CAZyme Information: MGYG000001246_01556

Basic Information

• Species: Enterocloster sp900541315
• Lineage: Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; Enterocloster; Enterocloster sp900541315
• CAZyme ID: MGYG000001246_01556
• CAZy Family: GH25
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
319	MGYG000001246_16|CGC1	35677.04	4.8694

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001246	3031447	MAG	Austria	Europe

• Gene Location: Start: 19552; End: 20511 Strand: -

Full Sequence      

MKQNGNKIRYMKYKGSLKLAAAVLAVSLAFPMAAQAKAWDFENGSYVDASGAPVEGAVAK
GITVTKYQNRANAENGIDWGKVAADGVGFAMIRIGYYKDRDPYFERNITEAAAHGIKTGV
FFYTQALDAQTAADEAEYVLQVIKDFPVSYPVAYDVESNYLLEQGLSAAQITENVNAFCK
VIADAGYCPIVYANNDWLTNHLNTADIPYDIWYARYGTVNSYPNRTIWQCTQEGNVDGIN
DHVTIELSFTDYSSKIPANSWKKIDGRWYYMKDYVKQTGWVQVGDNWYYMDANGAMVSNT
EMVIDGRTYRFAANGAMMY

Enzyme Prediction     

No EC number prediction in MGYG000001246_01556.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH25	72	239	9e-40	0.9491525423728814

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd06414	GH25_LytC-like	7.29e-66	60	249	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.
cd00599	GH25_muramidase	1.53e-25	60	240	1	178	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	1.04e-22	62	239	1	180	Glycosyl hydrolases family 25.
cd06413	GH25_muramidase_1	7.10e-18	60	243	4	184	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	1.46e-17	60	240	64	245	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
ASN93256.1	5.71e-144	20	304	65	349
QRP42084.1	5.71e-144	20	304	65	349
QJU22303.1	4.04e-143	20	302	71	353
ADL03867.1	1.70e-133	12	318	6	315
QRV22095.1	1.70e-133	12	318	6	315

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
5A6S_A	4.18e-11	101	243	59	196	Crystalstructure of the CTP1L endolysin reveals how its activity is regulated by a secondary translation product [Clostridium phage phiCTP1]

Swiss-Prot Hits     

has no Swissprot hit.

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	LIPO_Sec_SPII	TAT_Tat_SPI	TATLIP_Sec_SPII	PILIN_Sec_SPIII
0.000427	0.998708	0.000236	0.000216	0.000194	0.000174

TMHMM  Annotations     

start	end
13	35