dbCAN-seq: a database of CAZyme sequence and annotation

Basic Information help

Species

Haloferax massiliensis

Lineage

Archaea; Halobacteriota; Halobacteria; Halobacteriales; Haloferacaceae; Haloferax; Haloferax massiliensis

CAZyme ID

MGYG000001639_03264

CAZy Family

GH16

CAZyme Description

hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
588		63120.3	3.8527

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001639	3991467	Isolate	not provided	not provided

Gene Location

Start: 202821; End: 204587 Strand: -

Enzyme Prediction help

No EC number prediction in MGYG000001639_03264.

CAZyme Signature Domains help

Family	Start	End	Evalue	family coverage
GH16	66	291	3.1e-31	0.9841269841269841

CDD Domains download full data without filtering help

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd08023	GH16_laminarinase_like	1.19e-29	65	291	1	235	Laminarinase, member of the glycosyl hydrolase family 16. Laminarinase, also known as glucan endo-1,3-beta-D-glucosidase, is a glycosyl hydrolase family 16 member that hydrolyzes 1,3-beta-D-glucosidic linkages in 1,3-beta-D-glucans such as laminarins, curdlans, paramylons, and pachymans, with very limited action on mixed-link (1,3-1,4-)-beta-D-glucans.
cd00413	Glyco_hydrolase_16	4.58e-26	67	291	1	210	glycosyl hydrolase family 16. The O-Glycosyl hydrolases are a widespread group of enzymes that hydrolyse the glycosidic bond between two or more carbohydrates, or between a carbohydrate and a non-carbohydrate moiety. A glycosyl hydrolase classification system based on sequence similarity has led to the definition of more than 95 different families inlcuding glycosyl hydrolase family 16. Family 16 includes lichenase, xyloglucan endotransglycosylase (XET), beta-agarase, kappa-carrageenase, endo-beta-1,3-glucanase, endo-beta-1,3-1,4-glucanase, and endo-beta-galactosidase, all of which have a conserved jelly roll fold with a deep active site channel harboring the catalytic residues.
cd02178	GH16_beta_agarase	2.63e-24	56	291	14	257	Beta-agarase, member of glycosyl hydrolase family 16. Beta-agarase is a glycosyl hydrolase family 16 (GH16) member that hydrolyzes the internal beta-1,4-linkage of agarose, a hydrophilic polysaccharide found in the cell wall of Rhodophyceaea, marine red algae. Agarose is a linear chain of galactose units linked by alternating L-alpha-1,3- and D-beta-1,4-linkages that are additionally modified by a 3,6-anhydro-bridge. Agarose forms thermo-reversible gels that are widely used in the food industry or as a laboratory medium. While beta-agarases are also found in two other families derived from the sequence-based classification of glycosyl hydrolases (GH50, and GH86) the GH16 members are most abundant. This domain adopts a curved beta-sandwich conformation, with a tunnel-shaped active site cavity, referred to as a jellyroll fold.
COG2273	BglS	2.64e-17	47	289	27	261	Beta-glucanase, GH16 family [Carbohydrate transport and metabolism].
pfam00722	Glyco_hydro_16	3.94e-14	100	250	5	134	Glycosyl hydrolases family 16.

CAZyme Hits help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QCJ47429.1	3.34e-139	2	587	3	598
AGB39278.1	8.51e-30	46	297	41	307
ATW88142.1	1.58e-26	61	290	15	261
QNU67712.1	2.67e-21	55	297	356	596
QSG01745.1	1.32e-20	29	294	18	286

PDB Hits download full data without filtering help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
2VY0_A	4.27e-17	60	291	12	259	TheX-ray structure of endo-beta-1,3-glucanase from Pyrococcus furiosus [Pyrococcus furiosus],2VY0_B The X-ray structure of endo-beta-1,3-glucanase from Pyrococcus furiosus [Pyrococcus furiosus]
4DFS_A	2.61e-09	59	292	16	263	Structureof the catalytic domain of an endo-1,3-beta-glucanase (laminarinase) from Thermotoga petrophila RKU-1 [Thermotoga petrophila RKU-1],4DFS_B Structure of the catalytic domain of an endo-1,3-beta-glucanase (laminarinase) from Thermotoga petrophila RKU-1 [Thermotoga petrophila RKU-1]
3AZX_A	4.94e-09	59	291	8	254	Crystalstructure of the laminarinase catalytic domain from Thermotoga maritima MSB8 [Thermotoga maritima MSB8],3AZX_B Crystal structure of the laminarinase catalytic domain from Thermotoga maritima MSB8 [Thermotoga maritima MSB8],3AZY_A Crystal structure of the laminarinase catalytic domain from Thermotoga maritima MSB8 [Thermotoga maritima MSB8],3AZY_B Crystal structure of the laminarinase catalytic domain from Thermotoga maritima MSB8 [Thermotoga maritima MSB8],3AZY_C Crystal structure of the laminarinase catalytic domain from Thermotoga maritima MSB8 [Thermotoga maritima MSB8],3AZY_D Crystal structure of the laminarinase catalytic domain from Thermotoga maritima MSB8 [Thermotoga maritima MSB8],3AZZ_A Crystal structure of the laminarinase catalytic domain from Thermotoga maritima MSB8 in complex with gluconolactone [Thermotoga maritima MSB8],3AZZ_B Crystal structure of the laminarinase catalytic domain from Thermotoga maritima MSB8 in complex with gluconolactone [Thermotoga maritima MSB8],3AZZ_C Crystal structure of the laminarinase catalytic domain from Thermotoga maritima MSB8 in complex with gluconolactone [Thermotoga maritima MSB8],3AZZ_D Crystal structure of the laminarinase catalytic domain from Thermotoga maritima MSB8 in complex with gluconolactone [Thermotoga maritima MSB8],3B00_A Crystal structure of the laminarinase catalytic domain from Thermotoga maritima MSB8 in complex with cetyltrimethylammonium bromide [Thermotoga maritima MSB8],3B00_B Crystal structure of the laminarinase catalytic domain from Thermotoga maritima MSB8 in complex with cetyltrimethylammonium bromide [Thermotoga maritima MSB8],3B00_C Crystal structure of the laminarinase catalytic domain from Thermotoga maritima MSB8 in complex with cetyltrimethylammonium bromide [Thermotoga maritima MSB8],3B00_D Crystal structure of the laminarinase catalytic domain from Thermotoga maritima MSB8 in complex with cetyltrimethylammonium bromide [Thermotoga maritima MSB8],3B01_A Crystal structure of the laminarinase catalytic domain from Thermotoga maritima MSB8 [Thermotoga maritima MSB8],3B01_B Crystal structure of the laminarinase catalytic domain from Thermotoga maritima MSB8 [Thermotoga maritima MSB8],3B01_C Crystal structure of the laminarinase catalytic domain from Thermotoga maritima MSB8 [Thermotoga maritima MSB8],3B01_D Crystal structure of the laminarinase catalytic domain from Thermotoga maritima MSB8 [Thermotoga maritima MSB8]
3I4I_A	5.88e-09	72	246	29	190	Crystalstructure of a prokaryotic beta-1,3-1,4-glucanase (lichenase) derived from a mouse hindgut metagenome [uncultured murine large bowel bacterium BAC 14],3I4I_B Crystal structure of a prokaryotic beta-1,3-1,4-glucanase (lichenase) derived from a mouse hindgut metagenome [uncultured murine large bowel bacterium BAC 14]
6T2R_AAA	1.10e-08	60	289	28	259	ChainAAA, Beta-glycosidase [Bacteroides caccae]

Swiss-Prot Hits download full data without filtering help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P23903	3.08e-12	63	291	425	679	Glucan endo-1,3-beta-glucosidase A1 OS=Niallia circulans OX=1397 GN=glcA PE=1 SV=1
O33680	5.38e-09	137	291	320	457	Endo-1,3-1,4-beta-glycanase ExsH OS=Rhizobium meliloti (strain 1021) OX=266834 GN=exsH PE=1 SV=1
P37073	1.32e-08	72	289	46	248	Beta-glucanase OS=Brevibacillus brevis OX=1393 GN=bglBB PE=1 SV=1
P33693	1.52e-07	64	293	37	233	Endo-1,3-1,4-beta-glycanase ExoK OS=Rhizobium meliloti (strain 1021) OX=266834 GN=exoK PE=1 SV=1
Q9Z3Q2	2.04e-07	75	291	257	457	Endo-1,3-1,4-beta-glycanase EglC OS=Rhizobium meliloti (strain 1021) OX=266834 GN=eglC PE=3 SV=2

SignalP and Lipop Annotations help

This protein is predicted as TAT

Other	SP_Sec_SPI	LIPO_Sec_SPII	TAT_Tat_SPI	TATLIP_Sec_SPII	PILIN_Sec_SPIII
0.000003	0.000003	0.000001	0.993620	0.006357	0.000000

TMHMM Annotations help

There is no transmembrane helices in MGYG000001639_03264.

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