CAZyme Information: MGYG000004039_00993

Basic Information

• Lineage: Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; UMGS2037
• CAZyme ID: MGYG000004039_00993
• CAZy Family: GH24
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
324	MGYG000004039_7|CGC1	35063.68	8.9024

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000004039	2803182	MAG	United Kingdom	Europe

• Gene Location: Start: 2169; End: 3143 Strand: -

Full Sequence      

MVKLYRPKFISFFYGLFYFCEVYISDFIFFLFNVHVQNKIFGGKQMSFTTSQKGIDLIKS
FEGCRLTAYQDSVGVWTIGYGHTAGVYQGMTITEKEAEDFLRSDLGTSESAVNRLVTYSM
NQNQFDALVSFTFNVGSGNFGSSTLLKKLNQGDITGAANEFDKWIYAGGQVLEGLVKRRA
AEKELFLNGTVTGGGETPSTGDATISAFQTWLNSNYSAGLTVDGKYGNNTKKAAIKAYQK
ILGVTADGVFGAASKAAVKTLKAGSRGNDVHIMQGMLYCRGFNPNGVDGVFGPGCTTAVK
NFQSSKGLSADGIAGKDTMYALYN

Enzyme Prediction     

No EC number prediction in MGYG000004039_00993.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH24	51	182	1e-56	0.9854014598540146

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd00737	lyz_endolysin_autolysin	5.30e-84	54	187	1	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	1.13e-57	49	185	1	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.
COG3772	RrrD	2.43e-57	49	189	6	150	Phage-related lysozyme (muramidase), GH24 family [Cell wall/membrane/envelope biogenesis].
cd16900	endolysin_R21-like	1.03e-56	57	187	11	142	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	4.58e-26	75	180	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
QIX91555.1	2.09e-60	46	242	1	194
QKR11157.1	1.65e-52	50	187	3	140
AOJ72271.1	2.21e-52	48	189	4	158
AVE33918.1	3.30e-52	50	187	3	140
AWT29802.1	3.30e-52	50	187	3	140

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6ET6_A	2.02e-44	42	187	48	194	ChainA, Lysozyme [Acinetobacter baumannii]
6H9D_A	1.33e-33	51	187	7	147	ChainA, Lysozyme [Asticcacaulis excentricus],6H9D_B Chain B, Lysozyme [Asticcacaulis excentricus],6H9D_C Chain C, Lysozyme [Asticcacaulis excentricus]
3HDF_A	1.02e-28	62	189	10	138	ChainA, Lysozyme [Enterobacteria phage P21],3HDF_B Chain B, Lysozyme [Enterobacteria phage P21]
3HDE_A	2.04e-28	62	189	35	163	ChainA, Lysozyme [Enterobacteria phage P21],3HDE_B Chain B, Lysozyme [Enterobacteria phage P21],3HDE_C Chain C, Lysozyme [Enterobacteria phage P21],3HDE_D Chain D, Lysozyme [Enterobacteria phage P21]
4ZPU_A	5.22e-28	62	189	35	163	Thestructure of DLP12 endolysin exhibits likely active and inactive conformations. [Escherichia coli K-12],4ZPU_B The structure of DLP12 endolysin exhibits likely active and inactive conformations. [Escherichia coli K-12],4ZPU_C The structure of DLP12 endolysin exhibits likely active and inactive conformations. [Escherichia coli K-12],4ZPU_D The structure of DLP12 endolysin exhibits likely active and inactive conformations. [Escherichia coli K-12]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
Q9T1T5	8.02e-35	51	186	4	143	Endolysin OS=Acyrthosiphon pisum secondary endosymbiont phage 1 OX=2682836 GN=13 PE=3 SV=1
P11187	2.34e-33	51	190	4	146	Endolysin OS=Bacillus phage phi29 OX=10756 GN=15 PE=1 SV=1
P07540	4.59e-33	51	190	4	146	Endolysin OS=Bacillus phage PZA OX=10757 GN=15 PE=3 SV=1
Q37896	7.56e-32	51	189	4	145	Endolysin OS=Bacillus phage B103 OX=10778 GN=15 PE=3 SV=1
P78285	2.18e-27	62	189	35	163	Lysozyme RrrD OS=Escherichia coli (strain K12) OX=83333 GN=rrrD 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
1.000036	0.000002	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

start	end
12	34