| Basic Information | |
|---|---|
| Species | Medicago truncatula |
| Cazyme ID | Medtr3g086450.1 |
| Family | GH5 |
| Protein Properties | Length: 656 Molecular Weight: 73121.7 Isoelectric Point: 6.6609 |
| Chromosome | Chromosome/Scaffold: 3 Start: 28440874 End: 28446841 |
| Description | Cellulase (glycosyl hydrolase family 5) protein |
| View CDS | |
| External Links |
|---|
| NCBI Taxonomy |
| Plaza |
| CAZyDB |
| Signature Domain Download full data set without filtering | |||
|---|---|---|---|
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| Family | Start | End | Evalue |
| GH5 | 29 | 341 | 6.7e-39 |
| IVNESEKRVKLACVNWASHLDTSVAEGLSHQPLDVISKGIKSMGFNCVRLTWPLLLLTNDSFASIKVRHSLHNLGLLQSISGIQANNPSIIDLPLIKAYQ TVVKSLGDMDLMVILDNHVTQPGWCCSNSDGNGFFGDQYFDPDLWLMGLTKMATLFNGVTNVVGMSLRNELRGPRQNLNDWYRYMPKGAEVVHAANSNVL VILSGLNFDTDLSFITNQPVKLTFNGKLVFEEHWYSFSDSQAWTLENPNQVCGQVTSSFVRNSGFLLDQGWPLFVSEFGLDLRGKNMNQNRFFNCFMAVA AELDLDWAYWTLS | |||
| Full Sequence |
|---|
| Protein Sequence Length: 656 Download |
| MATMSVMVLL LLSIVRVTAL PLHTNGRWIV NESEKRVKLA CVNWASHLDT SVAEGLSHQP 60 LDVISKGIKS MGFNCVRLTW PLLLLTNDSF ASIKVRHSLH NLGLLQSISG IQANNPSIID 120 LPLIKAYQTV VKSLGDMDLM VILDNHVTQP GWCCSNSDGN GFFGDQYFDP DLWLMGLTKM 180 ATLFNGVTNV VGMSLRNELR GPRQNLNDWY RYMPKGAEVV HAANSNVLVI LSGLNFDTDL 240 SFITNQPVKL TFNGKLVFEE HWYSFSDSQA WTLENPNQVC GQVTSSFVRN SGFLLDQGWP 300 LFVSEFGLDL RGKNMNQNRF FNCFMAVAAE LDLDWAYWTL SGSYYIRQGV VDVDETFGIL 360 NGNWSQVRNT SFLQRISAIQ HPFQGPGLLE SEPYKVIFHP LRGLCVLSKS LHEPLKMGPC 420 SNSDGWEYTP QNILLLKGTK FCLQGEGEGK QVKLGTTCSG PESTWEMISD SKMHLSYNVN 480 NNGSTSSVCL DVDANNIVVT NSCKCISKVN TCDPASQWFK LLGASELKDK IVLLLISKPY 540 PLTMEQLFLL IKNTCDHHLN KRRKDNYKIV WVPSSSDDEP GSTTSSDHVL AELSAMLETD 600 DREEGWVVIG SSSSTDTFRL QGVQGMEFLK ICPKKLPRPS FSCRALQSLF LSSFK* 660 |
| Functional Domains Download unfiltered results here | ||||||||
|---|---|---|---|---|---|---|---|---|
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| Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
| cd00161 | RICIN | 0.004 | 394 | 521 | 138 | + Ricin-type beta-trefoil; Carbohydrate-binding domain formed from presumed gene triplication. The domain is found in a variety of molecules serving diverse functions such as enzymatic activity, inhibitory toxicity and signal transduction. Highly specific ligand binding occurs on exposed surfaces of the compact domain sturcture. | ||
| pfam00150 | Cellulase | 3.0e-13 | 68 | 342 | 284 | + Cellulase (glycosyl hydrolase family 5). | ||
| Gene Ontology | |
|---|---|
| GO Term | Description |
| GO:0004553 | hydrolase activity, hydrolyzing O-glycosyl compounds |
| GO:0005975 | carbohydrate metabolic process |
| Annotations - NR Download unfiltered results here | |||||||
|---|---|---|---|---|---|---|---|
| Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
| GenBank | AAD31066.1 | 0 | 19 | 526 | 2 | 507 | AC007357_15 F3F19.15 [Arabidopsis thaliana] |
| RefSeq | XP_002285424.1 | 0 | 4 | 537 | 13 | 541 | PREDICTED: hypothetical protein [Vitis vinifera] |
| RefSeq | XP_002312657.1 | 0 | 17 | 526 | 7 | 513 | predicted protein [Populus trichocarpa] |
| RefSeq | XP_002315653.1 | 0 | 19 | 526 | 2 | 506 | predicted protein [Populus trichocarpa] |
| RefSeq | XP_002515055.1 | 0 | 16 | 526 | 28 | 535 | hydrolase, hydrolyzing O-glycosyl compounds, putative [Ricinus communis] |
| Annotations - PDB Download unfiltered results here | |||||||
|---|---|---|---|---|---|---|---|
| Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
| PDB | 1vrx_B | 0.00000000002 | 23 | 367 | 7 | 339 | A Chain A, Endocellulase E1 From Acidothermus Cellulolyticus Mutant Y245g |
| PDB | 1vrx_A | 0.00000000002 | 23 | 367 | 7 | 339 | A Chain A, Endocellulase E1 From Acidothermus Cellulolyticus Mutant Y245g |
| PDB | 1ece_B | 0.00000000003 | 23 | 367 | 7 | 339 | A Chain A, Acidothermus Cellulolyticus Endocellulase E1 Catalytic Domain In Complex With A Cellotetraose |
| PDB | 1ece_A | 0.00000000003 | 23 | 367 | 7 | 339 | A Chain A, Acidothermus Cellulolyticus Endocellulase E1 Catalytic Domain In Complex With A Cellotetraose |
| PDB | 4dm1_C | 0.0003 | 29 | 198 | 20 | 168 | A Chain A, Contribution Of Disulfide Bond Toward Thermostability In Hyperthermostable Endocellulase |
