dbCAN-seq: a database of CAZyme sequence and annotation

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CAZyme Information: MGYG000001623_02439

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Basic Information help

Species

Terrisporobacter othiniensis

Lineage

Bacteria; Firmicutes_A; Clostridia; Peptostreptococcales; Peptostreptococcaceae; Terrisporobacter; Terrisporobacter othiniensis

CAZyme ID

MGYG000001623_02439

CAZy Family

GH25

CAZyme Description

Cell division suppressor protein YneA

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
446		50480.93	5.5642

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001623	3867293	MAG	China	Asia

Gene Location

Start: 5534; End: 6874 Strand: +

Full Sequence Download help

Enzyme Prediction help

No EC number prediction in MGYG000001623_02439.

CAZyme Signature Domains help

Family	Start	End	Evalue	family coverage
GH25	7	184	2.2e-51	0.9943502824858758
CBM50	221	263	1.2e-16	0.95
CBM50	345	387	6.1e-16	0.95

CDD Domains download full data without filtering help

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd06525	GH25_Lyc-like	2.27e-82	5	193	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.
pfam01183	Glyco_hydro_25	7.74e-61	7	184	1	180	Glycosyl hydrolases family 25.
cd00599	GH25_muramidase	2.86e-55	5	193	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.
COG3757	Acm	2.15e-43	3	193	62	253	Lyzozyme M1 (1,4-beta-N-acetylmuramidase), GH25 family [Cell wall/membrane/envelope biogenesis].
cd06414	GH25_LytC-like	2.45e-43	5	194	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.

CAZyme Hits help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QBJ75914.1	1.01e-128	5	445	10	442
ATD56705.1	1.01e-128	5	445	10	442
SLK20760.1	1.01e-128	5	445	10	442
ATD55618.1	1.01e-128	5	445	10	442
QAS60493.1	2.33e-115	5	387	10	384

PDB Hits download full data without filtering help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
4KRU_A	3.45e-57	5	200	21	214	X-raystructure of catalytic domain of endolysin from clostridium perfringens phage phiSM101 [Clostridium phage phiSM101]
4KRT_A	1.19e-55	5	200	21	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	9.36e-22	2	193	3	202	Crystalstructure of the bacterial lysozyme from Streptomyces coelicolor at 1.65 A resolution [Streptomyces coelicolor]
5A6S_A	1.65e-19	8	202	26	214	Crystalstructure of the CTP1L endolysin reveals how its activity is regulated by a secondary translation product [Clostridium phage phiCTP1]
4B8V_A	1.57e-18	219	383	42	212	ChainA, Extracellular Protein 6 [Fulvia fulva],4B9H_A Chain A, Extracellular Protein 6 [Fulvia fulva]

Swiss-Prot Hits download full data without filtering help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P26836	1.43e-53	5	204	10	206	Probable autolytic lysozyme OS=Clostridium perfringens (strain 13 / Type A) OX=195102 GN=lyc PE=3 SV=2
P34020	6.01e-38	5	199	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
Q8CMN2	9.12e-29	221	387	29	190	N-acetylmuramoyl-L-alanine amidase sle1 OS=Staphylococcus epidermidis (strain ATCC 12228 / FDA PCI 1200) OX=176280 GN=sle1 PE=3 SV=1
Q5HRU2	9.12e-29	221	387	29	190	N-acetylmuramoyl-L-alanine amidase sle1 OS=Staphylococcus epidermidis (strain ATCC 35984 / RP62A) OX=176279 GN=sle1 PE=3 SV=1
Q49UX4	3.46e-28	221	396	29	200	N-acetylmuramoyl-L-alanine amidase sle1 OS=Staphylococcus saprophyticus subsp. saprophyticus (strain ATCC 15305 / DSM 20229 / NCIMB 8711 / NCTC 7292 / S-41) OX=342451 GN=sle1 PE=3 SV=1

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
1.000053	0.000001	0.000000	0.000000	0.000000	0.000000

TMHMM Annotations help

There is no transmembrane helices in MGYG000001623_02439.