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CAZyme Information: MGYG000001560_00405

You are here: Home > Sequence: MGYG000001560_00405

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 Massilioclostridium coli
Lineage Bacteria; Firmicutes_A; Clostridia; Oscillospirales; Ruminococcaceae; Massilioclostridium; Massilioclostridium coli
CAZyme ID MGYG000001560_00405
CAZy Family CBM67
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
1754 MGYG000001560_1|CGC6 191902.14 4.1462
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000001560 2985330 Isolate not provided not provided
Gene Location Start: 491996;  End: 497260  Strand: +

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000001560_00405.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH78 531 1051 2.7e-161 0.996031746031746
CBM67 343 489 2.7e-26 0.7727272727272727
CBM67 167 313 5.2e-21 0.9375

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
pfam17389 Bac_rhamnosid6H 7.87e-114 643 985 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.
pfam08531 Bac_rhamnosid_N 1.44e-42 363 523 3 172
Alpha-L-rhamnosidase N-terminal domain. This family consists of bacterial rhamnosidase A and B enzymes. This domain is probably involved in substrate recognition.
pfam05592 Bac_rhamnosid 8.92e-32 531 639 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.
pfam17390 Bac_rhamnosid_C 9.32e-18 990 1064 2 76
Bacterial alpha-L-rhamnosidase C-terminal 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.
pfam07554 FIVAR 2.14e-05 1432 1494 3 68
FIVAR domain. This domain is found in a wide variety of contexts, but mostly occurring in cell wall associated proteins. A lack of conserved catalytic residues suggests that it is a binding domain. From context, possible substrates are hyaluronate or fibronectin (personal obs: C Yeats). This is further evidenced by. Possibly the exact substrate is N-acetyl glucosamine. Finding it in the same protein as pfam05089 further supports this proposal. It is found in the C-terminal part of Bacillus sp. Gellan lyase, which is removed during maturation. Some of the proteins it is found in are involved in methicillin resistance. The name FIVAR derives from Found In Various Architectures.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
SDT43619.1 1.39e-225 27 1159 44 1146
SDT43572.1 6.79e-213 38 1161 6 1097
QGH33563.1 8.41e-206 21 1173 29 1258
ASQ98318.1 2.39e-202 25 1095 27 1059
AQW48760.1 3.34e-202 25 1095 27 1059

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
3W5M_A 6.08e-194 43 1106 14 1037
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 9.31e-130 328 1052 111 847
Crystalstructure of native alfa-L-rhamnosidase from Aspergillus terreus [Aspergillus terreus]
6I60_A 2.73e-124 20 1095 14 939
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]
6KBJ_A 1.75e-10 164 466 50 331
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]
6T0Q_A 3.63e-10 164 466 30 311
PleurotusOstreatus Lectin (POL), apo form [Pleurotus ostreatus]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
Q82PP4 4.47e-193 43 1095 14 1028
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
T2KNB2 1.78e-140 332 1095 154 920
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
P9WF03 2.19e-120 326 1075 148 902
Alpha-L-rhamnosidase OS=Alteromonas sp. (strain LOR) OX=1537994 GN=LOR_34 PE=1 SV=1
T2KPL4 7.44e-79 41 1064 38 919
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
E8MGH9 7.56e-08 1500 1750 1667 1921
Beta-L-arabinobiosidase OS=Bifidobacterium longum subsp. longum (strain ATCC 15707 / DSM 20219 / JCM 1217 / NCTC 11818 / E194b) OX=565042 GN=hypBA2 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
0.000247 0.999096 0.000184 0.000180 0.000157 0.000142

TMHMM  Annotations      download full data without filtering help

start end
7 29
1731 1750