CAZyme Information: MGYG000000767_01412

Basic Information

• Species: Paraeggerthella hongkongensis
• Lineage: Bacteria; Actinobacteriota; Coriobacteriia; Coriobacteriales; Eggerthellaceae; Paraeggerthella; Paraeggerthella hongkongensis
• CAZyme ID: MGYG000000767_01412
• CAZy Family: GH25
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
297	MGYG000000767_110|CGC1	32053.84	5.9534

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000000767	2269129	MAG	Japan	Asia

• Gene Location: Start: 1487; End: 2380 Strand: -

Full Sequence      

MKSQTNKRRSHGKPRHAAAYAPAPRSSSQHARKSPLVGVLLVMLAGLLFAGMLVGLGQCA
APESAPKNAEYVSPYDWSSLERTGDRLAYRPGGILKSQVGVDVSDHQGFIDWNAVAADGI
DFAFVRVGNRGYTEGGLSVDARFDDNISGAQAAGLQAGAYFFSQATNVQEAVEEAEFVIS
HLGGRALELPVAFDHEPVADPNGRANNVDRDTLTACALAFCERLEKAGYVTMVYGNNGDM
ARYDRSALGNRPIWFAEYDAPTPRARFDFAIWQYTNGGTVTGINTSVDLNLRMTEAL

Enzyme Prediction     

No EC number prediction in MGYG000000767_01412.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH25	101	283	7.6e-44	0.9943502824858758

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd06414	GH25_LytC-like	4.18e-65	100	293	3	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	5.63e-30	100	291	2	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	1.45e-27	100	290	5	187	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	4.13e-23	100	290	2	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.
pfam01183	Glyco_hydro_25	5.05e-23	101	283	1	180	Glycosyl hydrolases family 25.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
ACV56468.1	6.17e-121	45	296	10	265
APO31195.1	6.17e-121	45	296	10	265
BAK43831.1	8.64e-114	74	297	3	226
QTU85263.1	1.05e-82	77	297	25	245
QKF07386.1	9.69e-77	48	296	55	315

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
5A6S_A	1.01e-11	133	290	52	199	Crystalstructure of the CTP1L endolysin reveals how its activity is regulated by a secondary translation product [Clostridium phage phiCTP1]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P34020	2.11e-15	100	290	3	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	1.23e-11	100	290	11	194	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
0.993149	0.006226	0.000374	0.000017	0.000015	0.000220

TMHMM  Annotations     

start	end
35	57