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CAZyme Information: APA07237.1

You are here: Home > Sequence: APA07237.1

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 Sclerotinia sclerotiorum
Lineage Ascomycota; Leotiomycetes; ; Sclerotiniaceae; Sclerotinia; Sclerotinia sclerotiorum
CAZyme ID APA07237.1
CAZy Family CE16
CAZyme Description unspecified product
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
953 106334.57 6.5412
Genome Property
Genome Version/Assembly ID Genes Strain NCBI Taxon ID Non Protein Coding Genes Protein Coding Genes
FungiDB-61_Ssclerotiorum1980UF-70 11368 665079 238 11130
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 55 300 8.2e-70 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 30 755 4 699
Dolichyl-phosphate-mannose--protein O-mannosyl transferase [Posttranslational modification, protein turnover, chaperones].
406576 PMT_4TMC 3.81e-96 554 747 2 198
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 1.46e-82 53 303 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 6.36e-47 352 527 13 183
MIR domain. The MIR (protein mannosyltransferase, IP3R and RyR) domain is a domain that may have a ligand transferase function.
197746 MIR 6.37e-12 481 532 5 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 1 953 1 953
0.0 1 952 1 952
0.0 1 952 1 952
0.0 1 953 1 944
0.0 26 952 34 966

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
6.97e-207 55 857 56 799
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]
8.93e-133 53 750 69 752
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]
2.42e-31 327 534 17 212
Structure of the Pmt2-MIR domain with bound ligands [Saccharomyces cerevisiae]
2.74e-31 330 534 3 195
Crystal structure of the MIR domain (aa 337-532) of the S. cerevisiae mannosyltransferase Pmt2 [Saccharomyces cerevisiae]
3.17e-29 330 537 12 208
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
3.59e-206 55 857 56 799
Dolichyl-phosphate-mannose--protein mannosyltransferase 1 OS=Saccharomyces cerevisiae (strain ATCC 204508 / S288c) OX=559292 GN=PMT1 PE=1 SV=1
3.61e-201 47 839 64 819
Dolichyl-phosphate-mannose--protein mannosyltransferase 1 OS=Candida albicans (strain SC5314 / ATCC MYA-2876) OX=237561 GN=PMT1 PE=2 SV=1
8.31e-162 55 763 52 737
Dolichyl-phosphate-mannose--protein mannosyltransferase 5 OS=Saccharomyces cerevisiae (strain ATCC 204508 / S288c) OX=559292 GN=PMT5 PE=1 SV=1
7.36e-149 48 767 33 728
Dolichyl-phosphate-mannose--protein mannosyltransferase 1 OS=Schizosaccharomyces pombe (strain 972 / ATCC 24843) OX=284812 GN=ogm1 PE=1 SV=1
1.78e-137 67 756 51 723
Dolichyl-phosphate-mannose--protein mannosyltransferase 5 OS=Candida albicans (strain SC5314 / ATCC MYA-2876) OX=237561 GN=PMT5 PE=2 SV=1

SignalP and Lipop Annotations help

This protein is predicted as OTHER

Other SP_Sec_SPI CS Position
0.999440 0.000550

TMHMM  Annotations      download full data without filtering help

Start End
134 156
163 180
185 207
220 237
241 263
276 298
605 627
648 665
670 692
705 727
92 114