CAZyme Information: MGYG000001681_00353

Basic Information

• Species: Ruminococcus sp900761275
• Lineage: Bacteria; Firmicutes_A; Clostridia; Oscillospirales; Ruminococcaceae; Ruminococcus; Ruminococcus sp900761275
• CAZyme ID: MGYG000001681_00353
• CAZy Family: GH25
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
397	MGYG000001681_17|CGC1	44571.2	3.9138

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001681	2557345	MAG	United States	North America

• Gene Location: Start: 140; End: 1333 Strand: +

Full Sequence      

MQNAQQVGIECGTYWYSYALTVEEAQQEAEACYEIIKDYDFKYPVYFDIEDPSQTNLSAA
QISAIIETFCTTLQEKGYYVGLYSYANFLTTHVFETVLKKYDVWVAHFDVPQPDFSGEYG
MWQYSSTGSVNGIAGNVDMDYSYINYPYLISPENYTPPVTTTTNTGTSSVDTTTTNTSVT
TTTTTSVAANNVIEKGMYVNSWQGDIDWQAAKEGGIDYAIIRAGYGKLASQKDEKFVRNV
LGAKSAGVNCGAYWYSYAVTVEEALQEAELFYETIKDYQFEYPVYFNIEDPVFSDLSVEE
ITAITDAFCSFMESKGYYVGIMSYVNFLNNKLEPSVFDKFDVAVAHYGVNAPSYSNFYGL
WNYTNTGSAAGVDGYVALSNCYEYYPQIMTSNHLNGF

Enzyme Prediction     

No EC number prediction in MGYG000001681_00353.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH25	198	372	8.2e-37	0.9887005649717514
GH25	2	133	3.3e-30	0.7570621468926554

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd06414	GH25_LytC-like	1.43e-62	195	382	2	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.
cd06414	GH25_LytC-like	2.72e-55	1	143	48	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	7.53e-29	195	379	1	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.
cd06525	GH25_Lyc-like	1.18e-26	195	380	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	5.57e-22	199	372	3	180	Glycosyl hydrolases family 25.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
CBL18130.1	6.95e-55	193	397	296	500
CCO05611.1	1.51e-52	195	395	5	204
QAR21437.1	2.05e-42	195	397	5	206
QQO42089.1	2.87e-42	195	397	5	206
QLI94930.1	7.66e-42	193	397	3	206

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
2WW5_A	4.69e-15	1	143	314	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	1.12e-14	1	143	314	468	3D-structureof the modular autolysin LytC from Streptococcus pneumoniae in complex with synthetic peptidoglycan ligand [Streptococcus pneumoniae R6]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P34020	3.24e-12	3	140	47	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	1.72e-07	189	374	6	189	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
1.000050	0.000007	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000001681_00353.