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CAZyme Information: FOXG_17687-t26_1-p1

You are here: Home > Sequence: FOXG_17687-t26_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 Fusarium oxysporum
Lineage Ascomycota; Sordariomycetes; ; Nectriaceae; Fusarium; Fusarium oxysporum
CAZyme ID FOXG_17687-t26_1-p1
CAZy Family GT69
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
510 55881.93 8.4676
Genome Property
Genome Version/Assembly ID Genes Strain NCBI Taxon ID Non Protein Coding Genes Protein Coding Genes
FungiDB-61_Foxysporum4287 21354 426428 429 20925
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 8.77e-07 384 428 1 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.
212030 LysM 9.12e-07 462 506 1 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 2.66e-05 58 331 343 576
1,4-beta-N-acetylmuramoylhydrolase.
197609 LysM 4.34e-04 385 430 1 44
Lysin motif.
224306 LysM 7.09e-04 316 413 1 96
LysM repeat [Cell wall/membrane/envelope biogenesis].

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
5.41e-240 1 510 1 523
5.50e-187 29 508 175 659
1.24e-186 29 508 200 684
1.24e-186 29 508 200 684
4.97e-186 29 508 200 684

PDB Hits      help

FOXG_17687-t26_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
9.94e-132 11 433 10 458
LysM domain-containing protein ARB_05157 OS=Arthroderma benhamiae (strain ATCC MYA-4681 / CBS 112371) OX=663331 GN=ARB_05157 PE=1 SV=1
1.59e-16 7 432 5 408
LysM domain-containing protein ARB_01488 OS=Arthroderma benhamiae (strain ATCC MYA-4681 / CBS 112371) OX=663331 GN=ARB_01488 PE=3 SV=1
4.47e-16 226 360 40 189
LysM domain-containing protein ARB_03438 OS=Arthroderma benhamiae (strain ATCC MYA-4681 / CBS 112371) OX=663331 GN=ARB_03438 PE=3 SV=1
7.23e-10 375 432 380 437
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
9.71e-07 287 508 248 534
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
0.000307 0.999655 CS pos: 20-21. Pr: 0.9786

TMHMM  Annotations      help

There is no transmembrane helices in FOXG_17687-t26_1-p1.