CAZyme Information: EAW16242.1

Basic Information

• Species: Aspergillus fischeri
• Lineage: Ascomycota; Eurotiomycetes; ; Aspergillaceae; Aspergillus; Aspergillus fischeri
• CAZyme ID: EAW16242.1
• CAZy Family: AA5
• CAZyme Description: N,O-diacetyl muramidase, putative

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
227	DS027698|CGC3	24540.18	6.0593

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_AfischeriNRRL181	10668	331117	278	10390

• Gene Location: location=DS027698:2609809-2610546(-)

Full Sequence      

MMLDLKQVAAVLLASASLAQATVQGFDISHYQANVNFAAAYNSGARFVMIKATESTTYTD
PAFSSHYTGATNAGFIRGGYHFAIPNDSSGAAQAKYFLAHGGGWSNDGITLPGMLDIEYN
PYGATCYGLSASQMVSWISDFVNTYKSSTGRYPMIYTTADWWNTCTGNSKSFTECPLVLA
RYSSSVGTIPGGWPYQSFWQNSDSYTYGGDSDIWNGSLNNLKTFAKG

Enzyme Prediction     

EC	3.2.1.17:41

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH25	27	209	1.8e-49	0.9830508474576272

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
119374	GH25_CH-type	6.75e-119	23	221	1	199	CH-type (Chalaropsis-type) lysozymes represent one of four functionally-defined classes of peptidoglycan hydrolases (also referred to as endo-N-acetylmuramidases) that cleave bacterial cell wall peptidoglycans. CH-type lysozymes exhibit both lysozyme (acetylmuramidase) and diacetylmuramidase activity. The first member of this family to be described was a muramidase from the fungus Chalaropsis. However, a majority of the CH-type lysozymes are found in bacteriophages and Gram-positive bacteria such as Streptomyces and Clostridium. CH-type lysozymes have a single glycosyl hydrolase family 25 (GH25) domain with an unusual beta/alpha-barrel fold in which the last strand of the barrel is antiparallel to strands beta7 and beta1. Most CH-type lysozymes appear to lack the cell wall-binding domain found in other GH25 muramidases.
395941	Glyco_hydro_25	3.08e-53	27	210	2	180	Glycosyl hydrolases family 25.
119373	GH25_muramidase	4.59e-48	24	209	1	176	Endo-N-acetylmuramidases (muramidases) are lysozymes (also referred to as peptidoglycan hydrolases) that degrade bacterial cell walls by catalyzing the hydrolysis of 1,4-beta-linkages between N-acetylmuramic acid and N-acetyl-D-glucosamine residues. This family of muramidases contains a glycosyl hydrolase family 25 (GH25) catalytic domain and is found in bacteria, fungi, slime molds, round worms, protozoans and bacteriophages. The bacteriophage members are referred to as endolysins which are involved in lysing the host cell at the end of the replication cycle to allow release of mature phage particles. Endolysins are typically modular enzymes consisting of a catalytically active domain that hydrolyzes the peptidoglycan cell wall and a cell wall-binding domain that anchors the protein to the cell wall. Endolysins generally have narrow substrate specificities with either intra-species or intra-genus bacteriolytic activity.
119384	GH25_YegX-like	3.15e-38	25	216	2	194	YegX is an uncharacterized bacterial protein with a glycosyl hydrolase family 25 (GH25) catalytic domain that is similar in sequence to the CH-type (Chalaropsis-type) lysozymes of the GH25 family of endolysins.
119375	GH25_muramidase_1	2.38e-31	22	213	2	186	Uncharacterized bacterial muramidase containing a glycosyl hydrolase family 25 (GH25) catalytic domain. Endo-N-acetylmuramidases are lysozymes (also referred to as peptidoglycan hydrolases) that degrade bacterial cell walls by catalyzing the hydrolysis of 1,4-beta-linkages between N-acetylmuramic acid and N-acetyl-D-glucosamine residues.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QNJ46238.1|GH25|3.2.1.17	1.79e-123	22	227	27	233
QGA14842.1|GH25	6.54e-120	18	227	17	227
QNJ46228.1|GH25|3.2.1.17	8.07e-120	23	227	27	232
CAP86879.1|GH25	3.36e-117	16	226	11	222
QNJ46251.1|GH25|3.2.1.17	8.06e-117	23	227	25	230

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6ZMV_A	1.54e-105	23	227	2	206	Chain A, muramidase [Trichobolus zukalii],6ZMV_B Chain B, muramidase [Trichobolus zukalii]
2X8R_A	5.41e-102	22	227	3	210	The structure of a family GH25 lysozyme from Aspergillus fumigatus [Aspergillus fumigatus Af293],2X8R_B The structure of a family GH25 lysozyme from Aspergillus fumigatus [Aspergillus fumigatus Af293],2X8R_C The structure of a family GH25 lysozyme from Aspergillus fumigatus [Aspergillus fumigatus Af293],2X8R_D The structure of a family GH25 lysozyme from Aspergillus fumigatus [Aspergillus fumigatus Af293],2X8R_E The structure of a family GH25 lysozyme from Aspergillus fumigatus [Aspergillus fumigatus Af293],2X8R_F The structure of a family GH25 lysozyme from Aspergillus fumigatus [Aspergillus fumigatus Af293]
6ZM8_A	1.66e-93	23	227	2	207	Chain A, muramidase [Sodiomyces alcalophilus]
1JFX_A	5.40e-70	23	225	5	213	Crystal structure of the bacterial lysozyme from Streptomyces coelicolor at 1.65 A resolution [Streptomyces coelicolor]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|D4ANU4|LYS_ARTBC	2.52e-98	22	227	29	234	N,O-diacetylmuramidase OS=Arthroderma benhamiae (strain ATCC MYA-4681 / CBS 112371) OX=663331 GN=ARB_05911 PE=1 SV=1
sp|P00721|LYS_CHASP	1.05e-96	22	227	1	211	N,O-diacetylmuramidase OS=Chalaropsis sp. OX=36534 PE=1 SV=1
sp|P25310|LYSM1_STRGL	3.04e-68	23	225	82	290	Lysozyme M1 OS=Streptomyces globisporus OX=1908 GN=acm PE=1 SV=1
sp|P34020|LYS_CLOAB	7.19e-12	23	211	1	172	Autolytic lysozyme OS=Clostridium acetobutylicum (strain ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787) OX=272562 GN=lyc PE=1 SV=1

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	CS Position
0.000254	0.999709	CS pos: 21-22. Pr: 0.9720

TMHMM  Annotations     

There is no transmembrane helices in EAW16242.1.