y
Basic Information | |
---|---|
Species | Populus trichocarpa |
Cazyme ID | Potri.001G089100.3 |
Family | GH3 |
Protein Properties | Length: 705 Molecular Weight: 76942.2 Isoelectric Point: 8.8623 |
Chromosome | Chromosome/Scaffold: 01 Start: 7035666 End: 7039509 |
Description | Glycosyl hydrolase family protein |
View CDS |
External Links |
---|
NCBI Taxonomy |
Plaza |
CAZyDB |
Signature Domain Download full data set without filtering | |||
---|---|---|---|
Family | Start | End | Evalue |
GH3 | 75 | 193 | 1.1e-31 |
GIPRLGIPHYEWWSESLHGISINGPGVSFKNGGPVTSATGFPQVIVSAASFNRTLWFLIGSAIAIEARAMYNVGQAGLTFWAPNINIFRDPRWGRGQETP GEDPMVASAYAIEFVKGFQ |
Full Sequence |
---|
Protein Sequence Length: 705 Download |
MVANGRCLFF LLLFLSLSPS NSKSVANPQF PCKPPTHNTY SFCNKSLPIT RRAQSLISHL 60 TLQEKIQQLS DNASGIPRLG IPHYEWWSES LHGISINGPG VSFKNGGPVT SATGFPQVIV 120 SAASFNRTLW FLIGSAIAIE ARAMYNVGQA GLTFWAPNIN IFRDPRWGRG QETPGEDPMV 180 ASAYAIEFVK GFQGGHWKNG TETESTDRHG IGQKRVLYIT SDCDAVATIF EYQNYSKSPE 240 DAVAIALKAG MDINCGTYVL RNAQSAVEKG KLQEEDIDRA LHNLFSVQLR LGLFDGDPRK 300 GQFGKLGPKN VCTKEHKTLA LEAARQGIVL LKNDKKLLPL NKKAVSSLAI IGPLANMANS 360 LGGDYTGYPC DPQSLFEGLK AYVKKTSYAI GCLDVACVSD TQFHKAIIVA KRADFVIIVA 420 GLDLSQETEE HDRVSLLLPG KQMSLVSSVA AASKKPVILV LTGGGPLDVS FAKGDPRIAS 480 ILWIGYPGEA GAKALAEIIF GEYNPGGRLP MTWYPESFTE VSMTDMNMRP NPSRGYPGRT 540 YRFYTGNRVY GFGGGLSYTN FTYKILSAPS KLSLSGSLSS NSRKRILQQG GERLSYININ 600 EITSCDSLRF YMQILVENVG NMDGGHVVML FSRVPTVFRG APEKQLVGFD RVHTISHRST 660 EMSILVDPCE HLSVANEQGK KIMLLGGHGL MLGDLEHFVT IQIY* 720 |
Functional Domains Download unfiltered results here | ||||||||
---|---|---|---|---|---|---|---|---|
Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
PRK15098 | PRK15098 | 1.0e-9 | 66 | 196 | 132 | + beta-D-glucoside glucohydrolase; Provisional | ||
PRK15098 | PRK15098 | 8.0e-33 | 236 | 652 | 456 | + beta-D-glucoside glucohydrolase; Provisional | ||
pfam01915 | Glyco_hydro_3_C | 7.0e-39 | 347 | 559 | 218 | + Glycosyl hydrolase family 3 C-terminal domain. This domain is involved in catalysis and may be involved in binding beta-glucan. This domain is found associated with pfam00933. | ||
PLN03080 | PLN03080 | 2.0e-123 | 1 | 208 | 208 | + Probable beta-xylosidase; Provisional | ||
PLN03080 | PLN03080 | 0 | 218 | 703 | 488 | + Probable beta-xylosidase; Provisional |
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 |
EMBL | CAJ86207.1 | 0 | 31 | 702 | 29 | 737 | B1011H02.4 [Oryza sativa (indica cultivar-group)] |
EMBL | CBI25718.1 | 0 | 218 | 703 | 284 | 768 | unnamed protein product [Vitis vinifera] |
RefSeq | XP_002299457.1 | 0 | 1 | 199 | 1 | 199 | predicted protein [Populus trichocarpa] |
RefSeq | XP_002299457.1 | 0 | 218 | 704 | 294 | 780 | predicted protein [Populus trichocarpa] |
RefSeq | XP_002527213.1 | 0 | 251 | 704 | 1 | 454 | Thermostable beta-glucosidase B, putative [Ricinus communis] |
Annotations - PDB Download unfiltered results here | |||||||
---|---|---|---|---|---|---|---|
Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
PDB | 3u4a_B | 3e-31 | 244 | 688 | 281 | 724 | A Chain A, Crystal Structure Of A Beta-Galactosidase From Bacteroides Thetaiotaomicron |
PDB | 3u4a_A | 3e-31 | 244 | 688 | 281 | 724 | A Chain A, Crystal Structure Of A Beta-Galactosidase From Bacteroides Thetaiotaomicron |
PDB | 3u48_B | 4e-31 | 244 | 688 | 281 | 724 | A Chain A, Crystal Structure Of A Beta-Galactosidase From Bacteroides Thetaiotaomicron |
PDB | 3u48_A | 4e-31 | 244 | 688 | 281 | 724 | A Chain A, Crystal Structure Of A Beta-Galactosidase From Bacteroides Thetaiotaomicron |
PDB | 4i8d_B | 1e-16 | 315 | 653 | 319 | 659 | A Chain A, Crystal Structure Of Beta-D-Glucoside Glucohydrolase From Trichoderma Reesei |
Metabolic Pathways | |||
---|---|---|---|
Pathway Name | Reaction | EC | Protein Name |
(1,4)-β-xylan degradation | 3.2.1.37-RXN | EC-3.2.1.37 | xylan 1,4-β-xylosidase |