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CAZyme Information: ASPBRDRAFT_167297-t33_1-p1

You are here: Home > Sequence: ASPBRDRAFT_167297-t33_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 Aspergillus brasiliensis
Lineage Ascomycota; Eurotiomycetes; ; Aspergillaceae; Aspergillus; Aspergillus brasiliensis
CAZyme ID ASPBRDRAFT_167297-t33_1-p1
CAZy Family GT71
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
340 35345.27 3.7273
Genome Property
Genome Version/Assembly ID Genes Strain NCBI Taxon ID Non Protein Coding Genes Protein Coding Genes
FungiDB-61_AbrasiliensisCBS101740 13263 767769 274 12989
Gene Location

Full Sequence      Download help

Enzyme Prediction      help

EC - -

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
212030 LysM 1.17e-09 234 269 1 36
Lysin Motif is a small domain involved in binding peptidoglycan. LysM, a small globular domain with approximately 40 amino acids, is a widespread protein module involved in binding peptidoglycan in bacteria and chitin in eukaryotes. The domain was originally identified in enzymes that degrade bacterial cell walls, but proteins involved in many other biological functions also contain this domain. It has been reported that the LysM domain functions as a signal for specific plant-bacteria recognition in bacterial pathogenesis. Many of these enzymes are modular and are composed of catalytic units linked to one or several repeats of LysM domains. LysM domains are found in bacteria and eukaryotes.
212030 LysM 5.28e-09 146 190 2 45
Lysin Motif is a small domain involved in binding peptidoglycan. LysM, a small globular domain with approximately 40 amino acids, is a widespread protein module involved in binding peptidoglycan in bacteria and chitin in eukaryotes. The domain was originally identified in enzymes that degrade bacterial cell walls, but proteins involved in many other biological functions also contain this domain. It has been reported that the LysM domain functions as a signal for specific plant-bacteria recognition in bacterial pathogenesis. Many of these enzymes are modular and are composed of catalytic units linked to one or several repeats of LysM domains. LysM domains are found in bacteria and eukaryotes.
180536 PRK06347 7.72e-09 131 262 317 434
1,4-beta-N-acetylmuramoylhydrolase.
197609 LysM 4.80e-08 146 192 1 44
Lysin motif.
180536 PRK06347 2.33e-07 129 262 394 508
1,4-beta-N-acetylmuramoylhydrolase.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
1.22e-168 1 337 1 335
7.84e-154 1 284 1 284
2.11e-122 1 337 1 281
1.26e-60 30 336 26 314
4.70e-56 132 336 70 283

PDB Hits      help

ASPBRDRAFT_167297-t33_1-p1 has no PDB hit.

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
7.56e-35 2 336 4 335
LysM domain-containing protein ARB_05157 OS=Arthroderma benhamiae (strain ATCC MYA-4681 / CBS 112371) OX=663331 GN=ARB_05157 PE=1 SV=1
7.66e-17 53 203 39 190
LysM domain-containing protein ARB_03438 OS=Arthroderma benhamiae (strain ATCC MYA-4681 / CBS 112371) OX=663331 GN=ARB_03438 PE=3 SV=1
3.59e-15 132 282 256 408
LysM domain-containing protein ARB_01488 OS=Arthroderma benhamiae (strain ATCC MYA-4681 / CBS 112371) OX=663331 GN=ARB_01488 PE=3 SV=1
1.40e-13 225 282 380 437
Probable peptidoglycan-N-acetylglucosamine deacetylase ARB_03699 OS=Arthroderma benhamiae (strain ATCC MYA-4681 / CBS 112371) OX=663331 GN=ARB_03699 PE=1 SV=2
1.84e-08 62 194 399 536
LysM domain-containing protein ARB_00327 OS=Arthroderma benhamiae (strain ATCC MYA-4681 / CBS 112371) OX=663331 GN=ARB_00327 PE=3 SV=2

SignalP and Lipop Annotations help

This protein is predicted as SP

Other SP_Sec_SPI CS Position
0.000363 0.999630 CS pos: 17-18. Pr: 0.9671

TMHMM  Annotations      help

There is no transmembrane helices in ASPBRDRAFT_167297-t33_1-p1.