| Basic Information | |
|---|---|
| Species | Gossypium raimondii |
| Cazyme ID | Gorai.003G062300.1 |
| Family | GT57 |
| Protein Properties | Length: 513 Molecular Weight: 58559.4 Isoelectric Point: 9.0911 |
| Chromosome | Chromosome/Scaffold: 03 Start: 11356807 End: 11362010 |
| Description | ALG6, ALG8 glycosyltransferase family |
| View CDS | |
| External Links |
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| NCBI Taxonomy |
| CAZyDB |
| Signature Domain Download full data set without filtering | |||
|---|---|---|---|
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| Family | Start | End | Evalue |
| GT57 | 24 | 504 | 0 |
| ATIVKLLLIPSYHSTDLEVHRHWLAITHSLPLSQWYTDETSEWTLDYPPFFAYLERFLSMFAHLIDPQIVHLHHGLNYKANSAIYFQRMSVIVSDLFLLY GVYRSTLALASLKRNLIWLLVIWSPGLLIVDHLHFQYNGFLFGWLLLSLSFLAQGRDVMGGFLFAVLLCFKHLFAVAAPVYFVYLLRHYCRGGLVRGFAR LSVMGAIVVAVFAAAYGPFVYHGQIQQVIRRMFPFGRGLCHAYWAPNFWVFYIMLDKGIAFLLRKFGFNIPAPVASFTGGLVGDASPFAILPRVTPLTTF IMVLLALSPCLFRTWKDPRPRLIVRSVAYAYTCGFLFGWHVHEKASLHFSIPLAIVAVESLEDAKHYFLLSIVSCYSLFPLLYEAQEYPIKVLLLLLHTI LMWFSFSAQYSGSLRGDKKGGEKQGFEVGWVTKSYLIGVVVVEIWGQFLHPYLFGDKLPFVPLMLISMYCAIGILYSWIWQ | |||
| Full Sequence |
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| Protein Sequence Length: 513 Download |
| MMEMQESPQT PLVMAQLSWF FGIATIVKLL LIPSYHSTDL EVHRHWLAIT HSLPLSQWYT 60 DETSEWTLDY PPFFAYLERF LSMFAHLIDP QIVHLHHGLN YKANSAIYFQ RMSVIVSDLF 120 LLYGVYRSTL ALASLKRNLI WLLVIWSPGL LIVDHLHFQY NGFLFGWLLL SLSFLAQGRD 180 VMGGFLFAVL LCFKHLFAVA APVYFVYLLR HYCRGGLVRG FARLSVMGAI VVAVFAAAYG 240 PFVYHGQIQQ VIRRMFPFGR GLCHAYWAPN FWVFYIMLDK GIAFLLRKFG FNIPAPVASF 300 TGGLVGDASP FAILPRVTPL TTFIMVLLAL SPCLFRTWKD PRPRLIVRSV AYAYTCGFLF 360 GWHVHEKASL HFSIPLAIVA VESLEDAKHY FLLSIVSCYS LFPLLYEAQE YPIKVLLLLL 420 HTILMWFSFS AQYSGSLRGD KKGGEKQGFE VGWVTKSYLI GVVVVEIWGQ FLHPYLFGDK 480 LPFVPLMLIS MYCAIGILYS WIWQLKSILI SS* |
| 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-110 | 22 | 503 | 497 | + 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 | 4 | 512 | 1 | 472 | unnamed protein product [Vitis vinifera] |
| RefSeq | NP_181994.5 | 0 | 2 | 509 | 1 | 505 | transferase, transferring glycosyl groups / transferase, transferring hexosyl groups [Arabidopsis thaliana] |
| Swiss-Prot | O80505 | 0 | 2 | 410 | 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 | 4 | 512 | 1 | 532 | PREDICTED: hypothetical protein [Vitis vinifera] |
| RefSeq | XP_002521523.1 | 0 | 13 | 512 | 14 | 493 | dolichyl glycosyltransferase, putative [Ricinus communis] |
