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CAZyme Information: ZTRI_11.155.mRNA-p1

You are here: Home > Sequence: ZTRI_11.155.mRNA-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 Zymoseptoria tritici
Lineage Ascomycota; Dothideomycetes; ; Mycosphaerellaceae; Zymoseptoria; Zymoseptoria tritici
CAZyme ID ZTRI_11.155.mRNA-p1
CAZy Family GT76
CAZyme Description similar to carbohydrate-binding module family 50 protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
232 Ztri_chr_11|CGC8 24065.10 4.2643
Genome Property
Genome Version/Assembly ID Genes Strain NCBI Taxon ID Non Protein Coding Genes Protein Coding Genes
FungiDB-61_ZtriticiIPO323 11839 336722 13 11826
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
180536 PRK06347 5.79e-17 23 216 307 518
1,4-beta-N-acetylmuramoylhydrolase.
180536 PRK06347 1.69e-15 3 205 365 576
1,4-beta-N-acetylmuramoylhydrolase.
396179 LysM 3.52e-13 49 92 1 43
LysM domain. The LysM (lysin motif) domain is about 40 residues long. It is found in a variety of enzymes involved in bacterial cell wall degradation. This domain may have a general peptidoglycan binding function. The structure of this domain is known.
212030 LysM 1.97e-12 49 91 3 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.
197609 LysM 7.39e-12 49 91 2 44
Lysin motif.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
1.84e-165 1 232 1 232
1.84e-165 1 232 1 232
7.48e-165 1 232 1 232
8.73e-164 1 232 1 232
2.35e-56 1 231 1 226

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
8.10e-58 1 231 1 226
Chain A, Extracellular Protein 6 [Fulvia fulva],4B9H_A Chain A, Extracellular Protein 6 [Fulvia fulva]
8.23e-09 41 103 13 78
Chain A, LysM domain-containing protein [Zymoseptoria tritici IPO323],6Q40_B Chain B, LysM domain-containing protein [Zymoseptoria tritici IPO323],6Q40_C Chain C, LysM domain-containing protein [Zymoseptoria tritici IPO323],6Q40_D Chain D, LysM domain-containing protein [Zymoseptoria tritici IPO323]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
7.29e-19 51 168 112 230
Intracellular hyphae protein 1 OS=Colletotrichum lindemuthianum OX=290576 GN=CIH1 PE=1 SV=1
2.15e-09 49 221 489 664
Muramidase-2 OS=Enterococcus hirae (strain ATCC 9790 / DSM 20160 / JCM 8729 / LMG 6399 / NBRC 3181 / NCIMB 6459 / NCDO 1258 / NCTC 12367 / WDCM 00089 / R) OX=768486 GN=EHR_05900 PE=1 SV=1
2.98e-09 33 205 349 525
Autolysin OS=Enterococcus faecalis (strain ATCC 700802 / V583) OX=226185 GN=EF_0799 PE=1 SV=2
5.90e-09 49 205 90 253
D-gamma-glutamyl-meso-diaminopimelic acid endopeptidase CwlS OS=Bacillus subtilis (strain 168) OX=224308 GN=cwlS PE=1 SV=1
3.98e-08 47 166 84 191
N-acetylmuramoyl-L-alanine amidase sle1 OS=Staphylococcus epidermidis (strain ATCC 35984 / RP62A) OX=176279 GN=sle1 PE=3 SV=1

SignalP and Lipop Annotations help

This protein is predicted as SP

Other SP_Sec_SPI CS Position
0.000274 0.999675 CS pos: 16-17. Pr: 0.9711

TMHMM  Annotations      help

There is no transmembrane helices in ZTRI_11.155.mRNA-p1.