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CAZyme Information: MGYG000001560_01334
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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_01334 | |||||||||||
| CAZy Family | CBM67 | |||||||||||
| CAZyme Description | hypothetical protein | |||||||||||
| CAZyme Property |
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| Genome Property |
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| Gene Location | Start: 1593155; End: 1597117 Strand: - | |||||||||||
CAZyme Signature Domains help
| Family | Start | End | Evalue | family coverage |
|---|---|---|---|---|
| GH78 | 501 | 1006 | 3.5e-58 | 0.8948412698412699 |
| CBM67 | 43 | 234 | 3e-29 | 0.9772727272727273 |
CDD Domains download full data without filtering help
| Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
|---|---|---|---|---|---|---|---|
| pfam17389 | Bac_rhamnosid6H | 7.94e-11 | 597 | 941 | 8 | 331 | 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. |
| pfam07554 | FIVAR | 2.07e-05 | 1202 | 1261 | 3 | 69 | 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. |
| pfam07554 | FIVAR | 7.91e-04 | 1061 | 1123 | 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. |
| COG1196 | Smc | 8.08e-04 | 1054 | 1258 | 333 | 536 | Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning]. |
| pfam02837 | Glyco_hydro_2_N | 0.002 | 67 | 148 | 69 | 144 | Glycosyl hydrolases family 2, sugar binding domain. This family contains beta-galactosidase, beta-mannosidase and beta-glucuronidase activities and has a jelly-roll fold. The domain binds the sugar moiety during the sugar-hydrolysis reaction. |
CAZyme Hits help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
|---|---|---|---|---|---|
| QEV28934.1 | 5.64e-121 | 1 | 1054 | 1 | 798 |
| QYX75380.1 | 3.31e-117 | 12 | 1026 | 12 | 758 |
| QJT00118.1 | 1.74e-112 | 1 | 1058 | 1 | 802 |
| AVV47733.1 | 3.93e-112 | 26 | 1058 | 1 | 777 |
| AXE90460.1 | 5.77e-111 | 43 | 1054 | 42 | 798 |
PDB Hits download full data without filtering help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| 2OKX_A | 1.21e-13 | 39 | 968 | 5 | 894 | Crystalstructure of GH78 family rhamnosidase of Bacillus SP. GL1 AT 1.9 A [Bacillus sp. GL1],2OKX_B Crystal structure of GH78 family rhamnosidase of Bacillus SP. GL1 AT 1.9 A [Bacillus sp. GL1] |
| 6I60_A | 1.06e-12 | 495 | 1051 | 384 | 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] |
| 3CIH_A | 3.92e-06 | 605 | 1032 | 314 | 712 | Crystalstructure of a putative alpha-rhamnosidase from Bacteroides thetaiotaomicron [Bacteroides thetaiotaomicron VPI-5482] |
Swiss-Prot Hits download full data without filtering help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| E8MGH9 | 5.38e-08 | 1088 | 1315 | 1694 | 1920 | 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 |
|---|---|---|---|---|---|
| 0.000294 | 0.998907 | 0.000190 | 0.000255 | 0.000179 | 0.000151 |
