CAZyme Information: MGYG000004651_02021

Basic Information

• Lineage: Bacteria; Actinobacteriota; Coriobacteriia; Coriobacteriales; Coriobacteriaceae; Collinsella
• CAZyme ID: MGYG000004651_02021
• CAZy Family: GH25
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
350		38654.45	6.0955

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000004651	2259550	Isolate	United States	North America

• Gene Location: Start: 64256; End: 65308 Strand: -

Full Sequence      

MAGSILPTCVDVSEHQGEIIWAQTKDGLWMAILRVQDGTYADIRLSRNVKYCEQLGIPYY
CYGFYRNGGAVEANRMVSRYKATGGKQCRGFIIDTEVTGFSKANLRSAFAALRQAMPDGK
HGHYIANHLWSEYGGEQYGEDWRWVPVYGVNDGYAHIAPAHKCDLWQFTSAGRVPGISGN
VDCNAIVSDDKSVAWFTDGTPPQQKPSAPADGVEQFDLTLEDYKLVALVMTDESCTGDVR
RAALGSRYDEIQALINHILRSSATTLAREVMEGRYGNGPYRHDALGPRYDEVQEKVMQIY
YGSPAKTYTVKSGDTLSEIGAKLGVAWKDIAAKNGISSPYTIYPGQVLEV

Enzyme Prediction     

No EC number prediction in MGYG000004651_02021.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH25	10	177	1.2e-22	0.9943502824858758

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd06523	GH25_PlyB-like	1.76e-27	10	186	3	177	PlyB is a bacteriophage endolysin that displays potent lytic activity toward Bacillus anthracis. PlyB has an N-terminal glycosyl hydrolase family 25 (GH25) catalytic domain and a C-terminal bacterial SH3-like domain, SH3b. Both domains are required for effective catalytic activity. Endolysins are produced by bacteriophages at the end of their life cycle and participate in lysing the bacterial cell in order to release the newly formed progeny. Endolysins (also referred to as endo-N-acetylmuramidases or peptidoglycan hydrolases) degrade bacterial cell walls by catalyzing the hydrolysis of 1,4-beta-linkages between N-acetylmuramic acid and N-acetyl-D-glucosamine residues.
cd06414	GH25_LytC-like	3.43e-17	10	184	4	188	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	9.85e-15	10	185	3	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.
cd00118	LysM	6.48e-14	306	350	1	45	Lysin Motif is a small domain involved in binding peptidoglycan. LysM, a small globular domain with approximately 40 amino acids, is a widespread protein module involved in binding peptidoglycan in bacteria and chitin in eukaryotes. The domain was originally identified in enzymes that degrade bacterial cell walls, but proteins involved in many other biological functions also contain this domain. It has been reported that the LysM domain functions as a signal for specific plant-bacteria recognition in bacterial pathogenesis. Many of these enzymes are modular and are composed of catalytic units linked to one or several repeats of LysM domains. LysM domains are found in bacteria and eukaryotes.
smart00257	LysM	3.25e-12	307	350	1	44	Lysin motif.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QQO40378.1	2.69e-35	10	350	5	316
QZA70103.1	2.78e-34	10	350	5	316
QFG05954.1	2.97e-34	10	350	8	319
QFG05873.1	2.97e-34	10	350	8	319
QXN70116.1	5.69e-30	10	350	5	333

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
3HMC_A	1.90e-25	3	198	1	190	Endolysinfrom Bacillus anthracis [Bacillus anthracis]
4JZ5_A	1.01e-16	10	189	26	215	High-resolutionstructure of catalytic domain of endolysin ply40 from bacteriophage P40 of Listeria monocytogenes [Listeria phage P40]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
Q49UX4	5.38e-06	307	350	87	129	N-acetylmuramoyl-L-alanine amidase sle1 OS=Staphylococcus saprophyticus subsp. saprophyticus (strain ATCC 15305 / DSM 20229 / NCIMB 8711 / NCTC 7292 / S-41) OX=342451 GN=sle1 PE=3 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
1.000053	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000004651_02021.