CAZyme Information: ASPVEDRAFT_137695-t33_1-p1

Basic Information

• Species: Aspergillus versicolor
• Lineage: Ascomycota; Eurotiomycetes; ; Aspergillaceae; Aspergillus; Aspergillus versicolor
• CAZyme ID: ASPVEDRAFT_137695-t33_1-p1
• CAZy Family: AA9
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
232		25116.05	4.4607

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_AversicolorCBS583.65	13364	1036611	142	13222

• Gene Location: location=KV878132:832118-832873(+)

Full Sequence      

MRITSWWLLSALASLASSTSLPVNGTRGIDLFEIHLPVNWKNAVADGVEFVFVKATEGTN
YKNLRYPSQTENAAPGVFHGAIHFASAASSSGADQAKFFLNNGGNWTADGETLPGVLEME
GNIAGKLCHGMEADEITDWMADFSNTYKQATGRPPLLFLSAKWWGQCAGNDTSFAAEHPL
WLANWADEMGALPVGWKEATFWQYAAMSGNGGEGDVFLGSRDELTRFALGEL

Enzyme Prediction     

EC	3.2.1.17:4

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH25	35	206	9e-41	0.9209039548022598

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
119374	GH25_CH-type	5.85e-85	26	224	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	1.77e-35	38	204	10	171	Glycosyl hydrolases family 25.
119373	GH25_muramidase	1.88e-33	27	216	1	181	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	2.64e-23	27	216	1	189	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	4.27e-14	26	206	3	173	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
BCS17651.1|GH25	1.98e-145	1	230	1	235
EAA58427.1|GH25	4.67e-102	4	211	5	223
QNJ46237.1|GH25|3.2.1.17	1.32e-62	27	228	20	222
AOU80705.1|GH25	1.70e-60	11	228	18	244
AJE86402.1|GH25	1.70e-60	11	228	18	244

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6ZM8_A	8.44e-53	28	231	4	208	Chain A, muramidase [Sodiomyces alcalophilus]
1JFX_A	8.88e-52	24	216	3	197	Crystal structure of the bacterial lysozyme from Streptomyces coelicolor at 1.65 A resolution [Streptomyces coelicolor]
6ZMV_A	7.47e-51	28	230	4	206	Chain A, muramidase [Trichobolus zukalii],6ZMV_B Chain B, muramidase [Trichobolus zukalii]
2X8R_A	5.94e-48	27	230	5	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]
4KRU_A	5.26e-08	27	205	21	190	X-ray structure of catalytic domain of endolysin from clostridium perfringens phage phiSM101 [Clostridium phage phiSM101]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|P25310|LYSM1_STRGL	4.06e-50	24	216	80	274	Lysozyme M1 OS=Streptomyces globisporus OX=1908 GN=acm PE=1 SV=1
sp|D4ANU4|LYS_ARTBC	3.96e-48	10	230	14	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	4.01e-45	27	230	3	211	N,O-diacetylmuramidase OS=Chalaropsis sp. OX=36534 PE=1 SV=1

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	CS Position
0.000405	0.999577	CS pos: 18-19. Pr: 0.9188

TMHMM  Annotations     

There is no transmembrane helices in ASPVEDRAFT_137695-t33_1-p1.