CAZyme Information: MGYG000003782.1_01340

Basic Information

• Lineage: Bacteria; Firmicutes_A; Clostridia; Tissierellales; Peptoniphilaceae; Anaerococcus
• CAZyme ID: MGYG000003782.1_01340
• CAZy Family: GH25
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
382		44438.66	4.5294

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000003782.1	1597372	MAG	Canada	North America

• Gene Location: Start: 94; End: 1242 Strand: +

Full Sequence      

MFEIYLYDIIYLTKETERGYIKINKKLVGSALIFTLLLSDIAYASEVVMYDDYDIDIIFE
DEQGPKENTDNGNYGNQNSNTEKPEDNKDEEIVVSEEEVEEIIEELNPEVQDSLDESDIY
PKVSVYEKVVDMSEYQNPKNIDYDKLANSIDGAILRTSIRQKDKSLSKDKKIETHYAELN
SRDIPLGFYHYSRAINENEAIEEANYVLDIVRNKKVSLPIYIDIEDNDRQAKASKKEITA
VADAFTKAIRRNGYVAGIYSYPWFANEYLTKEVRNENEFWIAEWKKDAPYPKYKDSHYDS
WQYSSKGGVYGYKGDLDKNILYRDYPLIMTGVSSKGFVKVAEEVIAGKWGNGNIRRKRLE
YAGYDYLVIQEEVNRLLKSRRI

Enzyme Prediction     

No EC number prediction in MGYG000003782.1_01340.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH25	130	311	3.8e-40	0.9887005649717514

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd06414	GH25_LytC-like	1.51e-45	128	322	2	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	1.66e-25	128	320	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.
pfam01183	Glyco_hydro_25	3.24e-20	130	311	1	179	Glycosyl hydrolases family 25.
cd06525	GH25_Lyc-like	3.63e-19	128	319	1	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.
COG3757	Acm	1.00e-17	128	319	64	251	Lyzozyme M1 (1,4-beta-N-acetylmuramidase), GH25 family [Cell wall/membrane/envelope biogenesis].

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
ACV28608.1	2.65e-228	22	382	2	364
ARP49604.1	1.02e-51	128	379	4	267
QDS38460.1	2.02e-51	128	379	4	267
ASD51116.1	2.02e-51	128	379	4	267
AMC93674.1	3.99e-51	128	379	4	267

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
2WW5_A	1.80e-12	128	322	270	468	3D-structureof the modular autolysin LytC from Streptococcus pneumoniae at 1.6 A resolution [Streptococcus pneumoniae R6],2WWD_A 3D-structure of the modular autolysin LytC from Streptococcus pneumoniae in complex with pneummococcal peptidoglycan fragment [Streptococcus pneumoniae R6]
4FF5_A	1.86e-12	129	321	54	249	Structurebasis of a novel virulence factor GHIP a glycosyl hydrolase 25 of Streptococcus pneumoniae participating in host cell invasion [Streptococcus pneumoniae]
2WWC_A	4.26e-12	128	322	270	468	3D-structureof the modular autolysin LytC from Streptococcus pneumoniae in complex with synthetic peptidoglycan ligand [Streptococcus pneumoniae R6]
4CVD_A	1.25e-06	340	382	4	46	ChainA, LYSOZYME [Streptococcus phage CP-7]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P19385	5.69e-13	181	376	51	244	Lysozyme OS=Streptococcus phage Cp-7 OX=10748 GN=CPL7 PE=1 SV=2

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
0.178990	0.816503	0.003737	0.000273	0.000231	0.000257

TMHMM  Annotations     

There is no transmembrane helices in MGYG000003782.1_01340.