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Protein

DNA-directed RNA polymerases I, II, and III subunit RPABC2

Gene

RPO26

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. Pol II is the central component of the basal RNA polymerase II transcription machinery. RNA polymerases are composed of mobile elements that move relative to each other. In Pol II, RPB6 is part of the clamp element and together with parts of RPB1 and RPB2 forms a pocket to which the RPB4-RPB7 subcomplex binds.3 Publications

GO - Molecular functioni

  • DNA binding Source: InterPro
  • 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

Enzyme and pathway databases

BioCyciYEAST:G3O-34310-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-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 RPABC2
Short name:
RNA polymerases I, II, and III subunit ABC2
Alternative name(s):
ABC23
DNA-directed RNA polymerases I, II, and III 23 kDa polypeptide
Gene namesi
Name:RPO26
Synonyms:RPB6
Ordered Locus Names:YPR187W
ORF Names:P9677.8
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome XVI

Organism-specific databases

EuPathDBiFungiDB:YPR187W.
SGDiS000006391. RPO26.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: UniProtKB-SubCell
  • 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

Cytoplasm, DNA-directed RNA polymerase, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 155155DNA-directed RNA polymerases I, II, and III subunit RPABC2PRO_0000133797Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei24 – 241PhosphoserineCombined sources

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP20435.
PRIDEiP20435.

PTM databases

iPTMnetiP20435.

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.9 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
RPA190P109643EBI-15786,EBI-15730

Protein-protein interaction databases

BioGridi36359. 95 interactions.
DIPiDIP-2194N.
IntActiP20435. 38 interactions.
MINTiMINT-569579.

Structurei

Secondary structure

1
155
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi56 – 7217Combined sources
Beta strandi76 – 783Combined sources
Helixi87 – 10216Combined sources
Helixi117 – 12610Combined sources
Beta strandi132 – 1376Combined sources
Beta strandi139 – 1413Combined sources
Beta strandi143 – 1475Combined sources
Turni148 – 1503Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1I3QX-ray3.10F1-155[»]
1I50X-ray2.80F1-155[»]
1I6HX-ray3.30F1-155[»]
1K83X-ray2.80F1-155[»]
1NIKX-ray4.10F1-155[»]
1NT9X-ray4.20F1-155[»]
1PQVX-ray3.80F1-155[»]
1R5UX-ray4.50F1-155[»]
1R9SX-ray4.25F1-155[»]
1R9TX-ray3.50F1-155[»]
1SFOX-ray3.61F1-155[»]
1TWAX-ray3.20F1-155[»]
1TWCX-ray3.00F1-155[»]
1TWFX-ray2.30F1-155[»]
1TWGX-ray3.30F1-155[»]
1TWHX-ray3.40F1-155[»]
1WCMX-ray3.80F1-155[»]
1Y1VX-ray3.80F1-155[»]
1Y1WX-ray4.00F1-155[»]
1Y1YX-ray4.00F1-155[»]
1Y77X-ray4.50F1-155[»]
2B63X-ray3.80F1-155[»]
2B8KX-ray4.15F1-155[»]
2E2HX-ray3.95F1-155[»]
2E2IX-ray3.41F1-155[»]
2E2JX-ray3.50F1-155[»]
2JA5X-ray3.80F1-155[»]
2JA6X-ray4.00F1-155[»]
2JA7X-ray3.80F/R1-155[»]
2JA8X-ray3.80F1-155[»]
2NVQX-ray2.90F1-155[»]
2NVTX-ray3.36F1-155[»]
2NVXX-ray3.60F1-155[»]
2NVYX-ray3.40F1-155[»]
2NVZX-ray4.30F1-155[»]
2R7ZX-ray3.80F1-155[»]
2R92X-ray3.80F1-155[»]
2R93X-ray4.00F1-155[»]
2VUMX-ray3.40F1-155[»]
2YU9X-ray3.40F1-155[»]
3CQZX-ray2.80F1-155[»]
3FKIX-ray3.88F1-155[»]
3GTGX-ray3.78F1-155[»]
3GTJX-ray3.42F1-155[»]
3GTKX-ray3.80F1-155[»]
3GTLX-ray3.38F1-155[»]
3GTMX-ray3.80F1-155[»]
3GTOX-ray4.00F1-155[»]
3GTPX-ray3.90F1-155[»]
3GTQX-ray3.80F1-155[»]
3H3VX-ray4.00G1-155[»]
3HOUX-ray3.20F/R1-155[»]
3HOVX-ray3.50F1-155[»]
3HOWX-ray3.60F1-155[»]
3HOXX-ray3.65F1-155[»]
3HOYX-ray3.40F1-155[»]
3HOZX-ray3.65F1-155[»]
3I4MX-ray3.70F1-155[»]
3I4NX-ray3.90F1-155[»]
3J0Kelectron microscopy36.00F72-155[»]
3J1Nelectron microscopy16.00F72-155[»]
3K1FX-ray4.30F1-155[»]
3K7AX-ray3.80F1-155[»]
3M3YX-ray3.18F1-155[»]
3M4OX-ray3.57F1-155[»]
3PO2X-ray3.30F1-155[»]
3PO3X-ray3.30F1-155[»]
3QT1X-ray4.30F1-155[»]
3RZDX-ray3.30F1-155[»]
3RZOX-ray3.00F1-155[»]
3S14X-ray2.85F1-155[»]
3S15X-ray3.30F1-155[»]
3S16X-ray3.24F1-155[»]
3S17X-ray3.20F1-155[»]
3S1MX-ray3.13F1-155[»]
3S1NX-ray3.10F1-155[»]
3S1QX-ray3.30F1-155[»]
3S1RX-ray3.20F1-155[»]
3S2DX-ray3.20F1-155[»]
3S2HX-ray3.30F1-155[»]
4A3BX-ray3.50F1-155[»]
4A3CX-ray3.50F1-155[»]
4A3DX-ray3.40F1-155[»]
4A3EX-ray3.40F1-155[»]
4A3FX-ray3.50F1-155[»]
4A3GX-ray3.50F1-155[»]
4A3IX-ray3.80F1-155[»]
4A3JX-ray3.70F1-155[»]
4A3KX-ray3.50F1-155[»]
4A3LX-ray3.50F1-155[»]
4A3MX-ray3.90F1-155[»]
4A93X-ray3.40F1-155[»]
4BBRX-ray3.40F1-155[»]
4BBSX-ray3.60F1-155[»]
4BXXX-ray3.28F1-155[»]
4BXZX-ray4.80F1-155[»]
4BY1X-ray3.60F1-155[»]
4BY7X-ray3.15F1-155[»]
4C2MX-ray2.80F/U1-155[»]
4C3HX-ray3.27F1-155[»]
4C3IX-ray3.0F1-155[»]
4C3JX-ray3.35F1-155[»]
4V1Melectron microscopy6.60F1-155[»]
4V1Nelectron microscopy7.80F1-155[»]
4V1Oelectron microscopy9.70F1-155[»]
4X67X-ray4.10F1-155[»]
4X6AX-ray3.96F1-155[»]
4Y52X-ray3.50F1-155[»]
4Y7NX-ray3.30F1-155[»]
4YM7X-ray5.50AF/BF/CF/DF/EF/FF1-155[»]
5C3EX-ray3.70F1-155[»]
5C44X-ray3.95F1-155[»]
5C4AX-ray4.20F1-155[»]
5C4JX-ray4.00F1-155[»]
5C4XX-ray4.00F1-155[»]
5FJ8electron microscopy3.90F1-155[»]
5FJ9electron microscopy4.60F1-155[»]
5FJAelectron microscopy4.65F1-155[»]
5FMFelectron microscopy6.00F72-155[»]
5FYWelectron microscopy4.35F1-155[»]
5FZ5electron microscopy8.80F1-155[»]
5IP7X-ray3.52F69-155[»]
5IP9X-ray3.90F69-155[»]
ProteinModelPortaliP20435.
SMRiP20435. Positions 55-154.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP20435.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni111 – 13222Leucine-zipperAdd
BLAST

Sequence similaritiesi

Phylogenomic databases

GeneTreeiENSGT00390000010415.
HOGENOMiHOG000225272.
InParanoidiP20435.
KOiK03014.
OMAiINGGFGP.
OrthoDBiEOG092C5A9A.

Family and domain databases

Gene3Di3.90.940.10. 1 hit.
HAMAPiMF_00192. RNApol_arch_K. 1 hit.
InterProiIPR020708. DNA-dir_RNA_polK_14-18kDa_CS.
IPR006110. Pol_omega/K/RPB6.
IPR012293. RNAP_RPB6_omega.
IPR028363. RPB6.
IPR006111. RpoK/Rpb6.
[Graphical view]
PANTHERiPTHR10773. PTHR10773. 1 hit.
PfamiPF01192. RNA_pol_Rpb6. 1 hit.
[Graphical view]
PIRSFiPIRSF500154. RPB6. 1 hit.
PIRSF000778. RpoK/RPB6. 1 hit.
SMARTiSM01409. RNA_pol_Rpb6. 1 hit.
[Graphical view]
SUPFAMiSSF63562. SSF63562. 1 hit.
PROSITEiPS01111. RNA_POL_K_14KD. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P20435-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSDYEEAFND GNENFEDFDV EHFSDEETYE EKPQFKDGET TDANGKTIVT
60 70 80 90 100
GGNGPEDFQQ HEQIRRKTLK EKAIPKDQRA TTPYMTKYER ARILGTRALQ
110 120 130 140 150
ISMNAPVFVD LEGETDPLRI AMKELAEKKI PLVIRRYLPD GSFEDWSVEE

LIVDL
Length:155
Mass (Da):17,910
Last modified:February 1, 1991 - v1
Checksum:iAA3DEF529F94A5E4
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X53288 Genomic DNA. Translation: CAA37382.1.
M33924 Genomic DNA. Translation: AAA34989.1.
U25841 Genomic DNA. Translation: AAB64616.1.
BK006949 Genomic DNA. Translation: DAA11603.1.
PIRiS13307. RNBYR6.
RefSeqiNP_015513.1. NM_001184284.1.

Genome annotation databases

EnsemblFungiiYPR187W; YPR187W; YPR187W.
GeneIDi856317.
KEGGisce:YPR187W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X53288 Genomic DNA. Translation: CAA37382.1.
M33924 Genomic DNA. Translation: AAA34989.1.
U25841 Genomic DNA. Translation: AAB64616.1.
BK006949 Genomic DNA. Translation: DAA11603.1.
PIRiS13307. RNBYR6.
RefSeqiNP_015513.1. NM_001184284.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1I3QX-ray3.10F1-155[»]
1I50X-ray2.80F1-155[»]
1I6HX-ray3.30F1-155[»]
1K83X-ray2.80F1-155[»]
1NIKX-ray4.10F1-155[»]
1NT9X-ray4.20F1-155[»]
1PQVX-ray3.80F1-155[»]
1R5UX-ray4.50F1-155[»]
1R9SX-ray4.25F1-155[»]
1R9TX-ray3.50F1-155[»]
1SFOX-ray3.61F1-155[»]
1TWAX-ray3.20F1-155[»]
1TWCX-ray3.00F1-155[»]
1TWFX-ray2.30F1-155[»]
1TWGX-ray3.30F1-155[»]
1TWHX-ray3.40F1-155[»]
1WCMX-ray3.80F1-155[»]
1Y1VX-ray3.80F1-155[»]
1Y1WX-ray4.00F1-155[»]
1Y1YX-ray4.00F1-155[»]
1Y77X-ray4.50F1-155[»]
2B63X-ray3.80F1-155[»]
2B8KX-ray4.15F1-155[»]
2E2HX-ray3.95F1-155[»]
2E2IX-ray3.41F1-155[»]
2E2JX-ray3.50F1-155[»]
2JA5X-ray3.80F1-155[»]
2JA6X-ray4.00F1-155[»]
2JA7X-ray3.80F/R1-155[»]
2JA8X-ray3.80F1-155[»]
2NVQX-ray2.90F1-155[»]
2NVTX-ray3.36F1-155[»]
2NVXX-ray3.60F1-155[»]
2NVYX-ray3.40F1-155[»]
2NVZX-ray4.30F1-155[»]
2R7ZX-ray3.80F1-155[»]
2R92X-ray3.80F1-155[»]
2R93X-ray4.00F1-155[»]
2VUMX-ray3.40F1-155[»]
2YU9X-ray3.40F1-155[»]
3CQZX-ray2.80F1-155[»]
3FKIX-ray3.88F1-155[»]
3GTGX-ray3.78F1-155[»]
3GTJX-ray3.42F1-155[»]
3GTKX-ray3.80F1-155[»]
3GTLX-ray3.38F1-155[»]
3GTMX-ray3.80F1-155[»]
3GTOX-ray4.00F1-155[»]
3GTPX-ray3.90F1-155[»]
3GTQX-ray3.80F1-155[»]
3H3VX-ray4.00G1-155[»]
3HOUX-ray3.20F/R1-155[»]
3HOVX-ray3.50F1-155[»]
3HOWX-ray3.60F1-155[»]
3HOXX-ray3.65F1-155[»]
3HOYX-ray3.40F1-155[»]
3HOZX-ray3.65F1-155[»]
3I4MX-ray3.70F1-155[»]
3I4NX-ray3.90F1-155[»]
3J0Kelectron microscopy36.00F72-155[»]
3J1Nelectron microscopy16.00F72-155[»]
3K1FX-ray4.30F1-155[»]
3K7AX-ray3.80F1-155[»]
3M3YX-ray3.18F1-155[»]
3M4OX-ray3.57F1-155[»]
3PO2X-ray3.30F1-155[»]
3PO3X-ray3.30F1-155[»]
3QT1X-ray4.30F1-155[»]
3RZDX-ray3.30F1-155[»]
3RZOX-ray3.00F1-155[»]
3S14X-ray2.85F1-155[»]
3S15X-ray3.30F1-155[»]
3S16X-ray3.24F1-155[»]
3S17X-ray3.20F1-155[»]
3S1MX-ray3.13F1-155[»]
3S1NX-ray3.10F1-155[»]
3S1QX-ray3.30F1-155[»]
3S1RX-ray3.20F1-155[»]
3S2DX-ray3.20F1-155[»]
3S2HX-ray3.30F1-155[»]
4A3BX-ray3.50F1-155[»]
4A3CX-ray3.50F1-155[»]
4A3DX-ray3.40F1-155[»]
4A3EX-ray3.40F1-155[»]
4A3FX-ray3.50F1-155[»]
4A3GX-ray3.50F1-155[»]
4A3IX-ray3.80F1-155[»]
4A3JX-ray3.70F1-155[»]
4A3KX-ray3.50F1-155[»]
4A3LX-ray3.50F1-155[»]
4A3MX-ray3.90F1-155[»]
4A93X-ray3.40F1-155[»]
4BBRX-ray3.40F1-155[»]
4BBSX-ray3.60F1-155[»]
4BXXX-ray3.28F1-155[»]
4BXZX-ray4.80F1-155[»]
4BY1X-ray3.60F1-155[»]
4BY7X-ray3.15F1-155[»]
4C2MX-ray2.80F/U1-155[»]
4C3HX-ray3.27F1-155[»]
4C3IX-ray3.0F1-155[»]
4C3JX-ray3.35F1-155[»]
4V1Melectron microscopy6.60F1-155[»]
4V1Nelectron microscopy7.80F1-155[»]
4V1Oelectron microscopy9.70F1-155[»]
4X67X-ray4.10F1-155[»]
4X6AX-ray3.96F1-155[»]
4Y52X-ray3.50F1-155[»]
4Y7NX-ray3.30F1-155[»]
4YM7X-ray5.50AF/BF/CF/DF/EF/FF1-155[»]
5C3EX-ray3.70F1-155[»]
5C44X-ray3.95F1-155[»]
5C4AX-ray4.20F1-155[»]
5C4JX-ray4.00F1-155[»]
5C4XX-ray4.00F1-155[»]
5FJ8electron microscopy3.90F1-155[»]
5FJ9electron microscopy4.60F1-155[»]
5FJAelectron microscopy4.65F1-155[»]
5FMFelectron microscopy6.00F72-155[»]
5FYWelectron microscopy4.35F1-155[»]
5FZ5electron microscopy8.80F1-155[»]
5IP7X-ray3.52F69-155[»]
5IP9X-ray3.90F69-155[»]
ProteinModelPortaliP20435.
SMRiP20435. Positions 55-154.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi36359. 95 interactions.
DIPiDIP-2194N.
IntActiP20435. 38 interactions.
MINTiMINT-569579.

PTM databases

iPTMnetiP20435.

Proteomic databases

MaxQBiP20435.
PRIDEiP20435.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYPR187W; YPR187W; YPR187W.
GeneIDi856317.
KEGGisce:YPR187W.

Organism-specific databases

EuPathDBiFungiDB:YPR187W.
SGDiS000006391. RPO26.

Phylogenomic databases

GeneTreeiENSGT00390000010415.
HOGENOMiHOG000225272.
InParanoidiP20435.
KOiK03014.
OMAiINGGFGP.
OrthoDBiEOG092C5A9A.

Enzyme and pathway databases

BioCyciYEAST:G3O-34310-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-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

EvolutionaryTraceiP20435.
PROiP20435.

Family and domain databases

Gene3Di3.90.940.10. 1 hit.
HAMAPiMF_00192. RNApol_arch_K. 1 hit.
InterProiIPR020708. DNA-dir_RNA_polK_14-18kDa_CS.
IPR006110. Pol_omega/K/RPB6.
IPR012293. RNAP_RPB6_omega.
IPR028363. RPB6.
IPR006111. RpoK/Rpb6.
[Graphical view]
PANTHERiPTHR10773. PTHR10773. 1 hit.
PfamiPF01192. RNA_pol_Rpb6. 1 hit.
[Graphical view]
PIRSFiPIRSF500154. RPB6. 1 hit.
PIRSF000778. RpoK/RPB6. 1 hit.
SMARTiSM01409. RNA_pol_Rpb6. 1 hit.
[Graphical view]
SUPFAMiSSF63562. SSF63562. 1 hit.
PROSITEiPS01111. RNA_POL_K_14KD. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiRPAB2_YEAST
AccessioniPrimary (citable) accession number: P20435
Secondary accession number(s): D6W4I7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1991
Last sequence update: February 1, 1991
Last modified: September 7, 2016
This is version 174 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 6090 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 XVI
    Yeast (Saccharomyces cerevisiae) chromosome XVI: 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.