CAZyme Information: MGYG000003119_00089

Basic Information

• Species: Capnocytophaga ochracea
• Lineage: Bacteria; Bacteroidota; Bacteroidia; Flavobacteriales; Flavobacteriaceae; Capnocytophaga; Capnocytophaga ochracea
• CAZyme ID: MGYG000003119_00089
• CAZy Family: GH25
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
291		34513.89	9.9225

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000003119	2451559	MAG	United States	North America

• Gene Location: Start: 18831; End: 19706 Strand: +

Full Sequence      

MYICKMKKKKLQRSKSRISAKKKSLFGNFFTVSLLCILLLGVGSVFYIRTYYPAIYQKIL
NKITARKINSTYESNRIEHIVSLYYDKVFGIDLSHYQEREEIEWDSLYIRNKTAKYPIQF
AIFRATMGNDGTDKNFAHFFSEAKKHQLIRGAYHYYRPDEDPKLQANSYLKSARLEKGDF
LPILDIEQLPKKKSKEQFIKDVQTWLDIIEKHYKRKPIIYTYISFYEDYLYPTFKQYPLW
IANYNNVSVPTSVFSWQLWQFTENGITAGAKVKIDFNIFNGDSSELNKLLL

Enzyme Prediction     

No EC number prediction in MGYG000003119_00089.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH25	91	269	1.6e-44	0.9887005649717514

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd06524	GH25_YegX-like	3.36e-71	89	281	1	194	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.
cd06413	GH25_muramidase_1	2.09e-47	87	281	2	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.
cd00599	GH25_muramidase	1.68e-44	90	279	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	1.37e-34	91	269	1	179	Glycosyl hydrolases family 25.
COG3757	Acm	4.32e-34	90	290	65	264	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
ACU93346.1	3.77e-206	6	291	1	286
AVM54747.1	6.25e-205	6	291	1	286
ALC96419.1	1.79e-204	6	291	1	286
QLF49263.1	2.54e-204	6	291	1	286
ASF43063.1	2.39e-163	9	291	2	284

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
2WAG_A	1.84e-22	87	285	15	212	TheStructure of a family 25 Glycosyl hydrolase from Bacillus anthracis. [Bacillus anthracis str. Ames]
1JFX_A	4.54e-13	88	286	5	209	Crystalstructure of the bacterial lysozyme from Streptomyces coelicolor at 1.65 A resolution [Streptomyces coelicolor]
4KRU_A	4.84e-12	90	287	22	219	X-raystructure of catalytic domain of endolysin from clostridium perfringens phage phiSM101 [Clostridium phage phiSM101]
4KRT_A	1.33e-11	90	287	22	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]
5JIP_A	2.96e-11	133	277	53	220	Crystalstructure of the Clostridium perfringens spore cortex lytic enzyme SleM [Clostridium perfringens],5JIP_B Crystal structure of the Clostridium perfringens spore cortex lytic enzyme SleM [Clostridium perfringens]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
Q8FFY2	7.42e-34	88	286	67	261	Uncharacterized protein YegX OS=Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC) OX=199310 GN=yegX PE=3 SV=2
P76421	1.04e-33	88	286	67	261	Uncharacterized protein YegX OS=Escherichia coli (strain K12) OX=83333 GN=yegX PE=3 SV=2
Q8X7H0	1.04e-33	79	286	60	261	Uncharacterized protein YegX OS=Escherichia coli O157:H7 OX=83334 GN=yegX PE=3 SV=2
P25310	6.13e-12	88	286	82	286	Lysozyme M1 OS=Streptomyces globisporus OX=1908 GN=acm PE=1 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
0.999973	0.000052	0.000000	0.000000	0.000000	0.000001

TMHMM  Annotations     

start	end
25	47