CAZyme Information: MGYG000000103_00470

Basic Information

• Species: Bacilliculturomica massiliensis
• Lineage: Bacteria; Firmicutes_A; Clostridia; Peptostreptococcales; Anaerovoracaceae; Bacilliculturomica; Bacilliculturomica massiliensis
• CAZyme ID: MGYG000000103_00470
• CAZy Family: GH25
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
443		47423.8	4.9688

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000000103	4467403	Isolate	Canada	North America

• Gene Location: Start: 531464; End: 532795 Strand: +

Full Sequence      

MIKMRKILGTALCALLLFSAPAPAFAAAVPTSDGERPALRGIDVSQWQGDIDFNKVAAAG
VEVVYIQSGAGSDYTDANFQANDTKAREAGLKIGFYHYVTAQTAGEAAAQAEFFYSLIRD
KTADCRPAVDFEQFGDLSREEINQIASVFSARLEQLIGYAPAFYSDAYNAENIWDARLSR
YPLWIADYSATRPESSGPWDTWSGFQYSDTGAIPGISGDVDLDYFRGSIFVDGLLPPDVS
GGSGNNSGDGNSGGQGTKTFRYTVQRGDTLWDIAVRYGTTVAELVSLNHIENPRLIYPGQ
ILLVPTRGDSGTGQSGSGAGNGNAGGSNSPEDQTPAFVTVRSGDTLWAIARRYGTTVNAL
VSLNHIKTPSLIYPGQVLLLPKGTAPGGNLSGSTHYRRYLIRSGDTLSAIARRFGTTVKT
LAQLNHISDPDLIYAGRTLIIPD

Enzyme Prediction     

No EC number prediction in MGYG000000103_00470.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH25	42	216	1.9e-47	0.9943502824858758
CBM50	262	305	1.6e-16	0.975
CBM50	339	381	5.2e-16	0.95

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd06525	GH25_Lyc-like	5.05e-80	40	225	1	184	Lyc muramidase is an autolytic lysozyme (autolysin) from Clostridium acetobutylicum encoded by the lyc gene. Lyc has 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	4.78e-51	40	225	1	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.
cd06414	GH25_LytC-like	4.50e-49	40	225	2	190	The LytC lysozyme of Streptococcus pneumoniae is a bacterial cell wall hydrolase that cleaves the beta1-4-glycosydic bond located between the N-acetylmuramoyl-N-glucosaminyl residues of the cell wall polysaccharide chains. LytC is composed of a C-terminal glycosyl hydrolase family 25 (GH25) domain and an N-terminal choline-binding module (CBM) consisting of eleven homologous repeats that specifically recognizes the choline residues of pneumococcal lipoteichoic and teichoic acids. This domain arrangement is the reverse of the major pneumococcal autolysin, LytA, and the CPL-1-like lytic enzymes of the pneumococcal bacteriophages, in which the CBM (consisting of six repeats) is at the C-terminus. This model represents the C-terminal catalytic domain of the LytC-like enzymes.
COG3757	Acm	1.89e-45	40	231	64	259	Lyzozyme M1 (1,4-beta-N-acetylmuramidase), GH25 family [Cell wall/membrane/envelope biogenesis].
pfam01183	Glyco_hydro_25	1.89e-43	42	216	1	180	Glycosyl hydrolases family 25.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QJS18123.1	1.93e-116	30	442	27	397
QIB56830.1	4.31e-114	28	441	25	402
QMW80393.1	4.31e-114	28	441	25	402
QBE96304.1	4.89e-113	28	441	25	402
ASN94242.1	8.55e-111	40	381	33	338

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
4KRU_A	1.00e-37	39	232	20	214	X-raystructure of catalytic domain of endolysin from clostridium perfringens phage phiSM101 [Clostridium phage phiSM101]
4KRT_A	1.92e-36	39	232	20	214	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]
1JFX_A	1.59e-24	39	228	5	205	Crystalstructure of the bacterial lysozyme from Streptomyces coelicolor at 1.65 A resolution [Streptomyces coelicolor]
2WAG_A	2.17e-15	35	228	12	209	TheStructure of a family 25 Glycosyl hydrolase from Bacillus anthracis. [Bacillus anthracis str. Ames]
2L9Y_A	1.05e-09	263	313	66	116	Solutionstructure of the MoCVNH-LysM module from the rice blast fungus Magnaporthe oryzae protein (MGG_03307) [Pyricularia oryzae 70-15]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P26836	4.21e-34	39	229	9	200	Probable autolytic lysozyme OS=Clostridium perfringens (strain 13 / Type A) OX=195102 GN=lyc PE=3 SV=2
P34020	5.27e-32	39	246	1	201	Autolytic lysozyme OS=Clostridium acetobutylicum (strain ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787) OX=272562 GN=lyc PE=1 SV=1
P76421	3.33e-25	21	234	53	268	Uncharacterized protein YegX OS=Escherichia coli (strain K12) OX=83333 GN=yegX PE=3 SV=2
Q8FFY2	3.33e-25	21	234	53	268	Uncharacterized protein YegX OS=Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC) OX=199310 GN=yegX PE=3 SV=2
Q8X7H0	6.30e-25	21	234	53	268	Uncharacterized protein YegX OS=Escherichia coli O157:H7 OX=83334 GN=yegX PE=3 SV=2

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
0.000266	0.998924	0.000195	0.000230	0.000197	0.000171

TMHMM  Annotations     

start	end
7	29