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CAZyme Information: APA09239.1

You are here: Home > Sequence: APA09239.1

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 APA09239.1
CAZy Family GH16
CAZyme Description unspecified product
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
492 CP017817|CGC8 55739.40 5.1332
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 3.2.1.113:7

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH47 28 488 2e-164 0.9932735426008968

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 27 488 1 452
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 6.42e-138 22 488 74 517
glycoside hydrolase family 47 protein; Provisional
271200 LanM-like 0.009 22 201 516 679
Cyclases involved in the biosynthesis of class II lantibiotics, and similar proteins. LanM-like proteins. LanM is a bifunctional enzyme, involved in the synthesis of class II lantibiotics. It is responsible for both the dehydration and the cyclization of the precursor-peptide during lantibiotic synthesis. The C-terminal domain shows similarity to LanC, the cyclase component of the lan operon, but the N terminus seems to be unrelated to the dehydratase, LanB.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
0.0 1 492 1 492
7.35e-310 19 492 93 566
7.35e-310 19 492 93 566
6.91e-262 22 490 93 567
4.69e-248 23 489 205 668

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
3.01e-77 22 487 7 449
Crystal structure of the class I human endoplasmic reticulum 1,2-alpha-mannosidase and Man9GlcNAc2-PA complex [Homo sapiens]
3.54e-77 22 487 12 454
Crystal Structure Of Human Class I Alpha1,2-Mannosidase [Homo sapiens]
3.73e-77 22 487 12 454
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]
1.79e-76 22 487 7 449
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]
2.73e-76 22 487 90 532
Crystal Structure Of Human Class I alpha-1,2-Mannosidase In Complex With Thio-Disaccharide Substrate Analogue [Homo sapiens]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
2.78e-77 22 488 100 536
Mannosyl-oligosaccharide 1,2-alpha-mannosidase MNS2 OS=Arabidopsis thaliana OX=3702 GN=MNS2 PE=1 SV=1
2.93e-77 22 488 99 535
Mannosyl-oligosaccharide 1,2-alpha-mannosidase MNS1 OS=Arabidopsis thaliana OX=3702 GN=MNS1 PE=1 SV=1
2.43e-74 22 487 202 645
Mannosyl-oligosaccharide alpha-1,2-mannosidase IA OS=Drosophila melanogaster OX=7227 GN=alpha-Man-Ia PE=2 SV=2
4.53e-74 22 487 251 693
Endoplasmic reticulum mannosyl-oligosaccharide 1,2-alpha-mannosidase OS=Homo sapiens OX=9606 GN=MAN1B1 PE=1 SV=2
5.27e-73 22 487 141 585
Mannosyl-oligosaccharide 1,2-alpha-mannosidase C52E4.5 OS=Caenorhabditis elegans OX=6239 GN=C52E4.5 PE=1 SV=1

SignalP and Lipop Annotations help

This protein is predicted as OTHER

Other SP_Sec_SPI CS Position
1.000068 0.000001

TMHMM  Annotations      help

There is no transmembrane helices in APA09239.1.