dbCAN-seq: a database of CAZyme sequence and annotation

You are browsing environment: HUMAN GUT

help

CAZyme Information: MGYG000001059_00259

You are here: Home > Sequence: MGYG000001059_00259

Basic Information help

Species

Porphyromonas_A somerae

Lineage

Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Porphyromonadaceae; Porphyromonas_A; Porphyromonas_A somerae

CAZyme ID

MGYG000001059_00259

CAZy Family

GH18

CAZyme Description

hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
370	MGYG000001059_15\|CGC1	42341.95	5.8781

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001059	2193999	MAG	Spain	Europe

Gene Location

Start: 51494; End: 52606 Strand: +

Full Sequence Download help

Enzyme Prediction help

No EC number prediction in MGYG000001059_00259.

CDD Domains download full data without filtering help

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd06542	GH18_EndoS-like	3.10e-59	74	355	1	254	Endo-beta-N-acetylglucosaminidases are bacterial chitinases that hydrolyze the chitin core of various asparagine (N)-linked glycans and glycoproteins. The endo-beta-N-acetylglucosaminidases have a glycosyl hydrolase family 18 (GH18) catalytic domain. Some members also have an additional C-terminal glycosyl hydrolase family 20 (GH20) domain while others have an N-terminal domain of unknown function (pfam08522). Members of this family include endo-beta-N-acetylglucosaminidase S (EndoS) from Streptococcus pyogenes, EndoF1, EndoF2, EndoF3, and EndoH from Flavobacterium meningosepticum, and EndoE from Enterococcus faecalis. EndoS is a secreted endoglycosidase from Streptococcus pyogenes that specifically hydrolyzes the glycan on human IgG between two core N-acetylglucosamine residues. EndoE is a secreted endoglycosidase, encoded by the ndoE gene in Enterococcus faecalis, that hydrolyzes the glycan on human RNase B.
pfam16141	DUF4849	1.19e-43	37	358	4	316	Putative glycoside hydrolase Family 18, chitinase_18. This DUF is likely to be a form of glycosyl hydrolase from CAZy family 18, possibly chitinase 18. This would have the EC number of EC:3.2.1.14.
pfam05697	Trigger_N	0.006	33	77	5	44	Bacterial trigger factor protein (TF). In the E. coli cytosol, a fraction of the newly synthesized proteins requires the activity of molecular chaperones for folding to the native state. The major chaperones implicated in this folding process are the ribosome-associated Trigger Factor (TF), and the DnaK and GroEL chaperones with their respective co-chaperones. Trigger Factor is an ATP-independent chaperone and displays chaperone and peptidyl-prolyl-cis-trans-isomerase (PPIase) activities in vitro. It is composed of at least three domains, an N-terminal domain which mediates association with the large ribosomal subunit, a central substrate binding and PPIase domain with homology to FKBP proteins, and a C-terminal domain of unknown function. The positioning of TF at the peptide exit channel, together with its ability to interact with nascent chains as short as 57 residues renders TF a prime candidate for being the first chaperone that binds to the nascent polypeptide chains. This family represents the N-terminal region of the protein.

CAZyme Hits help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QUT38382.1	4.03e-185	17	369	14	363
ALJ42200.1	8.12e-185	17	369	14	363
BCA50050.1	8.12e-185	17	369	14	363
AAO76151.1	8.12e-185	17	369	14	363
QQA06635.1	8.12e-185	17	369	14	363

PDB Hits download full data without filtering help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6Q64_A	1.09e-181	17	369	14	363	BT1044SeMetE190Q [Bacteroides thetaiotaomicron]

Swiss-Prot Hits help

has no Swissprot hit.

SignalP and Lipop Annotations help

This protein is predicted as LIPO

Other	SP_Sec_SPI	LIPO_Sec_SPII	TAT_Tat_SPI	TATLIP_Sec_SPII	PILIN_Sec_SPIII
0.000000	0.000011	1.000053	0.000000	0.000000	0.000000

TMHMM Annotations download full data without filtering help

start	end
7	26