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Protein

DNA-directed RNA polymerase I subunit RPA49

Gene

RPA49

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: -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. Subunit RPA49 can bind both single-stranded and double-stranded DNA.4 Publications

GO - Molecular functioni

  • DNA binding Source: UniProtKB-KW
  • RNA polymerase I activity Source: UniProtKB

GO - Biological processi

  • nucleolar large rRNA transcription by RNA polymerase I Source: SGD
  • ribosome biogenesis Source: UniProtKB-KW
  • transcription by RNA polymerase I Source: UniProtKB
  • transcription elongation from RNA polymerase I promoter Source: SGD

Keywordsi

Molecular functionDNA-binding, Nucleotidyltransferase, Transferase
Biological processRibosome biogenesis, Transcription

Enzyme and pathway databases

BioCyciYEAST:G3O-33245-MONOMER
ReactomeiR-SCE-73762 RNA Polymerase I Transcription Initiation

Names & Taxonomyi

Protein namesi
Recommended name:
DNA-directed RNA polymerase I subunit RPA49
Short name:
A49
Alternative name(s):
DNA-directed RNA polymerase I 49 kDa polypeptide
Gene namesi
Name:RPA49
Synonyms:RRN13
Ordered Locus Names:YNL248C
ORF Names:N0880
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome XIV

Organism-specific databases

EuPathDBiFungiDB:YNL248C
SGDiS000005192 RPA49

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cell wall Cytoskeleton Vacuole Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

DNA-directed RNA polymerase, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi325 – 326ED → AA: No effect on DNA binding. 1 Publication2
Mutagenesisi356K → A: Loss of DNA binding; when associated with A-358. 1 Publication1
Mutagenesisi358S → A: Loss of DNA binding; when associated with A-356. 1 Publication1
Mutagenesisi359K → A: Loss of DNA binding. 1 Publication1
Mutagenesisi365R → A: Loss of DNA binding. 1 Publication1
Mutagenesisi393K → A: Loss of DNA binding. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000739551 – 415DNA-directed RNA polymerase I subunit RPA49Add BLAST415

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei34PhosphoserineCombined sources1
Modified residuei151PhosphoserineCombined sources1

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ01080
PaxDbiQ01080
PRIDEiQ01080

PTM databases

iPTMnetiQ01080

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 RPA34; 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.6 Publications

Protein-protein interaction databases

BioGridi35591, 486 interactors
ComplexPortaliCPX-1664 DNA-directed RNA Polymerase I complex
DIPiDIP-6577N
IntActiQ01080, 16 interactors
MINTiQ01080
STRINGi4932.YNL248C

Structurei

Secondary structure

1415
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi11 – 16Combined sources6
Beta strandi22 – 25Combined sources4
Beta strandi37 – 42Combined sources6
Beta strandi51 – 56Combined sources6
Beta strandi58 – 65Combined sources8
Helixi70 – 72Combined sources3
Beta strandi74 – 82Combined sources9
Turni83 – 86Combined sources4
Beta strandi87 – 92Combined sources6
Beta strandi95 – 102Combined sources8
Helixi103 – 106Combined sources4
Helixi173 – 184Combined sources12
Helixi198 – 200Combined sources3
Helixi204 – 207Combined sources4
Helixi210 – 213Combined sources4
Helixi219 – 223Combined sources5
Helixi227 – 232Combined sources6
Helixi242 – 247Combined sources6
Helixi253 – 255Combined sources3
Helixi256 – 273Combined sources18
Turni274 – 276Combined sources3
Helixi280 – 284Combined sources5
Helixi292 – 302Combined sources11
Beta strandi303 – 305Combined sources3
Helixi309 – 314Combined sources6
Beta strandi317 – 319Combined sources3
Helixi322 – 339Combined sources18
Turni340 – 342Combined sources3
Beta strandi343 – 345Combined sources3
Helixi346 – 353Combined sources8
Helixi357 – 366Combined sources10
Beta strandi370 – 373Combined sources4
Helixi376 – 382Combined sources7
Helixi386 – 391Combined sources6
Beta strandi392 – 396Combined sources5

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3NFHX-ray2.17A/B154-399[»]
3NFIX-ray1.90A/B/C/D/E171-403[»]
4C2MX-ray2.802/M1-415[»]
4C3HX-ray3.27M1-415[»]
4C3IX-ray3.0M1-415[»]
4C3JX-ray3.35M1-415[»]
4YM7X-ray5.50AM/BM/CM/DM/EM/FM1-415[»]
5G5Lelectron microscopy4.80M1-415[»]
5LMXelectron microscopy4.90M1-415[»]
5M3Felectron microscopy3.80M1-415[»]
5M3Melectron microscopy4.00M1-415[»]
5M5Welectron microscopy3.80M1-415[»]
5M5Xelectron microscopy4.00M1-415[»]
5M5Yelectron microscopy4.00M1-415[»]
5M64electron microscopy4.60M1-415[»]
5N5Yelectron microscopy7.70M1-415[»]
5N5Zelectron microscopy7.70M1-415[»]
5N60electron microscopy7.70M1-415[»]
5N61electron microscopy3.40M1-415[»]
5OA1electron microscopy4.40M1-415[»]
5W5Yelectron microscopy3.80M1-415[»]
5W64electron microscopy4.20M1-415[»]
5W65electron microscopy4.30M1-415[»]
5W66electron microscopy3.90M1-415[»]
ProteinModelPortaliQ01080
SMRiQ01080
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ01080

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni322 – 415Interaction with DNAAdd BLAST94

Sequence similaritiesi

Phylogenomic databases

GeneTreeiENSGT00390000018004
HOGENOMiHOG000057118
InParanoidiQ01080
KOiK03005
OMAiRRMNRVG
OrthoDBiEOG092C2DAL

Family and domain databases

InterProiView protein in InterPro
IPR009668 RNA_pol-assoc_fac_A49-like
PANTHERiPTHR14440 PTHR14440, 1 hit
PfamiView protein in Pfam
PF06870 RNA_pol_I_A49, 1 hit

Sequencei

Sequence statusi: Complete.

Q01080-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSVKRSVSEI EIESVQDQPS VAVGSFFKGF RAPSDTTFDL YKKKKSEKDE
60 70 80 90 100
FVLHGENERL EYEGYTDSSS QASNQYVVGL FNPEKKSIQL YKAPVLVSKV
110 120 130 140 150
VSKSSKNLRG PKIKSKSDTR PSALRNALGE AFGTKKAKKA IADLERNRID
160 170 180 190 200
SDKLTDSAID IVDSVRTASK DLPTRAQLDE ITSNDRPTPL ANIDATDVEQ
210 220 230 240 250
IYPIESIIPK KELQFIRVSS ILKEADKEKK LELFPYQNNS KYVAKKLDSL
260 270 280 290 300
TQPSQMTKLQ LLYYLSLLLG VYENRRVNNK TKLLERLNSP PEILVDGILS
310 320 330 340 350
RFTVIKPGQF GRSKDRSYFI DPQNEDKILC YILAIIMHLD NFIVEITPLA
360 370 380 390 400
HELNLKPSKV VSLFRVLGAI VKGATVAQAE AFGIPKSTAA SYKIATMKVP
410
FKLPEMTRRG RGPRR
Length:415
Mass (Da):46,651
Last modified:October 1, 1996 - v2
Checksum:i3D9BF05440D26021
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti66T → P in AAA34380 (PubMed:1409638).Curated1
Sequence conflicti157S → C in AAA34380 (PubMed:1409638).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M96600 Genomic DNA Translation: AAA34380.1
X96722 Genomic DNA Translation: CAA65496.1
Z71524 Genomic DNA Translation: CAA96155.1
AY558027 Genomic DNA Translation: AAS56353.1
BK006947 Genomic DNA Translation: DAA10311.1
PIRiS63221
RefSeqiNP_014151.1, NM_001183086.1

Genome annotation databases

EnsemblFungiiYNL248C; YNL248C; YNL248C
GeneIDi855473
KEGGisce:YNL248C

Similar proteinsi

Entry informationi

Entry nameiRPA49_YEAST
AccessioniPrimary (citable) accession number: Q01080
Secondary accession number(s): D6W0U5
Entry historyiIntegrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: October 1, 1996
Last modified: June 20, 2018
This is version 155 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

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