y
Basic Information | |
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Species | Arabidopsis lyrata |
Cazyme ID | 903892 |
Family | GT57 |
Protein Properties | Length: 507 Molecular Weight: 58399.2 Isoelectric Point: 9.1587 |
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 |
GT57 | 19 | 500 | 0 |
ATAVKLLLIPSYRSTDFEVHRNWLAITNSLPLTKWYFDETSQWTLDYPPFFAYFERFLSIFARLIDPRIVDLQSGLDYSSESVIYFQRISVIVSDLCLLC GVYRLTRKLEPMKRNLICAMVIWSPGLLIVDHIHFQYNGFLLGWLLLSISFLQEGRDLLGGFLFAVLLCFKHLFAVAAPVYFVYLLRHYCWSGLVTGFRR LVTIGAVVVAVFAAAYGPFIYHGQIQQVISRMFPFGRGLCHAYWAPNFWVFYIILDKGLAFLLRKLGFEIQIPSASFTGGLVGDSSPFAVLPQITPLTTF AMVLLAISPCLIKAWKKTHPGHVARWIAYAYTCGFLFGWHVHEKASLHFTIPLSIVAVQSLEDAKHYFLVSIVSCYSLFPLLYEPQEYSIKVLLLLLHSM IMWLGFVAQYTNNNKVQKENRVSKSKLRIGCFEKSYLMGLVIVEIVSQFLHPYYLGDKFPFLPLMLISTYCTVGIMYSWIWQ |
Full Sequence |
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Protein Sequence Length: 507 Download |
MDHRENIDRR LLLWFFAVAT AVKLLLIPSY RSTDFEVHRN WLAITNSLPL TKWYFDETSQ 60 WTLDYPPFFA YFERFLSIFA RLIDPRIVDL QSGLDYSSES VIYFQRISVI VSDLCLLCGV 120 YRLTRKLEPM KRNLICAMVI WSPGLLIVDH IHFQYNGFLL GWLLLSISFL QEGRDLLGGF 180 LFAVLLCFKH LFAVAAPVYF VYLLRHYCWS GLVTGFRRLV TIGAVVVAVF AAAYGPFIYH 240 GQIQQVISRM FPFGRGLCHA YWAPNFWVFY IILDKGLAFL LRKLGFEIQI PSASFTGGLV 300 GDSSPFAVLP QITPLTTFAM VLLAISPCLI KAWKKTHPGH VARWIAYAYT CGFLFGWHVH 360 EKASLHFTIP LSIVAVQSLE DAKHYFLVSI VSCYSLFPLL YEPQEYSIKV LLLLLHSMIM 420 WLGFVAQYTN NNKVQKENRV SKSKLRIGCF EKSYLMGLVI VEIVSQFLHP YYLGDKFPFL 480 PLMLISTYCT VGIMYSWIWQ IRKILT* 540 |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
pfam03155 | Alg6_Alg8 | 1.0e-101 | 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: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 | 1 | 505 | 8 | 490 | dolichyl glycosyltransferase, putative [Ricinus communis] |