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CAZyme Information: KIS65793.1

You are here: Home > Sequence: KIS65793.1

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 Ustilago maydis
Lineage Basidiomycota; Ustilaginomycetes; ; Ustilaginaceae; Ustilago; Ustilago maydis
CAZyme ID KIS65793.1
CAZy Family AA1
CAZyme Description unspecified product
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
956 106388.24 7.5758
Genome Property
Genome Version/Assembly ID Genes Strain NCBI Taxon ID Non Protein Coding Genes Protein Coding Genes
FungiDB-61_Umaydis521 6910 237631 145 6765
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 88 332 7.4e-72 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 76 789 18 697
Dolichyl-phosphate-mannose--protein O-mannosyl transferase [Posttranslational modification, protein turnover, chaperones].
406576 PMT_4TMC 8.72e-82 596 783 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 6.25e-70 86 335 1 244
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 3.54e-44 384 568 13 183
MIR domain. The MIR (protein mannosyltransferase, IP3R and RyR) domain is a domain that may have a ligand transferase function.
197746 MIR 3.41e-14 525 573 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
0.0 1 956 1 963
0.0 1 956 1 966
0.0 1 955 1 964
0.0 1 949 1 983
0.0 1 956 1 984

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
5.83e-187 75 822 43 755
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]
4.19e-130 92 786 75 752
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]
5.72e-34 364 573 5 193
Crystal structure of the MIR domain (aa 337-532) of the S. cerevisiae mannosyltransferase Pmt2 [Saccharomyces cerevisiae]
9.49e-34 364 573 22 210
Structure of the Pmt2-MIR domain with bound ligands [Saccharomyces cerevisiae]
7.90e-31 364 573 14 203
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
1.47e-194 66 839 50 806
Dolichyl-phosphate-mannose--protein mannosyltransferase 1 OS=Candida albicans (strain SC5314 / ATCC MYA-2876) OX=237561 GN=PMT1 PE=2 SV=1
3.00e-186 75 822 43 755
Dolichyl-phosphate-mannose--protein mannosyltransferase 1 OS=Saccharomyces cerevisiae (strain ATCC 204508 / S288c) OX=559292 GN=PMT1 PE=1 SV=1
2.57e-153 75 789 39 727
Dolichyl-phosphate-mannose--protein mannosyltransferase 5 OS=Saccharomyces cerevisiae (strain ATCC 204508 / S288c) OX=559292 GN=PMT5 PE=1 SV=1
2.15e-129 92 786 75 752
Dolichyl-phosphate-mannose--protein mannosyltransferase 2 OS=Saccharomyces cerevisiae (strain ATCC 204508 / S288c) OX=559292 GN=PMT2 PE=1 SV=2
4.40e-127 85 787 131 820
Protein O-mannosyl-transferase 2 OS=Mus musculus OX=10090 GN=Pomt2 PE=1 SV=1

SignalP and Lipop Annotations help

This protein is predicted as OTHER

Other SP_Sec_SPI CS Position
1.000070 0.000003

TMHMM  Annotations      download full data without filtering help

Start End
125 147
170 192
194 211
221 243
255 270
274 292
313 335
648 670
691 708
713 732
745 764