CAZyme Information: GLOIN_2v1425256-t44_1-p1

Basic Information

• Species: Rhizophagus irregularis
• Lineage: Mucoromycota; Glomeromycetes; ; Glomeraceae; Rhizophagus; Rhizophagus irregularis
• CAZyme ID: GLOIN_2v1425256-t44_1-p1
• CAZy Family: AA1
• CAZyme Description: glycoside hydrolase family 24 protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
105		11902.93	10.1827

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_RirregularisDAOM181602	26245	747089	102	26143

• Gene Location: location=AUPC02000462:29846-30233(+)

Full Sequence      

NKAGLKLIKKFEGFRSRFYVDKGIITIGYGHACHVYDCSKIHPPISRAKGEALLKKDLVV
FEKCVDSLTQIKLNSNQFSALVSFTYNLCCEAYRRSTLRRKLNAG

Enzyme Prediction     

No EC number prediction in GLOIN_2v1425256-t44_1-p1.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH24	2	105	2.1e-30	0.7591240875912408

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
381599	lyz_endolysin_autolysin	6.57e-42	4	105	1	101	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.
226295	RrrD	3.05e-26	3	105	10	112	Phage-related lysozyme (muramidase), GH24 family [Cell wall/membrane/envelope biogenesis].
381620	lyz_P1	5.75e-23	1	105	3	105	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	4.14e-20	3	105	7	107	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.
395766	Phage_lysozyme	1.59e-11	26	105	3	80	Phage lysozyme. This family includes lambda phage lysozyme and E. coli endolysin.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
BCL40994.1|GH24	1.34e-22	3	105	7	110
QYO62642.1|GH24	1.38e-21	1	103	253	353
QLS00473.1|GH24	2.16e-21	4	105	8	110
QDS76536.1|GH24	2.27e-21	1	105	112	219
AGF74814.1|GH24	4.05e-21	1	105	5	106

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6H9D_A	4.50e-15	1	105	7	108	Chain A, Lysozyme [Asticcacaulis excentricus],6H9D_B Chain B, Lysozyme [Asticcacaulis excentricus],6H9D_C Chain C, Lysozyme [Asticcacaulis excentricus]
6ET6_A	4.45e-13	4	105	56	159	Chain A, Lysozyme [Acinetobacter baumannii]
2ANV_A	7.23e-13	4	103	8	109	Chain A, Lysozyme [Lederbergvirus P22],2ANV_B Chain B, Lysozyme [Lederbergvirus P22],2ANX_A Chain A, Lysozyme [Lederbergvirus P22],2ANX_B Chain B, Lysozyme [Lederbergvirus P22]
7M5I_A	1.09e-10	1	105	10	115	Chain A, Endolysin [Escherichia coli O157 typing phage 15],7M5I_B Chain B, Endolysin [Escherichia coli O157 typing phage 15]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|Q37896|ENLYS_BPB03	1.29e-16	1	105	4	108	Endolysin OS=Bacillus phage B103 OX=10778 GN=15 PE=3 SV=1
sp|P09963|ENLYS_BPP22	1.88e-12	4	103	8	109	Endolysin OS=Salmonella phage P22 OX=10754 GN=19 PE=1 SV=1
sp|P07540|ENLYS_BPPZA	6.56e-12	1	105	4	108	Endolysin OS=Bacillus phage PZA OX=10757 GN=15 PE=3 SV=1
sp|P11187|ENLYS_BPPH2	6.56e-12	1	105	4	108	Endolysin OS=Bacillus phage phi29 OX=10756 GN=15 PE=1 SV=1
sp|Q9T1X2|ENLYS_BPMU	5.37e-06	23	105	49	127	SAR-endolysin OS=Escherichia phage Mu OX=10677 GN=lys PE=2 SV=1

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
1.000061	0.000000

TMHMM  Annotations     

There is no transmembrane helices in GLOIN_2v1425256-t44_1-p1.