CAZyme Information: MGYG000001372_01061

Basic Information

• Species: Paraprevotella xylaniphila
• Lineage: Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; Paraprevotella; Paraprevotella xylaniphila
• CAZyme ID: MGYG000001372_01061
• CAZy Family: GH24
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
147		16631.17	9.9888

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001372	3789432	Isolate	not provided	not provided

• Gene Location: Start: 98374; End: 98817 Strand: +

Full Sequence      

MKASNTLIEAIKRFEGFRGTAYKCPAGVWTIGYGHTVGVKRGDKMTEGEAERQLRRDLAE
YEAFVDKLGVTERQNKFDALVDFAYNLGCDALAGSTLLKKIRACAPDAEVRAEFMRWVYA
TVAGKKRKLDGLVKRRKWEADRFFNIA

Enzyme Prediction     

No EC number prediction in MGYG000001372_01061.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH24	4	138	6.5e-42	0.9781021897810219

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd00737	lyz_endolysin_autolysin	1.84e-61	8	144	2	136	endolysin and autolysin. The dsDNA phages of eubacteria use endolysins or muralytic enzymes in conjunction with hollin, a small membrane protein, to degrade the peptidoglycan found in bacterial cell walls. Similarly, bacteria produce autolysins to facilitate the biosynthesis of its cell wall heteropolymer peptidoglycan and cell division. Endolysins and autolysins are found in viruses and bacteria, respectively. Both endolysin and autolysin enzymes cleave the glycosidic beta 1,4-bonds between the N-acetylmuramic acid and the N-acetylglucosamine of the peptidoglycan.
cd16901	lyz_P1	6.61e-40	9	139	8	135	P1 lysozyme Lyz-like proteins. Enterobacteria phage P1 lysozyme Lyz is secreted to the Escherichia coli periplasm where it is membrane bound and inactive. Activation involves the release from the membrane, an intramolecular thiol-disulfide isomerization and extensive structural rearrangement of the N-terminal region. The dsDNA phages of eubacteria use endolysins or muralytic enzymes in conjunction with hollin, a small membrane protein, to degrade the peptidoglycan found in bacterial cell walls. Similarly, bacteria produce autolysins to facilitate the biosynthesis of its cell wall heteropolymer peptidoglycan and cell division. Endolysins and autolysins are found in viruses and bacteria, respectively. Both endolysin and autolysin enzymes cleave the glycosidic beta 1,4-bonds between the N-acetylmuramic acid and the N-acetylglucosamine of the peptidoglycan.
COG3772	RrrD	7.35e-35	1	140	5	144	Phage-related lysozyme (muramidase), GH24 family [Cell wall/membrane/envelope biogenesis].
cd16900	endolysin_R21-like	2.73e-31	11	139	12	137	endolysin R21-like proteins. Unlike T4 E phage lysozyme, the endolysin R21 from Enterobacteria phage P21 has an N-terminal SAR (signal-arrest-release) domain that anchors the endolysin to the membrane in an inactive form, which act to prevent premature lysis of the infected bacterium. The dsDNA phages of eubacteria use endolysins or muralytic enzymes in conjunction with hollin, a small membrane protein, to degrade the peptidoglycan found in bacterial cell walls. Similarly, bacteria produce autolysins to facilitate the biosynthesis of its cell wall heteropolymer peptidoglycan and cell division. Endolysins and autolysins are found in viruses and bacteria, respectively. Both endolysin and autolysin enzymes cleave the glycosidic beta 1,4-bonds between the N-acetylmuramic acid and the N-acetylglucosamine of the peptidoglycan.
pfam00959	Phage_lysozyme	5.39e-12	28	137	1	107	Phage lysozyme. This family includes lambda phage lysozyme and E. coli endolysin.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QUT29423.1	2.10e-33	1	147	1	143
QGT70365.1	2.10e-33	1	147	1	143
ATW34373.1	9.17e-33	8	143	8	143
BBO78064.1	4.38e-32	8	141	10	145
AXF76626.1	4.42e-32	1	145	1	141

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
7M5I_A	1.64e-20	1	141	7	151	ChainA, Endolysin [Escherichia coli O157 typing phage 15],7M5I_B Chain B, Endolysin [Escherichia coli O157 typing phage 15]
6H9D_A	4.97e-20	2	143	5	146	ChainA, Lysozyme [Asticcacaulis excentricus],6H9D_B Chain B, Lysozyme [Asticcacaulis excentricus],6H9D_C Chain C, Lysozyme [Asticcacaulis excentricus]
6ET6_A	4.26e-18	8	139	57	189	ChainA, Lysozyme [Acinetobacter baumannii]
2ANV_A	1.36e-10	1	145	2	146	ChainA, Lysozyme [Lederbergvirus P22],2ANV_B Chain B, Lysozyme [Lederbergvirus P22],2ANX_A Chain A, Lysozyme [Lederbergvirus P22],2ANX_B Chain B, Lysozyme [Lederbergvirus P22]
1XJU_A	4.98e-10	8	118	7	119	ChainA, Lysozyme [Punavirus P1],1XJU_B Chain B, Lysozyme [Punavirus P1]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
Q9T1T5	1.07e-29	1	139	1	139	Endolysin OS=Acyrthosiphon pisum secondary endosymbiont phage 1 OX=2682836 GN=13 PE=3 SV=1
Q37896	9.83e-17	1	143	1	142	Endolysin OS=Bacillus phage B103 OX=10778 GN=15 PE=3 SV=1
P07540	3.47e-13	1	139	1	138	Endolysin OS=Bacillus phage PZA OX=10757 GN=15 PE=3 SV=1
P11187	1.28e-12	1	139	1	138	Endolysin OS=Bacillus phage phi29 OX=10756 GN=15 PE=1 SV=1
P62693	1.69e-10	1	143	1	136	Endolysin OS=Lactococcus phage phivML3 OX=10746 GN=L3 PE=3 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
1.000046	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000001372_01061.