CAZyme Information: MGYG000003496_00339

Basic Information

• Species: CAG-115 sp900768705
• Lineage: Bacteria; Firmicutes_A; Clostridia; Oscillospirales; Ruminococcaceae; CAG-115; CAG-115 sp900768705
• CAZyme ID: MGYG000003496_00339
• CAZy Family: GH25
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
291	MGYG000003496_20|CGC1	33435.22	9.0347

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000003496	2237307	MAG	Fiji	Oceania

• Gene Location: Start: 1167; End: 2042 Strand: +

Full Sequence      

MKIKGVDISHWQKGIDFSALKQAGVQFAIIRAGYSTKKDDAMDKFIAECKKYDIDYGFYW
YSYAMSIKQVEAEAEMCVEIIKGLSPTYPVFYDMEEKSQINGLDTETRTKMAVAFCEKVN
KAGFKAGIYVNPFFMENCFDKSKLIGKYDIWLAHWTNSPDRPSKYSYGQTMWQWGVDKIV
GYEIDGDICFTDYHNAKPIPEKKTVDQIADEVLAGKWGNGDERKKRLTDAGYDYAAVQKK
VNDKLYKKTVDGLANEVIRGKWGNGSERKRRLTKAGYDYNKVQKKVNEILK

Enzyme Prediction     

No EC number prediction in MGYG000003496_00339.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH25	6	174	5.5e-39	0.943502824858757

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd06414	GH25_LytC-like	7.91e-66	3	190	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	5.87e-29	4	173	1	167	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	2.94e-23	6	174	1	171	Glycosyl hydrolases family 25.
pfam08230	CW_7	7.82e-20	251	290	1	40	CW_7 repeat. This domain was originally found in the C-terminal moiety of the Cpl-7 lysozyme encoded by the Streptococcus pneumoniae bacteriophage Cp-7. It is also found in the cell wall hydrolases of human and life-stock pathogens. CW_7 repeats make up a cell wall binding motif.
pfam08230	CW_7	1.60e-19	206	245	1	40	CW_7 repeat. This domain was originally found in the C-terminal moiety of the Cpl-7 lysozyme encoded by the Streptococcus pneumoniae bacteriophage Cp-7. It is also found in the cell wall hydrolases of human and life-stock pathogens. CW_7 repeats make up a cell wall binding motif.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
CBK97096.1	3.47e-68	1	193	2	194
QKN24292.1	3.37e-51	1	245	1	258
ARP50082.1	3.37e-51	1	245	1	258
APW18536.1	2.13e-50	1	245	1	257
QQO40300.1	1.19e-49	1	245	1	257

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
4CVD_A	1.40e-07	208	245	4	41	ChainA, LYSOZYME [Streptococcus phage CP-7]
1JFX_A	1.92e-07	3	188	5	197	Crystalstructure of the bacterial lysozyme from Streptomyces coelicolor at 1.65 A resolution [Streptomyces coelicolor]
5I8L_A	1.57e-06	203	245	6	48	ChainA, Lysozyme [Streptococcus phage CP-7]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P19385	4.15e-10	6	243	9	243	Lysozyme OS=Streptococcus phage Cp-7 OX=10748 GN=CPL7 PE=1 SV=2
P25310	1.78e-06	3	188	82	274	Lysozyme M1 OS=Streptomyces globisporus OX=1908 GN=acm PE=1 SV=1

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	LIPO_Sec_SPII	TAT_Tat_SPI	TATLIP_Sec_SPII	PILIN_Sec_SPIII
1.000044	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000003496_00339.