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Protein

Proteasome subunit beta type-6

Gene

psmB6

Organism
Dictyostelium discoideum (Slime mold)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein 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.1 Publication

Catalytic activityi

Cleavage of peptide bonds with very broad specificity.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei15 – 151NucleophileBy similarity

GO - Molecular functioni

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

GO - Biological processi

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

Keywords - Molecular functioni

Hydrolase, Protease, Threonine protease

Protein family/group databases

MEROPSiT01.010.

Names & Taxonomyi

Protein namesi
Recommended name:
Proteasome subunit beta type-6 (EC:3.4.25.1)
Alternative name(s):
Differentiation-associated proteasome subunit 1
Short name:
DAPS-1
Gene namesi
Name:psmB6
Synonyms:dapA
ORF Names:DDB_G0267390
OrganismiDictyostelium discoideum (Slime mold)
Taxonomic identifieri44689 [NCBI]
Taxonomic lineageiEukaryotaAmoebozoaMycetozoaDictyosteliidaDictyostelium
ProteomesiUP000002195 Componentsi: Chromosome 1, Unassembled WGS sequence

Organism-specific databases

dictyBaseiDDB_G0267390. psmB6.

Subcellular locationi

Cytoplasm PROSITE-ProRule annotation1 Publication. Nucleus 1 Publication

GO - Cellular componenti

  1. cytoplasm Source: dictyBase
  2. nucleus Source: dictyBase
  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
Propeptidei1 – 1414Removed in mature form1 PublicationPRO_0000327384Add
BLAST
Chaini15 – 214200Proteasome subunit beta type-6PRO_0000327385Add
BLAST

Keywords - PTMi

Zymogen

Proteomic databases

PRIDEiQ55GJ6.

Expressioni

Developmental stagei

Maximally expressed 4-6 hours after starvation (around the aggregation-stream stage), followed by a drastic decrease from the mound to tipped aggregate stage.1 Publication

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).By similarity

Protein-protein interaction databases

STRINGi44689.DDB_0191199.

Structurei

3D structure databases

SMRiQ55GJ6. Positions 15-211.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase T1B family.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG0638.
InParanoidiQ55GJ6.
KOiK02738.
OMAiTSIMAVQ.
PhylomeDBiQ55GJ6.

Family and domain databases

Gene3Di3.60.20.10. 1 hit.
InterProiIPR029055. Ntn_hydrolases_N.
IPR000243. Pept_T1A_subB.
IPR016050. Proteasome_bsu_CS.
IPR001353. Proteasome_sua/b.
IPR023333. Proteasome_suB-type.
[Graphical view]
PfamiPF00227. Proteasome. 1 hit.
[Graphical view]
PRINTSiPR00141. PROTEASOME.
SUPFAMiSSF56235. SSF56235. 1 hit.
PROSITEiPS00854. PROTEASOME_BETA_1. 1 hit.
PS51476. PROTEASOME_BETA_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q55GJ6-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEAPEWLDNA VDLGTSIMAV EYDGGVIMGA DSRTTTGAYI ANRVTNKITP
60 70 80 90 100
IHERIYCCRS GSAADTQAIS DYVRYYLEMH TSELCDEPDV KTAASLFQLL
110 120 130 140 150
CYSNKNNLMA GIIVAGWDKH QGGSVYNISL GGSMVKQPFA IGGSGSTYIY
160 170 180 190 200
GYCDSKFKPK MTKDECIEFV QNSLALAMFR DGSSGGVIRL CIIDKNGVER
210
KMIPGNNLPR FWEG
Length:214
Mass (Da):23,446
Last modified:May 24, 2005 - v1
Checksum:i1EA0E6921D37AAE2
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti25 – 251G → R AA sequence (PubMed:8130037).Curated
Sequence conflicti28 – 281M → A AA sequence (PubMed:8130037).Curated
Sequence conflicti95 – 951S → C in BAA25923 (PubMed:9535814).Curated
Sequence conflicti122 – 1221Missing in BAA25923 (PubMed:9535814).Curated
Sequence conflicti165 – 1651E → R in BAA25923 (PubMed:9535814).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB007024 mRNA. Translation: BAA25923.1.
AAFI02000003 Genomic DNA. Translation: EAL73147.1.
PIRiJE0101.
RefSeqiXP_647188.1. XM_642096.1.

Genome annotation databases

EnsemblProtistsiDDB0191199; DDB0191199; DDB_G0267390.
GeneIDi8615992.
KEGGiddi:DDB_G0267390.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB007024 mRNA. Translation: BAA25923.1.
AAFI02000003 Genomic DNA. Translation: EAL73147.1.
PIRiJE0101.
RefSeqiXP_647188.1. XM_642096.1.

3D structure databases

SMRiQ55GJ6. Positions 15-211.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi44689.DDB_0191199.

Protein family/group databases

MEROPSiT01.010.

Proteomic databases

PRIDEiQ55GJ6.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblProtistsiDDB0191199; DDB0191199; DDB_G0267390.
GeneIDi8615992.
KEGGiddi:DDB_G0267390.

Organism-specific databases

dictyBaseiDDB_G0267390. psmB6.

Phylogenomic databases

eggNOGiCOG0638.
InParanoidiQ55GJ6.
KOiK02738.
OMAiTSIMAVQ.
PhylomeDBiQ55GJ6.

Miscellaneous databases

PROiQ55GJ6.

Family and domain databases

Gene3Di3.60.20.10. 1 hit.
InterProiIPR029055. Ntn_hydrolases_N.
IPR000243. Pept_T1A_subB.
IPR016050. Proteasome_bsu_CS.
IPR001353. Proteasome_sua/b.
IPR023333. Proteasome_suB-type.
[Graphical view]
PfamiPF00227. Proteasome. 1 hit.
[Graphical view]
PRINTSiPR00141. PROTEASOME.
SUPFAMiSSF56235. SSF56235. 1 hit.
PROSITEiPS00854. PROTEASOME_BETA_1. 1 hit.
PS51476. PROTEASOME_BETA_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Preferential expression of the cDNA encoding the proteasome subunit during the growth/differentiation transition of Dictyostelium cells."
    Chae S.-C., Maeda Y.
    Biochem. Biophys. Res. Commun. 245:231-234(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], DEVELOPMENTAL STAGE.
    Strain: AX2.
  2. "The genome of the social amoeba Dictyostelium discoideum."
    Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R., Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B., Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T., Lehmann R., Hamlin N.
    , Davies R., Gaudet P., Fey P., Pilcher K., Chen G., Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N., Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E., Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N., Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D., Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T., Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D., Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A., Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M., Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A., Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y., Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C., Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R., Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.
    Nature 435:43-57(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: AX4.
  3. "Proteasomes from Dictyostelium discoideum: characterization of structure and function."
    Schauer T.M., Nesper M., Kehl M., Lottspeich F., Mueller-Taubenberger A., Gerisch G., Baumeister W.
    J. Struct. Biol. 111:135-147(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 15-32, FUNCTION, SUBCELLULAR LOCATION.
    Strain: AX2.

Entry informationi

Entry nameiPSB6_DICDI
AccessioniPrimary (citable) accession number: Q55GJ6
Secondary accession number(s): O60953
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 8, 2008
Last sequence update: May 24, 2005
Last modified: April 1, 2015
This is version 73 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Dictyostelium discoideum
    Dictyostelium discoideum: entries, gene names and cross-references to dictyBase
  2. Peptidase families
    Classification of peptidase families and list of entries
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.