ID RPC6_YEAST Reviewed; 317 AA. AC P32910; D6W1H9; DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1993, sequence version 1. DT 08-MAY-2019, entry version 160. DE RecName: Full=DNA-directed RNA polymerase III subunit RPC6; DE Short=RNA polymerase III subunit C6; DE AltName: Full=C34; DE AltName: Full=DNA-directed RNA polymerase III 36 kDa polypeptide; GN Name=RPC34; OrderedLocusNames=YNR003C; ORFNames=N2031; OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; OC Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces. OX NCBI_TaxID=559292; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 26-38 AND RP 214-219. RC STRAIN=S288c / GRF88; RX PubMed=1400451; RA Stettler S., Mariotte S., Riva M., Sentenac A., Thuriaux P.; RT "An essential and specific subunit of RNA polymerase III (C) is RT encoded by gene RPC34 in Saccharomyces cerevisiae."; RL J. Biol. Chem. 267:21390-21395(1992). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=S288c / GRF88; RX PubMed=7941739; DOI=10.1002/yea.320100412; RA Lalo D., Stettler S., Mariotte S., Gendreau E., Thuriaux P.; RT "Organization of the centromeric region of chromosome XIV in RT Saccharomyces cerevisiae."; RL Yeast 10:523-533(1994). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 96604 / S288c / FY1679; RX PubMed=7900425; DOI=10.1002/yea.320101013; RA Verhasselt P., Aert R., Voet M., Volckaert G.; RT "Twelve open reading frames revealed in the 23.6 kb segment flanking RT the centromere on the Saccharomyces cerevisiae chromosome XIV right RT arm."; RL Yeast 10:1355-1361(1994). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 204508 / S288c; RX PubMed=9169873; RA Philippsen P., Kleine K., Poehlmann R., Duesterhoeft A., Hamberg K., RA Hegemann J.H., Obermaier B., Urrestarazu L.A., Aert R., Albermann K., RA Altmann R., Andre B., Baladron V., Ballesta J.P.G., Becam A.-M., RA Beinhauer J.D., Boskovic J., Buitrago M.J., Bussereau F., Coster F., RA Crouzet M., D'Angelo M., Dal Pero F., De Antoni A., del Rey F., RA Doignon F., Domdey H., Dubois E., Fiedler T.A., Fleig U., Floeth M., RA Fritz C., Gaillardin C., Garcia-Cantalejo J.M., Glansdorff N., RA Goffeau A., Gueldener U., Herbert C.J., Heumann K., Heuss-Neitzel D., RA Hilbert H., Hinni K., Iraqui Houssaini I., Jacquet M., Jimenez A., RA Jonniaux J.-L., Karpfinger-Hartl L., Lanfranchi G., Lepingle A., RA Levesque H., Lyck R., Maftahi M., Mallet L., Maurer C.T.C., RA Messenguy F., Mewes H.-W., Moestl D., Nasr F., Nicaud J.-M., RA Niedenthal R.K., Pandolfo D., Pierard A., Piravandi E., Planta R.J., RA Pohl T.M., Purnelle B., Rebischung C., Remacha M.A., Revuelta J.L., RA Rinke M., Saiz J.E., Sartorello F., Scherens B., Sen-Gupta M., RA Soler-Mira A., Urbanus J.H.M., Valle G., Van Dyck L., Verhasselt P., RA Vierendeels F., Vissers S., Voet M., Volckaert G., Wach A., RA Wambutt R., Wedler H., Zollner A., Hani J.; RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV RT and its evolutionary implications."; RL Nature 387:93-98(1997). RN [5] RP GENOME REANNOTATION. RC STRAIN=ATCC 204508 / S288c; RX PubMed=24374639; DOI=10.1534/g3.113.008995; RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R., RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S., RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., RA Cherry J.M.; RT "The reference genome sequence of Saccharomyces cerevisiae: Then and RT now."; RL G3 (Bethesda) 4:389-398(2014). RN [6] RP INTERACTION WITH BRF1. RX PubMed=8407894; RA Werner M., Chaussivert N., Willis I.M., Sentenac A.; RT "Interaction between a complex of RNA polymerase III subunits and the RT 70-kDa component of transcription factor IIIB."; RL J. Biol. Chem. 268:20721-20724(1993). RN [7] RP FUNCTION, INTERACTION WITH BRF1, AND MUTAGENESIS OF GLU-89; RP 102-ARG-GLU-103; LYS-135 AND 171-ASP-GLU-173. RX PubMed=9312031; DOI=10.1093/emboj/16.18.5730; RA Brun I., Sentenac A., Werner M.; RT "Dual role of the C34 subunit of RNA polymerase III in transcription RT initiation."; RL EMBO J. 16:5730-5741(1997). RN [8] RP REVIEW ON THE RNA POL III COMPLEX. RX PubMed=10384303; DOI=10.1101/sqb.1998.63.381; RA Chedin S., Ferri M.L., Peyroche G., Andrau J.-C., Jourdain S., RA Lefebvre O., Werner M., Carles C., Sentenac A.; RT "The yeast RNA polymerase III transcription machinery: a paradigm for RT eukaryotic gene activation."; RL Cold Spring Harb. Symp. Quant. Biol. 63:381-389(1998). CC -!- FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription CC of DNA into RNA using the four ribonucleoside triphosphates as CC substrates. Specific peripheric component of RNA polymerase III CC which synthesizes small RNAs, such as 5S rRNA and tRNAs. Involved CC in recruitment of Pol III to the preinitiation complex. Involved CC in the configuration of an initiation-competent form of RNA CC polymerase. {ECO:0000269|PubMed:9312031}. CC -!- SUBUNIT: Component of the RNA polymerase III (Pol III) complex CC consisting of 17 subunits. Interacts with BRF1/TDS4. CC {ECO:0000269|PubMed:8407894, ECO:0000269|PubMed:9312031}. CC -!- INTERACTION: CC P20436:RPB8; NbExp=3; IntAct=EBI-15835, EBI-15794; CC P47076:RPC17; NbExp=2; IntAct=EBI-15835, EBI-25782; CC P32349:RPC82; NbExp=3; IntAct=EBI-15835, EBI-15821; CC -!- SUBCELLULAR LOCATION: Nucleus. CC -!- SIMILARITY: Belongs to the eukaryotic RPC34/RPC39 RNA polymerase CC subunit family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; X63746; CAA45278.1; -; Genomic_DNA. DR EMBL; X77395; CAA54572.1; -; Genomic_DNA. DR EMBL; Z71618; CAA96279.1; -; Genomic_DNA. DR EMBL; BK006947; DAA10545.1; -; Genomic_DNA. DR PIR; A45107; A45107. DR RefSeq; NP_014400.1; NM_001183180.1. DR PDB; 5FJ8; EM; 3.90 A; P=1-317. DR PDB; 5FJ9; EM; 4.60 A; P=1-317. DR PDB; 5FJA; EM; 4.65 A; P=1-317. DR PDB; 6CNB; EM; 4.10 A; P=1-317. DR PDB; 6CNC; EM; 4.10 A; P=1-317. DR PDB; 6CND; EM; 4.80 A; P=1-317. DR PDB; 6CNF; EM; 4.50 A; P=1-317. DR PDB; 6EU0; EM; 4.00 A; P=1-317. DR PDB; 6EU1; EM; 3.40 A; P=1-317. DR PDB; 6EU2; EM; 3.40 A; P=1-317. DR PDB; 6EU3; EM; 3.30 A; P=1-317. DR PDB; 6F40; EM; 3.70 A; P=1-317. DR PDB; 6F41; EM; 4.30 A; P=1-317. DR PDB; 6F42; EM; 5.50 A; P=1-317. DR PDB; 6F44; EM; 4.20 A; P=1-317. DR PDBsum; 5FJ8; -. DR PDBsum; 5FJ9; -. DR PDBsum; 5FJA; -. DR PDBsum; 6CNB; -. DR PDBsum; 6CNC; -. DR PDBsum; 6CND; -. DR PDBsum; 6CNF; -. DR PDBsum; 6EU0; -. DR PDBsum; 6EU1; -. DR PDBsum; 6EU2; -. DR PDBsum; 6EU3; -. DR PDBsum; 6F40; -. DR PDBsum; 6F41; -. DR PDBsum; 6F42; -. DR PDBsum; 6F44; -. DR SMR; P32910; -. DR BioGrid; 35829; 471. DR ComplexPortal; CPX-2660; DNA-directed RNA polymerase III complex. DR DIP; DIP-202N; -. DR IntAct; P32910; 23. DR MINT; P32910; -. DR STRING; 4932.YNR003C; -. DR MaxQB; P32910; -. DR PaxDb; P32910; -. DR PRIDE; P32910; -. DR EnsemblFungi; YNR003C_mRNA; YNR003C_mRNA; YNR003C. DR GeneID; 855737; -. DR KEGG; sce:YNR003C; -. DR EuPathDB; FungiDB:YNR003C; -. DR SGD; S000005286; RPC34. DR GeneTree; ENSGT00390000009679; -. DR HOGENOM; HOG000186563; -. DR InParanoid; P32910; -. DR KO; K03025; -. DR OMA; ELKFQAV; -. DR BioCyc; YEAST:G3O-33322-MONOMER; -. DR Reactome; R-SCE-76061; RNA Polymerase III Transcription Initiation From Type 1 Promoter. DR Reactome; R-SCE-76066; RNA Polymerase III Transcription Initiation From Type 2 Promoter. DR PRO; PR:P32910; -. DR Proteomes; UP000002311; Chromosome XIV. DR GO; GO:0005737; C:cytoplasm; HDA:SGD. DR GO; GO:0005739; C:mitochondrion; IPI:SGD. DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome. DR GO; GO:0005634; C:nucleus; HDA:SGD. DR GO; GO:0005666; C:RNA polymerase III complex; IDA:SGD. DR GO; GO:0003899; F:DNA-directed 5'-3' RNA polymerase activity; IEA:UniProtKB-KW. DR GO; GO:0006386; P:termination of RNA polymerase III transcription; TAS:Reactome. DR GO; GO:0042797; P:tRNA transcription by RNA polymerase III; IDA:SGD. DR Gene3D; 1.10.10.10; -; 1. DR InterPro; IPR007832; RNA_pol_Rpc34. DR InterPro; IPR016049; RNA_pol_Rpc34-like. DR InterPro; IPR036388; WH-like_DNA-bd_sf. DR InterPro; IPR036390; WH_DNA-bd_sf. DR PANTHER; PTHR12780; PTHR12780; 1. DR Pfam; PF05158; RNA_pol_Rpc34; 1. DR PIRSF; PIRSF028763; RNA_pol_Rpc34; 1. DR SUPFAM; SSF46785; SSF46785; 1. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; Direct protein sequencing; KW DNA-directed RNA polymerase; Nucleus; Reference proteome; KW Transcription. FT CHAIN 1 317 DNA-directed RNA polymerase III subunit FT RPC6. FT /FTId=PRO_0000073977. FT MUTAGEN 89 89 E->A: Cold-sensitive. Abolishes FT interaction with BRF1/TDS4. FT {ECO:0000269|PubMed:9312031}. FT MUTAGEN 102 103 RE->VA: Cold-sensitive. No effect on FT interaction with BRF1/TDS4. FT {ECO:0000269|PubMed:9312031}. FT MUTAGEN 135 138 KSVK->ASVA: Temperature-sensitive; cold- FT sensitive. Abolishes interaction with FT BRF1/TDS4. Stabilizes Pol III open FT complex formation. FT MUTAGEN 135 135 K->A: Cold-sensitive. Abolishes FT interaction with BRF1/TDS4. FT {ECO:0000269|PubMed:9312031}. FT MUTAGEN 171 173 DIE->AIA: Cold-sensitive. Abolishes FT interaction with BRF1/TDS4. FT {ECO:0000269|PubMed:9312031}. FT MUTAGEN 171 171 D->H: Cold-sensitive. Abolishes FT interaction with BRF1/TDS4. FT HELIX 173 189 {ECO:0000244|PDB:6EU3}. FT STRAND 196 198 {ECO:0000244|PDB:6EU3}. FT HELIX 202 208 {ECO:0000244|PDB:6EU3}. FT HELIX 220 226 {ECO:0000244|PDB:6EU3}. FT STRAND 231 233 {ECO:0000244|PDB:6EU3}. FT HELIX 240 247 {ECO:0000244|PDB:6EU3}. FT STRAND 249 252 {ECO:0000244|PDB:6EU3}. FT HELIX 257 259 {ECO:0000244|PDB:6EU3}. FT HELIX 266 270 {ECO:0000244|PDB:6EU3}. FT STRAND 300 302 {ECO:0000244|PDB:6EU1}. FT STRAND 303 309 {ECO:0000244|PDB:6EU3}. FT STRAND 311 313 {ECO:0000244|PDB:6EU3}. SQ SEQUENCE 317 AA; 36135 MW; BDE5CD6FD08BDA7F CRC64; MSGMIENGLQ LSDNAKTLHS QMMSKGIGAL FTQQELQKQM GIGSLTDLMS IVQELLDKNL IKLVKQNDEL KFQGVLESEA QKKATMSAEE ALVYSYIEAS GREGIWSKTI KARTNLHQHV VLKCLKSLES QRYVKSVKSV KFPTRKIYML YSLQPSVDIT GGPWFTDGEL DIEFINSLLT IVWRFISENT FPNGFKNFEN GPKKNVFYAP NVKNYSTTQE ILEFITAAQV ANVELTPSNI RSLCEVLVYD DKLEKVTHDC YRVTLESILQ MNQGEGEPEA GNKALEDEEE FSIFNYFKMF PASKHDKEVV YFDEWTI //