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Q9UXC0

- RRP42_SULSO

UniProt

Q9UXC0 - RRP42_SULSO

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Protein
Exosome complex component Rrp42
Gene
rrp42, SSO0732, C20_023
Organism
Sulfolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)
Status
Reviewed - Annotation score: 3 out of 5 - Experimental evidence at protein leveli

Functioni

Non-catalytic component of the exosome, which is a complex involved in RNA degradation. Contributes to the structuring of the Rrp41 active site.2 Publications

GO - Molecular functioni

  1. 3'-5' exonuclease activity Source: InterPro

GO - Biological processi

  1. RNA catabolic process Source: UniProtKB-HAMAP
Complete GO annotation...

Enzyme and pathway databases

BioCyciSSOL273057:GCH2-695-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Exosome complex component Rrp42
Gene namesi
Name:rrp42
Ordered Locus Names:SSO0732
ORF Names:C20_023
OrganismiSulfolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)
Taxonomic identifieri273057 [NCBI]
Taxonomic lineageiArchaeaCrenarchaeotaThermoproteiSulfolobalesSulfolobaceaeSulfolobus
ProteomesiUP000001974: Chromosome

Subcellular locationi

Cytoplasm Reviewed prediction UniRule annotation

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-SubCell
  2. exosome (RNase complex) Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Exosome

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi112 – 1121R → E: Abolishes exoribonuclease activity of the complex; when associated with E-116. 1 Publication
Mutagenesisi116 – 1161R → E: Abolishes exoribonuclease activity of the complex; when associated with E-112. 1 Publication
Mutagenesisi218 – 2181E → A: Does not change activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 275275Exosome complex component Rrp42UniRule annotation
PRO_0000140006Add
BLAST

Interactioni

Subunit structurei

Component of the archaeal exosome complex. Forms a hexameric ring-like arrangement composed of 3 Rrp41-Rrp42 heterodimers. The hexameric ring associates with a trimer of Rrp4 and/or Csl4 subunits.5 Publications

Protein-protein interaction databases

DIPiDIP-60492N.
STRINGi273057.SSO0732.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi13 – 197
Turni20 – 223
Helixi23 – 253
Beta strandi29 – 313
Beta strandi40 – 445
Beta strandi50 – 589
Beta strandi61 – 7212
Beta strandi76 – 783
Beta strandi79 – 813
Beta strandi83 – 908
Turni92 – 943
Beta strandi100 – 1023
Helixi105 – 12016
Helixi126 – 1294
Beta strandi130 – 1323
Turni133 – 1353
Beta strandi136 – 14813
Helixi153 – 16614
Beta strandi169 – 1746
Beta strandi181 – 19010
Beta strandi193 – 1953
Beta strandi198 – 2058
Beta strandi208 – 2125
Helixi215 – 2206
Beta strandi222 – 2298
Turni231 – 2333
Beta strandi235 – 24410
Helixi248 – 27326

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2BR2X-ray2.80A/C/E/G/I/K/M/O/Q/S/U/W1-275[»]
2C37X-ray2.80A/C/E/G/I/K/M/O/Q/S/U/W1-275[»]
2C38X-ray3.10A/C/E/G/I/K/M/O/Q/S/U/W1-275[»]
2C39X-ray3.30A/C/E/G/I/K/M/O/Q/S/U/W1-275[»]
2JE6X-ray1.60A1-275[»]
2JEAX-ray2.33A1-275[»]
2JEBX-ray2.40A1-275[»]
3L7ZX-ray2.41A/D/G1-275[»]
4BA1X-ray1.80A1-275[»]
4BA2X-ray2.50A1-275[»]
ProteinModelPortaliQ9UXC0.
SMRiQ9UXC0. Positions 1-275.

Miscellaneous databases

EvolutionaryTraceiQ9UXC0.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG2123.
HOGENOMiHOG000229504.
KOiK12589.
OMAiFIDIWAL.

Family and domain databases

Gene3Di3.30.230.70. 1 hit.
HAMAPiMF_00622. Exosome_Rrp42.
InterProiIPR001247. ExoRNase_PH_dom1.
IPR015847. ExoRNase_PH_dom2.
IPR020869. Exosome_complex_exonuc_2_prob.
IPR027408. PNPase/RNase_PH_dom.
IPR020568. Ribosomal_S5_D2-typ_fold.
[Graphical view]
PfamiPF01138. RNase_PH. 1 hit.
PF03725. RNase_PH_C. 1 hit.
[Graphical view]
SUPFAMiSSF54211. SSF54211. 2 hits.
SSF55666. SSF55666. 1 hit.

Sequencei

Sequence statusi: Complete.

Q9UXC0-1 [UniParc]FASTAAdd to Basket

« Hide

MSSTPSNQNI IPIIKKESIV SLFEKGIRQD GRKLTDYRPL SITLDYAKKA    50
DGSALVKLGT TMVLAGTKLE IDKPYEDTPN QGNLIVNVEL LPLAYETFEP 100
GPPDENAIEL ARVVDRSLRD SKALDLTKLV IEPGKSVWTV WLDVYVLDYG 150
GNVLDACTLA SVAALYNTKV YKVEQHSNGI SVNKNEVVGK LPLNYPVVTI 200
SVAKVDKYLV VDPDLDEESI MDAKISFSYT PDLKIVGIQK SGKGSMSLQD 250
IDQAENTARS TAVKLLEELK KHLGI 275
Length:275
Mass (Da):30,194
Last modified:May 1, 2000 - v1
Checksum:i4188C9D6928A144C
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
Y18930 Genomic DNA. Translation: CAB57571.1.
AE006641 Genomic DNA. Translation: AAK41030.1.
PIRiG90221.
RefSeqiNP_342240.1. NC_002754.1.
WP_009991305.1. NC_002754.1.

Genome annotation databases

EnsemblBacteriaiAAK41030; AAK41030; SSO0732.
GeneIDi1454997.
KEGGisso:SSO0732.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
Y18930 Genomic DNA. Translation: CAB57571.1 .
AE006641 Genomic DNA. Translation: AAK41030.1 .
PIRi G90221.
RefSeqi NP_342240.1. NC_002754.1.
WP_009991305.1. NC_002754.1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2BR2 X-ray 2.80 A/C/E/G/I/K/M/O/Q/S/U/W 1-275 [» ]
2C37 X-ray 2.80 A/C/E/G/I/K/M/O/Q/S/U/W 1-275 [» ]
2C38 X-ray 3.10 A/C/E/G/I/K/M/O/Q/S/U/W 1-275 [» ]
2C39 X-ray 3.30 A/C/E/G/I/K/M/O/Q/S/U/W 1-275 [» ]
2JE6 X-ray 1.60 A 1-275 [» ]
2JEA X-ray 2.33 A 1-275 [» ]
2JEB X-ray 2.40 A 1-275 [» ]
3L7Z X-ray 2.41 A/D/G 1-275 [» ]
4BA1 X-ray 1.80 A 1-275 [» ]
4BA2 X-ray 2.50 A 1-275 [» ]
ProteinModelPortali Q9UXC0.
SMRi Q9UXC0. Positions 1-275.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

DIPi DIP-60492N.
STRINGi 273057.SSO0732.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAK41030 ; AAK41030 ; SSO0732 .
GeneIDi 1454997.
KEGGi sso:SSO0732.

Phylogenomic databases

eggNOGi COG2123.
HOGENOMi HOG000229504.
KOi K12589.
OMAi FIDIWAL.

Enzyme and pathway databases

BioCyci SSOL273057:GCH2-695-MONOMER.

Miscellaneous databases

EvolutionaryTracei Q9UXC0.

Family and domain databases

Gene3Di 3.30.230.70. 1 hit.
HAMAPi MF_00622. Exosome_Rrp42.
InterProi IPR001247. ExoRNase_PH_dom1.
IPR015847. ExoRNase_PH_dom2.
IPR020869. Exosome_complex_exonuc_2_prob.
IPR027408. PNPase/RNase_PH_dom.
IPR020568. Ribosomal_S5_D2-typ_fold.
[Graphical view ]
Pfami PF01138. RNase_PH. 1 hit.
PF03725. RNase_PH_C. 1 hit.
[Graphical view ]
SUPFAMi SSF54211. SSF54211. 2 hits.
SSF55666. SSF55666. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 35092 / DSM 1617 / JCM 11322 / P2.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 35092 / DSM 1617 / JCM 11322 / P2.
  3. Cited for: INTERACTION WITH EXOSOME.
    Strain: ATCC 35092 / DSM 1617 / JCM 11322 / P2.
  4. "Characterization of native and reconstituted exosome complexes from the hyperthermophilic archaeon Sulfolobus solfataricus."
    Walter P., Klein F., Lorentzen E., Ilchmann A., Klug G., Evguenieva-Hackenberg E.
    Mol. Microbiol. 62:1076-1089(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH EXOSOME.
  5. "The evolutionarily conserved subunits Rrp4 and Csl4 confer different substrate specificities to the archaeal exosome."
    Roppelt V., Klug G., Evguenieva-Hackenberg E.
    FEBS Lett. 584:2931-2936(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBUNIT.
  6. "Heterogeneous complexes of the RNA exosome in Sulfolobus solfataricus."
    Witharana C., Roppelt V., Lochnit G., Klug G., Evguenieva-Hackenberg E.
    Biochimie 94:1578-1587(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH EXOSOME.
    Strain: ATCC 35092 / DSM 1617 / JCM 11322 / P2.
  7. "Structural basis of 3' end RNA recognition and exoribonucleolytic cleavage by an exosome RNase PH core."
    Lorentzen E., Conti E.
    Mol. Cell 20:473-481(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS) IN COMPLEX WITH RRP41, SUBUNIT, MUTAGENESIS OF ARG-112 AND ARG-116.
  8. "The archaeal exosome core is a hexameric ring structure with three catalytic subunits."
    Lorentzen E., Walter P., Fribourg S., Evguenieva-Hackenberg E., Klug G., Conti E.
    Nat. Struct. Mol. Biol. 12:575-581(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS) IN COMPLEX WITH RRP41, FUNCTION, SUBUNIT, MUTAGENESIS OF GLU-218.
  9. Cited for: X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) IN COMPLEX WITH RRP41 AND RRP4, SUBUNIT.
  10. "Crystal structure of the S. solfataricus archaeal exosome reveals conformational flexibility in the RNA-binding ring."
    Lu C., Ding F., Ke A.
    PLoS ONE 5:E8739-E8739(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.41 ANGSTROMS) IN COMPLEX WITH RRP41 AND RRP4.
  11. "Crystal structure of a 9-subunit archaeal exosome in pre-catalytic states of the phosphorolytic reaction."
    Lorentzen E., Conti E.
    Archaea 2012:721869-721869(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) IN COMPLEX WITH RRP41 AND RRP4, SUBUNIT.

Entry informationi

Entry nameiRRP42_SULSO
AccessioniPrimary (citable) accession number: Q9UXC0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 25, 2003
Last sequence update: May 1, 2000
Last modified: September 3, 2014
This is version 79 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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