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Q9U794

- PSB1_TRYBB

UniProt

Q9U794 - PSB1_TRYBB

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Protein

Proteasome subunit beta type-1

Gene
N/A
Organism
Trypanosoma brucei brucei
Status
Reviewed - Annotation score: 2 out of 5 - Experimental evidence at transcript leveli

Functioni

The proteasome is a multicatalytic proteinase complex which is characterized by its ability to cleave peptides with Arg, Phe, Tyr, Leu, and Glu adjacent to the leaving group at neutral or slightly basic pH. The proteasome has an ATP-dependent proteolytic activity By similarity.

Catalytic activityi

Cleavage of peptide bonds with very broad specificity.

GO - Molecular functioni

  1. threonine-type endopeptidase activity Source: UniProtKB-KW

GO - Biological processi

  1. proteolysis involved in cellular protein catabolic process Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Threonine protease

Names & Taxonomyi

Protein namesi
Recommended name:
Proteasome subunit beta type-1 (EC:3.4.25.1)
Alternative name(s):
20S proteasome subunit beta-6
OrganismiTrypanosoma brucei brucei
Taxonomic identifieri5702 [NCBI]
Taxonomic lineageiEukaryotaEuglenozoaKinetoplastidaTrypanosomatidaeTrypanosoma

Subcellular locationi

Cytoplasm By similarity. Nucleus By similarity

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-SubCell
  2. nucleus Source: UniProtKB-SubCell
  3. proteasome core complex Source: InterPro
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus, Proteasome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 258258Proteasome subunit beta type-1PRO_0000148037Add
BLAST

Interactioni

Subunit structurei

The 26S proteasome consists of a 20S proteasome core and two 19S regulatory subunits. The 20S proteasome core is composed of 28 subunits that are arranged in four stacked rings, resulting in a barrel-shaped structure. The two end rings are each formed by seven alpha subunits, and the two central rings are each formed by seven beta subunits. The catalytic chamber with the active sites is on the inside of the barrel By similarity.

Structurei

3D structure databases

ProteinModelPortaliQ9U794.

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase T1B family.

Family and domain databases

Gene3Di3.60.20.10. 1 hit.
InterProiIPR029055. Ntn_hydrolases_N.
IPR016050. Proteasome_bsu_CS.
IPR001353. Proteasome_sua/b.
IPR023333. Proteasome_suB-type.
[Graphical view]
PfamiPF00227. Proteasome. 1 hit.
[Graphical view]
SUPFAMiSSF56235. SSF56235. 1 hit.
PROSITEiPS00854. PROTEASOME_BETA_1. 1 hit.
PS51476. PROTEASOME_BETA_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9U794-1 [UniParc]FASTAAdd to Basket

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MIEDFSEHHV GEANTLQHHG YPRKLGNSVL TLPLRQGAKG HPQHWSPYTD    50
NGGTIAAIAG SNYVVLGADT RLNGDFCIHT RSDTSKLFKL TDRIFLASSG 100
MQADRLQLQQ MLKYRIQWYQ YNNGGKVPST KAIAKLTSTM LYQRRFFPYY 150
TFNMIVGIDE KGAGVCYSYD PVGSTEPFRY GTCGSASSFV EPLLDCLLTR 200
QHMVTQAPAD LTMEEALGML KNAFTGAAER DIFTGDTVCF HIITADGVGT 250
EMFELRKD 258
Length:258
Mass (Da):28,716
Last modified:May 1, 2000 - v1
Checksum:iAA72EB9FAD9D7383
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF148124 mRNA. Translation: AAF05905.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF148124 mRNA. Translation: AAF05905.1 .

3D structure databases

ProteinModelPortali Q9U794.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Family and domain databases

Gene3Di 3.60.20.10. 1 hit.
InterProi IPR029055. Ntn_hydrolases_N.
IPR016050. Proteasome_bsu_CS.
IPR001353. Proteasome_sua/b.
IPR023333. Proteasome_suB-type.
[Graphical view ]
Pfami PF00227. Proteasome. 1 hit.
[Graphical view ]
SUPFAMi SSF56235. SSF56235. 1 hit.
PROSITEi PS00854. PROTEASOME_BETA_1. 1 hit.
PS51476. PROTEASOME_BETA_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "Functional assignment of the 20 S proteasome from Trypanosoma brucei using mass spectrometry and new bioinformatics approaches."
    Huang L., Jacob R.J., Pegg S.C.H., Baldwin M.A., Wang C.C., Burlingame A.L., Babbitt P.C.
    J. Biol. Chem. 276:28327-28339(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: 427.

Entry informationi

Entry nameiPSB1_TRYBB
AccessioniPrimary (citable) accession number: Q9U794
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 13, 2004
Last sequence update: May 1, 2000
Last modified: June 11, 2014
This is version 54 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)

Miscellaneousi

Documents

  1. Peptidase families
    Classification of peptidase families and list of entries
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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