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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: 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. 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

  • 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 - Molecular functioni

Nucleotidyltransferase, Transferase

Keywords - Biological processi

Ribosome biogenesis, Transcription

Keywords - Ligandi

DNA-binding

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

GO - Cellular componenti

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

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.
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. 181 interactors.
DIPiDIP-6577N.
IntActiQ01080. 15 interactors.
MINTiMINT-630569.

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[»]
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.
OMAiTHMFALC.
OrthoDBiEOG092C2DAL.

Family and domain databases

InterProiIPR009668. RNA_pol-assoc_fac_A49-like.
[Graphical view]
PfamiPF06870. RNA_pol_I_A49. 1 hit.
[Graphical view]

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.

Cross-referencesi

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.

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[»]
ProteinModelPortaliQ01080.
SMRiQ01080.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi35591. 181 interactors.
DIPiDIP-6577N.
IntActiQ01080. 15 interactors.
MINTiMINT-630569.

PTM databases

iPTMnetiQ01080.

Proteomic databases

MaxQBiQ01080.
PRIDEiQ01080.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYNL248C; YNL248C; YNL248C.
GeneIDi855473.
KEGGisce:YNL248C.

Organism-specific databases

EuPathDBiFungiDB:YNL248C.
SGDiS000005192. RPA49.

Phylogenomic databases

GeneTreeiENSGT00390000018004.
HOGENOMiHOG000057118.
InParanoidiQ01080.
KOiK03005.
OMAiTHMFALC.
OrthoDBiEOG092C2DAL.

Enzyme and pathway databases

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

Miscellaneous databases

EvolutionaryTraceiQ01080.
PROiQ01080.

Family and domain databases

InterProiIPR009668. RNA_pol-assoc_fac_A49-like.
[Graphical view]
PfamiPF06870. RNA_pol_I_A49. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiRPA49_YEAST
AccessioniPrimary (citable) accession number: Q01080
Secondary accession number(s): D6W0U5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: October 1, 1996
Last modified: November 2, 2016
This is version 140 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal 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
  3. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  4. Yeast chromosome XIV
    Yeast (Saccharomyces cerevisiae) chromosome XIV: entries and gene names

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 one 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.