CAZyme Information: MGYG000002285_02892

Basic Information

• Species: CAG-95 sp900066375
• Lineage: Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; CAG-95; CAG-95 sp900066375
• CAZyme ID: MGYG000002285_02892
• CAZy Family: GH25
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
516	MGYG000002285_19|CGC1	56152.8	4.2261

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000002285	3374269	Isolate	China	Asia

• Gene Location: Start: 1001; End: 2551 Strand: +

Full Sequence      

MKRNGNISESGKMLILGIGILLILAIIVIVLVVRMKDDVRKRDTVVETLQQEIPEDGEGQ
AESGSETEDGRLHEETALESEDKAQNDDSVQVGALEDEEDPQEQKAAENAGGIAVAITKG
AENTVPKSADENGQQSMGIDVSKHQGNIDWAKVKASGVEFAMVRVGYRAKSTGQLYEDPT
ARYNLQEAQAAGIRLGAYFFSSAVTEEEAREEARFTTDLIAKYKITYPVAYNCEGFQDAG
NRQYALSQTERTGLACAFLDEVAAAGYTPMFYASRNELAGNASWDTDILASRYKIWLAWY
PSVMTEQADYSGSYAMWQYTCQGTVDGISGKTDINTAYFSYTKEAEAKDDTPAERVTVNP
EVGINFTEVNETVTAKQETNLRTEPSTASDDTIVGKLTHGDTATRTGVGHNGWSRVVYQG
QTLYAVTSYLTTDMEDTGQQAPPQGPVYTPVGDQVTAKQETNLRTEPSTASDDTIVGKLH
NGEALTRIATGDNGWSQLEYNGQTVYAVSSYLMPAG

Enzyme Prediction     

No EC number prediction in MGYG000002285_02892.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH25	139	328	2.1e-44	0.9943502824858758

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd06414	GH25_LytC-like	1.98e-65	138	338	3	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	1.37e-28	138	335	2	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	7.62e-26	139	328	1	180	Glycosyl hydrolases family 25.
cd06413	GH25_muramidase_1	2.59e-22	138	338	5	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.
COG3757	Acm	6.13e-21	138	348	65	262	Lyzozyme M1 (1,4-beta-N-acetylmuramidase), GH25 family [Cell wall/membrane/envelope biogenesis].

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
CUH92515.1	2.57e-138	127	513	93	486
CBK89713.1	1.75e-131	131	512	89	481
ACR77025.1	3.50e-131	128	512	86	481
CBK93417.1	2.80e-130	128	512	86	481
ADL34859.1	1.67e-127	128	512	133	529

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
2WW5_A	1.75e-19	139	338	272	468	3D-structureof the modular autolysin LytC from Streptococcus pneumoniae at 1.6 A resolution [Streptococcus pneumoniae R6],2WWD_A 3D-structure of the modular autolysin LytC from Streptococcus pneumoniae in complex with pneummococcal peptidoglycan fragment [Streptococcus pneumoniae R6]
2WWC_A	4.17e-19	139	338	272	468	3D-structureof the modular autolysin LytC from Streptococcus pneumoniae in complex with synthetic peptidoglycan ligand [Streptococcus pneumoniae R6]
4KRT_A	9.35e-13	138	430	22	283	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]
4KRU_A	8.53e-12	138	335	22	205	X-raystructure of catalytic domain of endolysin from clostridium perfringens phage phiSM101 [Clostridium phage phiSM101]
1JFX_A	6.51e-10	130	335	1	200	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	2.46e-14	132	430	5	272	Probable autolytic lysozyme OS=Clostridium perfringens (strain 13 / Type A) OX=195102 GN=lyc PE=3 SV=2
P25310	2.62e-09	129	335	77	277	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
1.000036	0.000003	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

start	end
13	35