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A5DB52

- PSB4_PICGU

UniProt

A5DB52 - PSB4_PICGU

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Protein

Probable proteasome subunit beta type-4

Gene

PRO2

Organism
Meyerozyma guilliermondii (strain ATCC 6260 / CBS 566 / DSM 6381 / JCM 1539 / NBRC 10279 / NRRL Y-324) (Yeast) (Candida guilliermondii)
Status
Reviewed - Annotation score: 2 out of 5- Protein inferred from homologyi

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).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

Protein family/group databases

MEROPSiT01.984.

Names & Taxonomyi

Protein namesi
Recommended name:
Probable proteasome subunit beta type-4 (EC:3.4.25.1)
Gene namesi
Name:PRO2
ORF Names:PGUG_00507
OrganismiMeyerozyma guilliermondii (strain ATCC 6260 / CBS 566 / DSM 6381 / JCM 1539 / NBRC 10279 / NRRL Y-324) (Yeast) (Candida guilliermondii)
Taxonomic identifieri294746 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesDebaryomycetaceaeMeyerozyma
ProteomesiUP000001997: Unassembled WGS sequence

Subcellular locationi

Cytoplasm PROSITE-ProRule annotation. Nucleus By similarity

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-KW
  2. nucleus Source: UniProtKB-KW
  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 – 194194Probable proteasome subunit beta type-4PRO_0000295032Add
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).By similarity

Protein-protein interaction databases

STRINGi4929.A5DB52.

Structurei

3D structure databases

ProteinModelPortaliA5DB52.
SMRiA5DB52. Positions 1-194.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase T1B family.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG0638.
InParanoidiA5DB52.
KOiK02734.
OrthoDBiEOG7SJDGT.

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.

A5DB52-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MDIVLGIRVE DCTLVATSKA ATRGISVLKD TDDKTRQLNS HNLMAYSGEA
60 70 80 90 100
GDTVQFAEYI QANTQLYTMR ENDTELSPKA TASFVRNQLA TSIRSRKPYQ
110 120 130 140 150
VNVLLAGYDT NTGKPSLNWI DYLGTQVELP YAAHGYAGFY CTSLLDKHYK
160 170 180 190
KGMNFEDGLD LLKKCIKELE TRMPIDFKGC YIKVVDKEGI KLVE
Length:194
Mass (Da):21,766
Last modified:June 12, 2007 - v1
Checksum:i4D7964E1660B0634
GO

Sequence cautioni

The sequence AAN08876.1 differs from that shown. Reason: Frameshift at positions 16 and 23. Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CH408155 Genomic DNA. Translation: EDK36409.1.
AY138984 Genomic DNA. Translation: AAN08876.1. Frameshift.
RefSeqiXP_001487130.1. XM_001487080.1.

Genome annotation databases

GeneIDi5129627.
KEGGipgu:PGUG_00507.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CH408155 Genomic DNA. Translation: EDK36409.1 .
AY138984 Genomic DNA. Translation: AAN08876.1 . Frameshift.
RefSeqi XP_001487130.1. XM_001487080.1.

3D structure databases

ProteinModelPortali A5DB52.
SMRi A5DB52. Positions 1-194.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 4929.A5DB52.

Protein family/group databases

MEROPSi T01.984.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 5129627.
KEGGi pgu:PGUG_00507.

Phylogenomic databases

eggNOGi COG0638.
InParanoidi A5DB52.
KOi K02734.
OrthoDBi EOG7SJDGT.

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

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 6260 / CBS 566 / DSM 6381 / JCM 1539 / NBRC 10279 / NRRL Y-324.
  2. "Positive selection of mutants defective in transcriptional repression of riboflavin synthesis by iron in the flavinogenic yeast Pichia guilliermondii."
    Boretsky Y.R., Kapustyak K.Y., Fayura L.R., Stasyk O.V., Stenchuk M.M., Bobak Y.P., Drobot L.B., Sibirny A.A.
    FEMS Yeast Res. 5:829-837(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-192.

Entry informationi

Entry nameiPSB4_PICGU
AccessioniPrimary (citable) accession number: A5DB52
Secondary accession number(s): Q6YJJ9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 10, 2007
Last sequence update: June 12, 2007
Last modified: October 29, 2014
This is version 42 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

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