| Basic Information | |
|---|---|
| Species | Medicago truncatula |
| Cazyme ID | Medtr5g077540.1 |
| Family | GT57 |
| Protein Properties | Length: 516 Molecular Weight: 59069.6 Isoelectric Point: 8.8937 |
| Chromosome | Chromosome/Scaffold: 5 Start: 32096549 End: 32100678 |
| 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 | 29 | 507 | 0 |
| ACIKVLLFPSYRSTDFEVHRNWLALTHSLPLSQWYFDETSPWTLDYPPFFAYFEHFLSIFAHLVDPKIVHLQEGLNYSSNTVVYFQRFTVILSDLCLLYG VYRITRKLDSRKQKLIWSLVIWSPMLLIVDHVHFQYNGFLIGILLISLSYLEEGRDLLGGFVFAVLLCFKHLFAVAAPVYFIYLLRHYLVFASAFGPFFH LGQIQQVIQRLFPFGRGLCHAYWAPNFWVFYIMSDKGLAFILRKLGFNIQTPAASFTAGLVGDSSPFSVLPRITPSVTFIMVLLALSPCLFKAWKNPQPQ KITRWISYAYTCGFLFGWHVHEKASLHFVIPLAFVAAQTPEDAKHYFLLSIVSCYSLFPLLFEAQEYPIKILLLLLHSILMWSGFSAQFYDSAETGVSTA HTKKKAGQFESKGSLSADVRNNGFVIGLIEKIYLVGLVVVEIWGQVLHPLLLGDKLAFLPLMLISVYCALGIMYSWIWQ | |||
| Full Sequence |
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| Protein Sequence Length: 516 Download |
| MGKEKLSFKE LDDSSGPKTT LWWFFLLAAC IKVLLFPSYR STDFEVHRNW LALTHSLPLS 60 QWYFDETSPW TLDYPPFFAY FEHFLSIFAH LVDPKIVHLQ EGLNYSSNTV VYFQRFTVIL 120 SDLCLLYGVY RITRKLDSRK QKLIWSLVIW SPMLLIVDHV HFQYNGFLIG ILLISLSYLE 180 EGRDLLGGFV FAVLLCFKHL FAVAAPVYFI YLLRHYLVFA SAFGPFFHLG QIQQVIQRLF 240 PFGRGLCHAY WAPNFWVFYI MSDKGLAFIL RKLGFNIQTP AASFTAGLVG DSSPFSVLPR 300 ITPSVTFIMV LLALSPCLFK AWKNPQPQKI TRWISYAYTC GFLFGWHVHE KASLHFVIPL 360 AFVAAQTPED AKHYFLLSIV SCYSLFPLLF EAQEYPIKIL LLLLHSILMW SGFSAQFYDS 420 AETGVSTAHT KKKAGQFESK GSLSADVRNN GFVIGLIEKI YLVGLVVVEI WGQVLHPLLL 480 GDKLAFLPLM LISVYCALGI MYSWIWQLRS IVKSH* |
| Functional Domains Download unfiltered results here | ||||||||
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| Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
| pfam03155 | Alg6_Alg8 | 2.0e-95 | 26 | 506 | 516 | + 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 | 3 | 514 | 2 | 471 | unnamed protein product [Vitis vinifera] |
| RefSeq | NP_181994.5 | 0 | 18 | 512 | 9 | 505 | transferase, transferring glycosyl groups / transferase, transferring hexosyl groups [Arabidopsis thaliana] |
| Swiss-Prot | O80505 | 0 | 18 | 394 | 9 | 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 | 3 | 514 | 2 | 531 | PREDICTED: hypothetical protein [Vitis vinifera] |
| RefSeq | XP_002521523.1 | 0 | 10 | 514 | 7 | 492 | dolichyl glycosyltransferase, putative [Ricinus communis] |
