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Protein

DNA-directed RNA polymerases I, II, and III subunit RPABC3

Gene

RPB8

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. Common component of RNA polymerases I, II and III which synthesize ribosomal RNA precursors, mRNA precursors and many functional non-coding RNAs, and small RNAs, such as 5S rRNA and tRNAs, respectively.3 Publications

GO - Molecular functioni

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

GO - Biological processi

  • ribosome biogenesis Source: UniProtKB-KW
  • termination of RNA polymerase III transcription Source: Reactome
  • transcription, RNA-templated Source: GOC
  • transcription elongation from RNA polymerase III promoter Source: Reactome
  • transcription from RNA polymerase III promoter Source: SGD
  • transcription from RNA polymerase II promoter Source: SGD
  • transcription from RNA polymerase I promoter Source: UniProtKB
  • tRNA transcription from RNA polymerase III promoter Source: SGD
Complete GO annotation...

Keywords - Biological processi

Ribosome biogenesis, Transcription

Keywords - Ligandi

DNA-binding

Enzyme and pathway databases

BioCyciYEAST:G3O-33723-MONOMER.
ReactomeiR-SCE-113418. Formation of the Early Elongation Complex.
R-SCE-674695. RNA Polymerase II Pre-transcription Events.
R-SCE-6781823. Formation of TC-NER Pre-Incision Complex.
R-SCE-6782135. Dual incision in TC-NER.
R-SCE-6782210. Gap-filling DNA repair synthesis and ligation in TC-NER.
R-SCE-6796648. TP53 Regulates Transcription of DNA Repair Genes.
R-SCE-72086. mRNA Capping.
R-SCE-72165. mRNA Splicing - Minor Pathway.
R-SCE-73762. RNA Polymerase I Transcription Initiation.
R-SCE-73776. RNA Polymerase II Promoter Escape.
R-SCE-73779. RNA Polymerase II Transcription Pre-Initiation And Promoter Opening.
R-SCE-73780. RNA Polymerase III Chain Elongation.
R-SCE-73980. RNA Polymerase III Transcription Termination.
R-SCE-749476. RNA Polymerase III Abortive And Retractive Initiation.
R-SCE-75953. RNA Polymerase II Transcription Initiation.
R-SCE-76042. RNA Polymerase II Transcription Initiation And Promoter Clearance.
R-SCE-76061. RNA Polymerase III Transcription Initiation From Type 1 Promoter.
R-SCE-76066. RNA Polymerase III Transcription Initiation From Type 2 Promoter.
R-SCE-76071. RNA Polymerase III Transcription Initiation From Type 3 Promoter.
R-SCE-77075. RNA Pol II CTD phosphorylation and interaction with CE.

Names & Taxonomyi

Protein namesi
Recommended name:
DNA-directed RNA polymerases I, II, and III subunit RPABC3
Short name:
RNA polymerases I, II, and III subunit ABC3
Alternative name(s):
ABC14.4
ABC14.5
DNA-directed RNA polymerases I, II, and III 14.5 kDa polypeptide
Gene namesi
Name:RPB8
Ordered Locus Names:YOR224C
ORF Names:YOR50-14
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome XV

Organism-specific databases

EuPathDBiFungiDB:YOR224C.
SGDiS000005750. RPB8.

Subcellular locationi

GO - Cellular componenti

  • DNA-directed RNA polymerase I complex Source: UniProtKB
  • DNA-directed RNA polymerase II, core complex Source: SGD
  • DNA-directed RNA polymerase III complex Source: SGD
  • nucleoplasm Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

DNA-directed RNA polymerase, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedCombined sources
ChainiPRO_00000740012 – 146DNA-directed RNA polymerases I, II, and III subunit RPABC3Add BLAST145

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylserineCombined sources1
Modified residuei68PhosphothreonineCombined sources1

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiP20436.
PRIDEiP20436.

PTM databases

iPTMnetiP20436.

Interactioni

Subunit structurei

Component of the RNA polymerase I (Pol I), RNA polymerase II (Pol II) and RNA polymerase III (Pol III) complexes. 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. Component of the RNA polymerase II (Pol II) complex consisting of 12 subunits: RPO21, RPB2, RPB3, RPB4, RPB5, RPO26, RPB7, RPB8, RPB9, RPB10 and RPC10. Component of the RNA polymerase III (Pol III) complex consisting of 17 subunits. Directly interacts with POLR2A.7 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
RSP5P399403EBI-15794,EBI-16219

Protein-protein interaction databases

BioGridi34618. 68 interactors.
DIPiDIP-2195N.
IntActiP20436. 20 interactors.
MINTiMINT-507506.

Structurei

Secondary structure

1146
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi7 – 16Combined sources10
Beta strandi21 – 32Combined sources12
Beta strandi37 – 43Combined sources7
Helixi44 – 46Combined sources3
Beta strandi54 – 58Combined sources5
Turni84 – 86Combined sources3
Helixi89 – 92Combined sources4
Beta strandi93 – 101Combined sources9
Beta strandi108 – 110Combined sources3
Beta strandi112 – 118Combined sources7
Beta strandi121 – 128Combined sources8
Turni129 – 133Combined sources5
Beta strandi136 – 138Combined sources3
Beta strandi140 – 145Combined sources6

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1A1DNMR-A1-146[»]
1I3QX-ray3.10H1-146[»]
1I50X-ray2.80H1-146[»]
1I6HX-ray3.30H1-146[»]
1K83X-ray2.80H1-146[»]
1NIKX-ray4.10H1-146[»]
1NT9X-ray4.20H1-146[»]
1PQVX-ray3.80H1-146[»]
1R5UX-ray4.50H1-146[»]
1R9SX-ray4.25H1-146[»]
1R9TX-ray3.50H1-146[»]
1SFOX-ray3.61H1-146[»]
1TWAX-ray3.20H1-146[»]
1TWCX-ray3.00H1-146[»]
1TWFX-ray2.30H1-146[»]
1TWGX-ray3.30H1-146[»]
1TWHX-ray3.40H1-146[»]
1WCMX-ray3.80H1-146[»]
1Y1VX-ray3.80H1-146[»]
1Y1WX-ray4.00H1-146[»]
1Y1YX-ray4.00H1-146[»]
1Y77X-ray4.50H1-146[»]
2B63X-ray3.80H1-146[»]
2B8KX-ray4.15H1-146[»]
2E2HX-ray3.95H1-146[»]
2E2IX-ray3.41H1-146[»]
2E2JX-ray3.50H1-146[»]
2JA5X-ray3.80H1-146[»]
2JA6X-ray4.00H1-146[»]
2JA7X-ray3.80H/T1-146[»]
2JA8X-ray3.80H1-146[»]
2NVQX-ray2.90H1-146[»]
2NVTX-ray3.36H1-146[»]
2NVXX-ray3.60H1-146[»]
2NVYX-ray3.40H1-146[»]
2NVZX-ray4.30H1-146[»]
2R7ZX-ray3.80H1-146[»]
2R92X-ray3.80H1-146[»]
2R93X-ray4.00H1-146[»]
2VUMX-ray3.40H1-146[»]
2YU9X-ray3.40H1-146[»]
3CQZX-ray2.80H1-146[»]
3FKIX-ray3.88H1-146[»]
3GTGX-ray3.78H1-146[»]
3GTJX-ray3.42H1-146[»]
3GTKX-ray3.80H1-146[»]
3GTLX-ray3.38H1-146[»]
3GTMX-ray3.80H1-146[»]
3GTOX-ray4.00H1-146[»]
3GTPX-ray3.90H1-146[»]
3GTQX-ray3.80H1-146[»]
3H3VX-ray4.00I1-146[»]
3HOUX-ray3.20H/T1-146[»]
3HOVX-ray3.50H1-146[»]
3HOWX-ray3.60H1-146[»]
3HOXX-ray3.65H1-146[»]
3HOYX-ray3.40H1-146[»]
3HOZX-ray3.65H1-146[»]
3I4MX-ray3.70H1-146[»]
3I4NX-ray3.90H1-146[»]
3J0Kelectron microscopy36.00H1-146[»]
3J1Nelectron microscopy16.00H1-146[»]
3K1FX-ray4.30H1-146[»]
3K7AX-ray3.80H1-146[»]
3M3YX-ray3.18H1-146[»]
3M4OX-ray3.57H1-146[»]
3PO2X-ray3.30H1-146[»]
3PO3X-ray3.30H1-146[»]
3QT1X-ray4.30H1-146[»]
3RZDX-ray3.30H1-146[»]
3RZOX-ray3.00H1-146[»]
3S14X-ray2.85H1-146[»]
3S15X-ray3.30H1-146[»]
3S16X-ray3.24H1-146[»]
3S17X-ray3.20H1-146[»]
3S1MX-ray3.13H1-146[»]
3S1NX-ray3.10H1-146[»]
3S1QX-ray3.30H1-146[»]
3S1RX-ray3.20H1-146[»]
3S2DX-ray3.20H1-146[»]
3S2HX-ray3.30H1-146[»]
4A3BX-ray3.50H1-146[»]
4A3CX-ray3.50H1-146[»]
4A3DX-ray3.40H1-146[»]
4A3EX-ray3.40H1-146[»]
4A3FX-ray3.50H1-146[»]
4A3GX-ray3.50H1-146[»]
4A3IX-ray3.80H1-146[»]
4A3JX-ray3.70H1-146[»]
4A3KX-ray3.50H1-146[»]
4A3LX-ray3.50H1-146[»]
4A3MX-ray3.90H1-146[»]
4A93X-ray3.40H1-146[»]
4BBRX-ray3.40H1-146[»]
4BBSX-ray3.60H1-146[»]
4BXXX-ray3.28H1-146[»]
4BXZX-ray4.80H1-146[»]
4BY1X-ray3.60H1-146[»]
4BY7X-ray3.15H1-146[»]
4C2MX-ray2.80H/W1-146[»]
4C3HX-ray3.27H1-146[»]
4C3IX-ray3.0H1-146[»]
4C3JX-ray3.35H1-146[»]
4V1Melectron microscopy6.60H1-146[»]
4V1Nelectron microscopy7.80H1-146[»]
4V1Oelectron microscopy9.70H1-146[»]
4X67X-ray4.10H1-146[»]
4X6AX-ray3.96H1-146[»]
4Y52X-ray3.50H1-146[»]
4Y7NX-ray3.30H1-146[»]
4YM7X-ray5.50AH/BH/CH/DH/EH/FH1-146[»]
5C3EX-ray3.70H1-146[»]
5C44X-ray3.95H1-146[»]
5C4AX-ray4.20H1-146[»]
5C4JX-ray4.00H1-146[»]
5C4XX-ray4.00H1-146[»]
5FJ8electron microscopy3.90H1-146[»]
5FJ9electron microscopy4.60H1-146[»]
5FJAelectron microscopy4.65H1-146[»]
5FMFelectron microscopy6.00H1-146[»]
5FYWelectron microscopy4.35H1-146[»]
5FZ5electron microscopy8.80H1-146[»]
5G5Lelectron microscopy4.80H1-146[»]
5IP7X-ray3.52H2-146[»]
5IP9X-ray3.90H2-146[»]
5SVAelectron microscopy15.30H1-146[»]
ProteinModelPortaliP20436.
SMRiP20436.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP20436.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni16 – 39Non-specific ssDNA bindingBy similarityAdd BLAST24

Sequence similaritiesi

Phylogenomic databases

GeneTreeiENSGT00390000018195.
HOGENOMiHOG000175572.
InParanoidiP20436.
KOiK03016.
OMAiDMFDYVC.
OrthoDBiEOG092C57ZC.

Family and domain databases

InterProiIPR012340. NA-bd_OB-fold.
IPR005570. RNA_pol_Rpb8.
[Graphical view]
PANTHERiPTHR10917. PTHR10917. 1 hit.
PfamiPF03870. RNA_pol_Rpb8. 1 hit.
[Graphical view]
PIRSFiPIRSF000779. RNA_pol_Rpb8. 1 hit.
SMARTiSM00658. RPOL8c. 1 hit.
[Graphical view]
SUPFAMiSSF50249. SSF50249. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P20436-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSNTLFDDIF QVSEVDPGRY NKVCRIEAAS TTQDQCKLTL DINVELFPVA
60 70 80 90 100
AQDSLTVTIA SSLNLEDTPA NDSSATRSWR PPQAGDRSLA DDYDYVMYGT
110 120 130 140
AYKFEEVSKD LIAVYYSFGG LLMRLEGNYR NLNNLKQENA YLLIRR
Length:146
Mass (Da):16,511
Last modified:February 1, 1991 - v1
Checksum:i5B71693FE6FD8863
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X53289 Genomic DNA. Translation: CAA37383.1.
X92441 Genomic DNA. Translation: CAA63187.1.
Z75132 Genomic DNA. Translation: CAA99443.1.
AY693087 Genomic DNA. Translation: AAT93106.1.
BK006948 Genomic DNA. Translation: DAA10995.1.
PIRiC34588.
RefSeqiNP_014867.1. NM_001183643.1.

Genome annotation databases

EnsemblFungiiYOR224C; YOR224C; YOR224C.
GeneIDi854399.
KEGGisce:YOR224C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X53289 Genomic DNA. Translation: CAA37383.1.
X92441 Genomic DNA. Translation: CAA63187.1.
Z75132 Genomic DNA. Translation: CAA99443.1.
AY693087 Genomic DNA. Translation: AAT93106.1.
BK006948 Genomic DNA. Translation: DAA10995.1.
PIRiC34588.
RefSeqiNP_014867.1. NM_001183643.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1A1DNMR-A1-146[»]
1I3QX-ray3.10H1-146[»]
1I50X-ray2.80H1-146[»]
1I6HX-ray3.30H1-146[»]
1K83X-ray2.80H1-146[»]
1NIKX-ray4.10H1-146[»]
1NT9X-ray4.20H1-146[»]
1PQVX-ray3.80H1-146[»]
1R5UX-ray4.50H1-146[»]
1R9SX-ray4.25H1-146[»]
1R9TX-ray3.50H1-146[»]
1SFOX-ray3.61H1-146[»]
1TWAX-ray3.20H1-146[»]
1TWCX-ray3.00H1-146[»]
1TWFX-ray2.30H1-146[»]
1TWGX-ray3.30H1-146[»]
1TWHX-ray3.40H1-146[»]
1WCMX-ray3.80H1-146[»]
1Y1VX-ray3.80H1-146[»]
1Y1WX-ray4.00H1-146[»]
1Y1YX-ray4.00H1-146[»]
1Y77X-ray4.50H1-146[»]
2B63X-ray3.80H1-146[»]
2B8KX-ray4.15H1-146[»]
2E2HX-ray3.95H1-146[»]
2E2IX-ray3.41H1-146[»]
2E2JX-ray3.50H1-146[»]
2JA5X-ray3.80H1-146[»]
2JA6X-ray4.00H1-146[»]
2JA7X-ray3.80H/T1-146[»]
2JA8X-ray3.80H1-146[»]
2NVQX-ray2.90H1-146[»]
2NVTX-ray3.36H1-146[»]
2NVXX-ray3.60H1-146[»]
2NVYX-ray3.40H1-146[»]
2NVZX-ray4.30H1-146[»]
2R7ZX-ray3.80H1-146[»]
2R92X-ray3.80H1-146[»]
2R93X-ray4.00H1-146[»]
2VUMX-ray3.40H1-146[»]
2YU9X-ray3.40H1-146[»]
3CQZX-ray2.80H1-146[»]
3FKIX-ray3.88H1-146[»]
3GTGX-ray3.78H1-146[»]
3GTJX-ray3.42H1-146[»]
3GTKX-ray3.80H1-146[»]
3GTLX-ray3.38H1-146[»]
3GTMX-ray3.80H1-146[»]
3GTOX-ray4.00H1-146[»]
3GTPX-ray3.90H1-146[»]
3GTQX-ray3.80H1-146[»]
3H3VX-ray4.00I1-146[»]
3HOUX-ray3.20H/T1-146[»]
3HOVX-ray3.50H1-146[»]
3HOWX-ray3.60H1-146[»]
3HOXX-ray3.65H1-146[»]
3HOYX-ray3.40H1-146[»]
3HOZX-ray3.65H1-146[»]
3I4MX-ray3.70H1-146[»]
3I4NX-ray3.90H1-146[»]
3J0Kelectron microscopy36.00H1-146[»]
3J1Nelectron microscopy16.00H1-146[»]
3K1FX-ray4.30H1-146[»]
3K7AX-ray3.80H1-146[»]
3M3YX-ray3.18H1-146[»]
3M4OX-ray3.57H1-146[»]
3PO2X-ray3.30H1-146[»]
3PO3X-ray3.30H1-146[»]
3QT1X-ray4.30H1-146[»]
3RZDX-ray3.30H1-146[»]
3RZOX-ray3.00H1-146[»]
3S14X-ray2.85H1-146[»]
3S15X-ray3.30H1-146[»]
3S16X-ray3.24H1-146[»]
3S17X-ray3.20H1-146[»]
3S1MX-ray3.13H1-146[»]
3S1NX-ray3.10H1-146[»]
3S1QX-ray3.30H1-146[»]
3S1RX-ray3.20H1-146[»]
3S2DX-ray3.20H1-146[»]
3S2HX-ray3.30H1-146[»]
4A3BX-ray3.50H1-146[»]
4A3CX-ray3.50H1-146[»]
4A3DX-ray3.40H1-146[»]
4A3EX-ray3.40H1-146[»]
4A3FX-ray3.50H1-146[»]
4A3GX-ray3.50H1-146[»]
4A3IX-ray3.80H1-146[»]
4A3JX-ray3.70H1-146[»]
4A3KX-ray3.50H1-146[»]
4A3LX-ray3.50H1-146[»]
4A3MX-ray3.90H1-146[»]
4A93X-ray3.40H1-146[»]
4BBRX-ray3.40H1-146[»]
4BBSX-ray3.60H1-146[»]
4BXXX-ray3.28H1-146[»]
4BXZX-ray4.80H1-146[»]
4BY1X-ray3.60H1-146[»]
4BY7X-ray3.15H1-146[»]
4C2MX-ray2.80H/W1-146[»]
4C3HX-ray3.27H1-146[»]
4C3IX-ray3.0H1-146[»]
4C3JX-ray3.35H1-146[»]
4V1Melectron microscopy6.60H1-146[»]
4V1Nelectron microscopy7.80H1-146[»]
4V1Oelectron microscopy9.70H1-146[»]
4X67X-ray4.10H1-146[»]
4X6AX-ray3.96H1-146[»]
4Y52X-ray3.50H1-146[»]
4Y7NX-ray3.30H1-146[»]
4YM7X-ray5.50AH/BH/CH/DH/EH/FH1-146[»]
5C3EX-ray3.70H1-146[»]
5C44X-ray3.95H1-146[»]
5C4AX-ray4.20H1-146[»]
5C4JX-ray4.00H1-146[»]
5C4XX-ray4.00H1-146[»]
5FJ8electron microscopy3.90H1-146[»]
5FJ9electron microscopy4.60H1-146[»]
5FJAelectron microscopy4.65H1-146[»]
5FMFelectron microscopy6.00H1-146[»]
5FYWelectron microscopy4.35H1-146[»]
5FZ5electron microscopy8.80H1-146[»]
5G5Lelectron microscopy4.80H1-146[»]
5IP7X-ray3.52H2-146[»]
5IP9X-ray3.90H2-146[»]
5SVAelectron microscopy15.30H1-146[»]
ProteinModelPortaliP20436.
SMRiP20436.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi34618. 68 interactors.
DIPiDIP-2195N.
IntActiP20436. 20 interactors.
MINTiMINT-507506.

PTM databases

iPTMnetiP20436.

Proteomic databases

MaxQBiP20436.
PRIDEiP20436.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYOR224C; YOR224C; YOR224C.
GeneIDi854399.
KEGGisce:YOR224C.

Organism-specific databases

EuPathDBiFungiDB:YOR224C.
SGDiS000005750. RPB8.

Phylogenomic databases

GeneTreeiENSGT00390000018195.
HOGENOMiHOG000175572.
InParanoidiP20436.
KOiK03016.
OMAiDMFDYVC.
OrthoDBiEOG092C57ZC.

Enzyme and pathway databases

BioCyciYEAST:G3O-33723-MONOMER.
ReactomeiR-SCE-113418. Formation of the Early Elongation Complex.
R-SCE-674695. RNA Polymerase II Pre-transcription Events.
R-SCE-6781823. Formation of TC-NER Pre-Incision Complex.
R-SCE-6782135. Dual incision in TC-NER.
R-SCE-6782210. Gap-filling DNA repair synthesis and ligation in TC-NER.
R-SCE-6796648. TP53 Regulates Transcription of DNA Repair Genes.
R-SCE-72086. mRNA Capping.
R-SCE-72165. mRNA Splicing - Minor Pathway.
R-SCE-73762. RNA Polymerase I Transcription Initiation.
R-SCE-73776. RNA Polymerase II Promoter Escape.
R-SCE-73779. RNA Polymerase II Transcription Pre-Initiation And Promoter Opening.
R-SCE-73780. RNA Polymerase III Chain Elongation.
R-SCE-73980. RNA Polymerase III Transcription Termination.
R-SCE-749476. RNA Polymerase III Abortive And Retractive Initiation.
R-SCE-75953. RNA Polymerase II Transcription Initiation.
R-SCE-76042. RNA Polymerase II Transcription Initiation And Promoter Clearance.
R-SCE-76061. RNA Polymerase III Transcription Initiation From Type 1 Promoter.
R-SCE-76066. RNA Polymerase III Transcription Initiation From Type 2 Promoter.
R-SCE-76071. RNA Polymerase III Transcription Initiation From Type 3 Promoter.
R-SCE-77075. RNA Pol II CTD phosphorylation and interaction with CE.

Miscellaneous databases

EvolutionaryTraceiP20436.
PROiP20436.

Family and domain databases

InterProiIPR012340. NA-bd_OB-fold.
IPR005570. RNA_pol_Rpb8.
[Graphical view]
PANTHERiPTHR10917. PTHR10917. 1 hit.
PfamiPF03870. RNA_pol_Rpb8. 1 hit.
[Graphical view]
PIRSFiPIRSF000779. RNA_pol_Rpb8. 1 hit.
SMARTiSM00658. RPOL8c. 1 hit.
[Graphical view]
SUPFAMiSSF50249. SSF50249. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiRPAB3_YEAST
AccessioniPrimary (citable) accession number: P20436
Secondary accession number(s): D6W2S9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1991
Last sequence update: February 1, 1991
Last modified: November 30, 2016
This is version 171 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 6210 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 XV
    Yeast (Saccharomyces cerevisiae) chromosome XV: 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.