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CAZyme Information: MGYG000001910_00716

You are here: Home > Sequence: MGYG000001910_00716

Basic Information | Genomic context | Full Sequence | Enzyme annotations |  CAZy signature domains |  CDD domains | CAZyme hits | PDB hits | Swiss-Prot hits | SignalP and Lipop annotations | TMHMM annotations

Basic Information help

Species Duncaniella dubosii
Lineage Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Muribaculaceae; Duncaniella; Duncaniella dubosii
CAZyme ID MGYG000001910_00716
CAZy Family CBM67
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
1301 MGYG000001910_6|CGC1 145831.72 6.9767
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000001910 3154435 MAG Denmark Europe
Gene Location Start: 55893;  End: 59798  Strand: +

Full Sequence      Download help

Enzyme Prediction      help

EC 3.2.1.40 3.2.1.-

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH78 359 886 8.9e-154 0.9821428571428571
CBM67 150 328 1.6e-36 0.9261363636363636
GH33 946 1287 1.9e-36 0.9064327485380117

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
pfam17389 Bac_rhamnosid6H 5.88e-125 461 821 1 338
Bacterial alpha-L-rhamnosidase 6 hairpin glycosidase domain. This family consists of bacterial rhamnosidase A and B enzymes. L-Rhamnose is abundant in biomass as a common constituent of glycolipids and glycosides, such as plant pigments, pectic polysaccharides, gums or biosurfactants. Some rhamnosides are important bioactive compounds. For example, terpenyl glycosides, the glycosidic precursor of aromatic terpenoids, act as important flavouring substances in grapes. Other rhamnosides act as cytotoxic rhamnosylated terpenoids, as signal substances in plants or play a role in the antigenicity of pathogenic bacteria.
pfam13088 BNR_2 4.85e-95 963 1284 1 279
BNR repeat-like domain. This family of proteins contains BNR-like repeats suggesting these proteins may act as sialidases.
pfam08531 Bac_rhamnosid_N 2.46e-66 173 347 1 172
Alpha-L-rhamnosidase N-terminal domain. This family consists of bacterial rhamnosidase A and B enzymes. This domain is probably involved in substrate recognition.
cd15482 Sialidase_non-viral 8.74e-48 942 1300 4 339
Non-viral sialidases. Sialidases or neuraminidases function to bind and hydrolyze terminal sialic acid residues from various glycoconjugates, they play vital roles in pathogenesis, bacterial nutrition and cellular interactions. They have a six-bladed, beta-propeller fold with the non-viral sialidases containing 2-5 Asp-box motifs (most commonly Ser/Thr-X-Asp-[X]-Gly-X-Thr- Trp/Phe). This CD includes eubacterial and eukaryotic sialidases.
pfam05592 Bac_rhamnosid 8.49e-28 355 457 1 102
Bacterial alpha-L-rhamnosidase concanavalin-like domain. This family consists of bacterial rhamnosidase A and B enzymes. L-Rhamnose is abundant in biomass as a common constituent of glycolipids and glycosides, such as plant pigments, pectic polysaccharides, gums or biosurfactants. Some rhamnosides are important bioactive compounds. For example, terpenyl glycosides, the glycosidic precursor of aromatic terpenoids, act as important flavouring substances in grapes. Other rhamnosides act as cytotoxic rhamnosylated terpenoids, as signal substances in plants or play a role in the antigenicity of pathogenic bacteria.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
QCD40903.1 0.0 1 1301 1 1301
QUT83571.1 0.0 19 1301 19 1317
ABR40297.1 0.0 19 1301 19 1317
QQY37563.1 0.0 19 1301 22 1320
QUT58579.1 0.0 19 1301 22 1320

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
6I60_A 3.94e-160 27 921 35 938
Structureof alpha-L-rhamnosidase from Dictyoglumus thermophilum [Dictyoglomus thermophilum H-6-12],6I60_B Structure of alpha-L-rhamnosidase from Dictyoglumus thermophilum [Dictyoglomus thermophilum H-6-12]
3W5M_A 3.73e-119 20 930 2 1036
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]
6GSZ_A 2.45e-98 36 889 16 847
Crystalstructure of native alfa-L-rhamnosidase from Aspergillus terreus [Aspergillus terreus]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
T2KNB2 2.40e-139 29 909 41 899
Alpha-L-rhamnosidase OS=Formosa agariphila (strain DSM 15362 / KCTC 12365 / LMG 23005 / KMM 3901 / M-2Alg 35-1) OX=1347342 GN=BN863_22090 PE=1 SV=2
T2KPL4 3.32e-126 34 886 42 904
Alpha-L-rhamnosidase OS=Formosa agariphila (strain DSM 15362 / KCTC 12365 / LMG 23005 / KMM 3901 / M-2Alg 35-1) OX=1347342 GN=BN863_22170 PE=2 SV=1
P9WF03 1.34e-118 30 931 38 917
Alpha-L-rhamnosidase OS=Alteromonas sp. (strain LOR) OX=1537994 GN=LOR_34 PE=1 SV=1
Q82PP4 2.85e-117 20 924 2 1030
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
T2KM26 6.05e-20 43 902 491 1150
Bifunctional sulfatase/alpha-L-rhamnosidase OS=Formosa agariphila (strain DSM 15362 / KCTC 12365 / LMG 23005 / KMM 3901 / M-2Alg 35-1) OX=1347342 GN=BN863_22250 PE=1 SV=2

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
0.000218 0.999211 0.000141 0.000154 0.000134 0.000129

TMHMM  Annotations      download full data without filtering help

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