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CAZyme Information: QRD01632.1

You are here: Home > Sequence: QRD01632.1

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 Parastagonospora nodorum
Lineage Ascomycota; Dothideomycetes; ; Phaeosphaeriaceae; Parastagonospora; Parastagonospora nodorum
CAZyme ID QRD01632.1
CAZy Family GH3
CAZyme Description alpha-1,2-Mannosidase
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
922 CP069034|CGC1 103158.88 4.9910
Genome Property
Genome Version/Assembly ID Genes Strain NCBI Taxon ID Non Protein Coding Genes Protein Coding Genes
FungiDB-61_PnodorumSN15 17580 321614 132 17448
Gene Location

Full Sequence      Download help

Enzyme Prediction      help

EC 3.2.1.113:7

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH47 190 920 6.2e-176 0.9955156950672646

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
396217 Glyco_hydro_47 0.0 189 920 1 453
Glycosyl hydrolase family 47. Members of this family are alpha-mannosidases that catalyze the hydrolysis of the terminal 1,2-linked alpha-D-mannose residues in the oligo-mannose oligosaccharide Man(9)(GlcNAc)(2).
240427 PTZ00470 2.69e-94 130 921 30 519
glycoside hydrolase family 47 protein; Provisional
397323 Atrophin-1 0.004 74 159 177 255
Atrophin-1 family. Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are characteristic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.
237057 PRK12323 0.005 55 146 416 509
DNA polymerase III subunit gamma/tau.
275319 predic_Ig_block 0.006 96 165 75 141
putative immunoglobulin-blocking virulence protein. Members of this family are putative virulence proteins of Mycoplasma and Ureaplasma species. Members share a region of sequence similarity (see TIGR04524) with protein M, a Mycoplasma genitalium protein that binds a conserved light chain region of IgG and blocks its protective function of antigen-specific binding. The seed alignment for this model includes an N-terminal signal-anchor domain and a proline-rich linker domain, and a C-terminal extension, in addition to the protein M-like domain recognized by TIGR04524. [Cellular processes, Pathogenesis]

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
0.0 1 922 1 922
0.0 1 922 1 968
0.0 1 922 1 910
1.12e-234 123 922 148 978
7.57e-234 134 922 162 995

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
1.08e-38 189 917 12 448
Crystal structure of the class I human endoplasmic reticulum 1,2-alpha-mannosidase and Man9GlcNAc2-PA complex [Homo sapiens]
1.21e-38 189 917 17 453
Crystal Structure Of Human Class I Alpha1,2-Mannosidase [Homo sapiens]
1.25e-38 189 917 17 453
Crystal Structure Of Human Class I Alpha1,2-Mannosidase In Complex With 1-Deoxymannojirimycin [Homo sapiens],1FO3_A Crystal Structure Of Human Class I Alpha1,2-Mannosidase In Complex With Kifunensine [Homo sapiens]
4.22e-38 189 917 95 531
Crystal Structure Of Human Class I alpha-1,2-Mannosidase In Complex With Thio-Disaccharide Substrate Analogue [Homo sapiens]
5.12e-38 189 917 12 448
Crystal structure of the class I human endoplasmic reticulum 1,2-alpha-mannosidase T688A mutant and Thio-disaccharide substrate analog complex [Homo sapiens],5KK7_B Crystal structure of the class I human endoplasmic reticulum 1,2-alpha-mannosidase T688A mutant and Thio-disaccharide substrate analog complex [Homo sapiens]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
2.04e-45 144 917 158 623
Mannosyl-oligosaccharide 1,2-alpha-mannosidase IB OS=Homo sapiens OX=9606 GN=MAN1A2 PE=1 SV=1
3.70e-45 170 917 172 623
Mannosyl-oligosaccharide 1,2-alpha-mannosidase IB OS=Mus musculus OX=10090 GN=Man1a2 PE=1 SV=1
5.92e-39 189 917 214 650
Endoplasmic reticulum mannosyl-oligosaccharide 1,2-alpha-mannosidase OS=Rattus norvegicus OX=10116 GN=Man1b1 PE=2 SV=2
1.07e-38 189 917 215 651
Endoplasmic reticulum mannosyl-oligosaccharide 1,2-alpha-mannosidase OS=Mus musculus OX=10090 GN=Man1b1 PE=1 SV=1
2.85e-38 182 918 197 642
Mannosyl-oligosaccharide alpha-1,2-mannosidase IA OS=Spodoptera frugiperda OX=7108 PE=1 SV=1

SignalP and Lipop Annotations help

This protein is predicted as OTHER

Other SP_Sec_SPI CS Position
0.999985 0.000041

TMHMM  Annotations      download full data without filtering help

Start End
9 31