| Basic Information | |
|---|---|
| Species | Thellungiella halophila |
| Cazyme ID | Thhalv10007253m |
| Family | GH5 |
| Protein Properties | Length: 562 Molecular Weight: 62483.4 Isoelectric Point: 8.2332 |
| Chromosome | Chromosome/Scaffold: 5 Start: 11044495 End: 11048216 |
| 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 | 42 | 355 | 3.00018e-42 |
| IVDENGQRVKLACVNWPSHLQPVVAEGLSKQPVDAVAKKIVEMGFNCVRLTWPLDLMTNETLANNVTVRQSFQSFGLKDDIVGFQTNNPSIIDLSLIEAF KMVVTTLGNNDVMVILDNHLTKPGWCCANNDGNGFFGDRFFDPTVWTAALSKMATTFDGVTNVVGMSLRNELRGPKQNVNDWFKYMQQGAEAVHSANKNV LVVLSGLSFDADLSFVRSRPVKLSFTGKLVFELHWYSFTDGNSWTTNNPNDICGRVLNRIGNNGGFLLNKGFPLFLSEFGVDERGQNANDDRYFGCLSGW AAENDVDWSLWALT | |||
| Full Sequence |
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| Protein Sequence Length: 562 Download |
| MTTKEPKHMF CIFPFFCFFF SFIAQHTIPN MAYPLSTSSR WIVDENGQRV KLACVNWPSH 60 LQPVVAEGLS KQPVDAVAKK IVEMGFNCVR LTWPLDLMTN ETLANNVTVR QSFQSFGLKD 120 DIVGFQTNNP SIIDLSLIEA FKMVVTTLGN NDVMVILDNH LTKPGWCCAN NDGNGFFGDR 180 FFDPTVWTAA LSKMATTFDG VTNVVGMSLR NELRGPKQNV NDWFKYMQQG AEAVHSANKN 240 VLVVLSGLSF DADLSFVRSR PVKLSFTGKL VFELHWYSFT DGNSWTTNNP NDICGRVLNR 300 IGNNGGFLLN KGFPLFLSEF GVDERGQNAN DDRYFGCLSG WAAENDVDWS LWALTGSYYL 360 RQGVVGMIEY YGALDSDWIS VRNSSFLQKI SLLQSPLQGP GPRTDAYNLV FHPLTGLCVV 420 RSLKDTTMLT LGPCNSSQPW SYTKKTLRIK DQLLCLQSNG PKNRVTMTRT SCSKPGSIWQ 480 TISASRMHLA ATTSNKTSIC LDVDATNNVV ANACKCLSND SSCEPMSQWF KIIKATRPLK 540 SLGLYKQISS LDNLSPKSDL V* |
| Functional Domains Download unfiltered results here | ||||||||
|---|---|---|---|---|---|---|---|---|
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| Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
| smart00458 | RICIN | 2.0e-6 | 411 | 519 | 118 | + Ricin-type beta-trefoil. Carbohydrate-binding domain formed from presumed gene triplication. | ||
| cd00161 | RICIN | 9.0e-8 | 407 | 532 | 135 | + 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-8 | 43 | 356 | 328 | + 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 | 31 | 551 | 1 | 521 | AC007357_15 F3F19.15 [Arabidopsis thaliana] |
| RefSeq | NP_172772.2 | 0 | 1 | 551 | 1 | 551 | glycosyl hydrolase family 5 protein / cellulase family protein [Arabidopsis thaliana] |
| RefSeq | NP_189245.1 | 0 | 31 | 537 | 1 | 508 | glycosyl hydrolase family 5 protein / cellulase family protein [Arabidopsis thaliana] |
| RefSeq | XP_002285424.1 | 0 | 29 | 539 | 23 | 536 | PREDICTED: hypothetical protein [Vitis vinifera] |
| RefSeq | XP_002315653.1 | 0 | 31 | 537 | 1 | 506 | predicted protein [Populus trichocarpa] |
| Annotations - PDB Download unfiltered results here | |||||||
|---|---|---|---|---|---|---|---|
| Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
| PDB | 1vrx_B | 0.000000000000008 | 37 | 321 | 8 | 284 | A Chain A, Endocellulase E1 From Acidothermus Cellulolyticus Mutant Y245g |
| PDB | 1vrx_A | 0.000000000000008 | 37 | 321 | 8 | 284 | A Chain A, Endocellulase E1 From Acidothermus Cellulolyticus Mutant Y245g |
| PDB | 1ece_B | 0.00000000000008 | 37 | 321 | 8 | 284 | A Chain A, Acidothermus Cellulolyticus Endocellulase E1 Catalytic Domain In Complex With A Cellotetraose |
| PDB | 1ece_A | 0.00000000000008 | 37 | 321 | 8 | 284 | A Chain A, Acidothermus Cellulolyticus Endocellulase E1 Catalytic Domain In Complex With A Cellotetraose |
