CAZyme Information: KAG2010469.1

Basic Information

• Species: Coprinopsis cinerea
• Lineage: Basidiomycota; Agaricomycetes; ; Psathyrellaceae; Coprinopsis; Coprinopsis cinerea
• CAZyme ID: KAG2010469.1
• CAZy Family: GH131
• CAZyme Description: lysozyme

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
271		28332.17	8.2050

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_Ccinerea326	15250	N/A	238	15012

• Gene Location: location=JAAGWA010000007:2338366-2339242(+)

Full Sequence      

MKPTLLSTLIALALTTSVMGAINDACSVNGTPGVCLSTTTCSNGGGTSTAGYCPNDPSNV
RCCTKKCGSGGTCRFESTCSTGNTATGLCPGPSNFKCCLPASGGGGNCTPKAINKKTLDL
LKEFEGWAASPYKDVAGYPTVGYGHKCSKNDCSELGYKFPMTKAQGEELLAKDVKGFEKC
ISDYINDTIKLNDNQYGALVSWSFNVGCGAAKDSTLISRLNKGDSPNTVAGEELPRWNKA
GGKVVDGLTNRRKKEVELFKTSSTVIAHPPC

Enzyme Prediction     

No EC number prediction in KAG2010469.1.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH24	113	255	5.8e-42	0.9927007299270073

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
381599	lyz_endolysin_autolysin	4.41e-61	118	259	2	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.
381620	lyz_P1	6.04e-36	112	258	1	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	1.33e-35	120	258	11	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.
226295	RrrD	9.75e-32	118	262	12	150	Phage-related lysozyme (muramidase), GH24 family [Cell wall/membrane/envelope biogenesis].
395766	Phage_lysozyme	7.51e-19	138	253	1	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
QDS76536.1|GH24	4.99e-70	25	270	22	266
UKZ52746.1|GH24	2.09e-60	111	271	105	265
UKZ78548.1|GH24	2.09e-60	111	271	105	265
QYS99898.1|GH24	2.15e-60	111	271	106	266
BCS23042.1|GH24	1.72e-56	113	269	28	184

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6ET6_A	1.55e-21	111	259	50	193	Chain A, Lysozyme [Acinetobacter baumannii]
7M5I_A	3.62e-20	113	262	9	156	Chain A, Endolysin [Escherichia coli O157 typing phage 15],7M5I_B Chain B, Endolysin [Escherichia coli O157 typing phage 15]
3HDF_A	8.92e-17	125	258	10	134	Chain A, Lysozyme [Enterobacteria phage P21],3HDF_B Chain B, Lysozyme [Enterobacteria phage P21]
3HDE_A	1.60e-16	125	258	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]
4ZPU_A	3.82e-16	125	258	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	5.21e-24	113	263	3	146	Endolysin OS=Bacillus phage PZA OX=10757 GN=15 PE=3 SV=1
sp|P11187|ENLYS_BPPH2	1.96e-23	113	263	3	146	Endolysin OS=Bacillus phage phi29 OX=10756 GN=15 PE=1 SV=1
sp|Q37896|ENLYS_BPB03	8.15e-21	113	264	3	147	Endolysin OS=Bacillus phage B103 OX=10778 GN=15 PE=3 SV=1
sp|P78285|LYSD_ECOLI	1.58e-15	125	258	35	159	Lysozyme RrrD OS=Escherichia coli (strain K12) OX=83333 GN=rrrD PE=1 SV=1
sp|D4ATA2|A7466_ARTBC	1.92e-15	22	91	22	93	Uncharacterized secreted protein ARB_07466 OS=Arthroderma benhamiae (strain ATCC MYA-4681 / CBS 112371) OX=663331 GN=ARB_07466 PE=1 SV=1

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	CS Position
0.000198	0.999755	CS pos: 20-21. Pr: 0.9759

TMHMM  Annotations     

There is no transmembrane helices in KAG2010469.1.