dbCAN-seq: a database of CAZyme sequence and annotation

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CAZyme Information: MGYG000000201_02511

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Basic Information help

Species

Blautia_A sp900066145

Lineage

Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; Blautia_A; Blautia_A sp900066145

CAZyme ID

MGYG000000201_02511

CAZy Family

GH25

CAZyme Description

hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
524	MGYG000000201_9\|CGC3	59428.56	9.9681

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000000201	4593677	Isolate	China	Asia

Gene Location

Start: 144579; End: 146153 Strand: +

Full Sequence Download help

Enzyme Prediction help

No EC number prediction in MGYG000000201_02511.

CAZyme Signature Domains help

Family	Start	End	Evalue	family coverage
GH25	90	267	3.8e-45	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	1.06e-60	88	290	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	1.19e-29	88	287	1	184	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	8.48e-28	90	260	1	172	Glycosyl hydrolases family 25.
cd06413	GH25_muramidase_1	9.67e-21	87	287	3	187	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	2.08e-19	88	267	1	182	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 help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QCU01355.1	2.33e-155	1	519	1	506
CBL21600.1	3.12e-66	1	205	1	200
ASM68843.1	4.33e-54	66	307	73	303
CBK77005.1	7.82e-41	63	372	27	312
AWY97591.1	8.65e-41	64	288	72	283

PDB Hits download full data without filtering help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
4JZ5_A	4.35e-12	90	270	26	205	High-resolutionstructure of catalytic domain of endolysin ply40 from bacteriophage P40 of Listeria monocytogenes [Listeria phage P40]
1JFX_A	5.44e-09	83	269	1	194	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
Q8FFY2	6.28e-11	89	268	69	245	Uncharacterized protein YegX OS=Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC) OX=199310 GN=yegX PE=3 SV=2
P76421	1.14e-10	89	268	69	245	Uncharacterized protein YegX OS=Escherichia coli (strain K12) OX=83333 GN=yegX PE=3 SV=2
Q8X7H0	2.05e-10	89	268	69	245	Uncharacterized protein YegX OS=Escherichia coli O157:H7 OX=83334 GN=yegX PE=3 SV=2
P26836	6.67e-09	88	287	10	194	Probable autolytic lysozyme OS=Clostridium perfringens (strain 13 / Type A) OX=195102 GN=lyc PE=3 SV=2
P13470	7.55e-09	322	492	1179	1349	Glucosyltransferase-SI OS=Streptococcus mutans serotype c (strain ATCC 700610 / UA159) OX=210007 GN=gtfC PE=1 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
0.000442	0.998705	0.000208	0.000278	0.000189	0.000155

TMHMM Annotations download full data without filtering help

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