CAZyme Information: MGYG000003990_01726

Basic Information

• Species: Ruminococcus_E sp900314705
• Lineage: Bacteria; Firmicutes_A; Clostridia; Oscillospirales; Acutalibacteraceae; Ruminococcus_E; Ruminococcus_E sp900314705
• CAZyme ID: MGYG000003990_01726
• CAZy Family: GH25
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
321	MGYG000003990_20|CGC1	37618.41	10.1265

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000003990	2132910	MAG	United Kingdom	Europe

• Gene Location: Start: 19083; End: 20048 Strand: -

Full Sequence      

MQKAIDVSKWNGDIDYTGVKSIGINNVIIQCGYGMESNQKDPYFDKNYRKAKENKMRVGV
YHYSYAKSVNEARKEANTCLKWIKGKDLDLPIYIDMEEENLTYLGKEILTKIAIEFCKVI
EKSGYTAGVYANANWFKNYLNYNKIKKNYSIWLAQYGDKKDFSCDIWQYTSQGKIRKNAS
NFDMNYIYKNPVIYVTVKKKTGLYKYGYRDYITGTSKVKRTVEKGTKLKWIYDDMYGWSK
VQYQGKDYFVTNSVLNRSSLSTFPKEVLKKDTKVYVIKNNKIKKSKVLRKGKKVTLVCTF
ENGKFKGYDYLSSGINRYLRK

Enzyme Prediction     

No EC number prediction in MGYG000003990_01726.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH25	5	175	1.6e-47	0.9774011299435028

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd06414	GH25_LytC-like	3.38e-71	2	188	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	1.52e-32	3	186	1	185	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.
cd06525	GH25_Lyc-like	1.21e-31	3	186	1	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.
pfam01183	Glyco_hydro_25	2.63e-29	5	175	1	177	Glycosyl hydrolases family 25.
COG3757	Acm	2.38e-20	3	187	64	253	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
QCT06404.1	2.73e-238	1	321	1	321
QAR21437.1	3.58e-49	3	223	5	218
QLI94930.1	4.90e-49	3	230	5	227
QQO42089.1	5.04e-49	3	223	5	218
QHQ70934.1	2.05e-47	1	207	1	205

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
4KRT_A	2.51e-20	3	262	21	290	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	7.48e-16	3	185	21	205	X-raystructure of catalytic domain of endolysin from clostridium perfringens phage phiSM101 [Clostridium phage phiSM101]
4JZ5_A	1.26e-12	1	185	22	210	High-resolutionstructure of catalytic domain of endolysin ply40 from bacteriophage P40 of Listeria monocytogenes [Listeria phage P40]
3HMC_A	2.43e-09	1	175	4	168	Endolysinfrom Bacillus anthracis [Bacillus anthracis]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P26836	7.14e-18	3	262	10	279	Probable autolytic lysozyme OS=Clostridium perfringens (strain 13 / Type A) OX=195102 GN=lyc 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
1.000068	0.000001	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000003990_01726.