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UniProtKB/Swiss-Prot entry P04051


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name RPC1_YEAST
Primary accession number P04051
Secondary accession numbers None
Integrated into Swiss-Prot on November 1, 1986
Sequence was last modified on November 1, 1986 (Sequence version 1)
Annotations were last modified on    November 4, 2008 (Entry version 82)
Name and origin of the protein
Protein name DNA-directed RNA polymerase III subunit RPC1
Synonyms RNA polymerase III subunit C1
EC 2.7.7.6
DNA-directed RNA polymerase III largest subunit
C160
Gene name
Name: RPO31
Synonyms: RPC1, RPC160
OrderedLocusNames: YOR116C
ORFNames: O3254, YOR3254C
From
Saccharomyces cerevisiae (Baker's yeast) [TaxID: 4932] 
Taxonomy Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
DOI=10.1016/0092-8674(85)90117-5; PubMed=3896517 [NCBI, ExPASy, EBI, Israel, Japan]
Allison L.A., Moyle M., Shales M., Ingles C.J.;
"Extensive homology among the largest subunits of eukaryotic and prokaryotic RNA polymerases.";
Cell 42:599-610(1985).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ATCC 96604 / S288c / FY1679;
DOI=10.1002/(SICI)1097-0061(19960315)12:3<281::AID-YEA904>3.3.CO;2-F; PubMed=8904341 [NCBI, ExPASy, EBI, Israel, Japan]
Wiemann S., Rechmann S., Benes V., Voss H., Schwager C., Vlcek C., Stegemann J., Zimmermann J., Erfle H., Paces V., Ansorge W.;
"Sequencing and analysis of 51 kb on the right arm of chromosome XV from Saccharomyces cerevisiae reveals 30 open reading frames.";
Yeast 12:281-288(1996).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
DOI=10.1002/(SICI)1097-0061(19970615)13:7<655::AID-YEA120>3.0.CO;2-I; PubMed=9200815 [NCBI, ExPASy, EBI, Israel, Japan]
Voss H., Benes V., Andrade M.A., Valencia A., Rechmann S., Teodoru C., Schwager C., Paces V., Sander C., Ansorge W.;
"DNA sequencing and analysis of 130 kb from yeast chromosome XV.";
Yeast 13:655-672(1997).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 96604 / S288c / FY1679;
PubMed=9169874 [NCBI, ExPASy, EBI, Israel, Japan]
Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J., Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A., Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B., Dang V.-D., de Haan M., Delius H., Durand P., Fairhead C., Feldmann H., Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E., Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U., Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B., Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A., Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C., Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G., Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B., Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B., Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F., Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E., Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I., Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H., Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.;
"The nucleotide sequence of Saccharomyces cerevisiae chromosome XV.";
Nature 387:98-102(1997).
[5]
MUTAGENESIS.
PubMed=8164651 [NCBI, ExPASy, EBI, Israel, Japan]
Hermann-Ledenmat S., Werner M., Sentenac A., Thuriaux P.;
"Suppression of yeast RNA polymerase III mutations by FHL1, a gene coding for a fork head protein involved in rRNA processing.";
Mol. Cell. Biol. 14:2905-2913(1994).
[6]
MUTAGENESIS.
PubMed=8599945 [NCBI, ExPASy, EBI, Israel, Japan]
Thuillier V., Brun I., Sentenac A., Werner M.;
"Mutations in the alpha-amanitin conserved domain of the largest subunit of yeast RNA polymerase III affect pausing, RNA cleavage and transcriptional transitions.";
EMBO J. 15:618-629(1996).
[7]
REVIEW ON THE RNA POL III COMPLEX.
DOI=10.1101/sqb.1998.63.381; PubMed=10384303 [NCBI, ExPASy, EBI, Israel, Japan]
Chedin S., Ferri M.L., Peyroche G., Andrau J.-C., Jourdain S., Lefebvre O., Werner M., Carles C., Sentenac A.;
"The yeast RNA polymerase III transcription machinery: a paradigm for eukaryotic gene activation.";
Cold Spring Harb. Symp. Quant. Biol. 63:381-389(1998).
[8]
SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
DOI=10.1038/nature02026; PubMed=14562095 [NCBI, ExPASy, EBI, Israel, Japan]
Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W., Weissman J.S., O'Shea E.K.;
"Global analysis of protein localization in budding yeast.";
Nature 425:686-691(2003).
[9]
LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
DOI=10.1038/nature02046; PubMed=14562106 [NCBI, ExPASy, EBI, Israel, Japan]
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S.;
"Global analysis of protein expression in yeast.";
Nature 425:737-741(2003).
[10]
3D-STRUCTURE MODELING OF THE POL III CORE COMPLEX.
DOI=10.1016/j.molcel.2006.05.013; PubMed=16818233 [NCBI, ExPASy, EBI, Israel, Japan]
Jasiak A.J., Armache K.J., Martens B., Jansen R.P., Cramer P.;
"Structural biology of RNA polymerase III: subcomplex C17/25 X-ray structure and 11 subunit enzyme model.";
Mol. Cell 23:71-81(2006).
Comments
  • FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Largest and catalytic core component of RNA polymerase III which synthesizes small RNAs, such as 5S rRNA and tRNAs. Forms the polymerase active center together with the second largest subunit. A single stranded DNA template strand of the promoter is positioned within the central active site cleft of Pol III. A bridging helix emanates from RPC1 and crosses the cleft near the catalytic site and is thought to promote translocation of Pol III 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 (By similarity).
  • CATALYTIC ACTIVITY: Nucleoside triphosphate + RNA(n) = diphosphate + RNA(n+1).
  • SUBUNIT: Component of the RNA polymerase III (Pol III) complex consisting of 17 subunits.
  • SUBCELLULAR LOCATION: Nucleus.
  • MISCELLANEOUS: Present with 6020 molecules/cell in log phase SD medium.
  • SIMILARITY: Belongs to the RNA polymerase beta' chain family.
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
X03129; CAA26905.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X90518; CAA62123.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X94335; CAA64036.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
Z75024; CAA99314.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR A00694; RNBY3L.
RefSeq NP_014759.1; -.
3D structure databases
HSSP P04050; 1I6H. [HSSP ENTRY / PDB]
ModBase P04051.
Protein-protein interaction databases
DIP DIP:612N; -.
IntAct P04051; -.
Organism-specific databases
CYGD YOR116c; -.
SGD S000005642; RPO31.
Yeast-GFP YOR116C.
Gene expression databases
ArrayExpress P04051; -.
GermOnline YOR116C; Saccharomyces cerevisiae.
Ontologies
GO
GO:0005666; Cellular component: DNA-directed RNA polymerase III complex (traceable author statement from SGD).
GO:0003899; Molecular function: DNA-directed RNA polymerase activity (traceable author statement from SGD).
QuickGo view.
Family and domain databases
InterPro IPR015700; RNA_pol3.
IPR000722; RNA_pol_A.
IPR006592; RNA_pol_N.
IPR007080; RNA_pol_Rpb1_1.
IPR007066; RNA_pol_Rpb1_3.
IPR007083; RNA_pol_Rpb1_4.
IPR007081; RNA_pol_Rpb1_5.
Graphical view of domain structure.
Gene3D G3DSA:2.40.40.30; RNA_pol_A; 1.
G3DSA:3.90.1120.10; RNA_pol_Rpb1_1; 1.
PANTHER PTHR19376:SF15; RNA_pol3; 1.
Pfam PF04997; RNA_pol_Rpb1_1; 1.
PF00623; RNA_pol_Rpb1_2; 1.
PF04983; RNA_pol_Rpb1_3; 1.
PF05000; RNA_pol_Rpb1_4; 1.
PF04998; RNA_pol_Rpb1_5; 1.
Pfam graphical view of domain structure.
SMART SM00663; RPOLA_N; 1.
SMART graphical view of domain structure.
BLOCKS P04051.
ProtoNet P04051.
Proteomic databases
PeptideAtlas P04051; -.
Genome annotation databases
Ensembl YOR116C; Saccharomyces cerevisiae. [Contig view]
GeneID 854283; -.
GenomeReviews Y13140_GR; YOR116C.
KEGG sce:YOR116C; -.
NMPDR fig|4932.3.peg.5862; -.
Phylogenomic databases
HOGENOM P04051; -.
Other
LinkHub P04051; -.
NextBio 976257; -.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Complete proteome; DNA-directed RNA polymerase; Magnesium; Metal-binding; Nucleotidyltransferase; Nucleus; Transcription; Transferase; Zinc; Zinc-finger.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   1460  1460     DNA-directed RNA polymerase III subunit RPC1. PRO_0000073953
ZN_FING   67     80  14     C3H1-type (Potential). 
REGION   858    870  13     Bridging helix (By similarity). 
METAL   67     67        Zinc 1 (By similarity). 
METAL   70     70        Zinc 1 (By similarity). 
METAL   77     77        Zinc 1 (By similarity). 
METAL   80     80        Zinc 1 (By similarity). 
METAL   107    107        Zinc 2 (By similarity). 
METAL   110    110        Zinc 2 (By similarity). 
METAL   154    154        Zinc 2 (By similarity). 
METAL   511    511        Magnesium; catalytic (By similarity). 
METAL   513    513        Magnesium; catalytic (By similarity). 
METAL   515    515        Magnesium; catalytic (By similarity). 
MUTAGEN   506    506        T->I: Temperature-sensitive. 
MUTAGEN   509    509        N->Y: Temperature-sensitive. 
MUTAGEN   518    518        N->Q: Temperature-sensitive. 
Sequence information
Length: 1460 AA [This is the length of the unprocessed precursor] Molecular weight: 162301 Da [This is the MW of the unprocessed precursor] CRC64: D1697EB2352BCA4F [This is a checksum on the sequence]
        10         20         30         40         50         60 
MKEVVVSETP KRIKGLEFSA LSAADIVAQS EVEVSTRDLF DLEKDRAPKA NGALDPKMGV 

        70         80         90        100        110        120 
SSSSLECATC HGNLASCHGH FGHLKLALPV FHIGYFKATI QILQGICKNC SAILLSETDK 

       130        140        150        160        170        180 
RQFLHELRRP GVDNLRRMGI LKKILDQCKK QRRCLHCGAL NGVVKKAAAG AGSAALKIIH 

       190        200        210        220        230        240 
DTFRWVGKKS APEKDIWVGE WKEVLAHNPE LERYVKRCMD DLNPLKTLNL FKQIKSADCE 

       250        260        270        280        290        300 
LLGIDATVPS GRPETYIWRY LPAPPVCIRP SVMMQDSPAS NEDDLTVKLT EIVWTSSLIK 

       310        320        330        340        350        360 
AGLDKGISIN NMMEHWDYLQ LTVAMYINSD SVNPAMLPGS SNGGGKVKPI RGFCQRLKGK 

       370        380        390        400        410        420 
QGRFRGNLSG KRVDFSGRTV ISPDPNLSID EVAVPDRVAK VLTYPEKVTR YNRHKLQELI 

       430        440        450        460        470        480 
VNGPNVHPGA NYLLKRNEDA RRNLRYGDRM KLAKNLQIGD VVERHLEDGD VVLFNRQPSL 

       490        500        510        520        530        540 
HRLSILSHYA KIRPWRTFRL NECVCTPYNA DFDGDEMNLH VPQTEEARAE AINLMGVKNN 

       550        560        570        580        590        600 
LLTPKSGEPI IAATQDFITG SYLISHKDSF YDRATLTQLL SMMSDGIEHF DIPPPAIMKP 

       610        620        630        640        650        660 
YYLWTGKQVF SLLIKPNHNS PVVINLDAKN KVFVPPKSKS LPNEMSQNDG FVIIRGSQIL 

       670        680        690        700        710        720 
SGVMDKSVLG DGKKHSVFYT ILRDYGPQEA ANAMNRMAKL CARFLGNRGF SIGINDVTPA 

       730        740        750        760        770        780 
DDLKQKKEEL VEIAYHKCDE LITLFNKGEL ETQPGCNEEQ TLEAKIGGLL SKVREEVGDV 

       790        800        810        820        830        840 
CINELDNWNA PLIMATCGSK GSTLNVSQMV AVVGQQIISG NRVPDGFQDR SLPHFPKNSK 

       850        860        870        880        890        900 
TPQSKGFVRN SFFSGLSPPE FLFHAISGRE GLVDTAVKTA ETGYMSRRLM KSLEDLSCQY 

       910        920        930        940        950        960 
DNTVRTSANG IVQFTYGGDG LDPLEMEGNA QPVNFNRSWD HAYNITFNNQ DKGLLPYAIM 

       970        980        990       1000       1010       1020 
ETANEILGPL EERLVRYDNS GCLVKREDLN KAEYVDQYDA ERDFYHSLRE YINGKATALA 

      1030       1040       1050       1060       1070       1080 
NLRKSRGMLG LLEPPAKELQ GIDPDETVPD NVKTSVSQLY RISEKSVRKF LEIALFKYRK 

      1090       1100       1110       1120       1130       1140 
ARLEPGTAIG AIGAQSIGEP GTQMTLKTFH FAGVASMNVT LGVPRIKEII NASKVISTPI 

      1150       1160       1170       1180       1190       1200 
INAVLVNDND ERAARVVKGR VEKTLLSDVA FYVQDVYKDN LSFIQVRIDL GTIDKLQLEL 

      1210       1220       1230       1240       1250       1260 
TIEDIAVAIT RASKLKIQAS DVNIIGKDRI AINVFPEGYK AKSISTSAKE PSENDVFYRM 

      1270       1280       1290       1300       1310       1320 
QQLRRALPDV VVKGLPDISR AVINIRDDGK RELLVEGYGL RDVMCTDGVI GSRTTTNHVL 

      1330       1340       1350       1360       1370       1380 
EVFSVLGIEA ARYSIIREIN YTMSNHGMSV DPRHIQLLGD VMTYKGEVLG ITRFGLSKMR 

      1390       1400       1410       1420       1430       1440 
DSVLQLASFE KTTDHLFDAA FYMKKDAVEG VSECIILGQT MSIGTGSFKV VKGTNISEKD 

      1450       1460 
LVPKRCLFES LSNEAALKAN 

P04051 in FASTA format

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BLAST logo BLAST submission on ExPASy/SIB
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