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Protein

DNA-directed RNA polymerase I subunit RPA190

Gene

RPA190

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. RPA190 and RPA135 both contribute to the polymerase catalytic activity and together form the Pol I active center. In addition, subunit RPA12 contributes a catalytic zinc ribbon that is required for RNA cleavage by Pol I. A single stranded DNA template strand of the promoter is positioned within the central active site cleft of Pol I. A bridging helix emanates from RPA190 and crosses the cleft near the catalytic site and is thought to promote translocation of Pol I by acting as a ratchet that moves the RNA-DNA hybrid through the active site by switching from straight to bent conformations at each step of nucleotide addition.3 Publications

Miscellaneous

Present with 2840 molecules/cell in log phase SD medium.1 Publication

Catalytic activityi

Nucleoside triphosphate + RNA(n) = diphosphate + RNA(n+1).3 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi62Zinc 1Combined sources1 Publication1
Metal bindingi65Zinc 1Combined sources1 Publication1
Metal bindingi72Zinc 1Combined sources1 Publication1
Metal bindingi75Zinc 1; via tele nitrogenCombined sources1 Publication1
Metal bindingi102Zinc 2Combined sources1 Publication1
Metal bindingi105Zinc 2Combined sources1 Publication1
Metal bindingi233Zinc 2Combined sources1 Publication1
Metal bindingi236Zinc 2Combined sources1 Publication1
Metal bindingi627Magnesium; catalyticBy similarity1
Metal bindingi629Magnesium; catalyticBy similarity1
Metal bindingi631Magnesium; catalyticBy similarity1

GO - Molecular functioni

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

Keywordsi

Molecular functionNucleotidyltransferase, Transferase
Biological processRibosome biogenesis, Transcription
LigandMagnesium, Metal-binding, Zinc

Enzyme and pathway databases

BioCyciYEAST:G3O-33816-MONOMER
ReactomeiR-SCE-73762 RNA Polymerase I Transcription Initiation

Names & Taxonomyi

Protein namesi
Recommended name:
DNA-directed RNA polymerase I subunit RPA190 (EC:2.7.7.6)
Alternative name(s):
DNA-directed RNA polymerase I 190 kDa polypeptide
Short name:
A190
DNA-directed RNA polymerase I largest subunit
Gene namesi
Name:RPA190
Synonyms:RPA1, RRN1
Ordered Locus Names:YOR341W
ORF Names:O6276
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome XV

Organism-specific databases

SGDiS000005868 RPA190

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

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000739301 – 1664DNA-directed RNA polymerase I subunit RPA190Add BLAST1664

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei889PhosphoserineCombined sources1
Modified residuei1636PhosphoserineCombined sources1

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP10964
PaxDbiP10964
PRIDEiP10964
TopDownProteomicsiP10964

PTM databases

iPTMnetiP10964

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.6 Publications

Binary interactionsi

Protein-protein interaction databases

BioGridi34724, 460 interactors
ComplexPortaliCPX-1664 DNA-directed RNA Polymerase I complex
DIPiDIP-999N
IntActiP10964, 45 interactors
MINTiP10964
STRINGi4932.YOR341W

Structurei

Secondary structure

11664
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

ProteinModelPortaliP10964
SMRiP10964
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni992 – 1004Bridging helixBy similarityAdd BLAST13

Sequence similaritiesi

Belongs to the RNA polymerase beta' chain family.Curated

Phylogenomic databases

GeneTreeiENSGT00920000149138
HOGENOMiHOG000205401
InParanoidiP10964
KOiK02999
OMAiRFFNRED
OrthoDBiEOG092C19ZG

Family and domain databases

Gene3Di1.10.132.30, 1 hit
InterProiView protein in InterPro
IPR015699 DNA-dir_RNA_pol1_lsu
IPR000722 RNA_pol_asu
IPR006592 RNA_pol_N
IPR007080 RNA_pol_Rpb1_1
IPR007066 RNA_pol_Rpb1_3
IPR007083 RNA_pol_Rpb1_4
IPR007081 RNA_pol_Rpb1_5
IPR038120 Rpb1_funnel_sf
PANTHERiPTHR19376:SF11 PTHR19376:SF11, 1 hit
PfamiView protein in Pfam
PF04997 RNA_pol_Rpb1_1, 1 hit
PF00623 RNA_pol_Rpb1_2, 1 hit
PF04983 RNA_pol_Rpb1_3, 1 hit
PF05000 RNA_pol_Rpb1_4, 1 hit
PF04998 RNA_pol_Rpb1_5, 1 hit
SMARTiView protein in SMART
SM00663 RPOLA_N, 1 hit

Sequencei

Sequence statusi: Complete.

P10964-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MDISKPVGSE ITSVDFGILT AKEIRNLSAK QITNPTVLDN LGHPVSGGLY
60 70 80 90 100
DLALGAFLRN LCSTCGLDEK FCPGHQGHIE LPVPCYNPLF FNQLYIYLRA
110 120 130 140 150
SCLFCHHFRL KSVEVHRYAC KLRLLQYGLI DESYKLDEIT LGSLNSSMYT
160 170 180 190 200
DDEAIEDNED EMDGEGSKQS KDISSTLLNE LKSKRSEYVD MAIAKALSDG
210 220 230 240 250
RTTERGSFTA TVNDERKKLV HEFHKKLLSR GKCDNCGMFS PKFRKDGFTK
260 270 280 290 300
IFETALNEKQ ITNNRVKGFI RQDMIKKQKQ AKKLDGSNEA SANDEESFDV
310 320 330 340 350
GRNPTTRPKT GSTYILSTEV KNILDTVFRK EQCVLQYVFH SRPNLSRKLV
360 370 380 390 400
KADSFFMDVL VVPPTRFRLP SKLGEEVHEN SQNQLLSKVL TTSLLIRDLN
410 420 430 440 450
DDLSKLQKDK VSLEDRRVIF SRLMNAFVTI QNDVNAFIDS TKAQGRTSGK
460 470 480 490 500
VPIPGVKQAL EKKEGLFRKH MMGKRVNYAA RSVISPDPNI ETNEIGVPPV
510 520 530 540 550
FAVKLTYPEP VTAYNIAELR QAVINGPDKW PGATQIQNED GSLVSLIGMS
560 570 580 590 600
VEQRKALANQ LLTPSSNVST HTLNKKVYRH IKNRDVVLMN RQPTLHKASM
610 620 630 640 650
MGHKVRVLPN EKTLRLHYAN TGAYNADFDG DEMNMHFPQN ENARAEALNL
660 670 680 690 700
ANTDSQYLTP TSGSPVRGLI QDHISAGVWL TSKDSFFTRE QYQQYIYGCI
710 720 730 740 750
RPEDGHTTRS KIVTLPPTIF KPYPLWTGKQ IITTVLLNVT PPDMPGINLI
760 770 780 790 800
SKNKIKNEYW GKGSLENEVL FKDGALLCGI LDKSQYGASK YGIVHSLHEV
810 820 830 840 850
YGPEVAAKVL SVLGRLFTNY ITATAFTCGM DDLRLTAEGN KWRTDILKTS
860 870 880 890 900
VDTGREAAAE VTNLDKDTPA DDPELLKRLQ EILRDNNKSG ILDAVTSSKV
910 920 930 940 950
NAITSQVVSK CVPDGTMKKF PCNSMQAMAL SGAKGSNVNV SQIMCLLGQQ
960 970 980 990 1000
ALEGRRVPVM VSGKTLPSFK PYETDAMAGG YVKGRFYSGI KPQEYYFHCM
1010 1020 1030 1040 1050
AGREGLIDTA VKTSRSGYLQ RCLTKQLEGV HVSYDNSIRD ADGTLVQFMY
1060 1070 1080 1090 1100
GGDAIDITKE SHMTQFEFCL DNYYALLKKY NPSALIEHLD VESALKYSKK
1110 1120 1130 1140 1150
TLKYRKKHSK EPHYKQSVKY DPVLAKYNPA KYLGSVSENF QDKLESFLDK
1160 1170 1180 1190 1200
NSKLFKSSDG VNEKKFRALM QLKYMRSLIN PGEAVGIIAS QSVGEPSTQM
1210 1220 1230 1240 1250
TLNTFHFAGH GAANVTLGIP RLREIVMTAS AAIKTPQMTL PIWNDVSDEQ
1260 1270 1280 1290 1300
ADTFCKSISK VLLSEVIDKV IVTETTGTSN TAGGNAARSY VIHMRFFDNN
1310 1320 1330 1340 1350
EYSEEYDVSK EELQNVISNQ FIHLLEAAIV KEIKKQKRTT GPDIGVAVPR
1360 1370 1380 1390 1400
LQTDVANSSS NSKRLEEDND EEQSHKKTKQ AVSYDEPDED EIETMREAEK
1410 1420 1430 1440 1450
SSDEEGIDSD KESDSDSEDE DVDMNEQINK SIVEANNNMN KVQRDRQSAI
1460 1470 1480 1490 1500
ISHHRFITKY NFDDESGKWC EFKLELAADT EKLLMVNIVE EICRKSIIRQ
1510 1520 1530 1540 1550
IPHIDRCVHP EPENGKRVLV TEGVNFQAMW DQEAFIDVDG ITSNDVAAVL
1560 1570 1580 1590 1600
KTYGVEAARN TIVNEINNVF SRYAISVSFR HLDLIADMMT RQGTYLAFNR
1610 1620 1630 1640 1650
QGMETSTSSF MKMSYETTCQ FLTKAVLDNE REQLDSPSAR IVVGKLNNVG
1660
TGSFDVLAKV PNAA
Length:1,664
Mass (Da):186,432
Last modified:November 1, 1997 - v2
Checksum:iDF65A7AA459D5E6D
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti158N → T in AAA34890 (PubMed:2830265).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J03530 Genomic DNA Translation: AAA34890.1
X95720 Genomic DNA Translation: CAA65029.1
Z75249 Genomic DNA Translation: CAA99665.1
BK006948 Genomic DNA Translation: DAA11102.1
PIRiS67250
RefSeqiNP_014986.3, NM_001183761.3

Genome annotation databases

EnsemblFungiiYOR341W; YOR341W; YOR341W
GeneIDi854519
KEGGisce:YOR341W

Similar proteinsi

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J03530 Genomic DNA Translation: AAA34890.1
X95720 Genomic DNA Translation: CAA65029.1
Z75249 Genomic DNA Translation: CAA99665.1
BK006948 Genomic DNA Translation: DAA11102.1
PIRiS67250
RefSeqiNP_014986.3, NM_001183761.3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4C2MX-ray2.80A/P1-1664[»]
4C3HX-ray3.27A1-1664[»]
4C3IX-ray3.0A1-1664[»]
4C3JX-ray3.35A1-1664[»]
4YM7X-ray5.50AA/BA/CA/DA/EA/FA1-1664[»]
5G5Lelectron microscopy4.80A1-1664[»]
5LMXelectron microscopy4.90A1-1664[»]
5M3Felectron microscopy3.80A1-1664[»]
5M3Melectron microscopy4.00A1-1664[»]
5M5Welectron microscopy3.80A1-1664[»]
5M5Xelectron microscopy4.00A1-1664[»]
5M5Yelectron microscopy4.00A1-1664[»]
5M64electron microscopy4.60A1-1664[»]
5N5Yelectron microscopy7.70A1-1664[»]
5N5Zelectron microscopy7.70A1-1664[»]
5N60electron microscopy7.70A1-1664[»]
5N61electron microscopy3.40A1-1664[»]
5OA1electron microscopy4.40A1-1664[»]
5W5Yelectron microscopy3.80A1-1664[»]
5W64electron microscopy4.20A1-1664[»]
5W65electron microscopy4.30A1-1664[»]
5W66electron microscopy3.90A1-1664[»]
6H67electron microscopy3.60A1-1664[»]
6H68electron microscopy4.60A1-1664[»]
ProteinModelPortaliP10964
SMRiP10964
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi34724, 460 interactors
ComplexPortaliCPX-1664 DNA-directed RNA Polymerase I complex
DIPiDIP-999N
IntActiP10964, 45 interactors
MINTiP10964
STRINGi4932.YOR341W

PTM databases

iPTMnetiP10964

Proteomic databases

MaxQBiP10964
PaxDbiP10964
PRIDEiP10964
TopDownProteomicsiP10964

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYOR341W; YOR341W; YOR341W
GeneIDi854519
KEGGisce:YOR341W

Organism-specific databases

SGDiS000005868 RPA190

Phylogenomic databases

GeneTreeiENSGT00920000149138
HOGENOMiHOG000205401
InParanoidiP10964
KOiK02999
OMAiRFFNRED
OrthoDBiEOG092C19ZG

Enzyme and pathway databases

BioCyciYEAST:G3O-33816-MONOMER
ReactomeiR-SCE-73762 RNA Polymerase I Transcription Initiation

Miscellaneous databases

PROiPR:P10964

Family and domain databases

Gene3Di1.10.132.30, 1 hit
InterProiView protein in InterPro
IPR015699 DNA-dir_RNA_pol1_lsu
IPR000722 RNA_pol_asu
IPR006592 RNA_pol_N
IPR007080 RNA_pol_Rpb1_1
IPR007066 RNA_pol_Rpb1_3
IPR007083 RNA_pol_Rpb1_4
IPR007081 RNA_pol_Rpb1_5
IPR038120 Rpb1_funnel_sf
PANTHERiPTHR19376:SF11 PTHR19376:SF11, 1 hit
PfamiView protein in Pfam
PF04997 RNA_pol_Rpb1_1, 1 hit
PF00623 RNA_pol_Rpb1_2, 1 hit
PF04983 RNA_pol_Rpb1_3, 1 hit
PF05000 RNA_pol_Rpb1_4, 1 hit
PF04998 RNA_pol_Rpb1_5, 1 hit
SMARTiView protein in SMART
SM00663 RPOLA_N, 1 hit
ProtoNetiSearch...

Entry informationi

Entry nameiRPA1_YEAST
AccessioniPrimary (citable) accession number: P10964
Secondary accession number(s): D6W336, Q99330
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: November 1, 1997
Last modified: November 7, 2018
This is version 187 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

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. Yeast chromosome XV
    Yeast (Saccharomyces cerevisiae) chromosome XV: entries and gene names
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
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