Gene Ontology annotation through association of InterPro records with GO terms
Electronic Gene Ontology annotations created by ARBA machine learning models
Combined Automated Annotation using Multiple IEA Methods
UniProtKB/Swiss-Prot entry Q9V2V6 (PSA1_HALVD)
Halophilic 20S proteasomes of the archaeon Haloferax volcanii: purification, characterization, and gene sequence analysis.
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Alpha1 and beta form a four-ring 20S proteasome that hydrolyzes peptides and insulin B-chain; catalysis is assigned to the beta N-terminal threonine.
"The alpha(1)beta-proteasome also hydrolyzed insulin B-chain protein."
Subunit topology of two 20S proteasomes from Haloferax volcanii.
Chemical cross-linking, mass spectrometry, and in silico modeling of proteasomal 20S core particles of the haloarchaeon Haloferax volcanii.
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Alpha-type subunits form the outer rings; beta subunits carry the active sites.
"The α-type subunits form the outer rings and the β-type subunits form the two inner rings which harbor the proteolytic active sites"
Proteasomal components required for cell growth and stress responses in the haloarchaeon Haloferax volcanii.
The N-terminal penultimate residue of 20S proteasome alpha1 influences its N(alpha) acetylation and protein levels as well as growth rate and stress responses of Haloferax volcanii.
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The alpha1 N terminus forms the core particle gate, and its acetylated Met1 form dominates in cells.
"Quantitative mass spectrometry revealed this was the dominant N-terminal form of alpha1 in H. volcanii cells."
Posttranslational modification of the 20S proteasomal proteins of the archaeon Haloferax volcanii.
Phosphorylation and methylation of proteasomal proteins of the haloarcheon Haloferax volcanii.
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Alpha1 is phosphorylated, and a Rio1p kinase homolog phosphorylates it.
"provide evidence that Rio1p Ser/Thr kinase phosphorylates α1"
Analysis of proteasome-dependent proteolysis in Haloferax volcanii cells, using short-lived green fluorescent proteins.
Ubiquitin-like small archaeal modifier proteins (SAMPs) in Haloferax volcanii.