Reviewed, UniProtKB/Swiss-Prot P04051 (RPC1_YEAST)

Names and origin

Protein names

Recommended name:
    DNA-directed RNA polymerase III subunit RPC1
      Short name=RNA polymerase III subunit C1
    EC=2.7.7.6
Alternative name(s):
    DNA-directed RNA polymerase III largest subunit
    RNA polymerase III subunit C160

Gene names

Name:	RPO31
Synonyms:	RPC1, RPC160
Ordered Locus Names:	YOR116C
ORF Names:	O3254, YOR3254C

Organism

Saccharomyces cerevisiae (Baker's yeast) [Complete proteome]

Taxonomic identifier

4932 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces

Protein attributes

Sequence length	1460 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (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 structure	Component of the RNA polymerase III (Pol III) complex consisting of 17 subunits.
Subcellular location	Nucleus. Ref.8
Miscellaneous	Present with 6020 molecules/cell in log phase SD medium. Ref.9
Sequence similarities	Belongs to the RNA polymerase beta' chain family.

Ontologies

Keywords
Biological process	Transcription
Cellular component	DNA-directed RNA polymerase Nucleus
Domain	Zinc-finger
Ligand	Magnesium Metal-binding Zinc
Molecular function	Nucleotidyltransferase Transferase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	transcription Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	DNA-directed RNA polymerase III complex Traceable author statement. Source: SGD
Molecular function	DNA binding Inferred from electronic annotation. Source: InterPro DNA-directed RNA polymerase activity Traceable author statement. Source: SGD magnesium ion binding Inferred from electronic annotation. Source: UniProtKB-KW protein binding Inferred from physical interaction. Source: IntAct ribonucleoside binding Inferred from electronic annotation. Source: InterPro zinc ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
RPC25	P35718	1	EBI-15810,EBI-15854

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 1460	1460	DNA-directed RNA polymerase III subunit RPC1		PRO_0000073953
Regions
	Zinc finger	67 – 80	14	C3H1-type Potential
	Region	858 – 870	13	Bridging helix By similarity
Sites
	Metal binding	67	1	Zinc 1 By similarity
	Metal binding	70	1	Zinc 1 By similarity
	Metal binding	77	1	Zinc 1 By similarity
	Metal binding	80	1	Zinc 1 By similarity
	Metal binding	107	1	Zinc 2 By similarity
	Metal binding	110	1	Zinc 2 By similarity
	Metal binding	154	1	Zinc 2 By similarity
	Metal binding	511	1	Magnesium; catalytic By similarity
	Metal binding	513	1	Magnesium; catalytic By similarity
	Metal binding	515	1	Magnesium; catalytic By similarity
Experimental info
	Mutagenesis	506	1	T → I: Temperature-sensitive.
	Mutagenesis	509	1	N → Y: Temperature-sensitive.
	Mutagenesis	518	1	N → Q: Temperature-sensitive.

Sequences

	Sequence		Length	Mass (Da)
	P04051-1 [UniParc]. Last modified November 1, 1986. Version 1. Checksum: D1697EB2352BCA4F	FASTA	1,460	162,301
	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

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Extensive homology among the largest subunits of eukaryotic and prokaryotic RNA polymerases." Allison L.A., Moyle M., Shales M., Ingles C.J. Cell 42:599-610(1985) [PubMed: 3896517] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Sequencing and analysis of 51 kb on the right arm of chromosome XV from Saccharomyces cerevisiae reveals 30 open reading frames." Wiemann S., Rechmann S., Benes V., Voss H., Schwager C., Vlcek C., Stegemann J., Zimmermann J., Erfle H., Paces V., Ansorge W. Yeast 12:281-288(1996) [PubMed: 8904341] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 96604 / S288c / FY1679.
[3]	"DNA sequencing and analysis of 130 kb from yeast chromosome XV." Voss H., Benes V., Andrade M.A., Valencia A., Rechmann S., Teodoru C., Schwager C., Paces V., Sander C., Ansorge W. Yeast 13:655-672(1997) [PubMed: 9200815] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[4]	"The nucleotide sequence of Saccharomyces cerevisiae chromosome XV." 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. Nature 387:98-102(1997) [PubMed: 9169874] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 96604 / S288c / FY1679.
[5]	"Suppression of yeast RNA polymerase III mutations by FHL1, a gene coding for a fork head protein involved in rRNA processing." Hermann-Ledenmat S., Werner M., Sentenac A., Thuriaux P. Mol. Cell. Biol. 14:2905-2913(1994) [PubMed: 8164651] [Abstract] Cited for: MUTAGENESIS.
[6]	"Mutations in the alpha-amanitin conserved domain of the largest subunit of yeast RNA polymerase III affect pausing, RNA cleavage and transcriptional transitions." Thuillier V., Brun I., Sentenac A., Werner M. EMBO J. 15:618-629(1996) [PubMed: 8599945] [Abstract] Cited for: MUTAGENESIS.
[7]	"The yeast RNA polymerase III transcription machinery: a paradigm for eukaryotic gene activation." Chedin S., Ferri M.L., Peyroche G., Andrau J.-C., Jourdain S., Lefebvre O., Werner M., Carles C., Sentenac A. Cold Spring Harb. Symp. Quant. Biol. 63:381-389(1998) [PubMed: 10384303] [Abstract] Cited for: REVIEW ON THE RNA POL III COMPLEX.
[8]	"Global analysis of protein localization in budding yeast." Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W., Weissman J.S., O'Shea E.K. Nature 425:686-691(2003) [PubMed: 14562095] [Abstract] Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
[9]	"Global analysis of protein expression in yeast." Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S. Nature 425:737-741(2003) [PubMed: 14562106] [Abstract] Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[10]	"Structural biology of RNA polymerase III: subcomplex C17/25 X-ray structure and 11 subunit enzyme model." Jasiak A.J., Armache K.J., Martens B., Jansen R.P., Cramer P. Mol. Cell 23:71-81(2006) [PubMed: 16818233] [Abstract] Cited for: 3D-STRUCTURE MODELING OF THE POL III CORE COMPLEX.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	X03129 Genomic DNA. Translation: CAA26905.1. X90518 Genomic DNA. Translation: CAA62123.1. X94335 Genomic DNA. Translation: CAA64036.1. Z75024 Genomic DNA. Translation: CAA99314.1.
PIR	RNBY3L. A00694.
RefSeq	NP_014759.1.
3D structure databases
HSSP	HSSP built from PDB template 1I6H based on UniProtKB P04050.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP:612N.
IntAct	P04051. 44 interactions.
Proteomic databases
PeptideAtlas	P04051.
PRIDE	P04051.
Genome annotation databases
Ensembl	YOR116C. Saccharomyces cerevisiae. [Contig view]
GeneID	854283.
GenomeReviews	Gene locus YOR116C in contig Y13140_GR.
KEGG	sce:YOR116C.
NMPDR	fig|4932.3.peg.5862.
Organism-specific databases
CYGD	YOR116c.
SGD	S000005642. RPO31.
Yeast-GFP	Search...
Phylogenomic databases
HOGENOM	P04051.
OMA	P04051. CINELDN.
Enzyme and pathway databases
BRENDA	2.7.7.6. 250.
Gene expression databases
ArrayExpress	P04051.
GermOnline	YOR116C. Saccharomyces cerevisiae.
Family and domain databases
InterPro	IPR015700. DNA-dir_RNA_pol3_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. [Graphical view]
Gene3D	G3DSA:2.40.40.30. RNA_pol_A. 1 hit. G3DSA:3.90.1120.10. RNA_pol_Rpb1_1. 1 hit.
PANTHER	PTHR19376:SF15. RNA_pol3. 1 hit.
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. [Graphical view]
SMART	SM00663. RPOLA_N. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	976257.

Entry information

Entry name

RPC1_YEAST

Accession

Primary (citable) accession number: P04051

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1986
Last sequence update:	November 1, 1986
Last modified:	June 16, 2009
This is version 89 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)