You are browsing environment: HUMAN GUT
CAZyme Information: MGYG000002832_00118
You are here: Home > Sequence: MGYG000002832_00118
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 | Prevotella sp900548195 | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Lineage | Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; Prevotella; Prevotella sp900548195 | |||||||||||
| CAZyme ID | MGYG000002832_00118 | |||||||||||
| CAZy Family | GH53 | |||||||||||
| CAZyme Description | hypothetical protein | |||||||||||
| CAZyme Property |
|
|||||||||||
| Genome Property |
|
|||||||||||
| Gene Location | Start: 7226; End: 8962 Strand: + | |||||||||||
CAZyme Signature Domains help
| Family | Start | End | Evalue | family coverage |
|---|---|---|---|---|
| GH53 | 26 | 346 | 2e-92 | 0.9035087719298246 |
CDD Domains download full data without filtering help
| Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
|---|---|---|---|---|---|---|---|
| pfam07745 | Glyco_hydro_53 | 2.61e-88 | 26 | 363 | 3 | 333 | Glycosyl hydrolase family 53. This domain belongs to family 53 of the glycosyl hydrolase classification. These enzymes are enzymes are endo-1,4- beta-galactanases (EC:3.2.1.89). The structure of this domain is known and has a TIM barrel fold. |
| COG3867 | GanB | 3.46e-83 | 17 | 345 | 33 | 349 | Arabinogalactan endo-1,4-beta-galactosidase [Carbohydrate transport and metabolism]. |
| pfam00160 | Pro_isomerase | 9.68e-46 | 380 | 574 | 1 | 150 | Cyclophilin type peptidyl-prolyl cis-trans isomerase/CLD. The peptidyl-prolyl cis-trans isomerases, also known as cyclophilins, share this domain of about 109 amino acids. Cyclophilins have been found in all organisms studied so far and catalyze peptidyl-prolyl isomerisation during which the peptide bond preceding proline (the peptidyl-prolyl bond) is stabilized in the cis conformation. Mammalian cyclophilin A (CypA) is a major cellular target for the immunosuppressive drug cyclosporin A (CsA). Other roles for cyclophilins may include chaperone and cell signalling function. |
| cd00317 | cyclophilin | 6.04e-43 | 383 | 573 | 2 | 146 | cyclophilin: cyclophilin-type peptidylprolyl cis- trans isomerases. This family contains eukaryotic, bacterial and archeal proteins which exhibit a peptidylprolyl cis- trans isomerases activity (PPIase, Rotamase) and in addition bind the immunosuppressive drug cyclosporin (CsA). Immunosuppression in vertebrates is believed to be the result of the cyclophilin A-cyclosporin protein drug complex binding to and inhibiting the protein-phosphatase calcineurin. PPIase is an enzyme which accelerates protein folding by catalyzing the cis-trans isomerization of the peptide bonds preceding proline residues. Cyclophilins are a diverse family in terms of function and have been implicated in protein folding processes which depend on catalytic /chaperone-like activities. This group contains human cyclophilin 40, a co-chaperone of the hsp90 chaperone system; human cyclophilin A, a chaperone in the HIV-1 infectious process and; human cyclophilin H, a component of the U4/U6 snRNP, whose isomerization or chaperoning activities may play a role in RNA splicing. |
| COG0652 | PpiB | 1.78e-42 | 381 | 577 | 2 | 157 | Peptidyl-prolyl cis-trans isomerase (rotamase) - cyclophilin family [Posttranslational modification, protein turnover, chaperones]. |
CAZyme Hits help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
|---|---|---|---|---|---|
| QJR97948.1 | 8.28e-248 | 20 | 577 | 10 | 573 |
| ALJ58554.1 | 1.07e-133 | 22 | 362 | 44 | 392 |
| QUT90339.1 | 1.07e-133 | 22 | 362 | 44 | 392 |
| AVM53779.1 | 3.03e-133 | 19 | 362 | 41 | 391 |
| QDO71220.1 | 8.57e-133 | 22 | 362 | 44 | 392 |
PDB Hits download full data without filtering help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| 6GPA_A | 4.23e-87 | 21 | 362 | 5 | 312 | Beta-1,4-galactanasefrom Bacteroides thetaiotaomicron with galactose [Bacteroides thetaiotaomicron VPI-5482],6GPA_B Beta-1,4-galactanase from Bacteroides thetaiotaomicron with galactose [Bacteroides thetaiotaomicron VPI-5482] |
| 6GP5_A | 1.40e-86 | 21 | 362 | 41 | 348 | Beta-1,4-galactanasefrom Bacteroides thetaiotaomicron [Bacteroides thetaiotaomicron VPI-5482],6GP5_B Beta-1,4-galactanase from Bacteroides thetaiotaomicron [Bacteroides thetaiotaomicron VPI-5482] |
| 7OSK_A | 6.29e-38 | 22 | 336 | 49 | 352 | ChainA, Arabinogalactan endo-1,4-beta-galactosidase [Ignisphaera aggregans DSM 17230],7OSK_B Chain B, Arabinogalactan endo-1,4-beta-galactosidase [Ignisphaera aggregans DSM 17230] |
| 1R8L_A | 6.19e-36 | 17 | 342 | 18 | 326 | Thestructure of endo-beta-1,4-galactanase from Bacillus licheniformis [Bacillus licheniformis],1R8L_B The structure of endo-beta-1,4-galactanase from Bacillus licheniformis [Bacillus licheniformis],1UR0_A The structure of endo-beta-1,4-galactanase from Bacillus licheniformis in complex with two oligosaccharide products. [Bacillus licheniformis],1UR0_B The structure of endo-beta-1,4-galactanase from Bacillus licheniformis in complex with two oligosaccharide products. [Bacillus licheniformis],1UR4_A The structure of endo-beta-1,4-galactanase from Bacillus licheniformis in complex with two oligosaccharide products. [Bacillus licheniformis],1UR4_B The structure of endo-beta-1,4-galactanase from Bacillus licheniformis in complex with two oligosaccharide products. [Bacillus licheniformis],2CCR_A Structure of Beta-1,4-Galactanase [Bacillus licheniformis],2CCR_B Structure of Beta-1,4-Galactanase [Bacillus licheniformis],2J74_A Structure of Beta-1,4-Galactanase [Bacillus licheniformis],2J74_B Structure of Beta-1,4-Galactanase [Bacillus licheniformis] |
| 2GFT_A | 4.08e-35 | 17 | 342 | 18 | 326 | ChainA, Glycosyl Hydrolase Family 53 [Bacillus licheniformis],2GFT_B Chain B, Glycosyl Hydrolase Family 53 [Bacillus licheniformis] |
Swiss-Prot Hits download full data without filtering help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| P48843 | 1.59e-47 | 21 | 368 | 4 | 352 | Uncharacterized protein in bgaB 5'region (Fragment) OS=Niallia circulans OX=1397 PE=3 SV=1 |
| Q65CX5 | 5.26e-35 | 17 | 342 | 43 | 351 | Endo-beta-1,4-galactanase OS=Bacillus licheniformis (strain ATCC 14580 / DSM 13 / JCM 2505 / CCUG 7422 / NBRC 12200 / NCIMB 9375 / NCTC 10341 / NRRL NRS-1264 / Gibson 46) OX=279010 GN=ganB PE=1 SV=1 |
| O07013 | 7.83e-35 | 19 | 342 | 49 | 355 | Endo-beta-1,4-galactanase OS=Bacillus subtilis (strain 168) OX=224308 GN=ganB PE=1 SV=1 |
| Q4WJ80 | 2.30e-33 | 3 | 338 | 4 | 321 | Probable arabinogalactan endo-beta-1,4-galactanase A OS=Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) OX=330879 GN=galA PE=3 SV=2 |
| A1D3T4 | 8.09e-33 | 3 | 338 | 4 | 321 | Probable arabinogalactan endo-beta-1,4-galactanase A OS=Neosartorya fischeri (strain ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164 / JCM 1740 / NRRL 181 / WB 181) OX=331117 GN=galA PE=3 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 |
|---|---|---|---|---|---|
| 0.000621 | 0.537669 | 0.460909 | 0.000307 | 0.000258 | 0.000220 |