dbCAN-seq: a database of CAZyme sequence and annotation

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CAZyme Information: MGYG000003528_01822

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Basic Information help

Species

CAAGGB01 sp900769285

Lineage

Bacteria; Verrucomicrobiota; Lentisphaeria; UBA1407; UBA1407; CAAGGB01; CAAGGB01 sp900769285

CAZyme ID

MGYG000003528_01822

CAZy Family

CBM67

CAZyme Description

hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1164		129780.28	7.0974

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000003528	3662993	MAG	Fiji	Oceania

Gene Location

Start: 2158; End: 5652 Strand: +

Full Sequence Download help

Enzyme Prediction help

No EC number prediction in MGYG000003528_01822.

CAZyme Signature Domains help

Family	Start	End	Evalue	family coverage
CBM67	29	169	2e-26	0.9886363636363636

CDD Domains download full data without filtering help

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd09621	CBM9_like_5	2.68e-31	980	1162	1	187	DOMON-like type 9 carbohydrate binding module. Family 9 carbohydrate-binding modules (CBM9) play a role in the microbial degradation of cellulose and hemicellulose (materials found in plants). The domain has previously been called cellulose-binding domain. The polysaccharide binding sites of CBMs with available 3D structure have been found to be either flat surfaces with interactions formed by predominantly aromatic residues (tryptophan and tyrosine), or extended shallow grooves. CBM9 domains found in this uncharacterized heterogeneous subfamily are often located at the C-terminus of longer proteins and may co-occur with various other functional domains such as glycosyl hydrolases. The CBM9 module in these architectures may be involved in binding to carbohydrates.
pfam08531	Bac_rhamnosid_N	2.25e-07	68	161	17	153	Alpha-L-rhamnosidase N-terminal domain. This family consists of bacterial rhamnosidase A and B enzymes. This domain is probably involved in substrate recognition.
cd00241	DOMON_like	2.09e-06	995	1145	3	158	Domon-like ligand-binding domains. DOMON-like domains can be found in all three kindgoms of life and are a diverse group of ligand binding domains that have been shown to interact with sugars and hemes. DOMON domains were initially thought to confer protein-protein interactions. They were subsequently found as a heme-binding motif in cellobiose dehydrogenase, an extracellular fungal oxidoreductase that degrades both lignin and cellulose, and in ethylbenzene dehydrogenase, an enzyme that aids in the anaerobic degradation of hydrocarbons. The domain interacts with sugars in the type 9 carbohydrate binding modules (CBM9), which are present in a variety of glycosyl hydrolases, and it can also be found at the N-terminus of sensor histidine kinases.

CAZyme Hits help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
AHF92778.1	1.97e-225	25	1163	34	1177
AVM46501.1	4.26e-224	7	1164	6	1154
AVM46714.1	7.04e-134	197	1163	26	968
AVM46712.1	1.12e-125	197	1164	75	1012
AVM46271.1	2.55e-124	197	1160	22	962

PDB Hits download full data without filtering help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
3W5M_A	6.09e-16	19	175	129	298	CrystalStructure of Streptomyces avermitilis alpha-L-rhamnosidase [Streptomyces avermitilis MA-4680 = NBRC 14893],3W5N_A Crystal Structure of Streptomyces avermitilis alpha-L-rhamnosidase complexed with L-rhamnose [Streptomyces avermitilis MA-4680 = NBRC 14893]
6T0Q_A	1.16e-07	29	169	199	344	PleurotusOstreatus Lectin (POL), apo form [Pleurotus ostreatus]
6T1D_A	1.18e-07	29	169	202	347	PleurotusOstreatus Lectin (POL), compelx with melibiose [Pleurotus ostreatus],6T1D_B Pleurotus Ostreatus Lectin (POL), compelx with melibiose [Pleurotus ostreatus],6T1D_C Pleurotus Ostreatus Lectin (POL), compelx with melibiose [Pleurotus ostreatus],6T1D_D Pleurotus Ostreatus Lectin (POL), compelx with melibiose [Pleurotus ostreatus],6T1D_E Pleurotus Ostreatus Lectin (POL), compelx with melibiose [Pleurotus ostreatus],6T1D_F Pleurotus Ostreatus Lectin (POL), compelx with melibiose [Pleurotus ostreatus]
6KBJ_A	1.27e-07	29	169	219	364	Structureof Lectin from Pleurotus ostreatus in complex with malonate [Pleurotus ostreatus],6KBQ_A Crystal Structure of Lectin from Pleurotus ostreatus in complex with Glycerol [Pleurotus ostreatus],6KC2_A Crystal Structure of Lectin from Pleurotus ostreatus in complex with Rhamnose [Pleurotus ostreatus],6LI7_A Crystal Structure of Lectin from Pleurotus ostreatus in complex with GalNAc [Pleurotus ostreatus],6LIK_A Crystal Structure of Lectin from Pleurotus ostreatus in complex with Galactose [Pleurotus ostreatus]
4ZN2_A	1.36e-06	485	775	20	330	Glycosylhydrolase from Pseudomonas aeruginosa [Pseudomonas aeruginosa PAO1],4ZN2_B Glycosyl hydrolase from Pseudomonas aeruginosa [Pseudomonas aeruginosa PAO1],4ZN2_C Glycosyl hydrolase from Pseudomonas aeruginosa [Pseudomonas aeruginosa PAO1],4ZN2_D Glycosyl hydrolase from Pseudomonas aeruginosa [Pseudomonas aeruginosa PAO1]

Swiss-Prot Hits download full data without filtering help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
Q82PP4	3.31e-15	19	175	129	298	Alpha-L-rhamnosidase OS=Streptomyces avermitilis (strain ATCC 31267 / DSM 46492 / JCM 5070 / NBRC 14893 / NCIMB 12804 / NRRL 8165 / MA-4680) OX=227882 GN=SAVERM_828 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
0.000206	0.999255	0.000147	0.000144	0.000124	0.000121

TMHMM Annotations help

There is no transmembrane helices in MGYG000003528_01822.