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 29-SEP-2021, entry version 173. 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; Saccharomycetes; OC 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 encoded by RT 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 Saccharomyces RT 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 the RT centromere on the Saccharomyces cerevisiae chromosome XIV right 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., Doignon F., RA Domdey H., Dubois E., Fiedler T.A., Fleig U., Floeth M., Fritz C., RA Gaillardin C., Garcia-Cantalejo J.M., Glansdorff N., Goffeau A., RA Gueldener U., Herbert C.J., Heumann K., Heuss-Neitzel D., Hilbert H., RA Hinni K., Iraqui Houssaini I., Jacquet M., Jimenez A., Jonniaux J.-L., RA Karpfinger-Hartl L., Lanfranchi G., Lepingle A., Levesque H., Lyck R., RA Maftahi M., Mallet L., Maurer C.T.C., Messenguy F., Mewes H.-W., Moestl D., RA Nasr F., Nicaud J.-M., Niedenthal R.K., Pandolfo D., Pierard A., RA Piravandi E., Planta R.J., Pohl T.M., Purnelle B., Rebischung C., RA Remacha M.A., Revuelta J.L., Rinke M., Saiz J.E., Sartorello F., RA Scherens B., Sen-Gupta M., Soler-Mira A., Urbanus J.H.M., Valle G., RA Van Dyck L., Verhasselt P., Vierendeels F., Vissers S., Voet M., RA Volckaert G., Wach A., Wambutt R., Wedler H., Zollner A., Hani J.; RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV and its RT 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., Cherry J.M.; RT "The reference genome sequence of Saccharomyces cerevisiae: Then and 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 70- RT 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., Lefebvre O., RA 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 of CC DNA into RNA using the four ribonucleoside triphosphates as substrates. CC Specific peripheric component of RNA polymerase III which synthesizes CC small RNAs, such as 5S rRNA and tRNAs. Involved in recruitment of Pol CC III to the preinitiation complex. Involved in the configuration of an CC initiation-competent form of RNA polymerase. CC {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 P32910; P41910: MAF1; NbExp=3; IntAct=EBI-15835, EBI-10375; CC P32910; P20436: RPB8; NbExp=3; IntAct=EBI-15835, EBI-15794; CC P32910; P47076: RPC17; NbExp=2; IntAct=EBI-15835, EBI-25782; CC P32910; 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 PDB; 6TUT; EM; 3.25 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 PDBsum; 6TUT; -. DR SMR; P32910; -. DR BioGRID; 35829; 476. 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; YNR003C. DR GeneID; 855737; -. DR KEGG; sce:YNR003C; -. DR SGD; S000005286; RPC34. DR VEuPathDB; FungiDB:YNR003C; -. DR eggNOG; KOG3233; Eukaryota. DR GeneTree; ENSGT00390000009679; -. DR HOGENOM; CLU_033661_0_1_1; -. DR InParanoid; P32910; -. DR OMA; AVYFDEW; -. 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 RNAct; P32910; protein. 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: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; Direct protein sequencing; DNA-directed RNA polymerase; KW Nucleus; Reference proteome; Transcription. FT CHAIN 1..317 FT /note="DNA-directed RNA polymerase III subunit RPC6" FT /id="PRO_0000073977" FT MUTAGEN 89 FT /note="E->A: Cold-sensitive. Abolishes interaction with FT BRF1/TDS4." FT /evidence="ECO:0000269|PubMed:9312031" FT MUTAGEN 102..103 FT /note="RE->VA: Cold-sensitive. No effect on interaction FT with BRF1/TDS4." FT /evidence="ECO:0000269|PubMed:9312031" FT MUTAGEN 135..138 FT /note="KSVK->ASVA: Temperature-sensitive; cold-sensitive. FT Abolishes interaction with BRF1/TDS4. Stabilizes Pol III FT open complex formation." FT MUTAGEN 135 FT /note="K->A: Cold-sensitive. Abolishes interaction with FT BRF1/TDS4." FT /evidence="ECO:0000269|PubMed:9312031" FT MUTAGEN 171..173 FT /note="DIE->AIA: Cold-sensitive. Abolishes interaction with FT BRF1/TDS4." FT /evidence="ECO:0000269|PubMed:9312031" FT MUTAGEN 171 FT /note="D->H: Cold-sensitive. Abolishes interaction with FT BRF1/TDS4." FT HELIX 92..100 FT /evidence="ECO:0007829|PDB:6TUT" FT HELIX 110..112 FT /evidence="ECO:0007829|PDB:6TUT" FT HELIX 120..130 FT /evidence="ECO:0007829|PDB:6TUT" FT STRAND 133..137 FT /evidence="ECO:0007829|PDB:6TUT" FT STRAND 140..145 FT /evidence="ECO:0007829|PDB:6TUT" FT STRAND 147..151 FT /evidence="ECO:0007829|PDB:6TUT" FT TURN 171..174 FT /evidence="ECO:0007829|PDB:6EU1" FT HELIX 175..188 FT /evidence="ECO:0007829|PDB:6TUT" FT HELIX 193..195 FT /evidence="ECO:0007829|PDB:6TUT" FT STRAND 196..198 FT /evidence="ECO:0007829|PDB:6EU3" FT HELIX 202..208 FT /evidence="ECO:0007829|PDB:6EU3" FT HELIX 218..227 FT /evidence="ECO:0007829|PDB:6TUT" FT STRAND 231..233 FT /evidence="ECO:0007829|PDB:6TUT" FT STRAND 237..239 FT /evidence="ECO:0007829|PDB:6TUT" FT HELIX 240..243 FT /evidence="ECO:0007829|PDB:6TUT" FT STRAND 244..246 FT /evidence="ECO:0007829|PDB:6TUT" FT TURN 247..251 FT /evidence="ECO:0007829|PDB:6TUT" FT STRAND 252..256 FT /evidence="ECO:0007829|PDB:6TUT" FT TURN 257..259 FT /evidence="ECO:0007829|PDB:6TUT" FT STRAND 260..262 FT /evidence="ECO:0007829|PDB:6TUT" FT HELIX 266..269 FT /evidence="ECO:0007829|PDB:6TUT" FT TURN 270..275 FT /evidence="ECO:0007829|PDB:6EU1" FT STRAND 300..302 FT /evidence="ECO:0007829|PDB:6EU1" FT STRAND 303..309 FT /evidence="ECO:0007829|PDB:6EU3" FT STRAND 311..313 FT /evidence="ECO:0007829|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 //