CAZyme Information: KAG2010431.1

Basic Information

• Species: Coprinopsis cinerea
• Lineage: Basidiomycota; Agaricomycetes; ; Psathyrellaceae; Coprinopsis; Coprinopsis cinerea
• CAZyme ID: KAG2010431.1
• CAZy Family: GH13
• CAZyme Description: lysozyme

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
268	JAAGWA010000007|CGC1	28248.27	8.3084

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=JAAGWA010000007:2267568-2268441(+)

Full Sequence      

MKPIALLSTIVFALTVSVQGAINDPCSVNGTPGICITTTACANAGGTNAVGFCPNDPANV
RCCTKKCSTNGTCRFTNTCSSGNVLVGLCPGPSNFRCCIPSSSCAYSPVNSRTVQEIKNS
EGFVRSPAPDPIGLPTVGYGHLCKNKGCSEVPYSFPLTEAQATSLLMTDLKTFQKCISDQ
INDSIRLNENQYGALVSWAFNVGCGNTASSALISRLNKGESPNKVAEEELPRWKYAGGQV
LPGLVARRNREIALFKTASSVVGHPPRC

Enzyme Prediction     

No EC number prediction in KAG2010431.1.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH24	110	251	4.8e-38	0.9854014598540146

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
381599	lyz_endolysin_autolysin	1.98e-51	117	255	5	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	3.68e-33	109	254	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.
226295	RrrD	6.38e-31	117	255	15	147	Phage-related lysozyme (muramidase), GH24 family [Cell wall/membrane/envelope biogenesis].
381619	endolysin_R21-like	2.41e-24	113	254	8	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.
395766	Phage_lysozyme	4.95e-14	135	248	2	106	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	8.58e-65	1	268	1	268
QBZ63741.1|GH24	1.27e-62	6	267	2	355
UKZ52746.1|GH24	1.67e-61	101	265	98	263
UKZ78548.1|GH24	1.67e-61	101	265	98	263
QYS99898.1|GH24	1.72e-61	109	265	108	264

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
3HDF_A	4.43e-16	121	255	10	137	Chain A, Lysozyme [Enterobacteria phage P21],3HDF_B Chain B, Lysozyme [Enterobacteria phage P21]
3HDE_A	7.85e-16	121	255	35	162	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	1.87e-15	121	255	35	162	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]
6ET6_A	5.40e-15	117	255	60	193	Chain A, Lysozyme [Acinetobacter baumannii]
2ANV_A	1.84e-13	109	255	4	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|D4ATA2|A7466_ARTBC	1.92e-24	1	103	1	105	Uncharacterized secreted protein ARB_07466 OS=Arthroderma benhamiae (strain ATCC MYA-4681 / CBS 112371) OX=663331 GN=ARB_07466 PE=1 SV=1
sp|P07540|ENLYS_BPPZA	3.22e-16	136	259	32	146	Endolysin OS=Bacillus phage PZA OX=10757 GN=15 PE=3 SV=1
sp|P11187|ENLYS_BPPH2	1.16e-15	136	259	32	146	Endolysin OS=Bacillus phage phi29 OX=10756 GN=15 PE=1 SV=1
sp|O80292|ENLYS_BPPS1	1.58e-15	121	251	37	158	SAR-endolysin OS=Bacteriophage PS119 OX=83128 GN=19 PE=3 SV=1
sp|P78285|LYSD_ECOLI	7.77e-15	121	255	35	162	Lysozyme RrrD OS=Escherichia coli (strain K12) OX=83333 GN=rrrD PE=1 SV=1

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	CS Position
0.000215	0.999751	CS pos: 20-21. Pr: 0.9793

TMHMM  Annotations     

There is no transmembrane helices in KAG2010431.1.