CAZyme Information: FUN_010028-T1-p1

Basic Information

• Species: Rhizophagus irregularis
• Lineage: Mucoromycota; Glomeromycetes; ; Glomeraceae; Rhizophagus; Rhizophagus irregularis
• CAZyme ID: FUN_010028-T1-p1
• CAZy Family: GH38
• CAZyme Description: Lysozyme [Source:UniProtKB/TrEMBL;Acc:A0A2N1MZB5]

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
151		16782.46	10.3771

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_RirregularisC2	25634	N/A	90	25544

• Gene Location: location=CP080888:5025252-5025852(-)

Full Sequence      

MAKKLSNEGLALIERFEGFSPNFYKDPVGIKTIGYGHACHVNDCSKIRPPISRAEGEALL
KKDLARFEKCVESLTRIKLNSNQFSALCSFTFNLGCGAYQQSTLRRKLNAGNTKGASLEF
RKWVYGGGKKLPGLVRRRKAERDLFCKSGGC

Enzyme Prediction     

No EC number prediction in FUN_010028-T1-p1.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH24	6	141	9.8e-49	0.9854014598540146

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
381599	lyz_endolysin_autolysin	8.40e-72	9	145	1	135	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	9.41e-48	5	148	7	150	Phage-related lysozyme (muramidase), GH24 family [Cell wall/membrane/envelope biogenesis].
381620	lyz_P1	1.43e-45	5	144	2	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	8.50e-43	11	146	10	142	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	6.86e-22	32	139	3	107	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
QYO62642.1|GH24	4.40e-44	4	145	251	389
QQE65348.1|GH24	3.16e-41	2	147	76	222
AJE16588.1|GH24	9.00e-41	3	146	2	145
QLS00473.1|GH24	9.00e-41	3	145	2	144
AVV37816.1|GH24	9.44e-41	4	145	2	139

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6ET6_A	3.22e-33	3	147	50	195	Chain A, Lysozyme [Acinetobacter baumannii]
3HDF_A	2.16e-24	7	144	6	134	Chain A, Lysozyme [Enterobacteria phage P21],3HDF_B Chain B, Lysozyme [Enterobacteria phage P21]
3HDE_A	4.11e-24	7	144	31	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]
4ZPU_A	1.05e-23	7	144	31	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]
2ANV_A	8.00e-23	4	145	3	144	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]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|Q9T1T5|ENLYS_BPAPS	2.70e-31	5	145	3	143	Endolysin OS=Acyrthosiphon pisum secondary endosymbiont phage 1 OX=2682836 GN=13 PE=3 SV=1
sp|Q37896|ENLYS_BPB03	1.85e-26	5	145	3	142	Endolysin OS=Bacillus phage B103 OX=10778 GN=15 PE=3 SV=1
sp|P11187|ENLYS_BPPH2	2.08e-23	4	145	2	142	Endolysin OS=Bacillus phage phi29 OX=10756 GN=15 PE=1 SV=1
sp|O80292|ENLYS_BPPS1	2.22e-23	7	144	33	161	SAR-endolysin OS=Bacteriophage PS119 OX=83128 GN=19 PE=3 SV=1
sp|P07540|ENLYS_BPPZA	4.10e-23	4	145	2	142	Endolysin OS=Bacillus phage PZA OX=10757 GN=15 PE=3 SV=1

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
1.000064	0.000000

TMHMM  Annotations     

There is no transmembrane helices in FUN_010028-T1-p1.