CAZyme Information: FOZG_16833-t36_1-p1

Basic Information

• Species: Fusarium oxysporum
• Lineage: Ascomycota; Sordariomycetes; ; Nectriaceae; Fusarium; Fusarium oxysporum
• CAZyme ID: FOZG_16833-t36_1-p1
• CAZy Family: PL3
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
242	JH717912.1|CGC2	26767.69	10.5818

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_FoxysporumFo47	18556	660027	365	18191

• Gene Location: location=JH717912.1:95472-96357(-)

Full Sequence      

MRIHIFTVHFLAVASSTAFLITDKGVRCRSGPTTSHAIQRQFTKGTDVTITCQIEGTNIE
GNALWDKTTFGCYVSDYYVATGSSGYVTLKFRRVERPSRMRRLSISSPALRGSGPMICSE
VKYPVPLSVANGKKLLADDMKPASAGVRGLYHGHVEQQSKAQQKPVWRTHQLGINMGCGN
AESSTLIGRLNNGEDPNTVISQEIPHWVYASGQRLPGLVRRRNAEIELAQKPTRRRALPK
RC

Enzyme Prediction     

No EC number prediction in FOZG_16833-t36_1-p1.

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
381599	lyz_endolysin_autolysin	2.75e-18	121	228	35	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	2.76e-10	175	228	87	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.
381619	endolysin_R21-like	3.32e-10	133	228	53	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	1.14e-09	29	84	4	63	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.
411609	sporang_Gsm	1.36e-08	29	129	90	184	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
QKD62394.1|GH24	2.94e-176	1	242	1	242
QGJ01409.1|GH24	2.54e-107	1	242	1	258
QGI70519.1|GH24	2.54e-107	1	242	1	258
CCT75183.1|GH24	1.03e-106	1	242	1	258
QGI87874.1|GH24	2.07e-106	1	242	1	258

PDB Hits     

FOZG_16833-t36_1-p1 has no PDB hit.

Swiss-Prot Hits     

FOZG_16833-t36_1-p1 has no Swissprot hit.

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	CS Position
0.000265	0.999732	CS pos: 18-19. Pr: 0.9412

TMHMM  Annotations     

There is no transmembrane helices in FOZG_16833-t36_1-p1.