CAZyme Information: MGYG000000909_01911

Basic Information

• Species: UBA9502 sp900538475
• Lineage: Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; UBA9502; UBA9502 sp900538475
• CAZyme ID: MGYG000000909_01911
• CAZy Family: GH25
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
315		35786.42	5.0351

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000000909	3035568	MAG	China	Asia

• Gene Location: Start: 54242; End: 55189 Strand: +

Full Sequence      

MFRKRGRLRRAAAAGLCALMALQTPVMTARAELPEQLTVTNGQFIRANGTAVEGALAKGV
TISKYQNKAGEIDWNQVRGDGVTFAMVRLGYLNDLDPYFAANMQAASAHGIRTGVFFYTQ
ALDEETARQEARFVLEQIKDYPVSYPVAYDVESQYLLDMGKTPQEITSQVNAFCQVIAEA
GYRPVVYANNEWLTRHMDTSQIPYDIWYARYETSVNEYPNRTIWQYTKDGTVAGITGKVC
IEIAFADYTQLFPGTGWRPINGSWYYYENYQKKTGWLQLGENWYYLKEDGKMAVNESCQI
GDVMYSFAENGMWIP

Enzyme Prediction     

No EC number prediction in MGYG000000909_01911.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH25	60	235	8.2e-43	0.9943502824858758

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd06414	GH25_LytC-like	4.40e-69	58	245	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	8.02e-34	58	239	1	181	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	2.67e-25	62	235	3	180	Glycosyl hydrolases family 25.
cd06413	GH25_muramidase_1	2.26e-22	58	239	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	3.40e-17	58	239	64	248	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
SET59461.1	8.61e-106	19	314	17	315
ASN93256.1	1.13e-105	9	273	57	322
QRP42084.1	1.13e-105	9	273	57	322
QJU22303.1	2.76e-105	9	273	63	328
ADL03867.1	1.40e-104	13	314	14	315

PDB Hits     

has no PDB hit.

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
0.000253	0.999014	0.000198	0.000202	0.000170	0.000146

TMHMM  Annotations     

There is no transmembrane helices in MGYG000000909_01911.