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Protein

DNA-directed RNA polymerases I, II, and III subunit RPABC5

Gene

RPB10

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 a small RNAs, such as 5S rRNA and tRNAs, respectively. Pol II is the central component of the basal RNA polymerase II transcription machinery. Pols are composed of mobile elements that move relative to each other. In Pol II, RBP10 is part of the core element with the central large cleft.3 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi7Zinc1
Metal bindingi10Zinc1
Metal bindingi44Zinc1
Metal bindingi45Zinc1

GO - Molecular functioni

  • DNA binding Source: InterPro
  • RNA polymerase I activity Source: UniProtKB
  • zinc ion binding Source: SGD

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

Metal-binding, Zinc

Enzyme and pathway databases

BioCyciYEAST:G3O-33712-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 RPABC5
Short name:
RNA polymerases I, II, and III subunit ABC5
Alternative name(s):
ABC10-beta
ABC8
DNA-directed RNA polymerases I, II, and III 8.3 kDa polypeptide
Gene namesi
Name:RPB10
Ordered Locus Names:YOR210W
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome XV

Organism-specific databases

EuPathDBiFungiDB:YOR210W.
SGDiS000005736. RPB10.

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
ChainiPRO_00001213421 – 70DNA-directed RNA polymerases I, II, and III subunit RPABC5Add BLAST70

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Cross-linki59Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)Combined sources

Keywords - PTMi

Isopeptide bond, Ubl conjugation

Proteomic databases

MaxQBiP22139.
PRIDEiP22139.

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.6 Publications

Protein-protein interaction databases

BioGridi34605. 72 interactors.
DIPiDIP-825N.
IntActiP22139. 17 interactors.
MINTiMINT-384345.

Structurei

Secondary structure

170
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Turni8 – 10Combined sources3
Helixi15 – 17Combined sources3
Helixi18 – 26Combined sources9
Turni27 – 29Combined sources3
Helixi32 – 38Combined sources7
Helixi44 – 51Combined sources8
Helixi57 – 61Combined sources5

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1I3QX-ray3.10J1-70[»]
1I50X-ray2.80J1-70[»]
1I6HX-ray3.30J1-70[»]
1K83X-ray2.80J1-70[»]
1NIKX-ray4.10J1-70[»]
1NT9X-ray4.20J1-70[»]
1PQVX-ray3.80J1-70[»]
1R5UX-ray4.50J1-70[»]
1R9SX-ray4.25J1-70[»]
1R9TX-ray3.50J1-70[»]
1SFOX-ray3.61J1-70[»]
1TWAX-ray3.20J1-70[»]
1TWCX-ray3.00J1-70[»]
1TWFX-ray2.30J1-70[»]
1TWGX-ray3.30J1-70[»]
1TWHX-ray3.40J1-70[»]
1WCMX-ray3.80J1-70[»]
1Y1VX-ray3.80J1-70[»]
1Y1WX-ray4.00J1-70[»]
1Y1YX-ray4.00J1-70[»]
1Y77X-ray4.50J1-70[»]
2B63X-ray3.80J1-70[»]
2B8KX-ray4.15J1-70[»]
2E2HX-ray3.95J1-70[»]
2E2IX-ray3.41J1-70[»]
2E2JX-ray3.50J1-70[»]
2JA5X-ray3.80J1-70[»]
2JA6X-ray4.00J1-70[»]
2JA7X-ray3.80J/V1-70[»]
2JA8X-ray3.80J1-70[»]
2NVQX-ray2.90J1-70[»]
2NVTX-ray3.36J1-70[»]
2NVXX-ray3.60J1-70[»]
2NVYX-ray3.40J1-70[»]
2NVZX-ray4.30J1-70[»]
2R7ZX-ray3.80J1-70[»]
2R92X-ray3.80J1-70[»]
2R93X-ray4.00J1-70[»]
2VUMX-ray3.40J1-70[»]
2YU9X-ray3.40J1-70[»]
3CQZX-ray2.80J1-70[»]
3FKIX-ray3.88J1-70[»]
3GTGX-ray3.78J1-70[»]
3GTJX-ray3.42J1-70[»]
3GTKX-ray3.80J1-70[»]
3GTLX-ray3.38J1-70[»]
3GTMX-ray3.80J1-70[»]
3GTOX-ray4.00J1-70[»]
3GTPX-ray3.90J1-70[»]
3GTQX-ray3.80J1-70[»]
3H3VX-ray4.00K1-70[»]
3HOUX-ray3.20J/V1-70[»]
3HOVX-ray3.50J1-70[»]
3HOWX-ray3.60J1-70[»]
3HOXX-ray3.65J1-70[»]
3HOYX-ray3.40J1-70[»]
3HOZX-ray3.65J1-70[»]
3I4MX-ray3.70J1-70[»]
3I4NX-ray3.90J1-70[»]
3J0Kelectron microscopy36.00J1-70[»]
3J1Nelectron microscopy16.00J1-70[»]
3K1FX-ray4.30J1-70[»]
3K7AX-ray3.80J1-70[»]
3M3YX-ray3.18J1-70[»]
3M4OX-ray3.57J1-70[»]
3PO2X-ray3.30J1-70[»]
3PO3X-ray3.30J1-70[»]
3QT1X-ray4.30J1-70[»]
3RZDX-ray3.30J1-70[»]
3RZOX-ray3.00J1-70[»]
3S14X-ray2.85J1-70[»]
3S15X-ray3.30J1-70[»]
3S16X-ray3.24J1-70[»]
3S17X-ray3.20J1-70[»]
3S1MX-ray3.13J1-70[»]
3S1NX-ray3.10J1-70[»]
3S1QX-ray3.30J1-70[»]
3S1RX-ray3.20J1-70[»]
3S2DX-ray3.20J1-70[»]
3S2HX-ray3.30J1-70[»]
4A3BX-ray3.50J1-70[»]
4A3CX-ray3.50J1-70[»]
4A3DX-ray3.40J1-70[»]
4A3EX-ray3.40J1-70[»]
4A3FX-ray3.50J1-70[»]
4A3GX-ray3.50J1-70[»]
4A3IX-ray3.80J1-70[»]
4A3JX-ray3.70J1-70[»]
4A3KX-ray3.50J1-70[»]
4A3LX-ray3.50J1-70[»]
4A3MX-ray3.90J1-70[»]
4A93X-ray3.40J1-70[»]
4BBRX-ray3.40J1-70[»]
4BBSX-ray3.60J1-70[»]
4BXXX-ray3.28J1-70[»]
4BXZX-ray4.80J1-70[»]
4BY1X-ray3.60J1-70[»]
4BY7X-ray3.15J1-70[»]
4C2MX-ray2.80J/Y1-70[»]
4C3HX-ray3.27J1-70[»]
4C3IX-ray3.0J1-70[»]
4C3JX-ray3.35J1-70[»]
4V1Melectron microscopy6.60J1-70[»]
4V1Nelectron microscopy7.80J1-70[»]
4V1Oelectron microscopy9.70J1-70[»]
4X67X-ray4.10J1-70[»]
4X6AX-ray3.96J1-70[»]
4Y52X-ray3.50J1-70[»]
4Y7NX-ray3.30J1-70[»]
4YM7X-ray5.50AJ/BJ/CJ/DJ/EJ/FJ1-70[»]
5C3EX-ray3.70J1-70[»]
5C44X-ray3.95J1-70[»]
5C4AX-ray4.20J1-70[»]
5C4JX-ray4.00J1-70[»]
5C4XX-ray4.00J1-70[»]
5FJ8electron microscopy3.90J1-70[»]
5FJ9electron microscopy4.60J1-70[»]
5FJAelectron microscopy4.65J1-70[»]
5FMFelectron microscopy6.00J1-65[»]
5FYWelectron microscopy4.35J1-70[»]
5FZ5electron microscopy8.80J1-70[»]
5G5Lelectron microscopy4.80J1-70[»]
5IP7X-ray3.52J1-65[»]
5IP9X-ray3.90J1-65[»]
5SVAelectron microscopy15.30J1-70[»]
ProteinModelPortaliP22139.
SMRiP22139.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP22139.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

GeneTreeiENSGT00390000007087.
HOGENOMiHOG000109502.
InParanoidiP22139.
KOiK03007.
OMAiQLKRYCC.
OrthoDBiEOG092C5V63.

Family and domain databases

Gene3Di1.10.10.60. 1 hit.
HAMAPiMF_00250. RNApol_arch_N. 1 hit.
InterProiIPR009057. Homeodomain-like.
IPR023580. RNA_pol_su_RPB10.
IPR020789. RNA_pol_suN_Zn-BS.
IPR000268. RNAP_N/Rpb10.
[Graphical view]
PfamiPF01194. RNA_pol_N. 1 hit.
[Graphical view]
PIRSFiPIRSF005653. RNA_pol_N/8_sub. 1 hit.
ProDomiPD006539. RNA_pol_N/8_sub. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SUPFAMiSSF46924. SSF46924. 1 hit.
PROSITEiPS01112. RNA_POL_N_8KD. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P22139-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MIVPVRCFSC GKVVGDKWES YLNLLQEDEL DEGTALSRLG LKRYCCRRMI
60 70
LTHVDLIEKF LRYNPLEKRD
Length:70
Mass (Da):8,278
Last modified:October 1, 1993 - v2
Checksum:iE1F5733E8F466BE0
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M60479 Genomic DNA. Translation: AAA34995.1. Sequence problems.
S62098 Genomic DNA. Translation: AAB27020.1.
L11274 Genomic DNA. Translation: AAB59318.1.
Z75118 Genomic DNA. Translation: CAA99425.1.
AY558433 Genomic DNA. Translation: AAS56759.1.
BK006948 Genomic DNA. Translation: DAA10982.1.
PIRiS48885.
RefSeqiNP_014853.3. NM_001183629.3.

Genome annotation databases

EnsemblFungiiYOR210W; YOR210W; YOR210W.
GeneIDi854385.
KEGGisce:YOR210W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M60479 Genomic DNA. Translation: AAA34995.1. Sequence problems.
S62098 Genomic DNA. Translation: AAB27020.1.
L11274 Genomic DNA. Translation: AAB59318.1.
Z75118 Genomic DNA. Translation: CAA99425.1.
AY558433 Genomic DNA. Translation: AAS56759.1.
BK006948 Genomic DNA. Translation: DAA10982.1.
PIRiS48885.
RefSeqiNP_014853.3. NM_001183629.3.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1I3QX-ray3.10J1-70[»]
1I50X-ray2.80J1-70[»]
1I6HX-ray3.30J1-70[»]
1K83X-ray2.80J1-70[»]
1NIKX-ray4.10J1-70[»]
1NT9X-ray4.20J1-70[»]
1PQVX-ray3.80J1-70[»]
1R5UX-ray4.50J1-70[»]
1R9SX-ray4.25J1-70[»]
1R9TX-ray3.50J1-70[»]
1SFOX-ray3.61J1-70[»]
1TWAX-ray3.20J1-70[»]
1TWCX-ray3.00J1-70[»]
1TWFX-ray2.30J1-70[»]
1TWGX-ray3.30J1-70[»]
1TWHX-ray3.40J1-70[»]
1WCMX-ray3.80J1-70[»]
1Y1VX-ray3.80J1-70[»]
1Y1WX-ray4.00J1-70[»]
1Y1YX-ray4.00J1-70[»]
1Y77X-ray4.50J1-70[»]
2B63X-ray3.80J1-70[»]
2B8KX-ray4.15J1-70[»]
2E2HX-ray3.95J1-70[»]
2E2IX-ray3.41J1-70[»]
2E2JX-ray3.50J1-70[»]
2JA5X-ray3.80J1-70[»]
2JA6X-ray4.00J1-70[»]
2JA7X-ray3.80J/V1-70[»]
2JA8X-ray3.80J1-70[»]
2NVQX-ray2.90J1-70[»]
2NVTX-ray3.36J1-70[»]
2NVXX-ray3.60J1-70[»]
2NVYX-ray3.40J1-70[»]
2NVZX-ray4.30J1-70[»]
2R7ZX-ray3.80J1-70[»]
2R92X-ray3.80J1-70[»]
2R93X-ray4.00J1-70[»]
2VUMX-ray3.40J1-70[»]
2YU9X-ray3.40J1-70[»]
3CQZX-ray2.80J1-70[»]
3FKIX-ray3.88J1-70[»]
3GTGX-ray3.78J1-70[»]
3GTJX-ray3.42J1-70[»]
3GTKX-ray3.80J1-70[»]
3GTLX-ray3.38J1-70[»]
3GTMX-ray3.80J1-70[»]
3GTOX-ray4.00J1-70[»]
3GTPX-ray3.90J1-70[»]
3GTQX-ray3.80J1-70[»]
3H3VX-ray4.00K1-70[»]
3HOUX-ray3.20J/V1-70[»]
3HOVX-ray3.50J1-70[»]
3HOWX-ray3.60J1-70[»]
3HOXX-ray3.65J1-70[»]
3HOYX-ray3.40J1-70[»]
3HOZX-ray3.65J1-70[»]
3I4MX-ray3.70J1-70[»]
3I4NX-ray3.90J1-70[»]
3J0Kelectron microscopy36.00J1-70[»]
3J1Nelectron microscopy16.00J1-70[»]
3K1FX-ray4.30J1-70[»]
3K7AX-ray3.80J1-70[»]
3M3YX-ray3.18J1-70[»]
3M4OX-ray3.57J1-70[»]
3PO2X-ray3.30J1-70[»]
3PO3X-ray3.30J1-70[»]
3QT1X-ray4.30J1-70[»]
3RZDX-ray3.30J1-70[»]
3RZOX-ray3.00J1-70[»]
3S14X-ray2.85J1-70[»]
3S15X-ray3.30J1-70[»]
3S16X-ray3.24J1-70[»]
3S17X-ray3.20J1-70[»]
3S1MX-ray3.13J1-70[»]
3S1NX-ray3.10J1-70[»]
3S1QX-ray3.30J1-70[»]
3S1RX-ray3.20J1-70[»]
3S2DX-ray3.20J1-70[»]
3S2HX-ray3.30J1-70[»]
4A3BX-ray3.50J1-70[»]
4A3CX-ray3.50J1-70[»]
4A3DX-ray3.40J1-70[»]
4A3EX-ray3.40J1-70[»]
4A3FX-ray3.50J1-70[»]
4A3GX-ray3.50J1-70[»]
4A3IX-ray3.80J1-70[»]
4A3JX-ray3.70J1-70[»]
4A3KX-ray3.50J1-70[»]
4A3LX-ray3.50J1-70[»]
4A3MX-ray3.90J1-70[»]
4A93X-ray3.40J1-70[»]
4BBRX-ray3.40J1-70[»]
4BBSX-ray3.60J1-70[»]
4BXXX-ray3.28J1-70[»]
4BXZX-ray4.80J1-70[»]
4BY1X-ray3.60J1-70[»]
4BY7X-ray3.15J1-70[»]
4C2MX-ray2.80J/Y1-70[»]
4C3HX-ray3.27J1-70[»]
4C3IX-ray3.0J1-70[»]
4C3JX-ray3.35J1-70[»]
4V1Melectron microscopy6.60J1-70[»]
4V1Nelectron microscopy7.80J1-70[»]
4V1Oelectron microscopy9.70J1-70[»]
4X67X-ray4.10J1-70[»]
4X6AX-ray3.96J1-70[»]
4Y52X-ray3.50J1-70[»]
4Y7NX-ray3.30J1-70[»]
4YM7X-ray5.50AJ/BJ/CJ/DJ/EJ/FJ1-70[»]
5C3EX-ray3.70J1-70[»]
5C44X-ray3.95J1-70[»]
5C4AX-ray4.20J1-70[»]
5C4JX-ray4.00J1-70[»]
5C4XX-ray4.00J1-70[»]
5FJ8electron microscopy3.90J1-70[»]
5FJ9electron microscopy4.60J1-70[»]
5FJAelectron microscopy4.65J1-70[»]
5FMFelectron microscopy6.00J1-65[»]
5FYWelectron microscopy4.35J1-70[»]
5FZ5electron microscopy8.80J1-70[»]
5G5Lelectron microscopy4.80J1-70[»]
5IP7X-ray3.52J1-65[»]
5IP9X-ray3.90J1-65[»]
5SVAelectron microscopy15.30J1-70[»]
ProteinModelPortaliP22139.
SMRiP22139.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi34605. 72 interactors.
DIPiDIP-825N.
IntActiP22139. 17 interactors.
MINTiMINT-384345.

Proteomic databases

MaxQBiP22139.
PRIDEiP22139.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYOR210W; YOR210W; YOR210W.
GeneIDi854385.
KEGGisce:YOR210W.

Organism-specific databases

EuPathDBiFungiDB:YOR210W.
SGDiS000005736. RPB10.

Phylogenomic databases

GeneTreeiENSGT00390000007087.
HOGENOMiHOG000109502.
InParanoidiP22139.
KOiK03007.
OMAiQLKRYCC.
OrthoDBiEOG092C5V63.

Enzyme and pathway databases

BioCyciYEAST:G3O-33712-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

EvolutionaryTraceiP22139.
PROiP22139.

Family and domain databases

Gene3Di1.10.10.60. 1 hit.
HAMAPiMF_00250. RNApol_arch_N. 1 hit.
InterProiIPR009057. Homeodomain-like.
IPR023580. RNA_pol_su_RPB10.
IPR020789. RNA_pol_suN_Zn-BS.
IPR000268. RNAP_N/Rpb10.
[Graphical view]
PfamiPF01194. RNA_pol_N. 1 hit.
[Graphical view]
PIRSFiPIRSF005653. RNA_pol_N/8_sub. 1 hit.
ProDomiPD006539. RNA_pol_N/8_sub. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SUPFAMiSSF46924. SSF46924. 1 hit.
PROSITEiPS01112. RNA_POL_N_8KD. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiRPAB5_YEAST
AccessioniPrimary (citable) accession number: P22139
Secondary accession number(s): D6W2R6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1991
Last sequence update: October 1, 1993
Last modified: November 30, 2016
This is version 169 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 5300 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, 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.