CAZyme Information: MGYG000003783_00577

Basic Information

• Species: Anaerosacchariphilus sp002160765
• Lineage: Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; Anaerosacchariphilus; Anaerosacchariphilus sp002160765
• CAZyme ID: MGYG000003783_00577
• CAZy Family: GH25
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
520		58473.52	4.3215

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000003783	3019490	MAG	Canada	North America

• Gene Location: Start: 8056; End: 9618 Strand: -

Full Sequence      

MEEKELSQNREVQKGNSGPEEHRERLQRQQKKRKKRRKPQSRRSRKAQRKRKRMLLLLGE
AAAVLILFLMLFAVIFRGCGDGNAVEPAAVIQGAGMQNLELFRQATSEVMAEETEEEEER
VSTVKVIDTETDEVTLGIDVSEYQGNIDWSQAAEGQDFVMVRVGYRSSETGEITEDACAR
YNLQEAGAQGFYLGAYFFSTAVSEEEAREEAGWVCDLLDGYSITYPVAYNCEGFQNPDSR
QYQLTIEERSRIAQAFLDEVESRGYTGMFYAARNELQGNQLWDADTLELKYRIWVAQYGI
GDYPDTERPEYSGEHVMWQYTNEGTVAGIDGGVDRNVAYFGYSEAAEPKAAGTAQRIEAD
PEVGVDFTEVEEQVTAKELANLRSTMDQGDDSNVVTQLRNGETALRTGTGNNGWSRLEYN
GQTLYAVSSLLTTDLSYTPPAQEPESEFKTKFTTVSEQVTAKEVTNLRNRPSVEEPSQVI
AQLYNGEVITRTGVSDVGWSRVEYNGQTLYCISSYLQTVE

Enzyme Prediction     

No EC number prediction in MGYG000003783_00577.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH25	138	329	5.6e-38	0.9943502824858758

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd06414	GH25_LytC-like	8.00e-60	137	339	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	1.75e-26	137	338	2	186	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.
cd06523	GH25_PlyB-like	3.87e-21	138	336	3	175	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.
cd06413	GH25_muramidase_1	4.28e-20	137	339	5	190	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.
pfam01183	Glyco_hydro_25	4.87e-20	138	329	1	180	Glycosyl hydrolases family 25.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
ACR77025.1	2.26e-141	130	516	89	481
CBK89713.1	2.26e-141	130	516	89	481
CBK93417.1	7.28e-140	130	516	89	481
ADL34859.1	2.05e-135	129	520	135	533
CUH92515.1	1.22e-134	63	520	16	489

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
4KRU_A	9.55e-11	137	336	22	205	X-raystructure of catalytic domain of endolysin from clostridium perfringens phage phiSM101 [Clostridium phage phiSM101]
4KRT_A	3.04e-10	137	336	22	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     

has no Swissprot hit.

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
0.999956	0.000042	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

start	end
54	76