CAZyme Information: OJD23799.1

Basic Information

• Species: Blastomyces percursus
• Lineage: Ascomycota; Eurotiomycetes; ; Ajellomycetaceae; Blastomyces; Blastomyces percursus
• CAZyme ID: OJD23799.1
• CAZy Family: GH47
• CAZyme Description: N,O-diacetylmuramidase [Source:UniProtKB/TrEMBL;Acc:A0A1J9R5M9]

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
187		20352.90	9.9268

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_BpercursusEI222	10384	N/A	99	10285

• Gene Location: location=LGTZ01000704:1065-1671(-)

Full Sequence      

MSTTTIPAPPNIFVLINQTNNTRPSAATTQAPQRLALSVAATTSRTRALRRGTGPLFPRL
RGGWSGDSITLPGMLDLETSLNGHQCHGLSTSAMVSWIRDFVNTYKNKTGRYPMIYTSPS
WWQSCTGDSRVFASTCSLVMTRWAKSPGTAPGGLTHTIWQHTDEYEFGGNGDLFNGNEEG
LRKLATG

Enzyme Prediction     

EC	3.2.1.17:41

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH25	68	169	8.8e-20	0.536723163841808

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
119374	GH25_CH-type	3.90e-52	62	181	80	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.
119373	GH25_muramidase	5.96e-20	71	177	84	184	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.
395941	Glyco_hydro_25	1.32e-19	62	169	78	179	Glycosyl hydrolases family 25.
119384	GH25_YegX-like	8.95e-09	65	176	86	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.
119376	GH25_LytC-like	5.83e-05	69	164	88	175	The LytC lysozyme of Streptococcus pneumoniae is a bacterial cell wall hydrolase that cleaves the beta1-4-glycosydic bond located between the N-acetylmuramoyl-N-glucosaminyl residues of the cell wall polysaccharide chains. LytC is composed of a C-terminal glycosyl hydrolase family 25 (GH25) domain and an N-terminal choline-binding module (CBM) consisting of eleven homologous repeats that specifically recognizes the choline residues of pneumococcal lipoteichoic and teichoic acids. This domain arrangement is the reverse of the major pneumococcal autolysin, LytA, and the CPL-1-like lytic enzymes of the pneumococcal bacteriophages, in which the CBM (consisting of six repeats) is at the C-terminus. This model represents the C-terminal catalytic domain of the LytC-like enzymes.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QNJ46251.1|GH25|3.2.1.17	1.15e-55	62	187	104	230
QNJ46229.1|GH25|3.2.1.17	2.16e-54	62	187	109	235
QNJ46238.1|GH25|3.2.1.17	3.76e-52	62	187	107	233
QNJ46234.1|GH25|3.2.1.17	3.29e-51	62	187	98	224
QNJ46245.1|GH25|3.2.1.17	7.42e-51	62	187	102	228

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6ZMV_A	6.07e-46	62	187	81	206	Chain A, muramidase [Trichobolus zukalii],6ZMV_B Chain B, muramidase [Trichobolus zukalii]
6ZM8_A	9.15e-43	62	187	81	207	Chain A, muramidase [Sodiomyces alcalophilus]
2X8R_A	1.10e-41	62	187	83	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]
1JFX_A	5.98e-27	62	186	84	214	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	4.59e-51	62	187	108	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	8.74e-46	62	187	84	211	N,O-diacetylmuramidase OS=Chalaropsis sp. OX=36534 PE=1 SV=1
sp|P25310|LYSM1_STRGL	1.48e-25	62	186	161	291	Lysozyme M1 OS=Streptomyces globisporus OX=1908 GN=acm PE=1 SV=1

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
1.000054	0.000000

TMHMM  Annotations     

There is no transmembrane helices in OJD23799.1.