CAZyme Information: MGYG000001379_02858

Basic Information

• Species: Schaedlerella glycyrrhizinilytica
• Lineage: Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; Schaedlerella; Schaedlerella glycyrrhizinilytica
• CAZyme ID: MGYG000001379_02858
• CAZy Family: GH25
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
326		36211.27	4.1113

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001379	3227618	Isolate	not provided	not provided

• Gene Location: Start: 93943; End: 94923 Strand: +

Full Sequence      

MSQKGLDVSEFQGTIDWTQVQSAGYQFAMLRAGYGFGTVDRQFHRNAAECNRLGIPVGAY
WFCYAISPETARQEADGCLDAISSHRFDYPICYDIEQATLNYAAQNGVTITPQLAAQIVT
AFCNRLEERGYFAMYYSNRNFLTQYLPSDFSDRYALWYAYYNEQFDGTNCGIWQYTNEGT
IPGISGNVDLDAGFIDYPTIIHTAGLNHLSDAPVSPSPEPEPEPPDYITYIIQPGDTLSQ
LAVRFGTTVNVLASLNDLTDPDLIYAGQTLRIPENADASILYYTVQPGDTLSQIALQYHT
TVNALAALNHLADPNLIYAGQILRIS

Enzyme Prediction     

No EC number prediction in MGYG000001379_02858.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH25	7	184	1.8e-45	0.9887005649717514

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd06414	GH25_LytC-like	5.52e-83	3	194	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	1.64e-39	4	192	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.
cd06413	GH25_muramidase_1	4.12e-29	4	192	4	188	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.
cd06525	GH25_Lyc-like	4.95e-28	4	191	1	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.
cd06524	GH25_YegX-like	1.46e-24	4	191	1	190	YegX is an uncharacterized bacterial protein with a glycosyl hydrolase family 25 (GH25) catalytic domain that is similar in sequence to the CH-type (Chalaropsis-type) lysozymes of the GH25 family of endolysins.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QHB23957.1	3.90e-132	1	275	1	268
QEI31463.1	3.90e-132	1	275	1	268
QRT30197.1	3.90e-132	1	275	1	268
QYX27151.1	9.17e-118	1	325	1	325
QEK16471.1	3.99e-114	1	325	1	325

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
2WAG_A	5.87e-10	4	186	17	196	TheStructure of a family 25 Glycosyl hydrolase from Bacillus anthracis. [Bacillus anthracis str. Ames]
5A6S_A	6.48e-10	3	189	22	197	Crystalstructure of the CTP1L endolysin reveals how its activity is regulated by a secondary translation product [Clostridium phage phiCTP1]
4B8V_A	1.19e-09	228	325	42	160	ChainA, Extracellular Protein 6 [Fulvia fulva],4B9H_A Chain A, Extracellular Protein 6 [Fulvia fulva]
4KRU_A	4.02e-09	4	191	21	205	X-raystructure of catalytic domain of endolysin from clostridium perfringens phage phiSM101 [Clostridium phage phiSM101]
4KRT_A	8.97e-09	4	191	21	205	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]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
Q49UX4	2.55e-12	229	326	87	194	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
Q37896	4.82e-12	229	325	164	262	Endolysin OS=Bacillus phage B103 OX=10778 GN=15 PE=3 SV=1
P9WM39	1.37e-11	225	325	51	152	Esterase Rv1288 OS=Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) OX=83332 GN=Rv1288 PE=1 SV=1
P9WM38	1.37e-11	225	325	51	152	Esterase MT1326 OS=Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh) OX=83331 GN=MT1326 PE=3 SV=1
P07540	2.10e-11	230	326	163	258	Endolysin OS=Bacillus phage PZA OX=10757 GN=15 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	0.000003	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000001379_02858.