dbCAN-seq: a database of CAZyme sequence and annotation

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CAZyme Information: MGYG000002330_04086

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Basic Information help

Species

Eisenbergiella tayi

Lineage

Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; Eisenbergiella; Eisenbergiella tayi

CAZyme ID

MGYG000002330_04086

CAZy Family

GH25

CAZyme Description

hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
615	MGYG000002330_123\|CGC1	66239.91	4.4002

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000002330	7416064	Isolate	not provided	not provided

Gene Location

Start: 12144; End: 13991 Strand: -

Full Sequence Download help

Enzyme Prediction help

No EC number prediction in MGYG000002330_04086.

CAZyme Signature Domains help

Family	Start	End	Evalue	family coverage
GH25	145	338	5.4e-45	0.9943502824858758

CDD Domains download full data without filtering help

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd06414	GH25_LytC-like	1.01e-72	144	348	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	2.68e-37	144	347	2	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	2.54e-32	145	338	1	180	Glycosyl hydrolases family 25.
cd06524	GH25_YegX-like	5.89e-24	143	346	1	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.
COG3757	Acm	4.96e-23	144	346	65	252	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
CUH92515.1	3.35e-151	137	611	97	485
CBK89713.1	3.60e-143	105	525	52	482
ACR77025.1	4.07e-142	105	525	52	482
CBK93417.1	4.60e-141	105	525	52	482
ACR73526.1	2.00e-131	104	525	84	505

PDB Hits download full data without filtering help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
4KRT_A	9.37e-10	144	440	22	283	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]
4KRU_A	1.32e-09	144	345	22	205	X-raystructure of catalytic domain of endolysin from clostridium perfringens phage phiSM101 [Clostridium phage phiSM101]
3HMC_A	2.08e-08	145	340	8	173	Endolysinfrom Bacillus anthracis [Bacillus anthracis]
1JFX_A	2.22e-08	144	345	7	200	Crystalstructure of the bacterial lysozyme from Streptomyces coelicolor at 1.65 A resolution [Streptomyces coelicolor]

Swiss-Prot Hits download full data without filtering help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P25310	2.65e-07	144	345	84	277	Lysozyme M1 OS=Streptomyces globisporus OX=1908 GN=acm PE=1 SV=1
Q8HA43	2.77e-07	145	428	157	425	D-alanyl-L-alanine endopeptidase OS=Streptococcus phage B30 OX=209152 PE=1 SV=2

SignalP and Lipop Annotations help

This protein is predicted as OTHER

Other	SP_Sec_SPI	LIPO_Sec_SPII	TAT_Tat_SPI	TATLIP_Sec_SPII	PILIN_Sec_SPIII
1.000024	0.000026	0.000000	0.000000	0.000000	0.000001

TMHMM Annotations download full data without filtering help

start	end
20	39