ProGP1278 (Hypothetical protein)
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ProGP ID | ProGP1278 (Hypothetical protein) |
Validation Status | Characterized |
Organism Information | |
Organism Name | Haloferax volcanii DS2 |
Domain | Archaea |
Classification | Phylum : Euryarchaeota Class : Halobacteria Orders : Haloferacales Family : Haloferacaceae Genus : Haloferax Species : volcanii Strain : DS2 |
Taxonomic ID (NCBI) | 2246 |
Genome Information | |
GenBank | M62816 |
EMBL | M62816 |
Organism Additional Information | It is an easily culturable moderate halophile |
Gene Information | |
Gene Name | HVO_C0054 |
Protein Information | |
Protein Name | Hypothetical protein |
UniProtKB/SwissProt ID | D4H0E1 |
UniProtKB Sequence | >tr|D4H0E1|D4H0E1_HALVD Uncharacterized protein OS=Haloferax volcanii (strain ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2) OX=309800 GN=HVO_C0054 PE=4 SV=1 MSDKDITRRSILKKIGVGSAVGSFASTGAVAAAENNSTSKSPPKESQPQIEVLAENDSQAIFRLKESGVSHLYRDFSGGVHKSNKEEKNKQENSDNGEKSDDNVQKMTKSEQELRKEVSDKEGELLEVNTGTLQVISEKTEPTTQGEITSSGAEQSERLADRVSSSDIELDDEDFQIDGVEFTDDASSSKSKASATDLDPITEATLDTITKDYGYYSYQFGECNGLVYDTHNYLGIWVEFSDDVETTASGAVGGAICFIALKKLTIPAKWLGIANVSCGALLAVPTSELVDRKYTGGFWDAHGLQWGDEKVKYGYGYSIGKYVLPRAYEDFDIPGVHTEAVDYI |
Subcellular Location | twin arginine translocation pathway |
Function | signal peptidase I |
Glycosylation Status | |
Glycosylation Type | N- (Asn) linked |
Experimentally Validated Glycosite(s) in Full Length Protein | N35, N36, N56 |
Glycosite(s) Annotated Protein Sequence | NNSTSKSPPKE ESQPQIEVLAENDSQAIFR |
Technique(s) used for Glycosylation Detection | UPLC coupled via a nanospray source to a Q-Exactive HFX tandem MS |
Glycan Information | |
Glycan Annotation | Tetrasaccharide Glc-GlcA-GalA-MeGlcA |
Technique(s) used for Glycan Identification | UPLC coupled via a nanospray source to a Q-Exactive HFX tandem MS |
Protein Glycosylation linked (PGL) gene(s) | |
OST ProGT ID | ProGT15 (AglB) |
Additional Comment | Glycosylation and glycosites are predicted by glycoproteomic in-silico analysis of raw experimental data available on PRIDE and jPOST. |
Literature | |
Year of Identification | 2021 |
Reference | Schulze, S., Pfeiffer, F., Garcia, B.A. and Pohlschroder, M., 2021. Comprehensive glycoproteomics shines new light on the complexity and extent of glycosylation in archaea. PLoS biology, 19(6), p.e3001277. |
Corresponding Author | Mechthild Pohlschroder |
Contact | Department of Biology, University of Pennsylvania, Philadelphia, Pennsylvania, United States of America |