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Protein

DNA-directed RNA polymerase I subunit RPA34

Gene

RPA34

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

DNA-dependent RNA polymerases catalyze the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Component of RNA polymerase I (Pol I) which synthesizes ribosomal RNA precursors. Besides, RNA polymerase I has intrinsic RNA cleavage activity. The heterodimer formed by RPA34 and RPA49 stimulates transcript elongation by Pol I.5 Publications

GO - Molecular functioni

  • RNA polymerase I activity Source: UniProtKB

GO - Biological processi

  • ribosome biogenesis Source: UniProtKB-KW
  • transcription elongation from RNA polymerase I promoter Source: SGD
  • transcription from RNA polymerase I promoter Source: UniProtKB
  • transcription of nuclear large rRNA transcript from RNA polymerase I promoter Source: SGD
Complete GO annotation...

Keywords - Biological processi

Ribosome biogenesis, Transcription

Enzyme and pathway databases

BioCyciYEAST:G3O-31592-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
DNA-directed RNA polymerase I subunit RPA34
Short name:
A34
Alternative name(s):
DNA-directed DNA-dependent RNA polymerase 34.5 kDa polypeptide
Short name:
A34.5
Gene namesi
Name:RPA34
Ordered Locus Names:YJL148W
ORF Names:J0637
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311 Componenti: Chromosome X

Organism-specific databases

CYGDiYJL148w.
EuPathDBiFungiDB:YJL148W.
SGDiS000003684. RPA34.

Subcellular locationi

GO - Cellular componenti

  • DNA-directed RNA polymerase I complex Source: UniProtKB
  • nucleolus Source: SGD
  • nucleus Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

DNA-directed RNA polymerase, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 233233DNA-directed RNA polymerase I subunit RPA34PRO_0000203031Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei10 – 101Phosphoserine2 Publications
Modified residuei12 – 121Phosphoserine2 Publications
Modified residuei14 – 141Phosphoserine3 Publications
Modified residuei60 – 601Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP47006.
PaxDbiP47006.
PeptideAtlasiP47006.

Expressioni

Gene expression databases

GenevestigatoriP47006.

Interactioni

Subunit structurei

Component of the RNA polymerase I (Pol I) complex consisting of 14 subunits: RPA135, RPA190, RPC40, RPA14, RPB5, RPO26, RPA43, RPB8, RPA12, RPB10, RPC19, RPC10, RPA49 and RPA34. The complex is composed of a horseshoe-shaped core containing ten subunits (RPA135, RPA190, RPB5, RPO26, RPB8, RPB10, RPC10, RPA12, RPC19 and RPC40) where RPA135 and RPA190 form the DNA-binding cleft. Outside of the core, RPA14 and RPA43 form the stalk that mediates interactions with transcription initiation factors and newly synthesized RNA. Forms a TFIIF-like heterodimer with RPA49; the heterodimer formed by RPA34 and RPA49 can be dissociated from the Pol I core giving rise to a 12 subunit form A* of Pol I (formerly called pol A) that shows impaired transcript elongation activity and increased sensitivity to alpha-amanitin. The heterodimer formed by RPA34 and RPA49 stabilizes subunit RPA12 and stimulates RPA12-dependent RNA cleavage.8 Publications

Protein-protein interaction databases

BioGridi33610. 324 interactions.
DIPiDIP-7973N.
IntActiP47006. 27 interactions.
MINTiMINT-2732801.
STRINGi4932.YJL148W.

Structurei

Secondary structure

1
233
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi29 – 313Combined sources
Beta strandi52 – 598Combined sources
Turni64 – 663Combined sources
Beta strandi68 – 714Combined sources
Beta strandi74 – 763Combined sources
Beta strandi79 – 824Combined sources
Beta strandi85 – 917Combined sources
Helixi93 – 964Combined sources
Beta strandi99 – 1013Combined sources
Beta strandi106 – 1127Combined sources
Beta strandi116 – 1216Combined sources
Beta strandi125 – 1273Combined sources
Beta strandi134 – 1418Combined sources
Helixi150 – 1534Combined sources
Helixi177 – 1793Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4C2MX-ray2.803/N1-233[»]
4C3HX-ray3.27N1-233[»]
4C3IX-ray3.0N1-233[»]
4C3JX-ray3.35N1-233[»]
ProteinModelPortaliP47006.
SMRiP47006. Positions 25-181.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi184 – 23350Glu/Lys-richAdd
BLAST
Compositional biasi208 – 2158Poly-Lys
Compositional biasi221 – 23010Poly-Lys

Sequence similaritiesi

Phylogenomic databases

eggNOGiNOG39958.
InParanoidiP47006.
KOiK03003.
OMAiHFPTGYG.
OrthoDBiEOG7CK3K9.

Family and domain databases

InterProiIPR013240. DNA-dir_RNA_pol1_su_RPA34.
[Graphical view]
PfamiPF08208. RNA_polI_A34. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P47006-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSKLSKDYVS DSDSDDEVIS NEFSIPDGFK KCKHLKNFPL NGDNKKKAKQ
60 70 80 90 100
QQVWLIKFPS NVDISKLKSL PVDFESSTTM TIDKHDYKIM DDTDIESSLT
110 120 130 140 150
QDNLSNMTLL VPSESKESLK IASTAKDNAP LQFDKVFSVS ETAKIPAIDY
160 170 180 190 200
SKVRVPRKDV PKVEGLKLEH FATGYDAEDF HVAEEVKENK KEPKKRSHHD
210 220 230
DEEESSEKKK KKKEKREKRE KKDKKDKKKK HRD
Length:233
Mass (Da):26,875
Last modified:February 1, 1996 - v1
Checksum:iDCD42DFEC574EDB6
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z49423 Genomic DNA. Translation: CAA89443.1.
X87371 Genomic DNA. Translation: CAA60807.1.
BK006943 Genomic DNA. Translation: DAA08653.1.
PIRiS55165.
RefSeqiNP_012387.1. NM_001181581.1.

Genome annotation databases

EnsemblFungiiYJL148W; YJL148W; YJL148W.
GeneIDi853293.
KEGGisce:YJL148W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z49423 Genomic DNA. Translation: CAA89443.1.
X87371 Genomic DNA. Translation: CAA60807.1.
BK006943 Genomic DNA. Translation: DAA08653.1.
PIRiS55165.
RefSeqiNP_012387.1. NM_001181581.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4C2MX-ray2.803/N1-233[»]
4C3HX-ray3.27N1-233[»]
4C3IX-ray3.0N1-233[»]
4C3JX-ray3.35N1-233[»]
ProteinModelPortaliP47006.
SMRiP47006. Positions 25-181.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi33610. 324 interactions.
DIPiDIP-7973N.
IntActiP47006. 27 interactions.
MINTiMINT-2732801.
STRINGi4932.YJL148W.

Proteomic databases

MaxQBiP47006.
PaxDbiP47006.
PeptideAtlasiP47006.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYJL148W; YJL148W; YJL148W.
GeneIDi853293.
KEGGisce:YJL148W.

Organism-specific databases

CYGDiYJL148w.
EuPathDBiFungiDB:YJL148W.
SGDiS000003684. RPA34.

Phylogenomic databases

eggNOGiNOG39958.
InParanoidiP47006.
KOiK03003.
OMAiHFPTGYG.
OrthoDBiEOG7CK3K9.

Enzyme and pathway databases

BioCyciYEAST:G3O-31592-MONOMER.

Miscellaneous databases

NextBioi973600.
PROiP47006.

Gene expression databases

GenevestigatoriP47006.

Family and domain databases

InterProiIPR013240. DNA-dir_RNA_pol1_su_RPA34.
[Graphical view]
PfamiPF08208. RNA_polI_A34. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Sequence analysis of a 40.7 kb segment from the left arm of yeast chromosome X reveals 14 known genes and 13 new open reading frames including homologues of genes clustered on the right arm of chromosome XI."
    Katsoulou C., Tzermia M., Tavernarakis N., Alexandraki D.
    Yeast 12:787-797(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 96604 / S288c / FY1679.
  2. "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome X."
    Galibert F., Alexandraki D., Baur A., Boles E., Chalwatzis N., Chuat J.-C., Coster F., Cziepluch C., de Haan M., Domdey H., Durand P., Entian K.-D., Gatius M., Goffeau A., Grivell L.A., Hennemann A., Herbert C.J., Heumann K.
    , Hilger F., Hollenberg C.P., Huang M.-E., Jacq C., Jauniaux J.-C., Katsoulou C., Kirchrath L., Kleine K., Kordes E., Koetter P., Liebl S., Louis E.J., Manus V., Mewes H.-W., Miosga T., Obermaier B., Perea J., Pohl T.M., Portetelle D., Pujol A., Purnelle B., Ramezani Rad M., Rasmussen S.W., Rose M., Rossau R., Schaaff-Gerstenschlaeger I., Smits P.H.M., Scarcez T., Soriano N., To Van D., Tzermia M., Van Broekhoven A., Vandenbol M., Wedler H., von Wettstein D., Wambutt R., Zagulski M., Zollner A., Karpfinger-Hartl L.
    EMBO J. 15:2031-2049(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  3. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  4. "A34.5, a nonessential component of yeast RNA polymerase I, cooperates with subunit A14 and DNA topoisomerase I to produce a functional rRNA synthesis machine."
    Gadal O., Mariotte-Labarre S., Chedin S., Quemeneur E., Carles C., Sentenac A., Thuriaux P.
    Mol. Cell. Biol. 17:1787-1795(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, IDENTIFICATION IN THE RNA POL I COMPLEX, PHOSPHORYLATION.
  5. "Differential roles of phosphorylation in the formation of transcriptional active RNA polymerase I."
    Fath S., Milkereit P., Peyroche G., Riva M., Carles C., Tschochner H.
    Proc. Natl. Acad. Sci. U.S.A. 98:14334-14339(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN THE RNA POL I COMPLEX.
  6. "Large-scale phosphorylation analysis of alpha-factor-arrested Saccharomyces cerevisiae."
    Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J., Elias J.E., Gygi S.P.
    J. Proteome Res. 6:1190-1197(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-10; SER-12 AND SER-14, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Strain: ADR376.
  7. "A multidimensional chromatography technology for in-depth phosphoproteome analysis."
    Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.
    Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-14 AND SER-60, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  8. "Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution."
    Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.
    Science 325:1682-1686(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-10; SER-12 AND SER-14, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  9. "RNA polymerase I contains a TFIIF-related DNA-binding subcomplex."
    Geiger S.R., Lorenzen K., Schreieck A., Hanecker P., Kostrewa D., Heck A.J., Cramer P.
    Mol. Cell 39:583-594(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH RPA49, IDENTIFICATION BY MASS SPECTROMETRY, SUBUNIT.
  10. "Localization of the yeast RNA polymerase I-specific subunits."
    Bischler N., Brino L., Carles C., Riva M., Tschochner H., Mallouh V., Schultz P.
    EMBO J. 21:4136-4144(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: ELECTRON MICROSCOPY OF THE RNA POLYMERASE I COMPLEX.
  11. "Rpa12p, a conserved RNA polymerase I subunit with two functional domains."
    Van Mullem V., Landrieux E., Vandenhaute J., Thuriaux P.
    Mol. Microbiol. 43:1105-1113(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN THE RNA POL I COMPLEX.
  12. "The A14-A43 heterodimer subunit in yeast RNA pol I and their relationship to Rpb4-Rpb7 pol II subunits."
    Peyroche G., Levillain E., Siaut M., Callebaut I., Schultz P., Sentenac A., Riva M., Carles C.
    Proc. Natl. Acad. Sci. U.S.A. 99:14670-14675(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN THE RNA POL I COMPLEX.
  13. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
  14. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  15. Cited for: STRUCTURE BY ELECTRON MICROSCOPY (12.00 ANGSTROMS) OF THE POL I COMPLEX, FUNCTION, SUBUNIT.
  16. Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF THE POL I COMPLEX, FUNCTION, SUBUNIT.
  17. "RNA polymerase I structure and transcription regulation."
    Engel C., Sainsbury S., Cheung A.C., Kostrewa D., Cramer P.
    Nature 502:650-655(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF THE POL I COMPLEX, FUNCTION, SUBUNIT.

Entry informationi

Entry nameiRPA34_YEAST
AccessioniPrimary (citable) accession number: P47006
Secondary accession number(s): D6VW37
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: February 1, 1996
Last modified: May 27, 2015
This is version 117 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 3360 molecules/cell in log phase SD medium.1 Publication

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
  3. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  4. Yeast chromosome X
    Yeast (Saccharomyces cerevisiae) chromosome X: entries and gene names

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.