CAZyme Information: MGYG000004516_00769

Basic Information

• Species: Sneathia amnii
• Lineage: Bacteria; Fusobacteriota; Fusobacteriia; Fusobacteriales; Leptotrichiaceae; Sneathia; Sneathia amnii
• CAZyme ID: MGYG000004516_00769
• CAZy Family: GH25
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
234		27900.29	9.572

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000004516	1228854	MAG	Israel	Asia

• Gene Location: Start: 24453; End: 25157 Strand: +

Full Sequence      

MKKFIVFLVIINIMLIMANLEFSGVLYHNDLRASNYPIHGIDISHHQIRINWTKVDKNYK
FVLMKATEGKDFMDTDFLYNWNKAQLNGFKVGAYHFFSMLSSGRDQALYYMSKVPIVSDS
FPPIIDVEISRKYDKDRVIAELKEMIDLLEEKYNKRVIIYTDYKSYNNFLKGELEDNPLW
IRDIKNYPKIKESKRWIIWQYSNRGRVDGIDGFTDKNVLRYNDMNLYINKIQAK

Enzyme Prediction     

No EC number prediction in MGYG000004516_00769.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH25	41	210	1.2e-44	0.9943502824858758

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd06413	GH25_muramidase_1	3.44e-86	36	219	1	189	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.
cd06524	GH25_YegX-like	8.31e-51	39	220	1	193	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.
cd00599	GH25_muramidase	3.73e-45	39	218	1	185	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.
COG3757	Acm	3.43e-41	22	220	44	254	Lyzozyme M1 (1,4-beta-N-acetylmuramidase), GH25 family [Cell wall/membrane/envelope biogenesis].
pfam01183	Glyco_hydro_25	2.66e-38	41	210	1	180	Glycosyl hydrolases family 25.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
AKC95719.1	5.27e-172	1	234	1	234
BBM36160.1	1.64e-97	3	234	6	235
ALA95773.1	1.82e-96	1	220	1	223
ACZ00521.1	1.95e-93	20	230	21	228
AVL43061.1	1.95e-93	20	230	21	228

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
2WAG_A	9.03e-44	36	223	14	210	TheStructure of a family 25 Glycosyl hydrolase from Bacillus anthracis. [Bacillus anthracis str. Ames]
4KRU_A	5.14e-17	40	217	22	205	X-raystructure of catalytic domain of endolysin from clostridium perfringens phage phiSM101 [Clostridium phage phiSM101]
4KRT_A	2.15e-16	40	217	22	205	X-raystructure of endolysin from clostridium perfringens phage phiSM101 [Clostridium phage phiSM101],4KRT_B X-ray structure of endolysin from clostridium perfringens phage phiSM101 [Clostridium phage phiSM101]
1JFX_A	7.99e-16	38	217	5	200	Crystalstructure of the bacterial lysozyme from Streptomyces coelicolor at 1.65 A resolution [Streptomyces coelicolor]
5JIP_A	3.90e-12	40	217	16	220	Crystalstructure of the Clostridium perfringens spore cortex lytic enzyme SleM [Clostridium perfringens],5JIP_B Crystal structure of the Clostridium perfringens spore cortex lytic enzyme SleM [Clostridium perfringens]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
Q8FFY2	6.90e-32	34	218	63	253	Uncharacterized protein YegX OS=Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC) OX=199310 GN=yegX PE=3 SV=2
P76421	1.36e-31	34	218	63	253	Uncharacterized protein YegX OS=Escherichia coli (strain K12) OX=83333 GN=yegX PE=3 SV=2
Q8X7H0	3.76e-31	34	218	63	253	Uncharacterized protein YegX OS=Escherichia coli O157:H7 OX=83334 GN=yegX PE=3 SV=2
P26836	3.84e-19	32	217	4	194	Probable autolytic lysozyme OS=Clostridium perfringens (strain 13 / Type A) OX=195102 GN=lyc PE=3 SV=2
P25310	6.52e-15	33	217	77	277	Lysozyme M1 OS=Streptomyces globisporus OX=1908 GN=acm PE=1 SV=1

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	LIPO_Sec_SPII	TAT_Tat_SPI	TATLIP_Sec_SPII	PILIN_Sec_SPIII
0.067584	0.927319	0.004179	0.000285	0.000276	0.000312

TMHMM  Annotations     

start	end
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