dbCAN-seq: a database of CAZyme sequence and annotation

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CAZyme Information: MGYG000001527_03226

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Basic Information help

Species

Fournierella massiliensis

Lineage

Bacteria; Firmicutes_A; Clostridia; Oscillospirales; Ruminococcaceae; Fournierella; Fournierella massiliensis

CAZyme ID

MGYG000001527_03226

CAZy Family

GH25

CAZyme Description

hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
914	MGYG000001527_19\|CGC6	100000.21	4.0523

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001527	3828237	Isolate	not provided	not provided

Gene Location

Start: 425411; End: 428155 Strand: -

Full Sequence Download help

Enzyme Prediction help

No EC number prediction in MGYG000001527_03226.

CAZyme Signature Domains help

Family	Start	End	Evalue	family coverage
GH25	282	457	2.3e-43	0.9943502824858758
CBM13	775	910	5.1e-25	0.675531914893617
CBM13	479	572	1.9e-22	0.48404255319148937
CBM13	629	720	4.5e-19	0.46808510638297873
CBM13	723	817	1e-15	0.4627659574468085

CDD Domains download full data without filtering help

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd06414	GH25_LytC-like	1.58e-89	280	467	2	191	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.
cd00599	GH25_muramidase	3.50e-34	280	466	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.
pfam14200	RicinB_lectin_2	8.18e-32	518	605	2	89	Ricin-type beta-trefoil lectin domain-like.
pfam14200	RicinB_lectin_2	1.98e-28	811	899	1	89	Ricin-type beta-trefoil lectin domain-like.
pfam14200	RicinB_lectin_2	4.85e-26	666	753	2	89	Ricin-type beta-trefoil lectin domain-like.

CAZyme Hits help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QCP36075.1	1.30e-69	240	520	43	346
BAK44097.1	7.40e-69	243	828	570	1207
AWY97591.1	2.38e-68	243	465	46	283
ATP53732.1	8.14e-68	240	470	33	268
AZH69442.1	1.07e-67	244	470	37	268

PDB Hits download full data without filtering help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
2WW5_A	2.25e-18	282	467	272	468	3D-structureof the modular autolysin LytC from Streptococcus pneumoniae at 1.6 A resolution [Streptococcus pneumoniae R6],2WWD_A 3D-structure of the modular autolysin LytC from Streptococcus pneumoniae in complex with pneummococcal peptidoglycan fragment [Streptococcus pneumoniae R6]
2WWC_A	5.30e-18	282	467	272	468	3D-structureof the modular autolysin LytC from Streptococcus pneumoniae in complex with synthetic peptidoglycan ligand [Streptococcus pneumoniae R6]
1JFX_A	3.21e-12	278	468	4	204	Crystalstructure of the bacterial lysozyme from Streptomyces coelicolor at 1.65 A resolution [Streptomyces coelicolor]
5A6S_A	1.43e-08	283	465	26	200	Crystalstructure of the CTP1L endolysin reveals how its activity is regulated by a secondary translation product [Clostridium phage phiCTP1]

Swiss-Prot Hits download full data without filtering help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P25310	5.32e-11	278	468	81	281	Lysozyme M1 OS=Streptomyces globisporus OX=1908 GN=acm PE=1 SV=1
P34020	7.19e-11	281	464	3	178	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	1.15e-07	281	470	69	258	Uncharacterized protein YegX OS=Escherichia coli (strain K12) OX=83333 GN=yegX PE=3 SV=2
Q8X7H0	1.15e-07	281	468	69	256	Uncharacterized protein YegX OS=Escherichia coli O157:H7 OX=83334 GN=yegX PE=3 SV=2
Q8FFY2	1.54e-07	281	470	69	258	Uncharacterized protein YegX OS=Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC) OX=199310 GN=yegX PE=3 SV=2

SignalP and Lipop Annotations help

This protein is predicted as SP

Other	SP_Sec_SPI	LIPO_Sec_SPII	TAT_Tat_SPI	TATLIP_Sec_SPII	PILIN_Sec_SPIII
0.014357	0.981859	0.002397	0.000529	0.000412	0.000401

TMHMM Annotations download full data without filtering help

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