y
Basic Information | |
---|---|
Species | Glycine max |
Cazyme ID | Glyma15g38936.1 |
Family | GH17 |
Protein Properties | Length: 300 Molecular Weight: 33936.4 Isoelectric Point: 5.9897 |
Chromosome | Chromosome/Scaffold: 15 Start: 45431543 End: 45433571 |
Description | Glycosyl hydrolase superfamily protein |
View CDS |
External Links |
---|
NCBI Taxonomy |
Plaza |
CAZyDB |
Signature Domain Download full data set without filtering | |||
---|---|---|---|
Family | Start | End | Evalue |
GH17 | 138 | 236 | 4.3e-22 |
FVDVYDGQGMVDPKQVPLDHVLFQPNKGMVDPSSNLHYDNMLFTQIDAVYSALDSLAYRKLPVHISETSSPSKGDLDETSVNLENAKNYNGNLIKISLS |
Full Sequence |
---|
Protein Sequence Length: 300 Download |
MHSTTRFYDS SNKTDVTPTE VSVKVNKYTR SSAPTLSPSL LIFERGFVEV ATDIGCERFS 60 SEQQGLIIKW KKRGSISLIA RCWKPFGHGD DADNATIVGR ECKDDLLWYY DIEKFAANYF 120 SMVLEDQSQI ESDGFGNFVD VYDGQGMVDP KQVPLDHVLF QPNKGMVDPS SNLHYDNMLF 180 TQIDAVYSAL DSLAYRKLPV HISETSSPSK GDLDETSVNL ENAKNYNGNL IKISLSLPPF 240 RHYLVVPVVH IPTVKYLQRK TDDYYLVSHM LKVGKMLLNR DAPQSQHWAE SCLFHAYLE* 300 360 |
Functional Domains Download unfiltered results here | ||||||||
---|---|---|---|---|---|---|---|---|
Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
pfam11969 | DcpS_C | 0.005 | 242 | 280 | 39 | + Scavenger mRNA decapping enzyme C-term binding. This family consists of several scavenger mRNA decapping enzymes (DcpS) and is the C-terminal region. DcpS is a scavenger pyrophosphatase that hydrolyses the residual cap structure following 3' to 5' decay of an mRNA. The association of DcpS with 3' to 5' exonuclease exosome components suggests that these two activities are linked and there is a coupled exonucleolytic decay-dependent decapping pathway. The C-terminal domain contains a histidine triad (HIT) sequence with three histidines separated by hydrophobic residues. The central histidine within the DcpS HIT motif is critical for decapping activity and defines the HIT motif as a new mRNA decapping domain, making DcpS the first member of the HIT family of proteins with a defined biological function. | ||
cd01278 | aprataxin_related | 1.0e-6 | 240 | 282 | 43 | + aprataxin related: Aprataxin, a HINT family hydrolase is mutated in ataxia oculomotor apraxia syndrome. All the members of this subgroup have the conserved HxHxHxx (where x is a hydrophobic residue) signature motif. Members of this subgroup are predominantly eukaryotic in origin. | ||
pfam00332 | Glyco_hydro_17 | 3.0e-9 | 149 | 232 | 84 | + Glycosyl hydrolases family 17. |
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 |
RefSeq | NP_174563.2 | 1e-28 | 149 | 236 | 211 | 298 | glycosyl hydrolase family 17 protein [Arabidopsis thaliana] |
RefSeq | XP_002278950.1 | 1e-33 | 148 | 233 | 208 | 293 | PREDICTED: hypothetical protein [Vitis vinifera] |
RefSeq | XP_002300505.1 | 4e-33 | 149 | 232 | 197 | 280 | predicted protein [Populus trichocarpa] |
RefSeq | XP_002317055.1 | 4e-32 | 149 | 233 | 187 | 271 | predicted protein [Populus trichocarpa] |
RefSeq | XP_002518930.1 | 7e-32 | 149 | 232 | 208 | 291 | Glucan endo-1,3-beta-glucosidase precursor, putative [Ricinus communis] |
Annotations - PDB Download unfiltered results here | |||||||
---|---|---|---|---|---|---|---|
Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
PDB | 1ghs_B | 0.000003 | 149 | 232 | 176 | 256 | A Chain A, The Three-Dimensional Structures Of Two Plant Beta-Glucan Endohydrolases With Distinct Substrate Specificities |
PDB | 1ghs_A | 0.000003 | 149 | 232 | 176 | 256 | A Chain A, The Three-Dimensional Structures Of Two Plant Beta-Glucan Endohydrolases With Distinct Substrate Specificities |
PDB | 2cyg_A | 0.0003 | 149 | 232 | 182 | 262 | A Chain A, Crystal Structure At 1.45- Resolution Of The Major Allergen Endo-Beta-1,3-Glucanase Of Banana As A Molecular Basis For The Latex-Fruit Syndrome |
PDB | 3f55_D | 0.001 | 118 | 232 | 157 | 265 | A Chain A, Crystal Structure At 1.45- Resolution Of The Major Allergen Endo-Beta-1,3-Glucanase Of Banana As A Molecular Basis For The Latex-Fruit Syndrome |
PDB | 3f55_C | 0.001 | 118 | 232 | 157 | 265 | A Chain A, Crystal Structure At 1.45- Resolution Of The Major Allergen Endo-Beta-1,3-Glucanase Of Banana As A Molecular Basis For The Latex-Fruit Syndrome |