ProGP1235 (DUF192 family protein)
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| ProGP ID | ProGP1235 (DUF192 family 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_0504 |
| Protein Information | |
| Protein Name | DUF192 family protein |
| UniProtKB/SwissProt ID | D4GS41 |
| UniProtKB Sequence | >tr|D4GS41|D4GS41_HALVD DUF192 family protein OS=Haloferax volcanii (strain ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2) OX=309800 GN=HVO_0504 PE=4 SV=1 MTSRARTALLVVAVVVAVASVAYLTNPAVVPGSTDGYERTTLTVVDDETGETLATVNARVADTRAKRFTGLSDTESLAENEGMWFVHDSSGTYAYVMRDMDFPLDIVFVAENGTITRIHHAELDPEGTSESDLTRYRGTGKYVLELPYGYTNETGIDAGDRVEVE |
| Subcellular Location | Sec pathway |
| Function | signal peptidase I |
| Glycosylation Status | |
| Glycosylation Type | N- (Asn) linked |
| Experimentally Validated Glycosite(s) in Full Length Protein | N112 |
| Glycosite(s) Annotated Protein Sequence | NGTITRIHHAE |
| 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 |