| Basic Information | |
|---|---|
| Species | Thellungiella halophila |
| Cazyme ID | Thhalv10004045m |
| Family | GH5 |
| Protein Properties | Length: 508 Molecular Weight: 56347.6 Isoelectric Point: 7.7348 |
| Chromosome | Chromosome/Scaffold: 6 Start: 6495645 End: 6498220 |
| 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 | 37 | 349 | 1.99965e-42 |
| IIDEKGQRVKLACANWPAHLQPVVAEGLSKQPVDAVAKMIVAMGFNCVRLTWPLDLATNETLATNVTVRQSFQSLGLNADMSGFQTNNPSMIDLPLIEAY KRLVATLGNHNVMVILDNHSTKPGWCCGNDDGNGFFGDTFFDPATWIAGLTKMATIFKDVSNVVGMSLRNELRGPKQNVDDWFKYMQQGAEAVHGANPNV LVIISGLSFDTDLSFVRSRPVTLTFSGKLVFELHRYAFTNTEIWSSKNPNDACGEVQKIIDDGGGFNLRDFPVFLSEFGIDLRGGNVNDNRYIGCILGWA AENDVDWSIWALT | |||
| Full Sequence |
|---|
| Protein Sequence Length: 508 Download |
| MKKIKVLKRM FCFIFFLLFS FITKNMAYPL STKSRWIIDE KGQRVKLACA NWPAHLQPVV 60 AEGLSKQPVD AVAKMIVAMG FNCVRLTWPL DLATNETLAT NVTVRQSFQS LGLNADMSGF 120 QTNNPSMIDL PLIEAYKRLV ATLGNHNVMV ILDNHSTKPG WCCGNDDGNG FFGDTFFDPA 180 TWIAGLTKMA TIFKDVSNVV GMSLRNELRG PKQNVDDWFK YMQQGAEAVH GANPNVLVII 240 SGLSFDTDLS FVRSRPVTLT FSGKLVFELH RYAFTNTEIW SSKNPNDACG EVQKIIDDGG 300 GFNLRDFPVF LSEFGIDLRG GNVNDNRYIG CILGWAAEND VDWSIWALTG SYYIREGVAG 360 MVEYYGPVPQ PKVYNLVFHP LTGLCMVQTS SDPNKVTLGT CNTSPQWSYT LDNTLKIKDK 420 SLCLENTGPN QRVKLSETSC WSPNLSKWQT ISGSINMLLA SKSSDNSLCL DVDGHKNIVA 480 TNCKCVKGED SSCDPTSQWF KIVKVSR* |
| Functional Domains Download unfiltered results here | ||||||
|---|---|---|---|---|---|---|
| Cdd ID | Domain | E-Value | Start | End | Length | Domain Description |
| smart00458 | RICIN | 1.0e-5 | 378 | 499 | 130 | + Ricin-type beta-trefoil. Carbohydrate-binding domain formed from presumed gene triplication. |
| cd00161 | RICIN | 1.0e-7 | 374 | 474 | 106 | + 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 | 66 | 350 | 297 | + 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 | 26 | 507 | 1 | 507 | AC007357_15 F3F19.15 [Arabidopsis thaliana] |
| RefSeq | NP_172772.2 | 0 | 25 | 507 | 30 | 537 | glycosyl hydrolase family 5 protein / cellulase family protein [Arabidopsis thaliana] |
| RefSeq | NP_189245.1 | 0 | 26 | 507 | 1 | 508 | glycosyl hydrolase family 5 protein / cellulase family protein [Arabidopsis thaliana] |
| RefSeq | XP_002285424.1 | 0 | 26 | 506 | 25 | 529 | PREDICTED: hypothetical protein [Vitis vinifera] |
| RefSeq | XP_002315653.1 | 0 | 26 | 507 | 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 | 7e-17 | 32 | 319 | 8 | 288 | A Chain A, Endocellulase E1 From Acidothermus Cellulolyticus Mutant Y245g |
| PDB | 1vrx_A | 7e-17 | 32 | 319 | 8 | 288 | A Chain A, Endocellulase E1 From Acidothermus Cellulolyticus Mutant Y245g |
| PDB | 1ece_B | 8e-17 | 32 | 319 | 8 | 288 | A Chain A, Acidothermus Cellulolyticus Endocellulase E1 Catalytic Domain In Complex With A Cellotetraose |
| PDB | 1ece_A | 8e-17 | 32 | 319 | 8 | 288 | A Chain A, Acidothermus Cellulolyticus Endocellulase E1 Catalytic Domain In Complex With A Cellotetraose |
| PDB | 4dm1_C | 0.0005 | 45 | 273 | 28 | 267 | A Chain A, Contribution Of Disulfide Bond Toward Thermostability In Hyperthermostable Endocellulase |
