dbCAN-seq: a database of CAZyme sequence and annotation

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CAZyme Information: MGYG000001908_00426

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Basic Information help

Species

Ruminococcus_D sp900543145

Lineage

Bacteria; Firmicutes_A; Clostridia; Oscillospirales; Ruminococcaceae; Ruminococcus_D; Ruminococcus_D sp900543145

CAZyme ID

MGYG000001908_00426

CAZy Family

GH25

CAZyme Description

hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
827	MGYG000001908_1\|CGC6	91059.85	9.026

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001908	2355088	MAG	Denmark	Europe

Gene Location

Start: 474237; End: 476720 Strand: -

Full Sequence Download help

Enzyme Prediction help

No EC number prediction in MGYG000001908_00426.

CAZyme Signature Domains help

Family	Start	End	Evalue	family coverage
GH25	128	313	1.4e-47	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	2.68e-78	127	324	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	6.74e-33	126	322	1	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	1.88e-30	128	313	1	180	Glycosyl hydrolases family 25.
cd06525	GH25_Lyc-like	5.27e-29	127	321	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	9.82e-24	126	324	1	193	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
CCO05379.1	8.23e-133	44	748	12	751
ADU22705.1	5.08e-80	104	749	87	714
CBK82808.1	1.07e-64	90	806	75	850
BAK47549.1	1.45e-52	115	513	192	673
QYX28904.1	3.34e-51	127	330	91	291

PDB Hits download full data without filtering help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
4KRU_A	1.91e-12	127	321	22	205	X-raystructure of catalytic domain of endolysin from clostridium perfringens phage phiSM101 [Clostridium phage phiSM101]
4KRT_A	2.58e-12	127	343	22	231	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	2.16e-09	125	321	5	200	Crystalstructure of the bacterial lysozyme from Streptomyces coelicolor at 1.65 A resolution [Streptomyces coelicolor]
4PBX_A	2.42e-08	224	492	279	557	Crystalstructure of the six N-terminal domains of human receptor protein tyrosine phosphatase sigma [Homo sapiens]

Swiss-Prot Hits download full data without filtering help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
Q86KC1	6.48e-11	125	314	20	205	Probable GH family 25 lysozyme 2 OS=Dictyostelium discoideum OX=44689 GN=DDB_G0274181 PE=3 SV=1
Q63870	2.31e-10	337	741	236	670	Collagen alpha-1(VII) chain OS=Mus musculus OX=10090 GN=Col7a1 PE=1 SV=3
P50899	3.28e-10	340	566	803	1042	Exoglucanase B OS=Cellulomonas fimi (strain ATCC 484 / DSM 20113 / JCM 1341 / NBRC 15513 / NCIMB 8980 / NCTC 7547) OX=590998 GN=cbhB PE=1 SV=1
P34020	4.80e-10	127	319	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
Q00546	5.31e-09	337	741	328	757	Tenascin-R OS=Gallus gallus OX=9031 GN=TNR 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
0.000317	0.998987	0.000211	0.000174	0.000163	0.000143

TMHMM Annotations help

There is no transmembrane helices in MGYG000001908_00426.