Basic Information | |
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Species | Physcomitrella patens |
Cazyme ID | Pp1s34_140V6.1 |
Family | GT57 |
Protein Properties | Length: 515 Molecular Weight: 58068.6 Isoelectric Point: 8.432 |
Chromosome | Chromosome/Scaffold: 34 Start: 667988 End: 669532 |
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 | 16 | 505 | 0 |
ATCVKVLLVPAYHSTDFEVHRHWLAITHSLPLKEWYSDESSQWTLDYPPFFAFFERFLAIFASWFDPQIVDLVNGQNYAVRSVVLFQRGTVMAADLVLYW GLWEIGSGLSRMRRRILYLVVIFSPGLLIVDHIHFQYNGFLFGILFLSLAAMRDGNDLLGGIYFAALVCFKHLFAIAGPIYFVYILRHYCKGPQKIARFC IMASAVISIVALAFGPFLYHGQMPQLMKRLFPFGRGLCHAYWAPNVWALYSTGDKSATVVMRKLFGVYIDRPKAGLTGGLVGDFTPYAVFPQITPIVSAI LVIGSMMPCLVQAWRKPVPNAFIRWVVYTFTCGFMFGWHVHEKASLHMVIPFSVLAVERLEDARAFLFLSVVSTYSLFPLLFESKEYPIKVTLLLLYALV IWLNFSQLFGTSTKDSGDLKAKAASNTELNVQETVKPLIGPVEGAYLGGIMVIEIYGQCFHPLFFGGSFPFVPLMLTSVYCALGMTYYWL |
Full Sequence |
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Protein Sequence Length: 515 Download |
MGAADLQYLL WLVGIATCVK VLLVPAYHST DFEVHRHWLA ITHSLPLKEW YSDESSQWTL 60 DYPPFFAFFE RFLAIFASWF DPQIVDLVNG QNYAVRSVVL FQRGTVMAAD LVLYWGLWEI 120 GSGLSRMRRR ILYLVVIFSP GLLIVDHIHF QYNGFLFGIL FLSLAAMRDG NDLLGGIYFA 180 ALVCFKHLFA IAGPIYFVYI LRHYCKGPQK IARFCIMASA VISIVALAFG PFLYHGQMPQ 240 LMKRLFPFGR GLCHAYWAPN VWALYSTGDK SATVVMRKLF GVYIDRPKAG LTGGLVGDFT 300 PYAVFPQITP IVSAILVIGS MMPCLVQAWR KPVPNAFIRW VVYTFTCGFM FGWHVHEKAS 360 LHMVIPFSVL AVERLEDARA FLFLSVVSTY SLFPLLFESK EYPIKVTLLL LYALVIWLNF 420 SQLFGTSTKD SGDLKAKAAS NTELNVQETV KPLIGPVEGA YLGGIMVIEI YGQCFHPLFF 480 GGSFPFVPLM LTSVYCALGM TYYWLDQLHM VLSS* |
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-108 | 14 | 505 | 509 | + 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 | EAY87118.1 | 0 | 17 | 508 | 21 | 512 | hypothetical protein OsI_08520 [Oryza sativa Indica Group] |
RefSeq | NP_001047779.1 | 0 | 17 | 508 | 18 | 509 | Os02g0688500 [Oryza sativa (japonica cultivar-group)] |
RefSeq | NP_181994.5 | 0 | 4 | 513 | 7 | 506 | transferase, transferring glycosyl groups / transferase, transferring hexosyl groups [Arabidopsis thaliana] |
RefSeq | XP_001758748.1 | 0 | 1 | 514 | 1 | 514 | predicted protein [Physcomitrella patens subsp. patens] |
RefSeq | XP_002269114.1 | 0 | 3 | 514 | 13 | 531 | PREDICTED: hypothetical protein [Vitis vinifera] |
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 |