CAZyme Information: MGYG000001740_00379

Basic Information

• Species: UMGS1519 sp900552585
• Lineage: Bacteria; Actinobacteriota; Coriobacteriia; Coriobacteriales; Eggerthellaceae; UMGS1519; UMGS1519 sp900552585
• CAZyme ID: MGYG000001740_00379
• CAZy Family: GH25
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
317	MGYG000001740_14|CGC1	34677.27	4.2606

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001740	1799344	MAG	Hungary	Europe

• Gene Location: Start: 6582; End: 7535 Strand: +

Full Sequence      

MATRRPTASHSANARRPIRLILLAVAIACVIALFANLGTSGCQGGNDNQPTAAEQAEYAG
KTLYQYNLDRGALALNDYDYSNLESYDGNKYYVKGSNVVSTMGIDVSESQNSINWSKVAA
SGIDFAMVRLGYRGYTEGKVQKDVNYATNIKEAKAAGLKVGVYFFSQATTEDEAREEAKY
VVDHLGSTQLDYPVVFDLETDVNDNARTKDLTSDEITAVALAFCQTIEDAGYTPMVYLNK
EAATHKFDLSQLQSYPLWYAEYNDTPTLGFDFAMWQYTENGTAFGVDGNVDLDLLFDESK
LAVKTSDGQDSSSSTAS

Enzyme Prediction     

No EC number prediction in MGYG000001740_00379.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH25	104	286	2.3e-50	0.9943502824858758

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd06414	GH25_LytC-like	9.90e-82	103	296	3	191	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.
cd00599	GH25_muramidase	1.21e-42	103	294	2	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.
pfam01183	Glyco_hydro_25	7.05e-32	104	286	1	180	Glycosyl hydrolases family 25.
cd06525	GH25_Lyc-like	2.19e-30	103	293	2	182	Lyc muramidase is an autolytic lysozyme (autolysin) from Clostridium acetobutylicum encoded by the lyc gene. Lyc has 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	2.35e-29	103	295	2	192	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QYX28904.1	3.75e-70	27	297	7	286
QRO38911.1	1.85e-67	27	297	7	286
QBF76167.1	1.85e-67	27	297	7	286
QHI72152.1	1.68e-63	75	297	67	289
ACV23383.1	3.30e-62	78	294	51	268

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
5A6S_A	3.84e-14	127	307	39	213	Crystalstructure of the CTP1L endolysin reveals how its activity is regulated by a secondary translation product [Clostridium phage phiCTP1]
1JFX_A	5.31e-10	103	291	7	198	Crystalstructure of the bacterial lysozyme from Streptomyces coelicolor at 1.65 A resolution [Streptomyces coelicolor]
5JIP_A	1.94e-06	92	292	5	219	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
P26836	4.01e-19	93	304	1	204	Probable autolytic lysozyme OS=Clostridium perfringens (strain 13 / Type A) OX=195102 GN=lyc PE=3 SV=2
P25310	5.99e-09	103	291	84	275	Lysozyme M1 OS=Streptomyces globisporus OX=1908 GN=acm PE=1 SV=1

SignalP and Lipop Annotations

This protein is predicted as LIPO

Other	SP_Sec_SPI	LIPO_Sec_SPII	TAT_Tat_SPI	TATLIP_Sec_SPII	PILIN_Sec_SPIII
0.135746	0.224959	0.638171	0.000251	0.000442	0.000421

TMHMM  Annotations     

start	end
20	39