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CAZyme Information: FOMG_15065-t38_1-p1

You are here: Home > Sequence: FOMG_15065-t38_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 FOMG_15065-t38_1-p1
CAZy Family GH93
CAZyme Description lysozyme
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
258 JH659344.1|CGC3 27955.91 9.1503
Genome Property
Genome Version/Assembly ID Genes Strain NCBI Taxon ID Non Protein Coding Genes Protein Coding Genes
FungiDB-61_Foxysporum26406 20033 1089452 372 19661
Gene Location

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in FOMG_15065-t38_1-p1.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH24 101 241 1.1e-31 0.9781021897810219

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
381599 lyz_endolysin_autolysin 2.02e-44 104 244 2 134
endolysin and autolysin. The dsDNA phages of eubacteria use endolysins or muralytic enzymes in conjunction with hollin, a small membrane protein, to degrade the peptidoglycan found in bacterial cell walls. Similarly, bacteria produce autolysins to facilitate the biosynthesis of its cell wall heteropolymer peptidoglycan and cell division. Endolysins and autolysins are found in viruses and bacteria, respectively. Both endolysin and autolysin enzymes cleave the glycosidic beta 1,4-bonds between the N-acetylmuramic acid and the N-acetylglucosamine of the peptidoglycan.
381620 lyz_P1 4.42e-29 100 244 3 138
P1 lysozyme Lyz-like proteins. Enterobacteria phage P1 lysozyme Lyz is secreted to the Escherichia coli periplasm where it is membrane bound and inactive. Activation involves the release from the membrane, an intramolecular thiol-disulfide isomerization and extensive structural rearrangement of the N-terminal region. The dsDNA phages of eubacteria use endolysins or muralytic enzymes in conjunction with hollin, a small membrane protein, to degrade the peptidoglycan found in bacterial cell walls. Similarly, bacteria produce autolysins to facilitate the biosynthesis of its cell wall heteropolymer peptidoglycan and cell division. Endolysins and autolysins are found in viruses and bacteria, respectively. Both endolysin and autolysin enzymes cleave the glycosidic beta 1,4-bonds between the N-acetylmuramic acid and the N-acetylglucosamine of the peptidoglycan.
226295 RrrD 3.70e-24 104 248 12 150
Phage-related lysozyme (muramidase), GH24 family [Cell wall/membrane/envelope biogenesis].
381619 endolysin_R21-like 4.95e-21 101 244 6 140
endolysin R21-like proteins. Unlike T4 E phage lysozyme, the endolysin R21 from Enterobacteria phage P21 has an N-terminal SAR (signal-arrest-release) domain that anchors the endolysin to the membrane in an inactive form, which act to prevent premature lysis of the infected bacterium. The dsDNA phages of eubacteria use endolysins or muralytic enzymes in conjunction with hollin, a small membrane protein, to degrade the peptidoglycan found in bacterial cell walls. Similarly, bacteria produce autolysins to facilitate the biosynthesis of its cell wall heteropolymer peptidoglycan and cell division. Endolysins and autolysins are found in viruses and bacteria, respectively. Both endolysin and autolysin enzymes cleave the glycosidic beta 1,4-bonds between the N-acetylmuramic acid and the N-acetylglucosamine of the peptidoglycan.
411609 sporang_Gsm 3.24e-12 29 128 4 101
sporangiospore maturation cell wall hydrolase GsmA. The peptidoglycan-hydrolyzing enzyme GsmA occurs in some sporangia-forming members of the Actinobacteria, such as Actinoplanes missouriensis, and is required for proper separation of spores. GsmA proteins have one or two SH3 domains N-terminal to the hydrolase domain.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
4.93e-167 1 258 1 258
4.93e-167 1 258 1 258
2.01e-166 1 258 1 258
4.05e-166 1 258 1 258
1.35e-109 12 258 12 261

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
9.60e-11 104 244 57 192
Chain A, Lysozyme [Acinetobacter baumannii]
1.19e-07 98 248 5 149
Chain A, Lysozyme [Asticcacaulis excentricus],6H9D_B Chain B, Lysozyme [Asticcacaulis excentricus],6H9D_C Chain C, Lysozyme [Asticcacaulis excentricus]
9.23e-07 104 244 14 152
Chain A, Endolysin [Escherichia coli O157 typing phage 15],7M5I_B Chain B, Endolysin [Escherichia coli O157 typing phage 15]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
2.61e-11 102 244 6 141
Endolysin OS=Bacillus phage B103 OX=10778 GN=15 PE=3 SV=1
1.89e-09 102 244 6 141
Endolysin OS=Bacillus phage PZA OX=10757 GN=15 PE=3 SV=1
2.57e-09 102 244 6 141
Endolysin OS=Bacillus phage phi29 OX=10756 GN=15 PE=1 SV=1
9.85e-06 104 248 8 139
Endolysin OS=Lactococcus phage c2 OX=31537 GN=L3 PE=3 SV=1
9.85e-06 104 248 8 139
Endolysin OS=Lactococcus phage phivML3 OX=10746 GN=L3 PE=3 SV=1

SignalP and Lipop Annotations help

This protein is predicted as SP

Other SP_Sec_SPI CS Position
0.000258 0.999707 CS pos: 18-19. Pr: 0.6579

TMHMM  Annotations      help

There is no transmembrane helices in FOMG_15065-t38_1-p1.