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Protein

Transcription factor tau 91 kDa subunit

Gene

TFC6

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

TFIIIC mediates tRNA and 5S RNA gene activation by binding to intragenic promoter elements. Upstream of the transcription start site, TFIIIC assembles the initiation complex TFIIIB-TFIIIC-tDNA, which is sufficient for RNA polymerase III recruitment and function. Part of the tauB domain of TFIIIC that binds boxB DNA promoter sites of tRNA and similar genes. Cooperates with TFC3 in DNA binding.2 Publications

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
DNA bindingi6 – 1813A.T hookAdd
BLAST

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding

Enzyme and pathway databases

BioCyciYEAST:G3O-29912-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Transcription factor tau 91 kDa subunit
Alternative name(s):
TFIIIC 91 kDa subunit
Transcription factor C subunit 6
Gene namesi
Name:TFC6
Ordered Locus Names:YDR362C
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome IV

Organism-specific databases

EuPathDBiFungiDB:YDR362C.
SGDiS000002770. TFC6.

Subcellular locationi

GO - Cellular componenti

  • transcription factor TFIIIC complex Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 672672Transcription factor tau 91 kDa subunitPRO_0000252483Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi375 ↔ 3831 Publication

Keywords - PTMi

Disulfide bond

Proteomic databases

MaxQBiQ06339.
PeptideAtlasiQ06339.

PTM databases

iPTMnetiQ06339.

Interactioni

Subunit structurei

Heterodimer with TFC8. Component of the TFIIIC complex composed of TFC1, TFC3, TFC4, TFC6, TFC7 and TFC8. The subunits are organized in two globular domains, tauA and tauB, connected by a proteolysis-sensitive and flexible linker. Interacts with TFC1, TFC3, TFC4 and directly with TFC8.5 Publications

Protein-protein interaction databases

BioGridi32417. 22 interactions.
DIPiDIP-2952N.
IntActiQ06339. 6 interactions.
MINTiMINT-477678.

Structurei

Secondary structure

1
672
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi167 – 1748Combined sources
Helixi178 – 19114Combined sources
Helixi200 – 2034Combined sources
Beta strandi218 – 2203Combined sources
Helixi223 – 2253Combined sources
Turni226 – 2305Combined sources
Helixi241 – 2444Combined sources
Beta strandi253 – 2586Combined sources
Beta strandi261 – 2666Combined sources
Beta strandi270 – 2723Combined sources
Helixi273 – 2753Combined sources
Beta strandi283 – 2875Combined sources
Beta strandi298 – 3003Combined sources
Beta strandi308 – 31811Combined sources
Beta strandi339 – 3479Combined sources
Turni348 – 3503Combined sources
Beta strandi353 – 3619Combined sources
Beta strandi365 – 3717Combined sources
Beta strandi378 – 3814Combined sources
Beta strandi383 – 3886Combined sources
Beta strandi393 – 3975Combined sources
Beta strandi402 – 4098Combined sources
Beta strandi415 – 4184Combined sources
Turni421 – 4233Combined sources
Beta strandi425 – 44016Combined sources
Beta strandi443 – 4497Combined sources
Beta strandi457 – 4615Combined sources
Beta strandi463 – 4653Combined sources
Beta strandi467 – 4737Combined sources
Beta strandi481 – 4866Combined sources
Beta strandi489 – 4946Combined sources
Helixi496 – 4983Combined sources
Helixi499 – 5024Combined sources
Beta strandi504 – 5085Combined sources
Beta strandi517 – 5204Combined sources
Turni521 – 5244Combined sources
Beta strandi525 – 5295Combined sources
Beta strandi531 – 5399Combined sources
Beta strandi547 – 5515Combined sources
Beta strandi556 – 5605Combined sources
Beta strandi569 – 5724Combined sources
Turni573 – 5753Combined sources
Beta strandi576 – 5783Combined sources
Turni586 – 5883Combined sources
Beta strandi601 – 6044Combined sources
Beta strandi609 – 6113Combined sources
Beta strandi613 – 6164Combined sources
Beta strandi645 – 6473Combined sources
Turni651 – 6555Combined sources
Beta strandi656 – 6605Combined sources
Beta strandi664 – 6707Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2J04X-ray3.20B/D159-672[»]
ProteinModelPortaliQ06339.
SMRiQ06339. Positions 165-672.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ06339.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 158158Required for DNA-bindingAdd
BLAST
Regioni159 – 672514Sufficient for interaction with TFC8Add
BLAST

Sequence similaritiesi

Contains 1 A.T hook DNA-binding domain.Curated

Phylogenomic databases

HOGENOMiHOG000001063.
InParanoidiQ06339.
KOiK15205.
OMAiRLWKWDY.
OrthoDBiEOG7ZGXCQ.

Family and domain databases

Gene3Di2.130.10.10. 1 hit.
InterProiIPR015943. WD40/YVTN_repeat-like_dom.
IPR017986. WD40_repeat_dom.
[Graphical view]
SUPFAMiSSF50978. SSF50978. 3 hits.

Sequencei

Sequence statusi: Complete.

Q06339-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAVIPAKKRG RPRKSVVAEV PYDSLASPVS ENSGSKRPRR NASKKAVANF
60 70 80 90 100
AQLVHAGRDD VINTTQVNNV DDTDDDDFVL NDEGDGEESD NVEIEFENEL
110 120 130 140 150
ESTKNEVADL NSSGSGASVR PSGRRNTVQK LRLKKNSTKN MKSSSPGSSL
160 170 180 190 200
GQKGRPIRLL KDLSSARDKI ERIYGLNKEK LLLLAKVKEG FETSVFDFPF
210 220 230 240 250
KNIQPDSPYF VCLDPPCKKE SAYNKVIGDK NRTVYHEINK TEFENMIKLR
260 270 280 290 300
TKRLKLLIGE VDAEVSTGDK IEFPVLANGK RRGFIYNVGG LVTDIAWLNI
310 320 330 340 350
EENTDIGKDI QYLAVAVSQY MDEPLNEHLE MFDKEKHSSC IQIFKMNTST
360 370 380 390 400
LHCVKVQTIV HSFGEVWDLK WHEGCHAPHL VGCLSFVSQE GTINFLEIID
410 420 430 440 450
NATDVHVFKM CEKPSLTLSL ADSLITTFDF LSPTTVVCGF KNGFVAEFDL
460 470 480 490 500
TDPEVPSFYD QVHDSYILSV STAYSDFEDT VVSTVAVDGY FYIFNPKDIA
510 520 530 540 550
TTKTTVSRFR GSNLVPVVYC PQIYSYIYSD GASSLRAVPS RAAFAVHPLV
560 570 580 590 600
SRETTITAIG VSRLHPMVLA GSADGSLIIT NAARRLLHGI KNSSATQKSL
610 620 630 640 650
RLWKWDYSIK DDKYRIDSSY EVYPLTVNDV SKAKIDAHGI NITCTKWNET
660 670
SAGGKCYAFS NSAGLLTLEY LS
Length:672
Mass (Da):74,709
Last modified:November 1, 1996 - v1
Checksum:i744D6D6A1923B076
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U28372 Genomic DNA. Translation: AAB64796.1.
BK006938 Genomic DNA. Translation: DAA12200.1.
PIRiS61157.
RefSeqiNP_010649.1. NM_001180670.1.

Genome annotation databases

EnsemblFungiiYDR362C; YDR362C; YDR362C.
GeneIDi851964.
KEGGisce:YDR362C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U28372 Genomic DNA. Translation: AAB64796.1.
BK006938 Genomic DNA. Translation: DAA12200.1.
PIRiS61157.
RefSeqiNP_010649.1. NM_001180670.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2J04X-ray3.20B/D159-672[»]
ProteinModelPortaliQ06339.
SMRiQ06339. Positions 165-672.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi32417. 22 interactions.
DIPiDIP-2952N.
IntActiQ06339. 6 interactions.
MINTiMINT-477678.

PTM databases

iPTMnetiQ06339.

Proteomic databases

MaxQBiQ06339.
PeptideAtlasiQ06339.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYDR362C; YDR362C; YDR362C.
GeneIDi851964.
KEGGisce:YDR362C.

Organism-specific databases

EuPathDBiFungiDB:YDR362C.
SGDiS000002770. TFC6.

Phylogenomic databases

HOGENOMiHOG000001063.
InParanoidiQ06339.
KOiK15205.
OMAiRLWKWDY.
OrthoDBiEOG7ZGXCQ.

Enzyme and pathway databases

BioCyciYEAST:G3O-29912-MONOMER.

Miscellaneous databases

EvolutionaryTraceiQ06339.
PROiQ06339.

Family and domain databases

Gene3Di2.130.10.10. 1 hit.
InterProiIPR015943. WD40/YVTN_repeat-like_dom.
IPR017986. WD40_repeat_dom.
[Graphical view]
SUPFAMiSSF50978. SSF50978. 3 hits.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV."
    Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G., Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C., Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F., Delaveau T.
    , del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M., Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T., Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C., Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S., Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L., Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H., Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M., Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M., Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A., Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G., Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E., Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S., Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D., Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V., Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E., Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M., Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D., Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X., Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A., Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T., Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L., Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E., Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L., Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M., Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K., Mewes H.-W., Zollner A., Zaccaria P.
    Nature 387:75-78(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  2. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  3. "Expression, proteolytic analysis, reconstitution, and crystallization of the tau60/tau91 subcomplex of yeast TFIIIC."
    Mylona A., Acker J., Fernandez-Tornero C., Sentenac A., Mueller C.W.
    Protein Expr. Purif. 45:255-261(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF N-TERMINUS, CRYSTALLIZATION, INTERACTION WITH TFC8.
  4. "Two polypeptide chains in yeast transcription factor tau interact with DNA."
    Gabrielsen O.S., Marzouki N., Ruet A., Sentenac A., Fromageot P.
    J. Biol. Chem. 264:7505-7511(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  5. "On the subunit composition, stoichiometry, and phosphorylation of the yeast transcription factor TFIIIC/tau."
    Conesa C., Swanson R.N., Schultz P., Oudet P., Sentenac A.
    J. Biol. Chem. 268:18047-18052(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH TFC1; TFC3 AND TFC4.
  6. "Tau91, an essential subunit of yeast transcription factor IIIC, cooperates with tau138 in DNA binding."
    Arrebola R., Manaud N., Rozenfeld S., Marsolier M.C., Lefebvre O., Carles C., Thuriaux P., Conesa C., Sentenac A.
    Mol. Cell. Biol. 18:1-9(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, IDENTIFICATION IN THE TFIIIC COMPLEX.
  7. "The tau95 subunit of yeast TFIIIC influences upstream and downstream functions of TFIIIC.DNA complexes."
    Jourdain S., Acker J., Ducrot C., Sentenac A., Lefebvre O.
    J. Biol. Chem. 278:10450-10457(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH TFC1 AND TFC3.
  8. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
  9. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  10. "A multidimensional chromatography technology for in-depth phosphoproteome analysis."
    Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.
    Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  11. "Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution."
    Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.
    Science 325:1682-1686(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. "Structure of the tau60/Delta tau91 subcomplex of yeast transcription factor IIIC: insights into preinitiation complex assembly."
    Mylona A., Fernandez-Tornero C., Legrand P., Haupt M., Sentenac A., Acker J., Mueller C.W.
    Mol. Cell 24:221-232(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.20 ANGSTROMS) OF 159-672 IN COMPLEX WITH TFC8, REGION, DISULFIDE BOND.

Entry informationi

Entry nameiTFC6_YEAST
AccessioniPrimary (citable) accession number: Q06339
Secondary accession number(s): D6VSZ0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 17, 2006
Last sequence update: November 1, 1996
Last modified: June 8, 2016
This is version 109 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 1130 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 IV
    Yeast (Saccharomyces cerevisiae) chromosome IV: 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.