y
Basic Information | |
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Species | Arabidopsis thaliana |
Cazyme ID | AT2G44660.1 |
Family | GT57 |
Protein Properties | Length: 507 Molecular Weight: 58221.9 Isoelectric Point: 9.1194 |
Chromosome | Chromosome/Scaffold: 2 Start: 18420832 End: 18422839 |
Description | glucosyltransferase, putative, expressed |
View CDS |
Signature Domain Download full data set without filtering | |||
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Family | Start | End | Evalue |
GT57 | 19 | 500 | 0 |
ATAVKLLLIPSSRSTDFEVHRNWLAITNSLPLTKWYFDETSQWTLDYPPFFAYFERFLSIFARLVDPRIVDLQSGLDYNAESVIYFQRISVIVSDLCLLY GVYRLTRKLEPLKRNLICALVIWSPGLLIVDHIHFQYNGFLLGWLLLSISFLQEGRDLLGGFLFAVLLCFKHLFAVTAPVYFVYLLRHYCWSGLVTGFRR LVTIGAVVVAVFAAAYGPFIYHGQIQQVISRMFPFGRGLCHAYWAPNFWVFYIILDKGLAVLLRKLGYEIQIPSASFTGGLVGDSSPFAVLPQITPLTTF AMVLLAISPCLIKAWKKPHSGLVARWVAYAYTCGFLFGWHVHEKASLHFTIPLAIVAVQSLEDAKHYFLVSIVSCYSLYPLLYEPQEYPIKVLLLLLHSV VMWLGFAAQYTDYKAQKKETSEIKSKFRIGCFEKSYLMGLIIVEIVSQFLHPYFLGDKLPFLPLMLISTYCTVGIMYSWIWQ |
Full Sequence |
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Protein Sequence Length: 507 Download |
MDHREKSDRR LLLWFFAVAT AVKLLLIPSS RSTDFEVHRN WLAITNSLPL TKWYFDETSQ 60 WTLDYPPFFA YFERFLSIFA RLVDPRIVDL QSGLDYNAES VIYFQRISVI VSDLCLLYGV 120 YRLTRKLEPL KRNLICALVI WSPGLLIVDH IHFQYNGFLL GWLLLSISFL QEGRDLLGGF 180 LFAVLLCFKH LFAVTAPVYF VYLLRHYCWS GLVTGFRRLV TIGAVVVAVF AAAYGPFIYH 240 GQIQQVISRM FPFGRGLCHA YWAPNFWVFY IILDKGLAVL LRKLGYEIQI PSASFTGGLV 300 GDSSPFAVLP QITPLTTFAM VLLAISPCLI KAWKKPHSGL VARWVAYAYT CGFLFGWHVH 360 EKASLHFTIP LAIVAVQSLE DAKHYFLVSI VSCYSLYPLL YEPQEYPIKV LLLLLHSVVM 420 WLGFAAQYTD YKAQKKETSE IKSKFRIGCF EKSYLMGLII VEIVSQFLHP YFLGDKLPFL 480 PLMLISTYCT VGIMYSWIWQ LRKILT* 540 |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
pfam03155 | Alg6_Alg8 | 5.0e-104 | 18 | 499 | 498 | + ALG6, ALG8 glycosyltransferase family. N-linked (asparagine-linked) glycosylation of proteins is mediated by a highly conserved pathway in eukaryotes, in which a lipid (dolichol phosphate)-linked oligosaccharide is assembled at the endoplasmic reticulum membrane prior to the transfer of the oligosaccharide moiety to the target asparagine residues. This oligosaccharide is composed of Glc(3)Man(9)GlcNAc(2). The addition of the three glucose residues is the final series of steps in the synthesis of the oligosaccharide precursor. Alg6 transfers the first glucose residue, and Alg8 transfers the second one. In the human alg6 gene, a C->T transition, which causes Ala333 to be replaced with Val, has been identified as the cause of a congenital disorder of glycosylation, designated as type Ic OMIM:603147. |
Gene Ontology | |
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GO Term | Description |
GO:0005789 | endoplasmic reticulum membrane |
GO:0008150 | biological_process |
GO:0012505 | endomembrane system |
GO:0016757 | transferase activity, transferring glycosyl groups |
GO:0016758 | transferase activity, transferring hexosyl groups |
Annotations - NR Download unfiltered results here | |||||||
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Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
GenBank | AAC27468.1 | 0 | 1 | 405 | 1 | 370 | putative glucosyltransferase [Arabidopsis thaliana] |
RefSeq | NP_181994.5 | 0 | 1 | 506 | 1 | 506 | transferase, transferring glycosyl groups / transferase, transferring hexosyl groups [Arabidopsis thaliana] |
Swiss-Prot | O80505 | 0 | 1 | 405 | 1 | 405 | ALG8_ARATH RecName: Full=Probable dolichyl pyrophosphate Glc1Man9GlcNAc2 alpha-1,3-glucosyltransferase; AltName: Full=Dolichyl-P-Glc:Glc1Man9GlcNAc2-PP-dolichyl glucosyltransferase; AltName: Full=Asparagine-linked glycosylation protein 8 homolog |
RefSeq | XP_002269114.1 | 0 | 12 | 505 | 19 | 529 | PREDICTED: hypothetical protein [Vitis vinifera] |
RefSeq | XP_002521523.1 | 0 | 3 | 505 | 9 | 490 | dolichyl glycosyltransferase, putative [Ricinus communis] |
Metabolic Pathways | |||
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Pathway Name | Reaction | EC | Protein Name |
dolichyl-diphosphooligosaccharide biosynthesis | RXN-5471 | EC-2.4.1.265 | Dol-P-Glc:Glc1Man9GlcNAc2-PP-Dol α-1,3-glucosyltransferase |