CAZyme Information: MGYG000001761_01619

Basic Information

• Lineage: Bacteria; Firmicutes_A; Clostridia; Oscillospirales; Ruminococcaceae; Gemmiger
• CAZyme ID: MGYG000001761_01619
• CAZy Family: GH25
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
299		32941.28	6.9865

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001761	2495136	MAG	Finland	Europe

• Gene Location: Start: 3233; End: 4132 Strand: -

Full Sequence      

MYAIDVSKWQGTMDWRTVKKAGISHAMLRAGYGNSVRQTDPMFRQNAAGCAAQGVHWGAY
WYSYATSPAQARQEARCCLQTLQGLRPELPLAYDIEYEPGILALDNATRTAMVKAFLEEV
EAAGYYGILYASTDFIRNRLNWRELACYDVWAAQYGSACTCPLPYGIWQYSSKNALGVPG
FGNALDCNRLYKDYPALIQKAGLNGFAAPTPDPVPDASTRKQLLTIGPVTNGDAADLQQL
CESLGLTGAGLYTSAWADGDKLTQTLTIGPVSSGDAWYIMRRCAQLQLTDRGLYRSEYR

Enzyme Prediction     

No EC number prediction in MGYG000001761_01619.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH25	4	174	4.8e-44	0.9661016949152542

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd06414	GH25_LytC-like	6.00e-75	4	191	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	1.96e-33	2	188	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	5.05e-28	4	173	1	174	Glycosyl hydrolases family 25.
cd06525	GH25_Lyc-like	1.07e-27	4	189	3	183	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.
cd06413	GH25_muramidase_1	2.36e-26	4	191	6	190	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
CBL18130.1	6.29e-45	4	206	300	500
ADU22071.1	1.41e-43	4	206	6	205
CCO05611.1	2.43e-43	4	204	7	204
QEY35367.1	8.33e-43	4	207	7	208
QLI94930.1	2.42e-42	4	206	7	206

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
4KRU_A	1.11e-12	4	193	23	210	X-raystructure of catalytic domain of endolysin from clostridium perfringens phage phiSM101 [Clostridium phage phiSM101]
4KRT_A	3.28e-12	4	193	23	210	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]
2NW0_A	4.33e-08	2	193	2	177	ChainA, PlyB [Bacteriophage sp.],2NW0_B Chain B, PlyB [Bacteriophage sp.]
1JFX_A	8.21e-08	4	189	8	201	Crystalstructure of the bacterial lysozyme from Streptomyces coelicolor at 1.65 A resolution [Streptomyces coelicolor]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P26836	1.86e-10	4	180	12	189	Probable autolytic lysozyme OS=Clostridium perfringens (strain 13 / Type A) OX=195102 GN=lyc PE=3 SV=2
P25310	7.87e-07	4	189	85	278	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
0.999902	0.000137	0.000007	0.000001	0.000000	0.000001

TMHMM  Annotations     

There is no transmembrane helices in MGYG000001761_01619.