| Basic Information | |
|---|---|
| Species | Picea abies |
| Cazyme ID | MA_318998g0010 |
| Family | GH5 |
| Protein Properties | Length: 542 Molecular Weight: 59481.9 Isoelectric Point: 7.0553 |
| View CDS | |
| Signature Domain Download full data set without filtering | |||
|---|---|---|---|
 | |||
| Family | Start | End | Evalue |
| GH5 | 35 | 351 | 6.50062e-42 |
| IVDENGSRVKLACVNWASHVDIMVAEGLNKKPVDEITVNIRAMGFNCVRLTWSLYMFTNPSLGAMTMRKSLRKLNLSDAEVGVAANNPDLLDLPVVEVYK RVVSSLGASGVMAILDNHISRPGWCCGNTDGNGFFGDRDFEPDTWIKGLISVASMFNGTDQVVGMSLRNELRGPKQNQNDWYKYMQKGAEAVHRANPNVL VILSGLSFDTDLIFLSQRPVSLAFKEKLVFELHWYAFSDGQAWANGNPNHICGSVTSRVVSRGGFLITPNETYTAPLFFSEFGIDQRGSNVNDNRYINCF LAFAAGNDLDWAYWALQ | |||
| Full Sequence |
|---|
| Protein Sequence Length: 542 Download |
| MAMALQSVKA LALLLLLVSL QKSTSSPLYA SSRWIVDENG SRVKLACVNW ASHVDIMVAE 60 GLNKKPVDEI TVNIRAMGFN CVRLTWSLYM FTNPSLGAMT MRKSLRKLNL SDAEVGVAAN 120 NPDLLDLPVV EVYKRVVSSL GASGVMAILD NHISRPGWCC GNTDGNGFFG DRDFEPDTWI 180 KGLISVASMF NGTDQVVGMS LRNELRGPKQ NQNDWYKYMQ KGAEAVHRAN PNVLVILSGL 240 SFDTDLIFLS QRPVSLAFKE KLVFELHWYA FSDGQAWANG NPNHICGSVT SRVVSRGGFL 300 ITPNETYTAP LFFSEFGIDQ RGSNVNDNRY INCFLAFAAG NDLDWAYWAL QGSYYIRSGI 360 PALDETYGIL NGEWSQPRNS SFLSRLSFIQ QPFQGPGLSE RSPYKLIYHP ATGLCLQRCS 420 LFGLDIRLGP CTEAESWDYT PQGNIVLKGT LFCVEAVGLG KAARLGMFCM GDNTQWSTIS 480 DSNLHLSAKL ENGTTVCLDG SSIPSVVTNK CKCLSGDSSC DPGSQWFKIV TTTRSLSLVS 540 GV |
| Functional Domains Download unfiltered results here | ||||||||
|---|---|---|---|---|---|---|---|---|
 | ||||||||
| Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
| smart00458 | RICIN | 0.004 | 407 | 526 | 130 | + Ricin-type beta-trefoil. Carbohydrate-binding domain formed from presumed gene triplication. | ||
| cd00161 | RICIN | 0.001 | 404 | 511 | 120 | + 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 | 1.0e-9 | 36 | 350 | 334 | + Cellulase (glycosyl hydrolase family 5). | ||
| Annotations - NR Download unfiltered results here | |||||||
|---|---|---|---|---|---|---|---|
| Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
| GenBank | EEE61202.1 | 0 | 33 | 537 | 36 | 550 | hypothetical protein OsJ_15212 [Oryza sativa Japonica Group] |
| RefSeq | XP_002285424.1 | 0 | 14 | 533 | 15 | 529 | PREDICTED: hypothetical protein [Vitis vinifera] |
| RefSeq | XP_002312657.1 | 0 | 17 | 540 | 1 | 519 | predicted protein [Populus trichocarpa] |
| RefSeq | XP_002315653.1 | 0 | 27 | 538 | 4 | 510 | predicted protein [Populus trichocarpa] |
| RefSeq | XP_002515055.1 | 0 | 24 | 535 | 30 | 536 | 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 | 2e-18 | 29 | 374 | 7 | 336 | A Chain A, Endocellulase E1 From Acidothermus Cellulolyticus Mutant Y245g |
| PDB | 1vrx_A | 2e-18 | 29 | 374 | 7 | 336 | A Chain A, Endocellulase E1 From Acidothermus Cellulolyticus Mutant Y245g |
| PDB | 1ece_B | 1e-17 | 29 | 374 | 7 | 336 | A Chain A, Acidothermus Cellulolyticus Endocellulase E1 Catalytic Domain In Complex With A Cellotetraose |
| PDB | 1ece_A | 1e-17 | 29 | 374 | 7 | 336 | A Chain A, Acidothermus Cellulolyticus Endocellulase E1 Catalytic Domain In Complex With A Cellotetraose |
| PDB | 2zun_C | 0.0000001 | 41 | 270 | 59 | 300 | A Chain A, Acidothermus Cellulolyticus Endocellulase E1 Catalytic Domain In Complex With A Cellotetraose |
