dbCAN-seq: a database of CAZyme sequence and annotation

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CAZyme Information: MGYG000002040_01634

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Basic Information help

Species

Faecalibacterium sp900758465

Lineage

Bacteria; Firmicutes_A; Clostridia; Oscillospirales; Ruminococcaceae; Faecalibacterium; Faecalibacterium sp900758465

CAZyme ID

MGYG000002040_01634

CAZy Family

GH25

CAZyme Description

hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
498	MGYG000002040_14\|CGC1	53108.76	4.2942

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000002040	2277187	MAG	China	Asia

Gene Location

Start: 16493; End: 17989 Strand: -

Full Sequence Download help

Enzyme Prediction help

No EC number prediction in MGYG000002040_01634.

CAZyme Signature Domains help

Family	Start	End	Evalue	family coverage
GH25	305	485	3.7e-42	0.9887005649717514

CDD Domains download full data without filtering help

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd06414	GH25_LytC-like	1.21e-81	303	496	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	6.25e-33	304	494	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.
cd06525	GH25_Lyc-like	4.12e-31	304	493	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.
pfam01183	Glyco_hydro_25	3.23e-30	305	485	1	179	Glycosyl hydrolases family 25.
COG3757	Acm	6.58e-25	304	493	65	251	Lyzozyme M1 (1,4-beta-N-acetylmuramidase), GH25 family [Cell wall/membrane/envelope biogenesis].

CAZyme Hits help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
AXA82288.1	1.10e-271	1	498	1	497
CBL00364.1	1.33e-251	1	498	1	497
QIA44074.1	2.02e-203	10	498	11	498
ATL90379.1	6.58e-203	10	498	86	572
ATP00196.1	2.75e-202	10	498	86	573

PDB Hits download full data without filtering help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
4KRU_A	9.23e-16	304	493	22	205	X-raystructure of catalytic domain of endolysin from clostridium perfringens phage phiSM101 [Clostridium phage phiSM101]
4KRT_A	4.62e-15	304	493	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	2.25e-11	293	493	1	200	Crystalstructure of the bacterial lysozyme from Streptomyces coelicolor at 1.65 A resolution [Streptomyces coelicolor]
2WAG_A	2.36e-08	304	496	18	207	TheStructure of a family 25 Glycosyl hydrolase from Bacillus anthracis. [Bacillus anthracis str. Ames]
3HMC_A	3.26e-07	305	493	8	177	Endolysinfrom Bacillus anthracis [Bacillus anthracis]

Swiss-Prot Hits download full data without filtering help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P25310	3.18e-10	293	493	78	277	Lysozyme M1 OS=Streptomyces globisporus OX=1908 GN=acm PE=1 SV=1
P26836	6.12e-10	296	493	3	194	Probable autolytic lysozyme OS=Clostridium perfringens (strain 13 / Type A) OX=195102 GN=lyc PE=3 SV=2
P76421	2.02e-09	304	494	69	253	Uncharacterized protein YegX OS=Escherichia coli (strain K12) OX=83333 GN=yegX PE=3 SV=2
Q8X7H0	2.71e-09	304	494	69	253	Uncharacterized protein YegX OS=Escherichia coli O157:H7 OX=83334 GN=yegX PE=3 SV=2
Q8FFY2	3.64e-09	304	494	69	253	Uncharacterized protein YegX OS=Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC) OX=199310 GN=yegX PE=3 SV=2

SignalP and Lipop Annotations help

This protein is predicted as SP

Other	SP_Sec_SPI	LIPO_Sec_SPII	TAT_Tat_SPI	TATLIP_Sec_SPII	PILIN_Sec_SPIII
0.118735	0.872714	0.001096	0.005814	0.001008	0.000604

TMHMM Annotations download full data without filtering help

start	end
21	43