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CAZyme Information: MGYG000003252_04411

You are here: Home > Sequence: MGYG000003252_04411

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 Bacteroides sp900761785
Lineage Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; Bacteroides; Bacteroides sp900761785
CAZyme ID MGYG000003252_04411
CAZy Family CBM67
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
1286 MGYG000003252_424|CGC2 145443.16 8.1761
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000003252 8296673 MAG United States North America
Gene Location Start: 45986;  End: 49846  Strand: -

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000003252_04411.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH78 354 884 7.4e-164 0.9880952380952381
GH33 918 1269 6.9e-38 0.9093567251461988
CBM67 141 325 7.6e-38 0.9431818181818182

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
pfam17389 Bac_rhamnosid6H 1.64e-149 456 817 1 340
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 2.64e-99 936 1266 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 2.06e-78 172 343 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 4.01e-47 915 1282 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 1.43e-39 351 451 1 101
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
QIU95828.1 0.0 1 1286 1 1288
QDH55645.1 0.0 1 1286 1 1286
QUT23583.1 0.0 1 1286 1 1286
QUT29077.1 0.0 1 1286 1 1286
QUR43127.1 0.0 1 1286 1 1286

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
6I60_A 4.18e-188 26 885 34 899
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 2.11e-133 20 892 2 1002
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 7.20e-107 22 901 2 865
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 1.49e-147 30 914 42 905
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 9.66e-136 2 910 4 933
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 8.58e-133 20 892 2 1002
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 6.26e-131 25 885 32 879
Alpha-L-rhamnosidase OS=Alteromonas sp. (strain LOR) OX=1537994 GN=LOR_34 PE=1 SV=1
T2KM26 1.76e-19 23 886 468 1138
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
0.043827 0.954635 0.000651 0.000299 0.000263 0.000294

TMHMM  Annotations      download full data without filtering help

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