| Basic Information | |
|---|---|
| Species | Eucalyptus grandis |
| Cazyme ID | Eucgr.H02457.1 |
| Family | GH5 |
| Protein Properties | Length: 528 Molecular Weight: 59542.2 Isoelectric Point: 8.2878 |
| Chromosome | Chromosome/Scaffold: 8 Start: 33543622 End: 33545769 |
| Description | Cellulase (glycosyl hydrolase family 5) protein |
| View CDS | |
| External Links |
|---|
| CAZyDB |
| Signature Domain Download full data set without filtering | |||
|---|---|---|---|
 | |||
| Family | Start | End | Evalue |
| GH5 | 38 | 349 | 8.1e-40 |
| IVDKHGHRVKLACVNWASHLEPMVAEGLDKKPVDWISKQIASMGFNCVRLTWPLFMVTNDSLGSMSVAQSFRDLGLVDYIGGIRQNNPSLLDVSVLAAFR AVVTSLGDNSVMVILDNHISKPGWCCSNRDGNGFFGDQYFDPNLWIKGLTRMATMIRRIGNVVGMSLRNELRGPKENLRDWLRYMERGAEVVHSANPHVL VIASGLYYDTDLWFLGHIPMKVSFARKLVFELHWYASSSGTVWEDGNTNERCKDATDKVMSKAGFILNQGMPLFVSEFGGELSGQNVNDDRYFNCFFGVA AKLDFDWALWTI | |||
| Full Sequence |
|---|
| Protein Sequence Length: 528 Download |
| MRRRPSYLCF IALWALVASQ HAEPAKASWR LHTESRWIVD KHGHRVKLAC VNWASHLEPM 60 VAEGLDKKPV DWISKQIASM GFNCVRLTWP LFMVTNDSLG SMSVAQSFRD LGLVDYIGGI 120 RQNNPSLLDV SVLAAFRAVV TSLGDNSVMV ILDNHISKPG WCCSNRDGNG FFGDQYFDPN 180 LWIKGLTRMA TMIRRIGNVV GMSLRNELRG PKENLRDWLR YMERGAEVVH SANPHVLVIA 240 SGLYYDTDLW FLGHIPMKVS FARKLVFELH WYASSSGTVW EDGNTNERCK DATDKVMSKA 300 GFILNQGMPL FVSEFGGELS GQNVNDDRYF NCFFGVAAKL DFDWALWTIV GSYYLRKGIV 360 GMEETFGVLN KDFSGPRNAS FLQRISALQA PFQGATSSSP TRRILFHPLT GLCIQRKREQ 420 EQLQLGACNE SEAWTHTRHH TIRMRGTDLC MQADRLEKPV KLSTDCADHG SRWKTISESK 480 MHFSSNIVGS NVTVCLDIDF STKTVIASPC KCLREDATCN PASQWFEL |
| Functional Domains Download unfiltered results here | ||||||||
|---|---|---|---|---|---|---|---|---|
 | ||||||||
| Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
| cd00161 | RICIN | 0.0004 | 406 | 510 | 117 | + 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. | ||
| smart00458 | RICIN | 8.0e-5 | 406 | 525 | 128 | + Ricin-type beta-trefoil. Carbohydrate-binding domain formed from presumed gene triplication. | ||
| pfam00150 | Cellulase | 1.0e-11 | 75 | 349 | 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 | 28 | 528 | 2 | 502 | AC007357_15 F3F19.15 [Arabidopsis thaliana] |
| RefSeq | XP_002285424.1 | 0 | 31 | 528 | 29 | 525 | PREDICTED: hypothetical protein [Vitis vinifera] |
| RefSeq | XP_002312657.1 | 0 | 31 | 528 | 12 | 508 | predicted protein [Populus trichocarpa] |
| RefSeq | XP_002315653.1 | 0 | 31 | 528 | 5 | 501 | predicted protein [Populus trichocarpa] |
| RefSeq | XP_002515055.1 | 0 | 31 | 528 | 34 | 530 | 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 | 0.0000000000009 | 32 | 319 | 7 | 287 | A Chain A, Endocellulase E1 From Acidothermus Cellulolyticus Mutant Y245g |
| PDB | 1vrx_A | 0.0000000000009 | 32 | 319 | 7 | 287 | A Chain A, Endocellulase E1 From Acidothermus Cellulolyticus Mutant Y245g |
| PDB | 1ece_B | 0.000000000006 | 32 | 319 | 7 | 287 | A Chain A, Acidothermus Cellulolyticus Endocellulase E1 Catalytic Domain In Complex With A Cellotetraose |
| PDB | 1ece_A | 0.000000000006 | 32 | 319 | 7 | 287 | A Chain A, Acidothermus Cellulolyticus Endocellulase E1 Catalytic Domain In Complex With A Cellotetraose |
| PDB | 3axx_C | 0.00005 | 46 | 318 | 61 | 346 | A Chain A, Functional Analysis Of Hyperthermophilic Endocellulase From The Archaeon Pyrococcus Horikoshii |
