1 SV=1
9.67e-130 67 753 135 820
Protein O-mannosyl-transferase 2 OS=Mus musculus OX=10090 GN=Pomt2 PE=1 SV=1
2.11e-125 62 753 60 750
Protein O-mannosyl-transferase 2 OS=Homo sapiens OX=9606 GN=POMT2 PE=1 SV=2

SignalP and Lipop Annotations help

This protein is predicted as OTHER

Other SP_Sec_SPI CS Position
0.999430 0.000580

TMHMM  Annotations      download full data without filtering help

Start End
144 166
195 214
229 251
287 309
613 635
655 674
679 701
714 736
107 129