CAZyme Information: MGYG000002298_00208

Basic Information

• Species: Blautia_A sp000436615
• Lineage: Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; Blautia_A; Blautia_A sp000436615
• CAZyme ID: MGYG000002298_00208
• CAZy Family: GH24
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
424		46670.07	4.0072

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000002298	4216146	Isolate	China	Asia

• Gene Location: Start: 238335; End: 239609 Strand: +

Full Sequence      

MKKKAKKWFSCITAAALVMSTVNLPIDVLASDFEDGVETSVEDEQMDFSDMENSEDLEIE
DVPEDVLVEEETDTEEGASDLEIETELFTDTEEITESTDEILSETGSEINTFSSRAGGMT
TGENGYSLIKQFESCRLTAYKAVSTEKYYTIGWGHYGSDVYAGMTITQAQADQYLKQDVA
KTENSVNSFLNSNRITIGQNQFDALVSFTYNLGNVWVSTETFQLKTILKNGYTKYSDAQI
RTAFTNWNKSGGQVLAGLTRRRNAEADLFLSNRKPDPTPTPIPIPQGSVTISDGEYHIVS
ALDSSKALDVCNQSKDNTANIQIYSNLADGTETFHITYIGNGAYKIINSNSGRCLDVDGA
GMTAGTNVQQYDYVGADQQQWIIQEDNGWFNIISKKNGLYLDVEDGNSSNGANVRVWNGN
GSDA

Enzyme Prediction     

No EC number prediction in MGYG000002298_00208.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH24	123	265	4.8e-36	0.9781021897810219
CBM13	290	385	7.4e-19	0.48936170212765956

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd00737	lyz_endolysin_autolysin	1.50e-53	125	270	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.
COG3772	RrrD	1.12e-29	116	272	2	150	Phage-related lysozyme (muramidase), GH24 family [Cell wall/membrane/envelope biogenesis].
pfam14200	RicinB_lectin_2	2.57e-27	334	417	5	89	Ricin-type beta-trefoil lectin domain-like.
cd16901	lyz_P1	6.68e-24	120	268	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.
cd16900	endolysin_R21-like	1.64e-19	128	270	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
ACR76485.1	1.58e-62	115	362	72	353
QKS48534.1	4.18e-39	123	269	7	138
BCK01394.1	2.28e-37	120	270	4	145
BAK99222.1	5.92e-36	120	269	10	149
QKS43439.1	3.53e-35	125	269	9	138

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6ET6_A	6.65e-22	117	270	48	194	ChainA, Lysozyme [Acinetobacter baumannii]
7M5I_A	4.48e-14	117	275	5	159	ChainA, Endolysin [Escherichia coli O157 typing phage 15],7M5I_B Chain B, Endolysin [Escherichia coli O157 typing phage 15]
2ANV_A	5.34e-13	119	271	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]
6H9D_A	1.29e-09	125	271	10	148	ChainA, Lysozyme [Asticcacaulis excentricus],6H9D_B Chain B, Lysozyme [Asticcacaulis excentricus],6H9D_C Chain C, Lysozyme [Asticcacaulis excentricus]
3PG0_A	4.34e-07	337	381	22	66	Crystalstructure of designed 3-fold symmetric protein, ThreeFoil [synthetic construct]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P62692	5.54e-30	119	269	1	136	Endolysin OS=Lactococcus phage c2 OX=31537 GN=L3 PE=3 SV=1
P62693	5.54e-30	119	269	1	136	Endolysin OS=Lactococcus phage phivML3 OX=10746 GN=L3 PE=3 SV=1
P07540	1.62e-28	119	271	1	144	Endolysin OS=Bacillus phage PZA OX=10757 GN=15 PE=3 SV=1
Q37896	1.82e-28	119	271	1	144	Endolysin OS=Bacillus phage B103 OX=10778 GN=15 PE=3 SV=1
P11187	2.25e-28	119	271	1	144	Endolysin OS=Bacillus phage phi29 OX=10756 GN=15 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
0.000568	0.998640	0.000240	0.000185	0.000171	0.000156

TMHMM  Annotations     

There is no transmembrane helices in MGYG000002298_00208.