CAZyme Information: MGYG000002480_01714

Basic Information

• Species: Adlercreutzia celatus_A
• Lineage: Bacteria; Actinobacteriota; Coriobacteriia; Coriobacteriales; Eggerthellaceae; Adlercreutzia; Adlercreutzia celatus_A
• CAZyme ID: MGYG000002480_01714
• CAZy Family: GH25
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
289	MGYG000002480_22|CGC1	31217.74	4.1574

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000002480	2680191	Isolate	Canada	North America

• Gene Location: Start: 16810; End: 17679 Strand: -

Full Sequence      

MILNGRNIDGLRAPRIATLTRRRFVAGAACAVACAAAGLLVGCGSASRSAEVAAIEPYVS
PYDWSGLVRDGEKLSYYENDALCSRWGIDVSEHQGNDIDWAAVADAGVQFAFARIGNRGA
TEGALSADEFFFQNAVRAGEVGIQVSAYFFSQALTEDEAREEAQFALDNLRETEASGATF
AYVAYDHEPVEIEGARANNLSSEQLTANARAFCEVIAAAGYAPMLYGNQRDLLRLAPELR
AAYPVWLAEYDVEAPTAPLDFAIWQYTNAGTVPGIPTDVDLNVWLEPQK

Enzyme Prediction     

No EC number prediction in MGYG000002480_01714.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH25	88	275	2.1e-39	0.9943502824858758

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd06414	GH25_LytC-like	1.05e-62	85	284	1	190	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	5.45e-34	86	284	1	186	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	9.94e-30	88	275	1	180	Glycosyl hydrolases family 25.
cd06413	GH25_muramidase_1	1.00e-29	87	283	5	188	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	5.10e-29	87	283	2	191	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
BCA89803.1	8.17e-208	1	289	1	289
BCS58359.1	9.15e-205	1	289	1	289
BAN78104.1	6.83e-179	32	289	1	258
ACV56468.1	1.08e-77	38	289	22	266
APO31195.1	1.08e-77	38	289	22	266

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1JFX_A	3.56e-11	87	282	7	200	Crystalstructure of the bacterial lysozyme from Streptomyces coelicolor at 1.65 A resolution [Streptomyces coelicolor]
5A6S_A	4.07e-08	120	282	51	199	Crystalstructure of the CTP1L endolysin reveals how its activity is regulated by a secondary translation product [Clostridium phage phiCTP1]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P25310	4.22e-10	87	282	84	277	Lysozyme M1 OS=Streptomyces globisporus OX=1908 GN=acm PE=1 SV=1
P34020	8.45e-06	87	286	3	182	Autolytic lysozyme OS=Clostridium acetobutylicum (strain ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787) OX=272562 GN=lyc PE=1 SV=1

SignalP and Lipop Annotations

This protein is predicted as TATLIPO

Other	SP_Sec_SPI	LIPO_Sec_SPII	TAT_Tat_SPI	TATLIP_Sec_SPII	PILIN_Sec_SPIII
0.000000	0.000002	0.000013	0.002687	0.997304	0.000000

TMHMM  Annotations     

start	end
24	46