CAZyme Information: MGYG000003427_03056

Basic Information

• Species: HGM12587 sp900766915
• Lineage: Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; HGM12587; HGM12587 sp900766915
• CAZyme ID: MGYG000003427_03056
• CAZy Family: GH25
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
491	MGYG000003427_391|CGC1	55010.18	4.3054

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000003427	3377258	MAG	Fiji	Oceania

• Gene Location: Start: 8068; End: 9543 Strand: +

Full Sequence      

MSRKKHRKAKLETREIVVIALAVLLAVLICAGILKVMFGILSPKQEEETTTSIEVIDEDT
EAEKEDAEDPQSEENLVEEETGAQTEITKIMVAENTAETDTITMGIDVSKFQGTIDWEKV
ADAGIDFAMVRVGYRTQSGGEIMEDNNARYNMQEATANGLKIGAYFFSTAISEAEAREEA
KWVADYISQYQITYPVAYNCEGFENPDNRQYSLTKTERTDIAIAFLNEIYEQGYTPMFYA
SKNEMQEDAKWETSRIEKSYKIWVSQYPEAPYPQTPGSSYNGTHDMWQYTNQGKIAGISK
PVDVNVAYFGYEKHAEAQNQEAPIEAKADVEALMNFREVDETVTSKDVTNLRDIPSQGED
STVLRKLNNGETAQRTGISDSGWSRLIIDGQKYYAVSNYLTTDLSYHTPVKEADDGLKTK
FSAVSENVTPKIEVNLRKLPSVTNPDAVVVATVSAGEVFVRTGINKDYGWSRVEYNGQTL
YCVSSYLNVVE

Enzyme Prediction     

No EC number prediction in MGYG000003427_03056.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH25	106	298	7.7e-44	0.9943502824858758

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd06414	GH25_LytC-like	2.07e-71	105	308	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	6.36e-34	105	307	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.
pfam01183	Glyco_hydro_25	9.70e-28	106	298	1	180	Glycosyl hydrolases family 25.
cd06525	GH25_Lyc-like	1.15e-21	105	305	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.
cd06413	GH25_muramidase_1	1.95e-21	105	308	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
CBK93417.1	4.36e-185	18	489	7	483
CBK89713.1	1.24e-184	18	489	7	483
ACR77025.1	3.54e-184	82	489	73	483
CBK74296.1	1.11e-164	2	491	15	522
ADL34859.1	3.20e-164	81	491	119	533

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
4KRT_A	2.06e-09	105	473	22	335	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	7.85e-09	105	305	22	205	X-raystructure of catalytic domain of endolysin from clostridium perfringens phage phiSM101 [Clostridium phage phiSM101]
5A6S_A	8.33e-08	107	320	26	214	Crystalstructure of the CTP1L endolysin reveals how its activity is regulated by a secondary translation product [Clostridium phage phiCTP1]
3HMC_A	6.47e-06	106	300	8	173	Endolysinfrom Bacillus anthracis [Bacillus anthracis]
1JFX_A	8.61e-06	105	305	7	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	4.02e-14	105	473	11	324	Probable autolytic lysozyme OS=Clostridium perfringens (strain 13 / Type A) OX=195102 GN=lyc PE=3 SV=2
Q8FFY2	9.02e-08	105	306	69	253	Uncharacterized protein YegX OS=Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC) OX=199310 GN=yegX PE=3 SV=2
P76421	1.21e-07	105	306	69	253	Uncharacterized protein YegX OS=Escherichia coli (strain K12) OX=83333 GN=yegX PE=3 SV=2
Q8X7H0	2.24e-06	105	317	69	263	Uncharacterized protein YegX OS=Escherichia coli O157:H7 OX=83334 GN=yegX PE=3 SV=2

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
0.999243	0.000467	0.000017	0.000005	0.000002	0.000306

TMHMM  Annotations     

start	end
16	38