y
Basic Information | |
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Species | Glycine max |
Cazyme ID | Glyma08g13880.2 |
Family | GH5 |
Protein Properties | Length: 575 Molecular Weight: 63116 Isoelectric Point: 5.6412 |
Chromosome | Chromosome/Scaffold: 08 Start: 10112714 End: 10116635 |
Description | Cellulase (glycosyl hydrolase family 5) protein |
View CDS |
External Links |
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NCBI Taxonomy |
Plaza |
CAZyDB |
Signature Domain Download full data set without filtering | |||
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Family | Start | End | Evalue |
GH5 | 55 | 366 | 1.49995e-41 |
ILNQGGQRVKLACVNWVSHLEVAVAEGLSKKPVDAISKGIKSMGFNCVRLTWPTLLATNDSLASLSVRRSFQSLGLLESVAGVQTNNPSIIDLPLIQAFQ AVVKSLGDNDVMVILDNHLTNPGWCCGYSDGNGFFGDKFFNPDQWIFGLTKMATLFNGVTNVVGMSLRNELRGPKQNVNDWYKYMVKGAEAVHAANPDVL VILSGINFDTSLSFIRDRPVSLTFKGKLVFEVHRYGFTDGGAWADGNPNQVCGKVTADIKQTSTFLVDQGWPLFVSEFGGDLRGTNVNDNRYLNCFLALV AELDLDWAYWTL |
Full Sequence |
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Protein Sequence Length: 575 Download |
MGRWRPSTLV FTILSAPIII IIALLSSGGT TTVEDVDNDH TMAVTGLLHT DSRWILNQGG 60 QRVKLACVNW VSHLEVAVAE GLSKKPVDAI SKGIKSMGFN CVRLTWPTLL ATNDSLASLS 120 VRRSFQSLGL LESVAGVQTN NPSIIDLPLI QAFQAVVKSL GDNDVMVILD NHLTNPGWCC 180 GYSDGNGFFG DKFFNPDQWI FGLTKMATLF NGVTNVVGMS LRNELRGPKQ NVNDWYKYMV 240 KGAEAVHAAN PDVLVILSGI NFDTSLSFIR DRPVSLTFKG KLVFEVHRYG FTDGGAWADG 300 NPNQVCGKVT ADIKQTSTFL VDQGWPLFVS EFGGDLRGTN VNDNRYLNCF LALVAELDLD 360 WAYWTLVGSY YFREGVIGME EFYGLLTWDW TQVRSTSFLN RISALQIPFR GPGIIEGSAY 420 KLIFHPLTGL CVISKSQLTS LTLGPCSSSD AWTYTPQKTL LINNTNFCIH AEQEGKPATL 480 SITCSDANSK WEMISDSNMH LSSKLSDGSN LCLDVDDNNI IVTTACKCLN QDKTCDPASQ 540 WFKLIDSGRR SISTTSTLSM LNSPDILWQP LSSI* 600 |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
pfam00652 | Ricin_B_lectin | 0.002 | 427 | 519 | 102 | + Ricin-type beta-trefoil lectin domain. | ||
smart00458 | RICIN | 5.0e-7 | 423 | 520 | 104 | + Ricin-type beta-trefoil. Carbohydrate-binding domain formed from presumed gene triplication. | ||
cd00161 | RICIN | 1.0e-7 | 420 | 544 | 134 | + 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 | 5.0e-15 | 84 | 366 | 290 | + Cellulase (glycosyl hydrolase family 5). |
Gene Ontology | |
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GO Term | Description |
GO:0004553 | hydrolase activity, hydrolyzing O-glycosyl compounds |
GO:0005975 | carbohydrate metabolic process |
Annotations - NR Download unfiltered results here | |||||||
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Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
RefSeq | NP_172772.2 | 0 | 48 | 549 | 35 | 537 | glycosyl hydrolase family 5 protein / cellulase family protein [Arabidopsis thaliana] |
RefSeq | XP_002285424.1 | 0 | 48 | 560 | 29 | 545 | PREDICTED: hypothetical protein [Vitis vinifera] |
RefSeq | XP_002312657.1 | 0 | 44 | 574 | 7 | 544 | predicted protein [Populus trichocarpa] |
RefSeq | XP_002315653.1 | 0 | 48 | 554 | 5 | 511 | predicted protein [Populus trichocarpa] |
RefSeq | XP_002515055.1 | 0 | 44 | 560 | 29 | 546 | hydrolase, hydrolyzing O-glycosyl compounds, putative [Ricinus communis] |
Annotations - PDB Download unfiltered results here | |||||||
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Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
PDB | 1vrx_B | 0.000000000006 | 43 | 365 | 1 | 320 | A Chain A, Endocellulase E1 From Acidothermus Cellulolyticus Mutant Y245g |
PDB | 1vrx_A | 0.000000000006 | 43 | 365 | 1 | 320 | A Chain A, Endocellulase E1 From Acidothermus Cellulolyticus Mutant Y245g |
PDB | 1ece_B | 0.00000000002 | 46 | 365 | 4 | 320 | A Chain A, Acidothermus Cellulolyticus Endocellulase E1 Catalytic Domain In Complex With A Cellotetraose |
PDB | 1ece_A | 0.00000000002 | 46 | 365 | 4 | 320 | A Chain A, Acidothermus Cellulolyticus Endocellulase E1 Catalytic Domain In Complex With A Cellotetraose |
PDB | 4dm1_C | 0.00000002 | 63 | 290 | 28 | 267 | A Chain A, Contribution Of Disulfide Bond Toward Thermostability In Hyperthermostable Endocellulase |