| Basic Information | |
|---|---|
| Species | Eucalyptus grandis |
| Cazyme ID | Eucgr.D01800.1 |
| Family | GH5 |
| Protein Properties | Length: 539 Molecular Weight: 60311.5 Isoelectric Point: 6.9571 |
| Chromosome | Chromosome/Scaffold: 4 Start: 31987798 End: 31990681 |
| Description | Cellulase (glycosyl hydrolase family 5) protein |
| View CDS | |
| External Links |
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| CAZyDB |
| Signature Domain Download full data set without filtering | |||
|---|---|---|---|
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| Family | Start | End | Evalue |
| GH5 | 41 | 353 | 7.5e-40 |
| ATGRRMKLACVNWASHLEPMLAEGLDKKPLGVIVAEIRRLRFNCVRLTWATYMFTQPGHGDQPVEETLDSLGLAEAKGGVARNNPLVLNMTHVEAYAAVV DELGKQGVMVVLDNHVSKPKWCCAYDDGNGFFGDEYFDPEEWLRGLVAVAEHFNGKSQVVGMSVRNELRGPRQNDYDWYQYIRTAATKVHQANPNVLVIL SGLNWASDLSFLRKRPVGLSLGRKLVYEAHWYSFSGDRKIWEVQPVDRVCANAVQRMEDQAGFLSSGPGAVPLFLGEFGFDQTGKSQADDRFLSCFMGYA AGKDLDWALWALQ | |||
| Full Sequence |
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| Protein Sequence Length: 539 Download |
| MPFSSSQASL VLFLFLLLVL SINFTSPLPL STNGRWIVDS ATGRRMKLAC VNWASHLEPM 60 LAEGLDKKPL GVIVAEIRRL RFNCVRLTWA TYMFTQPGHG DQPVEETLDS LGLAEAKGGV 120 ARNNPLVLNM THVEAYAAVV DELGKQGVMV VLDNHVSKPK WCCAYDDGNG FFGDEYFDPE 180 EWLRGLVAVA EHFNGKSQVV GMSVRNELRG PRQNDYDWYQ YIRTAATKVH QANPNVLVIL 240 SGLNWASDLS FLRKRPVGLS LGRKLVYEAH WYSFSGDRKI WEVQPVDRVC ANAVQRMEDQ 300 AGFLSSGPGA VPLFLGEFGF DQTGKSQADD RFLSCFMGYA AGKDLDWALW ALQGSYYYRQ 360 GVVGPEETFG VLDFNWDGLR NPKFKERFQL VQTMVQDPSS NSPMSYIMYH PQSGLCIRAN 420 NNHEIGTAEC QHWSRWIHYR DGSPIRLMGT PLCLKALGDG LPPVLSNDCS NRRSAWRSIS 480 NSKLHVAATD EHGNRLCLEK KSNESSVILT RKCICVDDDS GCTENPQGQW FKFVPTNT* 540 |
| Functional Domains Download unfiltered results here | ||||||||
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| Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
| smart00458 | RICIN | 0.005 | 413 | 530 | 125 | + Ricin-type beta-trefoil. Carbohydrate-binding domain formed from presumed gene triplication. | ||
| pfam00227 | Proteasome | 0.003 | 226 | 327 | 104 | + Proteasome subunit. The proteasome is a multisubunit structure that degrades proteins. Protein degradation is an essential component of regulation because proteins can become misfolded, damaged, or unnecessary. Proteasomes and their homologues vary greatly in complexity: from HslV (heat shock locus v), which is encoded by 1 gene in bacteria, to the eukaryotic 20S proteasome, which is encoded by more than 14 genes. Recently evidence of two novel groups of bacterial proteasomes was proposed. The first is Anbu, which is sparsely distributed among cyanobacteria and proteobacteria. The second is call beta-proteobacteria proteasome homologue (BPH). | ||
| pfam00150 | Cellulase | 9.0e-11 | 118 | 352 | 246 | + 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 |
| EMBL | CBI34404.1 | 0 | 7 | 537 | 20 | 559 | unnamed protein product [Vitis vinifera] |
| RefSeq | XP_002272386.1 | 0 | 9 | 537 | 5 | 530 | PREDICTED: hypothetical protein [Vitis vinifera] |
| RefSeq | XP_002272534.1 | 0 | 7 | 537 | 4 | 543 | PREDICTED: hypothetical protein [Vitis vinifera] |
| RefSeq | XP_002509877.1 | 0 | 11 | 537 | 5 | 545 | hydrolase, hydrolyzing O-glycosyl compounds, putative [Ricinus communis] |
| RefSeq | XP_002509879.1 | 0 | 33 | 537 | 30 | 534 | 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 | 0.0000000000005 | 32 | 351 | 8 | 320 | A Chain A, Endocellulase E1 From Acidothermus Cellulolyticus Mutant Y245g |
| PDB | 1vrx_A | 0.0000000000005 | 32 | 351 | 8 | 320 | A Chain A, Endocellulase E1 From Acidothermus Cellulolyticus Mutant Y245g |
| PDB | 1ece_B | 0.0000000000009 | 32 | 351 | 8 | 320 | A Chain A, Acidothermus Cellulolyticus Endocellulase E1 Catalytic Domain In Complex With A Cellotetraose |
| PDB | 1ece_A | 0.0000000000009 | 32 | 351 | 8 | 320 | A Chain A, Acidothermus Cellulolyticus Endocellulase E1 Catalytic Domain In Complex With A Cellotetraose |
| PDB | 4dm1_C | 0.001 | 38 | 272 | 20 | 266 | A Chain A, Contribution Of Disulfide Bond Toward Thermostability In Hyperthermostable Endocellulase |
