| Basic Information | |
|---|---|
| Species | Ricinus communis |
| Cazyme ID | 29634.m002078 |
| Family | GT57 |
| Protein Properties | Length: 493 Molecular Weight: 56872.1 Isoelectric Point: 8.9763 |
| Chromosome | Chromosome/Scaffold: 29634 Start: 165590 End: 168978 |
| Description | ALG6, ALG8 glycosyltransferase family |
| 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 | 26 | 163 | 0 |
| ACIKLVLIPSYHSTDFEVHRHWLALTHSLPLSQWYFDETSPWTLDYPPFFAYYEYILSLFAQFIDPQMVDIYRGLNYKSNTVIYFQRISVIISDLCLLYG IYRLTKNLESRKRILMWVLVVWSPGLIMVDHMHFQYNV | |||
| GT57 | 164 | 485 | 0 |
| AAPVYFVYLLRHYCWKGISMGFRRFSAMGAVVVVVFAVAYGPFLYYGQIQQVVRRMFPFGRGLCHAYWAPNFWVFYMVLDKCLAIVLRKLRFNIQAPTAS FTGGLVGDSSPFAVLPQITPLTTFIMVLLALSPCLLKAWKNPQPRLVARWIAYAYTCGFVFGWHVHEKASLHFVIPLAIVATHSLEDARHYFLLAIGSCY SLFPLLYEAQEYPIKVLLLLLHSILMWYCFSAQFTKDAAAKENAPAKRGGEQFGSQGTSSSTVEGGIHIGRIGKCYLVGLLAVETWGQLLHPYLLGDKLP FLPLILISTFCALEIMYSWIWQ | |||
| Full Sequence |
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| Protein Sequence Length: 493 Download |
| MECQTLQMHA RSAIIQQLFW FFSLAACIKL VLIPSYHSTD FEVHRHWLAL THSLPLSQWY 60 FDETSPWTLD YPPFFAYYEY ILSLFAQFID PQMVDIYRGL NYKSNTVIYF QRISVIISDL 120 CLLYGIYRLT KNLESRKRIL MWVLVVWSPG LIMVDHMHFQ YNVAAPVYFV YLLRHYCWKG 180 ISMGFRRFSA MGAVVVVVFA VAYGPFLYYG QIQQVVRRMF PFGRGLCHAY WAPNFWVFYM 240 VLDKCLAIVL RKLRFNIQAP TASFTGGLVG DSSPFAVLPQ ITPLTTFIMV LLALSPCLLK 300 AWKNPQPRLV ARWIAYAYTC GFVFGWHVHE KASLHFVIPL AIVATHSLED ARHYFLLAIG 360 SCYSLFPLLY EAQEYPIKVL LLLLHSILMW YCFSAQFTKD AAAKENAPAK RGGEQFGSQG 420 TSSSTVEGGI HIGRIGKCYL VGLLAVETWG QLLHPYLLGD KLPFLPLILI STFCALEIMY 480 SWIWQLRWIL KST |
| Functional Domains Download unfiltered results here | ||||||||
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| Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
| pfam03155 | Alg6_Alg8 | 3.0e-90 | 32 | 484 | 503 | + 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 | |
|---|---|
| GO Term | Description |
| GO:0005789 | endoplasmic reticulum membrane |
| GO:0016758 | transferase activity, transferring hexosyl groups |
| Annotations - NR Download unfiltered results here | |||||||
|---|---|---|---|---|---|---|---|
| Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
| EMBL | CBI16712.1 | 0 | 1 | 493 | 1 | 472 | unnamed protein product [Vitis vinifera] |
| RefSeq | NP_181994.5 | 0 | 9 | 490 | 3 | 505 | transferase, transferring glycosyl groups / transferase, transferring hexosyl groups [Arabidopsis thaliana] |
| Swiss-Prot | O80505 | 0 | 9 | 374 | 3 | 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 | 1 | 493 | 1 | 532 | PREDICTED: hypothetical protein [Vitis vinifera] |
| RefSeq | XP_002521523.1 | 0 | 1 | 493 | 1 | 493 | dolichyl glycosyltransferase, putative [Ricinus communis] |
