dbCAN-seq: a database of CAZyme sequence and annotation

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CAZyme Information: MGYG000001563_00093

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Basic Information help

Species

Murdochiella vaginalis

Lineage

Bacteria; Firmicutes_A; Clostridia; Tissierellales; Peptoniphilaceae; Murdochiella; Murdochiella vaginalis

CAZyme ID

MGYG000001563_00093

CAZy Family

GH25

CAZyme Description

hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
761		86343.03	5.832

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001563	1671491	Isolate	not provided	not provided

Gene Location

Start: 111278; End: 113563 Strand: -

Full Sequence Download help

Enzyme Prediction help

No EC number prediction in MGYG000001563_00093.

CAZyme Signature Domains help

Family	Start	End	Evalue	family coverage
GH25	555	735	4.6e-39	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	1.42e-51	555	746	4	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	4.42e-24	554	745	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.
cd06525	GH25_Lyc-like	4.19e-23	555	741	3	180	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	2.92e-20	555	731	1	175	Glycosyl hydrolases family 25.
cd06523	GH25_PlyB-like	7.08e-20	554	743	2	175	PlyB is a bacteriophage endolysin that displays potent lytic activity toward Bacillus anthracis. PlyB has an N-terminal glycosyl hydrolase family 25 (GH25) catalytic domain and a C-terminal bacterial SH3-like domain, SH3b. Both domains are required for effective catalytic activity. Endolysins are produced by bacteriophages at the end of their life cycle and participate in lysing the bacterial cell in order to release the newly formed progeny. Endolysins (also referred to as endo-N-acetylmuramidases or peptidoglycan hydrolases) degrade bacterial cell walls by catalyzing the hydrolysis of 1,4-beta-linkages between N-acetylmuramic acid and N-acetyl-D-glucosamine residues.

CAZyme Hits help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QEK17162.1	1.52e-64	133	745	450	1037
QBE96747.1	3.05e-62	555	759	6	208
QBX31317.1	3.05e-62	555	759	6	208
ARP49604.1	8.19e-62	555	759	6	208
AZP03752.1	3.05e-61	555	759	6	208

PDB Hits download full data without filtering help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
4KRU_A	4.27e-12	555	760	23	200	X-raystructure of catalytic domain of endolysin from clostridium perfringens phage phiSM101 [Clostridium phage phiSM101]
4KRT_A	1.73e-11	555	760	23	200	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]
4FF5_A	6.55e-09	554	741	54	245	Structurebasis of a novel virulence factor GHIP a glycosyl hydrolase 25 of Streptococcus pneumoniae participating in host cell invasion [Streptococcus pneumoniae]

Swiss-Prot Hits download full data without filtering help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P11001	1.27e-16	141	546	1111	1496	Glucosyltransferase-I OS=Streptococcus downei OX=1317 GN=gtfI PE=3 SV=1
P27470	1.74e-14	141	527	1105	1476	Glucosyltransferase-I OS=Streptococcus downei OX=1317 PE=3 SV=1
P49331	1.99e-13	195	403	1194	1403	Glucosyltransferase-S OS=Streptococcus mutans serotype c (strain ATCC 700610 / UA159) OX=210007 GN=gtfD PE=3 SV=3
P13470	1.02e-12	141	349	1200	1411	Glucosyltransferase-SI OS=Streptococcus mutans serotype c (strain ATCC 700610 / UA159) OX=210007 GN=gtfC PE=1 SV=2
P08987	1.42e-08	141	349	1172	1383	Glucosyltransferase-I OS=Streptococcus mutans serotype c (strain ATCC 700610 / UA159) OX=210007 GN=gtfB PE=3 SV=3

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
0.000396	0.998794	0.000272	0.000180	0.000165	0.000145

TMHMM Annotations download full data without filtering help

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