dbCAN-seq: a database of CAZyme sequence and annotation

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CAZyme Information: MGYG000002294_01522

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Basic Information help

Species

Collinsella sp002232035

Lineage

Bacteria; Actinobacteriota; Coriobacteriia; Coriobacteriales; Coriobacteriaceae; Collinsella; Collinsella sp002232035

CAZyme ID

MGYG000002294_01522

CAZy Family

GH25

CAZyme Description

hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1330	MGYG000002294_11\|CGC2	141025.03	4.4854

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000002294	2254616	Isolate	China	Asia

Gene Location

Start: 23331; End: 27323 Strand: -

Full Sequence Download help

Enzyme Prediction help

No EC number prediction in MGYG000002294_01522.

CAZyme Signature Domains help

Family	Start	End	Evalue	family coverage
GH25	108	293	7.3e-35	0.9943502824858758
CBM13	1036	1175	2.3e-21	0.6436170212765957
CBM13	463	610	8.2e-21	0.7446808510638298
CBM13	1179	1317	5.4e-18	0.6914893617021277
CBM13	929	1028	7.1e-18	0.5106382978723404

CDD Domains download full data without filtering help

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd06414	GH25_LytC-like	1.53e-48	106	303	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.
cd00599	GH25_muramidase	6.04e-28	106	303	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	5.18e-27	659	747	2	89	Ricin-type beta-trefoil lectin domain-like.
cd06523	GH25_PlyB-like	2.67e-25	106	302	1	176	PlyB is a bacteriophage endolysin that displays potent lytic activity toward Bacillus anthracis. PlyB has an N-terminal glycosyl hydrolase family 25 (GH25) catalytic domain and a C-terminal bacterial SH3-like domain, SH3b. Both domains are required for effective catalytic activity. Endolysins are produced by bacteriophages at the end of their life cycle and participate in lysing the bacterial cell in order to release the newly formed progeny. Endolysins (also referred to as endo-N-acetylmuramidases or peptidoglycan hydrolases) degrade bacterial cell walls by catalyzing the hydrolysis of 1,4-beta-linkages between N-acetylmuramic acid and N-acetyl-D-glucosamine residues.
pfam14200	RicinB_lectin_2	5.63e-20	499	586	2	89	Ricin-type beta-trefoil lectin domain-like.

CAZyme Hits help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QGM63437.1	1.82e-86	82	677	171	785
AIZ15211.1	1.84e-84	82	677	204	818
BAQ29887.1	2.56e-84	82	677	171	785
AXM90834.1	3.23e-84	82	677	167	781
ALE10489.1	1.90e-82	82	677	171	785

PDB Hits download full data without filtering help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
2WW5_A	2.32e-30	83	303	246	467	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	5.60e-30	83	303	246	467	3D-structureof the modular autolysin LytC from Streptococcus pneumoniae in complex with synthetic peptidoglycan ligand [Streptococcus pneumoniae R6]
4JZ5_A	8.97e-13	107	312	25	220	High-resolutionstructure of catalytic domain of endolysin ply40 from bacteriophage P40 of Listeria monocytogenes [Listeria phage P40]
1JFX_A	3.73e-09	108	306	8	205	Crystalstructure of the bacterial lysozyme from Streptomyces coelicolor at 1.65 A resolution [Streptomyces coelicolor]
4KRU_A	1.09e-08	105	323	20	224	X-raystructure of catalytic domain of endolysin from clostridium perfringens phage phiSM101 [Clostridium phage phiSM101]

Swiss-Prot Hits download full data without filtering help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P25310	1.61e-08	95	306	68	282	Lysozyme M1 OS=Streptomyces globisporus OX=1908 GN=acm PE=1 SV=1
P26836	5.48e-08	105	313	9	205	Probable autolytic lysozyme OS=Clostridium perfringens (strain 13 / Type A) OX=195102 GN=lyc PE=3 SV=2
P34020	2.72e-07	105	304	1	181	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

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
0.000314	0.998943	0.000218	0.000177	0.000174	0.000150

TMHMM Annotations download full data without filtering help

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