dbCAN-seq: a database of CAZyme sequence and annotation

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CAZyme Information: MGYG000001977_03439

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Basic Information help

Species

Lineage

Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; Bacteroides;

CAZyme ID

MGYG000001977_03439

CAZy Family

CBM50

CAZyme Description

hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
596		67593.1	8.6452

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001977	4322077	MAG	Denmark	Europe

Gene Location

Start: 1013; End: 2803 Strand: -

Full Sequence Download help

Enzyme Prediction help

No EC number prediction in MGYG000001977_03439.

CDD Domains download full data without filtering help

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
pfam01476	LysM	1.11e-09	32	74	1	43	LysM domain. The LysM (lysin motif) domain is about 40 residues long. It is found in a variety of enzymes involved in bacterial cell wall degradation. This domain may have a general peptidoglycan binding function. The structure of this domain is known.
cd00118	LysM	2.50e-09	84	128	1	45	Lysin Motif is a small domain involved in binding peptidoglycan. LysM, a small globular domain with approximately 40 amino acids, is a widespread protein module involved in binding peptidoglycan in bacteria and chitin in eukaryotes. The domain was originally identified in enzymes that degrade bacterial cell walls, but proteins involved in many other biological functions also contain this domain. It has been reported that the LysM domain functions as a signal for specific plant-bacteria recognition in bacterial pathogenesis. Many of these enzymes are modular and are composed of catalytic units linked to one or several repeats of LysM domains. LysM domains are found in bacteria and eukaryotes.
cd00118	LysM	3.85e-09	32	73	3	45	Lysin Motif is a small domain involved in binding peptidoglycan. LysM, a small globular domain with approximately 40 amino acids, is a widespread protein module involved in binding peptidoglycan in bacteria and chitin in eukaryotes. The domain was originally identified in enzymes that degrade bacterial cell walls, but proteins involved in many other biological functions also contain this domain. It has been reported that the LysM domain functions as a signal for specific plant-bacteria recognition in bacterial pathogenesis. Many of these enzymes are modular and are composed of catalytic units linked to one or several repeats of LysM domains. LysM domains are found in bacteria and eukaryotes.
smart00257	LysM	6.19e-09	32	73	2	44	Lysin motif.
smart00257	LysM	3.86e-08	165	208	2	44	Lysin motif.

CAZyme Hits help

Hit ID	Query Start	Query End	Hit Start	Hit End
BBK88149.1	1	596	1	596
QUT36281.1	1	596	1	596
QUT63939.1	1	596	1	596
QQA28500.1	1	596	1	596
QUT67528.1	1	596	1	596

PDB Hits help

has no PDB hit.

Swiss-Prot Hits download full data without filtering help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
Q6GC24	2.45e-08	5	191	3	186	N-acetylmuramoyl-L-alanine amidase sle1 OS=Staphylococcus aureus (strain MSSA476) OX=282459 GN=sle1 PE=3 SV=1
Q5HIL2	2.45e-08	5	191	3	186	N-acetylmuramoyl-L-alanine amidase sle1 OS=Staphylococcus aureus (strain COL) OX=93062 GN=sle1 PE=3 SV=1
Q7A7E0	2.45e-08	5	191	3	186	N-acetylmuramoyl-L-alanine amidase sle1 OS=Staphylococcus aureus (strain N315) OX=158879 GN=sle1 PE=1 SV=1
P0C1U7	2.45e-08	5	191	3	186	N-acetylmuramoyl-L-alanine amidase sle1 OS=Staphylococcus aureus OX=1280 GN=sle1 PE=3 SV=1
Q7A1T4	2.45e-08	5	191	3	186	N-acetylmuramoyl-L-alanine amidase sle1 OS=Staphylococcus aureus (strain MW2) OX=196620 GN=sle1 PE=3 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
0.000695	0.566353	0.432190	0.000275	0.000247	0.000217

TMHMM Annotations download full data without filtering help

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