dbCAN-seq: a database of CAZyme sequence and annotation

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CAZyme Information: MGYG000003517_02515

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Basic Information help

Species

UBA3766 sp900769175

Lineage

Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; UBA3766; UBA3766 sp900769175

CAZyme ID

MGYG000003517_02515

CAZy Family

GH25

CAZyme Description

hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1085	MGYG000003517_259\|CGC1	116866.71	4.4937

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000003517	2831393	MAG	Fiji	Oceania

Gene Location

Start: 9449; End: 12706 Strand: -

Full Sequence Download help

Enzyme Prediction help

No EC number prediction in MGYG000003517_02515.

CAZyme Signature Domains help

Family	Start	End	Evalue	family coverage
GH25	892	1072	1e-49	0.9943502824858758

CDD Domains download full data without filtering help

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd06414	GH25_LytC-like	3.34e-81	891	1082	3	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	5.58e-40	891	1080	2	185	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	9.91e-32	892	1072	1	180	Glycosyl hydrolases family 25.
cd06525	GH25_Lyc-like	1.86e-31	891	1079	2	182	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.
cd06524	GH25_YegX-like	9.37e-29	890	1080	1	191	YegX is an uncharacterized bacterial protein with a glycosyl hydrolase family 25 (GH25) catalytic domain that is similar in sequence to the CH-type (Chalaropsis-type) lysozymes of the GH25 family of endolysins.

CAZyme Hits help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QNM02116.1	1.79e-145	251	1085	216	1102
ADL33290.1	1.48e-137	285	1082	288	1225
AOZ95561.1	4.23e-126	285	1082	302	1213
CBK74089.1	9.39e-78	803	1081	244	516
QFJ53990.1	1.01e-73	799	1083	602	881

PDB Hits download full data without filtering help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
2WW5_A	2.24e-22	812	1082	147	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	3.99e-22	812	1082	147	468	3D-structureof the modular autolysin LytC from Streptococcus pneumoniae in complex with synthetic peptidoglycan ligand [Streptococcus pneumoniae R6]
4JZ5_A	6.66e-16	889	1079	23	210	High-resolutionstructure of catalytic domain of endolysin ply40 from bacteriophage P40 of Listeria monocytogenes [Listeria phage P40]
4KRU_A	9.56e-14	891	1079	22	205	X-raystructure of catalytic domain of endolysin from clostridium perfringens phage phiSM101 [Clostridium phage phiSM101]
1JFX_A	1.40e-13	888	1079	4	200	Crystalstructure of the bacterial lysozyme from Streptomyces coelicolor at 1.65 A resolution [Streptomyces coelicolor]

Swiss-Prot Hits download full data without filtering help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P34020	6.80e-17	891	1079	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
P25310	2.58e-12	888	1079	81	277	Lysozyme M1 OS=Streptomyces globisporus OX=1908 GN=acm PE=1 SV=1
P26836	1.84e-11	891	1079	11	194	Probable autolytic lysozyme OS=Clostridium perfringens (strain 13 / Type A) OX=195102 GN=lyc PE=3 SV=2
P76421	1.22e-10	889	1080	67	253	Uncharacterized protein YegX OS=Escherichia coli (strain K12) OX=83333 GN=yegX PE=3 SV=2
Q8FFY2	1.64e-10	889	1080	67	253	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 OTHER

Other	SP_Sec_SPI	LIPO_Sec_SPII	TAT_Tat_SPI	TATLIP_Sec_SPII	PILIN_Sec_SPIII
1.000066	0.000002	0.000000	0.000000	0.000000	0.000000

TMHMM Annotations download full data without filtering help

start	end
257	279