CAZyme Information: MGYG000002321_02281

Basic Information

• Species: Ruminococcus_D bicirculans
• Lineage: Bacteria; Firmicutes_A; Clostridia; Oscillospirales; Ruminococcaceae; Ruminococcus_D; Ruminococcus_D bicirculans
• CAZyme ID: MGYG000002321_02281
• CAZy Family: GH25
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
287	MGYG000002321_2|CGC1	33804.37	6.8651

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000002321	2968500	Isolate	not provided	not provided

• Gene Location: Start: 144281; End: 145144 Strand: -

Full Sequence      

MKRSKKFKLDKEAINKIDSEYDDRDLSNYTNYEVYEEEKPRHRFLKKLVKRLIILCAVVL
VINLAVLLYTGRLWFNEPKKRDYPIRGPVVTESMGEIRWKSFAKQNIQTAYIRATKGTTF
EDGAFRDNWNGSKDTDISVGAYHVLELDTDGTKQAEHFINAVGEDLSGRLIPAVEVRLRG
LYRLLPPDYYEAADNLADFCDRIEKQYGIRPVIYCTERTYKNIVASDSRFNKDKIWYESL
FSKPDEDMDWTFWTYTNRVKFSFYESGEYLHMTVFNGSEDDFKKLII

Enzyme Prediction     

No EC number prediction in MGYG000002321_02281.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH25	94	260	2.9e-34	0.9378531073446328

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd06413	GH25_muramidase_1	4.85e-41	83	277	1	191	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.
cd00599	GH25_muramidase	4.16e-28	95	256	10	169	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.
cd06524	GH25_YegX-like	1.04e-26	95	260	10	179	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.
cd06419	GH25_muramidase_2	9.19e-22	83	261	6	176	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.
cd06412	GH25_CH-type	1.59e-21	85	282	1	199	CH-type (Chalaropsis-type) lysozymes represent one of four functionally-defined classes of peptidoglycan hydrolases (also referred to as endo-N-acetylmuramidases) that cleave bacterial cell wall peptidoglycans. CH-type lysozymes exhibit both lysozyme (acetylmuramidase) and diacetylmuramidase activity. The first member of this family to be described was a muramidase from the fungus Chalaropsis. However, a majority of the CH-type lysozymes are found in bacteriophages and Gram-positive bacteria such as Streptomyces and Clostridium. CH-type lysozymes have a single glycosyl hydrolase family 25 (GH25) domain with an unusual beta/alpha-barrel fold in which the last strand of the barrel is antiparallel to strands beta7 and beta1. Most CH-type lysozymes appear to lack the cell wall-binding domain found in other GH25 muramidases.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
CCO05908.1	1.87e-212	1	287	1	287
ADU22017.1	7.34e-73	2	287	8	308
CDZ24955.1	9.12e-44	51	284	7	238
AOZ96796.1	9.38e-44	50	282	4	238
QJU19847.1	2.11e-41	64	283	25	243

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
2WAG_A	6.09e-36	83	283	14	214	TheStructure of a family 25 Glycosyl hydrolase from Bacillus anthracis. [Bacillus anthracis str. Ames]
4KRU_A	4.09e-09	85	267	20	193	X-raystructure of catalytic domain of endolysin from clostridium perfringens phage phiSM101 [Clostridium phage phiSM101]
1JFX_A	6.60e-09	85	259	5	190	Crystalstructure of the bacterial lysozyme from Streptomyces coelicolor at 1.65 A resolution [Streptomyces coelicolor]
4KRT_A	8.54e-09	85	267	20	193	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]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P34020	6.64e-10	85	257	1	164	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
P26836	1.87e-08	85	253	9	173	Probable autolytic lysozyme OS=Clostridium perfringens (strain 13 / Type A) OX=195102 GN=lyc PE=3 SV=2
P25310	6.70e-08	85	259	82	267	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
0.999948	0.000053	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

start	end
52	74