CAZyme Information: MGYG000001707_01412

Basic Information

• Species: Coprococcus sp000154245
• Lineage: Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; Coprococcus; Coprococcus sp000154245
• CAZyme ID: MGYG000001707_01412
• CAZy Family: GH25
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
337		38560.54	4.4984

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001707	2954116	Isolate	not provided	not provided

• Gene Location: Start: 126912; End: 127925 Strand: -

Full Sequence      

MVQSESNFKRLVADMREIDRKKQLEKRMKYAVCIIIGIMIGIIAGICIGVEHNKTTRSKP
TLYTEVTYGVELPPGELANLIYENYWNYIKQSYIIVGDDRETCQLYKISSKVARHNYDLE
RFQMDDDGYMRYSDDNIKKAKLGIDVSGHQGTIDWDQVKEAGIQFAMIRLGYRGYTQGGL
ALDDNYVTNIETALESKMPVGVYFYTQAVSYEEGVEEAQYVLKNIADYKISYPVVIDTEK
MEADGARANDISNEERTDAIVGFCDTIKDAGYTPMIYANRNWYAQNLDMDRLGDYQLWLA
QYSNVPDFPYLFTGWQYTSEGSVPGISGSVDIDVWMK

Enzyme Prediction     

No EC number prediction in MGYG000001707_01412.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH25	144	326	4e-48	0.9943502824858758

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd06414	GH25_LytC-like	1.29e-89	141	336	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	1.31e-40	143	335	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.
cd06413	GH25_muramidase_1	1.14e-31	143	334	5	188	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.
pfam01183	Glyco_hydro_25	2.91e-31	144	326	1	180	Glycosyl hydrolases family 25.
cd06525	GH25_Lyc-like	3.41e-28	143	333	2	182	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
CBK83179.1	1.97e-111	31	337	19	321
QNL99368.1	5.06e-101	54	337	39	325
QWT52701.1	2.79e-100	48	336	32	323
QHI72152.1	2.24e-66	99	334	52	286
ABX43465.1	1.20e-65	105	334	388	616

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
4KRU_A	4.57e-13	143	333	22	205	X-raystructure of catalytic domain of endolysin from clostridium perfringens phage phiSM101 [Clostridium phage phiSM101]
4KRT_A	1.48e-12	143	333	22	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]
2WAG_A	1.87e-12	143	335	18	206	TheStructure of a family 25 Glycosyl hydrolase from Bacillus anthracis. [Bacillus anthracis str. Ames]
1JFX_A	1.11e-09	143	331	7	198	Crystalstructure of the bacterial lysozyme from Streptomyces coelicolor at 1.65 A resolution [Streptomyces coelicolor]
1OBA_A	5.32e-07	137	319	2	178	ChainA, Lysozyme [Streptococcus phage Cp1]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P34020	2.24e-16	143	333	3	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
P26836	8.93e-09	143	333	11	194	Probable autolytic lysozyme OS=Clostridium perfringens (strain 13 / Type A) OX=195102 GN=lyc PE=3 SV=2
P25310	1.25e-08	143	331	84	275	Lysozyme M1 OS=Streptomyces globisporus OX=1908 GN=acm PE=1 SV=1
Q8X7H0	1.44e-08	143	335	69	254	Uncharacterized protein YegX OS=Escherichia coli O157:H7 OX=83334 GN=yegX PE=3 SV=2
P19386	5.15e-07	137	319	2	178	Lysozyme OS=Streptococcus phage Cp-9 OX=10749 GN=CPL9 PE=3 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
0.999994	0.000016	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

start	end
30	52