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CAZyme Information: MGYG000000442_02448

You are here: Home > Sequence: MGYG000000442_02448

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 CAG-462 sp003489705
Lineage Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; CAG-462; CAG-462 sp003489705
CAZyme ID MGYG000000442_02448
CAZy Family CBM67
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
1282 144731.16 7.2801
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000000442 3125088 MAG Sweden Europe
Gene Location Start: 22557;  End: 26405  Strand: +

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000000442_02448.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH78 357 884 7.5e-160 0.9861111111111112
GH33 951 1268 9.4e-37 0.8801169590643275
CBM67 149 327 4.1e-32 0.9431818181818182

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
pfam17389 Bac_rhamnosid6H 1.07e-122 461 817 3 338
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 1.58e-99 959 1266 1 280
BNR repeat-like domain. This family of proteins contains BNR-like repeats suggesting these proteins may act as sialidases.
pfam08531 Bac_rhamnosid_N 2.82e-61 175 344 3 171
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 7.40e-52 938 1281 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 1.08e-32 357 455 6 102
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
AND21950.1 0.0 21 1282 20 1317
QUT83571.1 0.0 21 1282 20 1317
QJR76251.1 0.0 21 1282 23 1320
QJR72182.1 0.0 21 1282 23 1320
QUT58579.1 0.0 21 1282 23 1320

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
6I60_A 9.75e-179 31 909 38 915
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 5.13e-131 36 922 17 1032
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 1.44e-108 35 885 14 847
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 4.82e-133 29 916 40 918
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 3.40e-132 19 921 26 950
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
Q82PP4 4.04e-130 36 920 17 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
P9WF03 3.89e-121 31 927 38 917
Alpha-L-rhamnosidase OS=Alteromonas sp. (strain LOR) OX=1537994 GN=LOR_34 PE=1 SV=1
T2KM26 4.05e-15 433 791 700 1047
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
0.109240 0.659374 0.230036 0.000639 0.000335 0.000331

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000000442_02448.