psmA

Functionⁱ

Component of the proteasome core, a large protease complex with broad specificity involved in protein degradation. The T.acidophilum proteasome is able to cleave oligopeptides after Tyr, Leu, Phe, and to a lesser extent after Glu and Arg. Thus, displays chymotrypsin-like activity and low level of caspase-like and trypsin-like activities.UniRule annotation1 Publication

Miscellaneous

The configuration of the closed gate contains an opening large enough to allow rapid entry of tetrapeptides but able to impede the entry of proteins and longer peptides.

Catalytic activityⁱ

Cleavage of peptide bonds with very broad specificity.UniRule annotation1 Publication

Enzyme regulationⁱ

The formation of the proteasomal ATPase PAN-20S proteasome complex, via the docking of the C-termini of PAN into the intersubunit pockets in the alpha-rings, triggers opening of the gate for substrate entry. Interconversion between the open-gate and close-gate conformations leads to a dynamic regulation of the 20S proteasome proteolysis activity.UniRule annotation2 Publications

Keywordsⁱ

Molecular function	Hydrolase, Protease, Threonine protease

Molecular function

Hydrolase, Protease, Threonine protease

Protein family/group databases

MEROPS protease database More...MEROPSⁱ	T01.970.

MEROPSⁱ

T01.970.

Names & Taxonomyⁱ

Protein namesⁱ	Recommended name: Proteasome subunit alphaUniRule annotation (EC:3.4.25.1UniRule annotation) Alternative name(s): 20S proteasome alpha subunitUniRule annotation Proteasome core protein PsmAUniRule annotation
Gene namesⁱ	Name:psmAUniRule annotation Ordered Locus Names:Ta1288
Organismⁱ	Thermoplasma acidophilum (strain ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165)
Taxonomic identifierⁱ	273075 [NCBI]
Taxonomic lineageⁱ	cellular organisms › Archaea › Euryarchaeota › Thermoplasmata › Thermoplasmatales › Thermoplasmataceae › Thermoplasma › Thermoplasma acidophilum
Proteomesⁱ	UP000001024 Componentⁱ: Chromosome

Subcellular locationⁱ

Cytoplasm
UniRule annotation
Manual assertion according to rulesⁱ
- HAMAP-Rule:MF_00289

GO - Cellular componentⁱ

cytoplasm Source: UniProtKB-SubCell
proteasome core complex, alpha-subunit complex
Source: UniProtKB
Inferred from direct assayⁱ

Complete GO annotation...

Keywords - Cellular componentⁱ

Cytoplasm, Proteasome

Pathology & Biotechⁱ

Mutagenesis

Feature key	Position(s)	DescriptionActions	Length
Mutagenesisⁱ	1 – 12	Missing : Markedly increases peptidolytic activity. Designated open-gate mutant. 1 PublicationAdd BLAST	12
Mutagenesisⁱ	66	K → A: Prevents PAN to associate with the proteasome and stimulate gate opening. 1 Publication	1
Mutagenesisⁱ	81	L → A, E or G: Prevents PAN to stimulate gate opening. 1 Publication	1
Mutagenesisⁱ	82	V → A: No effect on PAN's ability to stimulate gate opening. 1 Publication	1
Mutagenesisⁱ	82	V → D or G: Prevents PAN to stimulate gate opening. 1 Publication	1

PTM / Processingⁱ

Molecule processing

Feature key	Position(s)	DescriptionActions	Graphical view	Length
ChainⁱPRO_0000124189	1 – 233	Proteasome subunit alphaAdd BLAST		233

Post-translational modificationⁱ

The N-terminus is blocked.

Proteomic databases

PRIDEⁱ	P25156.

PRIDEⁱ

P25156.

Interactionⁱ

Subunit structureⁱ

The 20S proteasome core is composed of 14 alpha and 14 beta subunits that assemble into four stacked heptameric rings, resulting in a barrel-shaped structure. The two inner rings, each composed of seven catalytic beta subunits, are sandwiched by two outer rings, each composed of seven alpha subunits. The catalytic chamber with the active sites is on the inside of the barrel. Has a gated structure, the ends of the cylinder being occluded by the N-termini of the alpha-subunits. Is capped at one or both ends by the proteasome regulatory ATPase, PAN.UniRule annotation6 Publications

Protein-protein interaction databases

STRINGⁱ	273075.Ta1288.

STRINGⁱ

273075.Ta1288.

Structureⁱ

Secondary structure

Legend: HelixTurnBeta strandPDB Structure known for this area

Show more details

Feature key	Position(s)	DescriptionActions	Length
Beta strandⁱ	13 – 15	Combined sources	3
Helixⁱ	22 – 31	Combined sources	10
Beta strandⁱ	37 – 42	Combined sources	6
Beta strandⁱ	45 – 50	Combined sources	6
Beta strandⁱ	57 – 59	Combined sources	3
Beta strandⁱ	61 – 63	Combined sources	3
Beta strandⁱ	66 – 71	Combined sources	6
Beta strandⁱ	74 – 81	Combined sources	8
Helixⁱ	82 – 103	Combined sources	22
Helixⁱ	109 – 122	Combined sources	14
Turnⁱ	123 – 125	Combined sources	3
Beta strandⁱ	126 – 129	Combined sources	4
Beta strandⁱ	134 – 141	Combined sources	8
Beta strandⁱ	146 – 151	Combined sources	6
Beta strandⁱ	157 – 166	Combined sources	10
Helixⁱ	169 – 179	Combined sources	11
Helixⁱ	186 – 199	Combined sources	14
Helixⁱ	202 – 204	Combined sources	3
Beta strandⁱ	211 – 216	Combined sources	6
Beta strandⁱ	222 – 224	Combined sources	3
Helixⁱ	226 – 230	Combined sources	5

3D structure databases

Select the link destinations: Protein Data Bank Europe More...PDBeⁱ Protein Data Bank RCSB More...RCSB PDBⁱ Protein Data Bank Japan More...PDBjⁱ Links Updated	PDB entry	Method	Resolution (Å)	Chain	Positions	PDBsum
	1PMA	X-ray	3.40	A/C/D/E/F/G/H/I/J/K/L/M/N/O	1-233	[»]
	1YA7	X-ray	2.30	A/B/C/D/E/F/G	1-233	[»]
	1YAR	X-ray	1.90	A/B/C/D/E/F/G	1-233	[»]
	1YAU	X-ray	2.40	A/B/C/D/E/F/G	1-233	[»]
	2KU1	NMR	-	A/B/C/D/E/F/G	1-233	[»]
	2KU2	NMR	-	A/B/C/D/E/F/G	1-233	[»]
	3C91	electron microscopy	6.80	A/B/C/D/E/F/G/O/P/Q/R/S/T/U	1-233	[»]
	3C92	electron microscopy	6.80	A/B/C/D/E/F/G/O/P/Q/R/S/T/U	1-233	[»]
	3IPM	X-ray	4.00	A/B/C/D/E/F/G	1-233	[»]
	3J9I	electron microscopy	3.30	A/B/C/D/E/F/G/O/P/Q/R/S/T/U	10-233	[»]
	3JRM	X-ray	2.90	A/B/C/D/E/F/G	7-233	[»]
	3JSE	X-ray	2.90	A/B/C/D/E/F/G	7-233	[»]
	3JTL	X-ray	3.20	A/B/C/D/E/F/G	7-233	[»]
ProteinModelPortalⁱ	P25156.
SMRⁱ	P25156.
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Miscellaneous databases

EvolutionaryTraceⁱ	P25156.

EvolutionaryTraceⁱ

P25156.

Family & Domainsⁱ

Sequence similaritiesⁱ

Belongs to the peptidase T1A family.UniRule annotation

Phylogenomic databases

eggNOGⁱ	arCOG00971. Archaea. COG0638. LUCA.
HOGENOMⁱ	HOG000091085.
KEGG Orthology (KO) More...KOⁱ	K03432.
OMAⁱ	QMGYDRA.
Database of Orthologous Groups More...OrthoDBⁱ	POG093Z086S.

Family and domain databases

Conserved Domains Database More...CDDⁱ	cd03756. proteasome_alpha_archeal. 1 hit.
Gene3Dⁱ	3.60.20.10. 1 hit.
HAMAPⁱ	MF_00289_A. Proteasome_A_A. 1 hit.
InterProⁱ	View protein in InterPro IPR029055. Ntn_hydrolases_N. IPR023332. Proteasome_alpha-type. IPR019982. Proteasome_asu_arc. IPR000426. Proteasome_asu_N. IPR001353. Proteasome_sua/b.
Pfam protein domain database More...Pfamⁱ	View protein in Pfam PF00227. Proteasome. 1 hit. PF10584. Proteasome_A_N. 1 hit.
SMARTⁱ	View protein in SMART SM00948. Proteasome_A_N. 1 hit.
SUPFAMⁱ	SSF56235. SSF56235. 1 hit.
TIGRFAMsⁱ	TIGR03633. arc_protsome_A. 1 hit.
PROSITEⁱ	View protein in PROSITE PS00388. PROTEASOME_ALPHA_1. 1 hit. PS51475. PROTEASOME_ALPHA_2. 1 hit.

Sequenceⁱ

Sequence statusⁱ: Complete.

P25156-1 [UniParc]FASTA Add to basket

« Hide

        10         20         30         40         50
MQQGQMAYDR AITVFSPDGR LFQVEYAREA VKKGSTALGM KFANGVLLIS 
        60         70         80         90        100
DKKVRSRLIE QNSIEKIQLI DDYVAAVTSG LVADARVLVD FARISAQQEK 
       110        120        130        140        150
VTYGSLVNIE NLVKRVADQM QQYTQYGGVR PYGVSLIFAG IDQIGPRLFD 
       160        170        180        190        200
CDPAGTINEY KATAIGSGKD AVVSFLEREY KENLPEKEAV TLGIKALKSS 
       210        220        230 
LEEGEELKAP EIASITVGNK YRIYDQEEVK KFL

Length:233

Mass (Da):25,799

Last modified:October 1, 1994 - v2

Checksum:ⁱ141A48581DA0DFB5

GO

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	X59507 Genomic DNA. Translation: CAA42094.1. AL445067 Genomic DNA. Translation: CAC12411.1.
PIRⁱ	S55350.
NCBI Reference Sequences More...RefSeqⁱ	WP_010901695.1. NC_002578.1.

Genome annotation databases

EnsemblBacteriaⁱ	CAC12411; CAC12411; CAC12411.
GeneIDⁱ	1456771.
KEGGⁱ	tac:Ta1288.

Similar proteinsⁱ

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:

100%	UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%	UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%	UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.

Cross-referencesⁱ

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	X59507 Genomic DNA. Translation: CAA42094.1. AL445067 Genomic DNA. Translation: CAC12411.1.
PIRⁱ	S55350.
NCBI Reference Sequences More...RefSeqⁱ	WP_010901695.1. NC_002578.1.

3D structure databases

Select the link destinations: Protein Data Bank Europe More...PDBeⁱ Protein Data Bank RCSB More...RCSB PDBⁱ Protein Data Bank Japan More...PDBjⁱ Links Updated	PDB entry	Method	Resolution (Å)	Chain	Positions	PDBsum
	1PMA	X-ray	3.40	A/C/D/E/F/G/H/I/J/K/L/M/N/O	1-233	[»]
	1YA7	X-ray	2.30	A/B/C/D/E/F/G	1-233	[»]
	1YAR	X-ray	1.90	A/B/C/D/E/F/G	1-233	[»]
	1YAU	X-ray	2.40	A/B/C/D/E/F/G	1-233	[»]
	2KU1	NMR	-	A/B/C/D/E/F/G	1-233	[»]
	2KU2	NMR	-	A/B/C/D/E/F/G	1-233	[»]
	3C91	electron microscopy	6.80	A/B/C/D/E/F/G/O/P/Q/R/S/T/U	1-233	[»]
	3C92	electron microscopy	6.80	A/B/C/D/E/F/G/O/P/Q/R/S/T/U	1-233	[»]
	3IPM	X-ray	4.00	A/B/C/D/E/F/G	1-233	[»]
	3J9I	electron microscopy	3.30	A/B/C/D/E/F/G/O/P/Q/R/S/T/U	10-233	[»]
	3JRM	X-ray	2.90	A/B/C/D/E/F/G	7-233	[»]
	3JSE	X-ray	2.90	A/B/C/D/E/F/G	7-233	[»]
	3JTL	X-ray	3.20	A/B/C/D/E/F/G	7-233	[»]
ProteinModelPortalⁱ	P25156.
SMRⁱ	P25156.
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Protein-protein interaction databases

STRINGⁱ	273075.Ta1288.

STRINGⁱ

273075.Ta1288.

Protein family/group databases

MEROPS protease database More...MEROPSⁱ	T01.970.

MEROPSⁱ

T01.970.

Proteomic databases

PRIDEⁱ	P25156.

PRIDEⁱ

P25156.

Protocols and materials databases

Structural Biology Knowledgebase	Search...

Structural Biology Knowledgebase

Search...

Genome annotation databases

EnsemblBacteriaⁱ	CAC12411; CAC12411; CAC12411.
GeneIDⁱ	1456771.
KEGGⁱ	tac:Ta1288.

Phylogenomic databases

eggNOGⁱ	arCOG00971. Archaea. COG0638. LUCA.
HOGENOMⁱ	HOG000091085.
KEGG Orthology (KO) More...KOⁱ	K03432.
OMAⁱ	QMGYDRA.
Database of Orthologous Groups More...OrthoDBⁱ	POG093Z086S.

Miscellaneous databases

EvolutionaryTraceⁱ	P25156.

EvolutionaryTraceⁱ

P25156.

Family and domain databases

Conserved Domains Database More...CDDⁱ	cd03756. proteasome_alpha_archeal. 1 hit.
Gene3Dⁱ	3.60.20.10. 1 hit.
HAMAPⁱ	MF_00289_A. Proteasome_A_A. 1 hit.
InterProⁱ	View protein in InterPro IPR029055. Ntn_hydrolases_N. IPR023332. Proteasome_alpha-type. IPR019982. Proteasome_asu_arc. IPR000426. Proteasome_asu_N. IPR001353. Proteasome_sua/b.
Pfam protein domain database More...Pfamⁱ	View protein in Pfam PF00227. Proteasome. 1 hit. PF10584. Proteasome_A_N. 1 hit.
SMARTⁱ	View protein in SMART SM00948. Proteasome_A_N. 1 hit.
SUPFAMⁱ	SSF56235. SSF56235. 1 hit.
TIGRFAMsⁱ	TIGR03633. arc_protsome_A. 1 hit.
PROSITEⁱ	View protein in PROSITE PS00388. PROTEASOME_ALPHA_1. 1 hit. PS51475. PROTEASOME_ALPHA_2. 1 hit.
ProtoNetⁱ	Search...

Entry informationⁱ

Entry nameⁱ	PSA_THEAC
Accessionⁱ	P25156Primary (citable) accession number: P25156
Entry historyⁱ	Integrated into UniProtKB/Swiss-Prot:	May 1, 1992
	Last sequence update:	October 1, 1994
	Last modified:	June 7, 2017
	This is version 140 of the entry and version 2 of the sequence. See complete history.
Entry statusⁱ	Reviewed (UniProtKB/Swiss-Prot)
Annotation program	Prokaryotic Protein Annotation Program

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UniProtKB - P25156 (PSA_THEAC)

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Proteasome subunit alpha

Select a section on the left to see content.

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Miscellaneous

<p>This subsection of the ‘Function’ section describes an enzyme regulatory mechanism and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/enzyme_regulation' target='_top'>More...</a></p>Enzyme regulationi

<p>This subsection of the ‘Function’ section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>Kineticsi

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Biological processi

Protein family/group databases

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Cellular componenti

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Mutagenesis

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Proteomic databases

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

Protein-protein interaction databases

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

3D structure databases

Miscellaneous databases

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Phylogenomic databases

Family and domain databases

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including length and molecular weight.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

Sequence databases

Genome annotation databases

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

3D structure databases

Protein-protein interaction databases

Protein family/group databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Phylogenomic databases

Miscellaneous databases

Family and domain databases

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Documents

Functionⁱ

Enzyme regulationⁱ

Kineticsⁱ

GO - Molecular functionⁱ

GO - Biological processⁱ

Names & Taxonomyⁱ

Subcellular locationⁱ

GO - Cellular componentⁱ

Pathology & Biotechⁱ

PTM / Processingⁱ

Interactionⁱ

Structureⁱ

Family & Domainsⁱ

Sequence similaritiesⁱ

Sequenceⁱ

Cross-referencesⁱ

Entry informationⁱ

Miscellaneousⁱ