Basic Information | |
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Species | Physcomitrella patens |
Cazyme ID | Pp1s290_38V6.1 |
Family | GT57 |
Protein Properties | Length: 518 Molecular Weight: 58812.1 Isoelectric Point: 9.0642 |
Chromosome | Chromosome/Scaffold: 290 Start: 524847 End: 529410 |
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 | 41 | 496 | 0 |
LLLRMMLSLQPYSGAGVAPKYGDYEAQRHWMEITVHTPVKEWYVNTTNNDLRYWGLDYPPLTAYQSWIHGRIIHALEPAAVALNTSRGHEDARSKFLMRW TVLSSDILVFFPAALAFVSLYYKLAIFEEQAWALSMILLQPALILIDHGHFQFNCISLGLAAGAAAAVVSRHELVACVLYSLSLNHKQMSAYYAPAFFAH LLGRCIQRRSPVFGVVKLGIMVLTTFTICWWPFLSSRHSALQVLNRLAPFERGLYEDYVANFWCGTSMLIKWKQLFSVPVLARLALGATITAALPSMVQQ IRAPSARGFLLAMLNSSFAFYFFSFQVHEKSVLLPLLPATLLALEEPGLLQWLVPYAVVSMLPLLRRDDLVLPYFALLALFFLLLKCPRHFEYKIAEDKL IKIFRAPILRNCSLAGAAILHLLYFYVQPPPRYSFLFEAFITSYCFAHFLVLFIYA |
Full Sequence |
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Protein Sequence Length: 518 Download |
MAEEDETTVR HAYKESPSWS WPATTSMQRK FSFGAICGFA LLLRMMLSLQ PYSGAGVAPK 60 YGDYEAQRHW MEITVHTPVK EWYVNTTNND LRYWGLDYPP LTAYQSWIHG RIIHALEPAA 120 VALNTSRGHE DARSKFLMRW TVLSSDILVF FPAALAFVSL YYKLAIFEEQ AWALSMILLQ 180 PALILIDHGH FQFNCISLGL AAGAAAAVVS RHELVACVLY SLSLNHKQMS AYYAPAFFAH 240 LLGRCIQRRS PVFGVVKLGI MVLTTFTICW WPFLSSRHSA LQVLNRLAPF ERGLYEDYVA 300 NFWCGTSMLI KWKQLFSVPV LARLALGATI TAALPSMVQQ IRAPSARGFL LAMLNSSFAF 360 YFFSFQVHEK SVLLPLLPAT LLALEEPGLL QWLVPYAVVS MLPLLRRDDL VLPYFALLAL 420 FFLLLKCPRH FEYKIAEDKL IKIFRAPILR NCSLAGAAIL HLLYFYVQPP PRYSFLFEAF 480 ITSYCFAHFL VLFIYANCKQ WYVPGDGQWV SSSKKIN* |
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-98 | 40 | 497 | 466 | + 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 |
DDBJ | BAC79743.1 | 0 | 40 | 516 | 38 | 517 | putative alpha 3 glucosyltransferase [Oryza sativa Japonica Group] |
RefSeq | NP_001145139.1 | 0 | 40 | 516 | 40 | 519 | hypothetical protein LOC100278369 [Zea mays] |
RefSeq | XP_001780921.1 | 0 | 53 | 517 | 1 | 466 | predicted protein [Physcomitrella patens subsp. patens] |
RefSeq | XP_002305159.1 | 0 | 44 | 517 | 15 | 491 | predicted protein [Populus trichocarpa] |
RefSeq | XP_002329281.1 | 0 | 44 | 516 | 11 | 485 | predicted protein [Populus trichocarpa] |
Metabolic Pathways | |||
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Pathway Name | Reaction | EC | Protein Name |
dolichyl-diphosphooligosaccharide biosynthesis | RXN-5470 | EC-2.4.1.267 | Dol-P-Glc:Man9GlcNAc2-PP-Dol α-1,3-glucosyltransferase |