CAZyme Information: FOYG_15285-t42_1-p1

Basic Information

• Species: Fusarium oxysporum
• Lineage: Ascomycota; Sordariomycetes; ; Nectriaceae; Fusarium; Fusarium oxysporum
• CAZyme ID: FOYG_15285-t42_1-p1
• CAZy Family: GT22
• CAZyme Description: lysozyme

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
258		28340.29	9.2634

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_FoxysporumNRRL32931	17642	660029	362	17280

• Gene Location: location=JH717849.1:280736-281622(+)

Full Sequence      

MRIHIFTVHFLAIASSTAFLITDEGVRCRSGPTTSHAIQRQFTKGTDVTITCQIEGTNIE
GNALWDKTTFGCYLSDYYVATGSSGYVTSKCRSCRAPKSNAATVNLVASFEGFKPDVYND
PTGNPTVGYGHLCDAPQCSEVRYPVPLSVANGKKLLADDMKGFAVCISAMLNSKARLNRN
QYGALISWAFNMGCGNAESSTLIGRLNNWEDPNTVISQELPRWVYASGKRLPGLVRRRNA
EIELAQKPTRRRALPKRC

Enzyme Prediction     

No EC number prediction in FOYG_15285-t42_1-p1.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH24	101	241	1.1e-34	0.9781021897810219

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
381599	lyz_endolysin_autolysin	1.17e-48	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	8.57e-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	4.23e-27	104	248	12	150	Phage-related lysozyme (muramidase), GH24 family [Cell wall/membrane/envelope biogenesis].
381619	endolysin_R21-like	2.44e-24	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	5.94e-11	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     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QGJ01409.1|GH24	3.10e-170	1	258	1	258
QGI70519.1|GH24	3.10e-170	1	258	1	258
CCT75183.1|GH24	1.26e-169	1	258	1	258
QGI87874.1|GH24	2.55e-169	1	258	1	258
QKD62394.1|GH24	5.52e-114	1	258	1	242

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6ET6_A	3.72e-11	104	244	57	192	Chain A, Lysozyme [Acinetobacter baumannii]
3HDF_A	8.11e-09	111	244	10	134	Chain A, Lysozyme [Enterobacteria phage P21],3HDF_B Chain B, Lysozyme [Enterobacteria phage P21]
3HDE_A	1.26e-08	111	244	35	159	Chain A, Lysozyme [Enterobacteria phage P21],3HDE_B Chain B, Lysozyme [Enterobacteria phage P21],3HDE_C Chain C, Lysozyme [Enterobacteria phage P21],3HDE_D Chain D, Lysozyme [Enterobacteria phage P21]
6H9D_A	1.80e-08	98	248	5	149	Chain A, Lysozyme [Asticcacaulis excentricus],6H9D_B Chain B, Lysozyme [Asticcacaulis excentricus],6H9D_C Chain C, Lysozyme [Asticcacaulis excentricus]
4ZPU_A	2.75e-08	111	244	35	159	The structure of DLP12 endolysin exhibits likely active and inactive conformations. [Escherichia coli K-12],4ZPU_B The structure of DLP12 endolysin exhibits likely active and inactive conformations. [Escherichia coli K-12],4ZPU_C The structure of DLP12 endolysin exhibits likely active and inactive conformations. [Escherichia coli K-12],4ZPU_D The structure of DLP12 endolysin exhibits likely active and inactive conformations. [Escherichia coli K-12]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|P07540|ENLYS_BPPZA	2.22e-13	102	244	6	141	Endolysin OS=Bacillus phage PZA OX=10757 GN=15 PE=3 SV=1
sp|P11187|ENLYS_BPPH2	7.86e-13	102	244	6	141	Endolysin OS=Bacillus phage phi29 OX=10756 GN=15 PE=1 SV=1
sp|Q37896|ENLYS_BPB03	2.93e-12	102	244	6	141	Endolysin OS=Bacillus phage B103 OX=10778 GN=15 PE=3 SV=1
sp|O80288|ENLYS_BPPS3	1.39e-08	111	244	37	161	SAR-endolysin OS=Bacteriophage PS34 OX=83127 GN=19 PE=3 SV=1
sp|O80292|ENLYS_BPPS1	2.60e-08	111	244	37	161	SAR-endolysin OS=Bacteriophage PS119 OX=83128 GN=19 PE=3 SV=1

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	CS Position
0.000248	0.999755	CS pos: 18-19. Pr: 0.9495

TMHMM  Annotations     

There is no transmembrane helices in FOYG_15285-t42_1-p1.