CAZyme Information: MGYG000001415_01896

Basic Information

• Species: Alistipes communis
• Lineage: Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Rikenellaceae; Alistipes; Alistipes communis
• CAZyme ID: MGYG000001415_01896
• CAZy Family: GH24
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
170		19730.32	10.2573

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001415	3134723	Isolate	not provided	not provided

• Gene Location: Start: 139734; End: 140246 Strand: +

Full Sequence      

MVMLCSLMAVCSVSARISRREGMDGQAAIYRLPLFERAVCCTKYFEGWHSEKHHPYVGWG
HKILPDERYSARTMTKRQADVLLRKDLRKFCAMFRQFGKDSLLLATLAYNVGPYRLLGSK
TIPKSTLIKKLEAGDRNIYHEYIAFCSYKGKRHAMLLTRRKVEFALLYIP

Enzyme Prediction     

No EC number prediction in MGYG000001415_01896.

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd00737	lyz_endolysin_autolysin	1.74e-13	43	166	6	134	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.
COG3772	RrrD	7.60e-08	34	166	7	146	Phage-related lysozyme (muramidase), GH24 family [Cell wall/membrane/envelope biogenesis].
cd16901	lyz_P1	1.51e-05	55	166	28	138	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.
cd16900	endolysin_R21-like	3.97e-05	42	166	12	140	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QDM09807.1	1.69e-124	1	170	6	175
QCQ41261.1	1.69e-124	1	170	6	175
QJE28800.1	5.81e-114	1	168	6	173
QUT38165.1	8.55e-114	1	170	8	177
AND19514.1	4.61e-113	1	170	6	175

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
0.014406	0.983982	0.000588	0.000439	0.000282	0.000267

TMHMM  Annotations     

There is no transmembrane helices in MGYG000001415_01896.