dbCAN-seq: a database of CAZyme sequence and annotation

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CAZyme Information: MGYG000001528_02134

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Basic Information help

Species

Mediterraneibacter massiliensis

Lineage

Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; Mediterraneibacter; Mediterraneibacter massiliensis

CAZyme ID

MGYG000001528_02134

CAZy Family

GH25

CAZyme Description

hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1266		140858.49	6.3306

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001528	3068303	Isolate	not provided	not provided

Gene Location

Start: 1313744; End: 1317544 Strand: +

Full Sequence Download help

Enzyme Prediction help

No EC number prediction in MGYG000001528_02134.

CAZyme Signature Domains help

Family	Start	End	Evalue	family coverage
GH25	1068	1253	1.5e-43	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	8.27e-67	1065	1263	1	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	6.26e-37	1066	1261	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	2.11e-30	1068	1253	1	180	Glycosyl hydrolases family 25.
cd06413	GH25_muramidase_1	1.16e-27	1066	1260	4	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	3.47e-26	1066	1261	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.

CAZyme Hits help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QDW73665.1	2.37e-192	207	1266	181	1225
QUO20801.1	8.59e-45	1063	1266	859	1060
ASS37354.1	3.08e-35	1066	1265	2	196
BCN31970.1	1.32e-34	695	1266	46	585
AVM48757.1	1.63e-33	1063	1265	19	216

PDB Hits download full data without filtering help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
4KRU_A	2.33e-12	1066	1260	21	205	X-raystructure of catalytic domain of endolysin from clostridium perfringens phage phiSM101 [Clostridium phage phiSM101]
1JFX_A	4.67e-12	1066	1260	6	200	Crystalstructure of the bacterial lysozyme from Streptomyces coelicolor at 1.65 A resolution [Streptomyces coelicolor]
4KRT_A	1.06e-11	1066	1260	21	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]
2WW5_A	1.92e-11	1066	1263	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]
2WAG_A	4.07e-11	1066	1263	17	207	TheStructure of a family 25 Glycosyl hydrolase from Bacillus anthracis. [Bacillus anthracis str. Ames]

Swiss-Prot Hits download full data without filtering help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P26836	7.00e-12	1061	1260	5	194	Probable autolytic lysozyme OS=Clostridium perfringens (strain 13 / Type A) OX=195102 GN=lyc PE=3 SV=2
P25310	5.89e-11	1060	1260	77	277	Lysozyme M1 OS=Streptomyces globisporus OX=1908 GN=acm PE=1 SV=1
P34020	6.13e-08	1066	1260	2	178	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 help

This protein is predicted as SP

Other	SP_Sec_SPI	LIPO_Sec_SPII	TAT_Tat_SPI	TATLIP_Sec_SPII	PILIN_Sec_SPIII
0.000378	0.998850	0.000219	0.000189	0.000176	0.000159

TMHMM Annotations download full data without filtering help

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7	26