Basic Information | |
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Species | Selaginella moellendorffii |
Cazyme ID | 45405 |
Family | GT57 |
Protein Properties | Length: 357 Molecular Weight: 40139 Isoelectric Point: 8.3176 |
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 | 8 | 176 | 0 |
ATCVKILLVPSYHSTDFEVHRNWLAITHSLPVDRWYVDETSEWTLDYPPFFAWFERLLSAFAAVWDPRIVDLSAGKNYASSSCVLFQRGSVMVADSVLYL GLWSYCKGMAPDKRKLVYAVVVFSPGLLIVDHIHFQYNGFLLGILLLSLAALKQGKDLLGGVIFAALLA | |||
GT57 | 175 | 356 | 0 |
LAISVLGVVVFAFGPFAYYGQIQQVLRRLFPFGRGLCHAYWAPNIWAMYNTADKALSILFKAAGFKVNSTTAAYTGGLVGEFSSYAVLPSITPLITFAMV LSSLVPWLYKIWRNPQPSRVVYYITYAYMCGFMFGWHVHEKASLHFVVPFSLIAVESMDNANDYLFLSTVCYYSLFPLLYEA |
Full Sequence |
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Protein Sequence Length: 357 Download |
LLVMAAIATC VKILLVPSYH STDFEVHRNW LAITHSLPVD RWYVDETSEW TLDYPPFFAW 60 FERLLSAFAA VWDPRIVDLS AGKNYASSSC VLFQRGSVMV ADSVLYLGLW SYCKGMAPDK 120 RKLVYAVVVF SPGLLIVDHI HFQYNGFLLG ILLLSLAALK QGKDLLGGVI FAALLAISVL 180 GVVVFAFGPF AYYGQIQQVL RRLFPFGRGL CHAYWAPNIW AMYNTADKAL SILFKAAGFK 240 VNSTTAAYTG GLVGEFSSYA VLPSITPLIT FAMVLSSLVP WLYKIWRNPQ PSRVVYYITY 300 AYMCGFMFGW HVHEKASLHF VVPFSLIAVE SMDNANDYLF LSTVCYYSLF PLLYEAR 360 |
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-84 | 7 | 356 | 400 | + 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. |
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 | 357 | 12 | 369 | putative glucosyltransferase [Arabidopsis thaliana] |
RefSeq | NP_181994.5 | 0 | 1 | 357 | 12 | 404 | transferase, transferring glycosyl groups / transferase, transferring hexosyl groups [Arabidopsis thaliana] |
Swiss-Prot | O80505 | 0 | 1 | 357 | 12 | 404 | 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_001758748.1 | 0 | 1 | 357 | 9 | 400 | predicted protein [Physcomitrella patens subsp. patens] |
RefSeq | XP_002521523.1 | 0 | 6 | 357 | 23 | 373 | 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 |