CAZyme Information: MGYG000003424_00776

Basic Information

• Species: SFTJ01 sp004557385
• Lineage: Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Muribaculaceae; SFTJ01; SFTJ01 sp004557385
• CAZyme ID: MGYG000003424_00776
• CAZy Family: GH25
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
253		29570.1	10.2113

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000003424	2699357	MAG	Fiji	Oceania

• Gene Location: Start: 46572; End: 47333 Strand: +

Full Sequence      

MRSCAKGIASQLACSVKQIYIFALTILMLAVSGAACATHAKKRVKKVDVDGIDISHHNGK
IDWKKVQKGHPEIRFVYIKATEGASWVDSNYEYNLKNARKKGFKVGSYHFFNYRVGAREQ
FDNFAKNVDRNKQDIIPMVDFEKYGSEKNASKVVAELKEFCRLVKRHFGVYPMIYTNERI
YNLHLYKDFKRYHLFIANYKQRSPELKGDARYTIWQFSERGRIEGVKECVDLDRFHPDFS
LNSITYSKKKHKK

Enzyme Prediction     

No EC number prediction in MGYG000003424_00776.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH25	52	226	5.3e-51	0.9943502824858758

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd06413	GH25_muramidase_1	1.10e-59	49	237	3	191	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.
cd06524	GH25_YegX-like	7.04e-57	51	235	2	192	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.
cd00599	GH25_muramidase	3.50e-56	51	235	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.
pfam01183	Glyco_hydro_25	6.47e-44	52	226	1	180	Glycosyl hydrolases family 25.
cd06525	GH25_Lyc-like	8.14e-40	51	235	2	184	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
AUI55844.1	2.85e-61	31	244	21	234
QUB79331.1	5.72e-61	32	244	22	234
ASE18613.1	8.09e-61	31	244	21	234
ADK96557.1	8.09e-61	31	244	21	234
QUB82805.1	1.15e-60	31	244	21	234

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
2WAG_A	1.58e-33	46	236	13	207	TheStructure of a family 25 Glycosyl hydrolase from Bacillus anthracis. [Bacillus anthracis str. Ames]
4KRU_A	7.60e-18	48	247	19	219	X-raystructure of catalytic domain of endolysin from clostridium perfringens phage phiSM101 [Clostridium phage phiSM101]
4KRT_A	3.53e-17	48	247	19	219	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]
5A6S_A	3.51e-16	53	239	26	205	Crystalstructure of the CTP1L endolysin reveals how its activity is regulated by a secondary translation product [Clostridium phage phiCTP1]
1JFX_A	1.44e-13	49	236	5	203	Crystalstructure of the bacterial lysozyme from Streptomyces coelicolor at 1.65 A resolution [Streptomyces coelicolor]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P34020	9.03e-15	51	235	3	180	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
P25310	1.94e-12	49	236	82	280	Lysozyme M1 OS=Streptomyces globisporus OX=1908 GN=acm PE=1 SV=1
D4ANU4	2.19e-10	30	177	10	164	N,O-diacetylmuramidase OS=Arthroderma benhamiae (strain ATCC MYA-4681 / CBS 112371) OX=663331 GN=ARB_05911 PE=1 SV=1

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
0.110629	0.825421	0.062627	0.000534	0.000357	0.000412

TMHMM  Annotations     

start	end
15	37