dbCAN-seq: a database of CAZyme sequence and annotation

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CAZyme Information: MGYG000000982_00878

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Basic Information help

Species

CAG-354 sp900552655

Lineage

Bacteria; Firmicutes_A; Clostridia; TANB77; CAG-508; CAG-354; CAG-354 sp900552655

CAZyme ID

MGYG000000982_00878

CAZy Family

GH25

CAZyme Description

Cell division suppressor protein YneA

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
467	MGYG000000982_24\|CGC1	53906.37	9.6166

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000000982	1595406	MAG	Denmark	Europe

Gene Location

Start: 14898; End: 16301 Strand: -

Full Sequence Download help

Enzyme Prediction help

No EC number prediction in MGYG000000982_00878.

CAZyme Signature Domains help

Family	Start	End	Evalue	family coverage
GH25	38	213	5.7e-50	0.9943502824858758

CDD Domains download full data without filtering help

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd06525	GH25_Lyc-like	8.39e-64	37	222	2	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	8.53e-57	37	222	2	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.
pfam01183	Glyco_hydro_25	4.47e-47	38	213	1	180	Glycosyl hydrolases family 25.
cd06414	GH25_LytC-like	2.78e-43	37	218	3	186	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	8.62e-39	8	237	38	268	Lyzozyme M1 (1,4-beta-N-acetylmuramidase), GH25 family [Cell wall/membrane/envelope biogenesis].

CAZyme Hits help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QWT55024.1	5.83e-121	24	467	24	465
QJS18123.1	3.38e-118	24	465	21	448
QBJ75914.1	3.05e-114	36	467	10	442
ATD56705.1	3.05e-114	36	467	10	442
SLK20760.1	3.05e-114	36	467	10	442

PDB Hits download full data without filtering help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
4KRU_A	5.89e-52	36	229	21	214	X-raystructure of catalytic domain of endolysin from clostridium perfringens phage phiSM101 [Clostridium phage phiSM101]
4KRT_A	1.29e-50	36	261	21	244	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	5.53e-25	36	222	6	202	Crystalstructure of the bacterial lysozyme from Streptomyces coelicolor at 1.65 A resolution [Streptomyces coelicolor]
5A6S_A	5.19e-24	28	236	14	217	Crystalstructure of the CTP1L endolysin reveals how its activity is regulated by a secondary translation product [Clostridium phage phiCTP1]
2WAG_A	8.05e-19	36	236	17	215	TheStructure of a family 25 Glycosyl hydrolase from Bacillus anthracis. [Bacillus anthracis str. Ames]

Swiss-Prot Hits download full data without filtering help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P26836	1.09e-48	36	227	10	201	Probable autolytic lysozyme OS=Clostridium perfringens (strain 13 / Type A) OX=195102 GN=lyc PE=3 SV=2
P34020	5.87e-34	36	228	2	186	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	3.21e-31	24	226	55	258	Uncharacterized protein YegX OS=Escherichia coli (strain K12) OX=83333 GN=yegX PE=3 SV=2
Q8FFY2	4.43e-31	24	226	55	258	Uncharacterized protein YegX OS=Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC) OX=199310 GN=yegX PE=3 SV=2
Q8X7H0	8.47e-31	24	227	55	261	Uncharacterized protein YegX OS=Escherichia coli O157:H7 OX=83334 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
0.001050	0.998145	0.000233	0.000192	0.000168	0.000180

TMHMM Annotations download full data without filtering help

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