eF-site ID 5fja-ABCDEFGHIJKLMNOPQ PDB Code 5fja Chain A, B, C, D, E, F, G, H, I, J, K, L, M, N, O, P, Q Title Cryo-EM structure of yeast RNA polymerase III at 4.7 A Classification TRANSCRIPTION Compound DNA-DIRECTED RNA POLYMERASE III SUBUNIT RPC1 Source ORGANISM_COMMON: BAKER'S YEAST; ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE; Sequence A:  KEVVVSETPKRIKGLEFSALSAADIVAQSEVEVSTRDLFD LEKDRAPKANGALDPKMGVSSSSLECATCHGNLASCHGHF GHLKLALPVFHIGYFKATIQILQGICKNCSAILLSETDKR QFLHELRRPGVDNLRRMGILKKILDQCKKQRRCLHCGALN GVVKKAAALKIIHDTFRWVGKKSAPEKDIWVGEWKEVLAH NPELERYVKRCMDDLNPLKTLNLFKQIKSADCELLGIDAT VPSGRPETYIWRYLPAPPVCIRPSVMMQDSPASNEDDLTV KLTEIVWTSSLIKAGLDKGISINNMMEHWDYLQLTVAMYI NKPIRGFCQRLKGKQGRFRGNLSGKRVDFSGRTVISPDPN LSIDEVAVPDRVAKVLTYPEKVTRYNRHKLQELIVNGPNV HPGANYLLKRNEDARRNLRYGDRMKLAKNLQIGDVVERHL EDGDVVLFNRQPSLHRLSILSHYAKIRPWRTFRLNECVCT PYNADFDGDEMNLHVPQTEEARAEAINLMGVKNNLLTPKS GEPIIAATQDFITGSYLISHKDSFYDRATLTQLLSMMSDG IEHFDIPPPAIMKPYYLWTGKQVFSLLIKPNHNSPVVINL DAKNKVFVPPKSKSLPNEMSQNDGFVIIRGSQILSGVMDK SVLGDGKKHSVFYTILRDYGPQEAANAMNRMAKLCARFLG NRGFSIGINDVTPADDLKQKKEELVEIAYHKCDELITLFN KGELETQPGCNEEQTLEAKIGGLLSKVREEVGDVCINELD NWNAPLIMATCGSKGSTLNVSQMVAVVGQQIISGNRVPDG FQDRSLPHFPKNSKTPQSKGFVRNSFFSGLSPPEFLFHAI SGREGLVDTAVKTAETGYMSRRLMKSLEDLSCQYDNTVRT SANGIVQFTYGGDGLDPLEMEGNAQPVNFNRSWDHAYNIT FNNQDKGLLPYAIMETANEILGPLEERLVRYDNSGCLVKR EDLNKAEYVDQYDAERDFYHSLREYINGKATALANLRKSR GMLGLLEPPAKELQGIDPDETVPDNVKTSVSQLYRISEKS VRKFLEIALFKYRKARLEPGTAIGAIGAQSIGEPMNVTLG VPRIKEIINASKVISTPIINAVLVNDNDERAARVVKGRVE KTLLSDVAFYVQDVYKDNLSFIQVRIDLGTIDKLQLELTI EDIAVAITRASKLKIQASDVNIIGKDRIAINVFPSENDVF YRMQQLRRALPDVVVKGLPDISRAVINIRDDGKRELLVEG YGLRDVMCTDGVIGSRTTTNHVLEVFSVLGIEAARYSIIR EINYTMSNHGMSVDPRHIQLLGDVMTYKGEVLGITRFGLS KMRDSVLQLASFEKTTDHLFDAAFYMKKDAVEGVSECIIL GQTMSIGTGSFKVVKGTNISEKDLVPKRCLFESLSNEAAL KAN B:  DEINTAQDKWHLLPAFLKVKGLVKQHLDSFNYFVDTDLKK IIKANQLILSDVDPEFYLKYVDIRVGKKSSSSTKDYLTPP HECRLRDMTYSAPIYVDIEYTRGRNIIMHKDVEIGRMPIM LRSNKCILYDADESKMAKLNECPLDPGGYFIVNGTEKVIL VQEQLSKNRIIVEADEKKGIVQASVTSSTHERKSKTYVIT KNGKIYLKHNSIAEEIPIAIVLKACGILSDLEIMQLVCGN DSSYQDIFAVNLEESSKLDIYTQQQALEYIGAKVKTMRRQ KLTILQEGIEAIATTVIAHLTVEALDFREKALYIAMMTRR VVMAMYNPKMIDDRDYVGNKRLELAGQLISLLFEDLFKKF NNDFKLSIDKVLKKPNRAMEYDALLSINVHSNNITSGLNR AISTGNWSLKRFKMERAGVTHVLSRLSYISALGMMTRISS QFEKSRKVSGPRALQPSQFGMLCTADTPEGEACGLVKNLA LMTHITTDDEEEPIKKLCYVLGVEDITLIDSASLHLNYGV YLNGTLIGSIRFPTKFVTQFRHLRRTGKVSEFISIYSNSH QMAVHIATDGGRICRPLIIVSDGQSRVKDIHLRKLLDGEL DFDDFLKLGLVEYLDVNEENDSYIALYEKDIVPSMTHLEI EPFTILGAVAGLIPYPHHNQSPRNTYQCAMGKQAIGAIAY NQFKRIDTLLYLMTYPQQPMVKTKTIELIDYDKLPAGQNA TVAVMSYSGYDIEDALVLNKSSIDRGFGRCETRRKTTTVL KRYANHTQDIIGGMRVDENGDPIWQHQSLGPDGLGEVGMK VQSGQIYINKSVPTNSADAPNPNNVNVQTQYREAPVIYRG PEPSHIDQVMMSVSDNDQALIKVLLRQNRRPELGDKFSSR HGQKGVCGIIVKQEDMPFNDQGIVPDIIMNPHGFPSRMTV GKMIELISGKAGVLNGTLEYGTCFGGSKLEDMSKILVDQG FNYSGKDMLYSGITGECLQAYIFFGPIYYQKLKHMVLDKM HARARGPRAVLTRQPTEGRSRDGGLRLGEMERDCVIAYGA SQLLLERLMISSDAFEVDVCDKCGLMGYSGWCTTCKSAEN IIKMTIPYAAKLLFQELLSMNIAPRLRLEDIFQQ C:  MSNIVGIEYNRVTNTTSTDFPGFSKDAENEWNVEKFKKDF EVNISSLDAREANFDLINIDTSIANAFRRIMISEVPSVAA EYVYFFNNTSVIQDEVLAHRIGLVPLKVDPDMLTWVDSNL PDDEKFTDENTIVLSLNVKCTRNPDAPKGSTDPKELYNNA HVYARDLKFEPQGRQSTTFADCPVVPADPDILLAKLRPGQ EISLKAHCILGIGGDHAKFSPVSTASYRLLPQINILQPIK GESARRFQKCFPPGVIGIDEGSDEAYVKDARKDTVSREVL RYEEFADKVKLGRVRNHFIFNVESAGAMTPEEIFFKSVRI LKNKAEYLKNCPITQ D:  MKVLEERNAFLSDYEVLKFLTDLEKKHLWDQKSLAPELQG ITRNVVNYLSINKNFMSDESFAELMTKLNSFKLFKAEKLQ IVNQLPANMVHLYSIVEECDARFDEKTIEEMLEIISGYA E:  MDQENERNISRLWRAFRTVKEMVKDRGYFITQEEVELPLE DFKAKYCDSMGRPQRKMMSFQANPTEESISKFPDMGSLWV EFCDEPSVGVKTMKTFVIHIQEKNFQTGIFVYQNNITPSA MKLVPSIPPATIETFNEAALVVNITHHELVPKHIRLSSDE KRELLKRYRLKESQLPRIQRADPVALYLGLKRGEVVKIIR KSETSGRYASYRICM F:  EKAIPKDQRATTPYMTKYERARILGTRALQISMNAPVFVD LEGETDPLRIAMKELAEKKIPLVIRRYLPDGSFEDWSVEE LIV G:  FILSKIADLVRIPPDQFHRDTISAITHQLNNKFANKIIPN VGLCITIYDLLTVEEGQLKPGDGSSYINVTFRAVVFKPFL GEIVTGWISKCTAEGIKVSLLGIFDDIFIPQNMLFEGCYY TPEESAWIWPKLYFDVNEKIRFRIEREVFVDVKPKSPKEK PPAYALLGSCQTDGMGLVSWWE H:  MSNTLFDDIFQVSEVDPGRYNKVCRIEAASTTQDQCKLTL DINVELFPVAAQDSLTVTIASSLNLEDSATRSWRPPQAGD RSLADDYDYVMYGTAYKFEEVSKDLIAVYYSFGGLLMRLE GNYRNLNNLKQENAYLLIRR I:  MLSFCPSCNNMLLITSGDSGVYTLACRSCPYEFPIEGIEI YDNVDQTKTQCPNYDTCGGESAYFFQLQIRSADEPMTTFY KCVNCGHRWKEN J:  MIVPVRCFSCGKVVGDKWESYLNLLQEDELDEGTALSRLG LKRYCCRRMILTHVDLIEKFLRYNPLE K:  PDREKIKLLTQATSEDGTSASFQIVEEDHTLGNALRYVIM KNPDVEFCGYSIPHPSENLLNIRIQTYGETTAVDALQKGL KDLMDLCDVVESKFTEKIKSM L:  TLKYICAECSSKLSLSRTDAVRCKDCGHRILLKARTKRLV QFEAR M:  IEEFPLKISGEEESLHVFQYANRPRLVGRKPAEHPFISAA RYKPKSHLWEIDIPLDEQAFYNKDKAESEWNGVNVQTLKG VGVENNGQYAAFVKDMQVYLVPIERVAQLKPFFKYIDDAN VTRKQENRLTGSLLAHKVADEEANIELTWAEGTFEQFKDT IVKE N:  KEAAAELELLNADHQHILRKLKKMNNKPERFMVFQLPTRL PAFERPAVGSIRVHKSGKLSVKIGNVVMDIGKGAETTFLQ DVIALSIADDASSAELLGRVDGKIVVTPQI O:  VMTISSLEQRTLNPDLFLYKELVKAHLGERAASVIGMLVA LGRLSVRELVEKIDGMDVDSVKTTLVSLTQLRCVKYLQET AISGKKTTYYYYNEEGIHILLYSGLIIDEIITQMRVNDEE EHKQLVAEIVQNVISLGSLTVEDYLSSVTSDSMKYTISSL FVQLCEMGYLIQISKLHYTPIEDLWQFLYEKHYKNIPRNS PLSDLKKRSQAKMNAKTDFAKIINKPNELSQILTVDPKTS LRIVKPTVSLTINLDRFMKGRRSKQLINLAKTRVGSVTAQ VYKIALRLTEQKSPKIRDPLTQTGLLQDLEEAKSFQDEAE LVEEKTPGLTFNAIDLARHLPSASLINSHLKILASSNFPF LNETKPGVYYVPYSKLMPVLKSSVYEYVIASTLGPSAMRL SRCIRDNKLVSEKIINSTALMKEKDIRSTLASLIRYNSVE IQEVPRTADRSASRAVFLFRCKETHSYNFMRQNLEWNMAN LLFKKEKLKQENSTLLKKANRDDLLPSELNQLKMVNEREL NVFARLSRLLSLWEVFQMA P:  DIEFINSLLTIVWRFISENYSTTQEILEFITAAQVANVEL TPSNIRSLCEVLVYDDKLEKVTHDCYRVTLESILQMSKHD KEVVYFDEW Q:  PINGPITNKERSLAVKYINFGKTVKDGPXXXXXXXXXXXX XXXXXXX Description (1)  DNA-DIRECTED RNA POLYMERASE III SUBUNIT RPC1 (E.C.2.7.7.6), DNA-DIRECTED RNA POLYMERASE III SUBUNIT RPC2 (E.C.2.7.7.6), DNA-DIRECTED RNA POLYMERASES I AND III SUBUNIT RPAC1, DNA-DIRECTED RNA POLYMERASE III SUBUNIT RPC9, DNA-DIRECTED RNA POLYMERASES I, II, AND III SUBUNIT RPABC 1, DNA-DIRECTED RNA POLYMERASES I, II, AND III SUBUNIT RPABC 2, DNA-DIRECTED RNA POLYMERASE III SUBUNIT RPC8, DNA-DIRECTED RNA POLYMERASES I, II, AND III SUBUNIT RPABC 3, DNA-DIRECTED RNA POLYMERASE III SUBUNIT RPC10, DNA-DIRECTED RNA POLYMERASES I, II, AND III SUBUNIT RPABC 5, DNA-DIRECTED RNA POLYMERASES I AND III SUBUNIT RPAC2, DNA-DIRECTED RNA POLYMERASES I, II, AND III SUBUNIT RPABC 4, DNA-DIRECTED RNA POLYMERASE III SUBUNIT RPC5, DNA-DIRECTED RNA POLYMERASE III SUBUNIT RPC4, DNA-DIRECTED RNA POLYMERASE III SUBUNIT RPC3, DNA-DIRECTED RNA POLYMERASE III SUBUNIT RPC6, DNA-DIRECTED RNA POLYMERASE III SUBUNIT RPC7 Functional site 1) chain A residue 67 type sequence C description BINDING SITE FOR RESIDUE ZN A 2000 source : AC1 2) chain A residue 69 type sequence T description BINDING SITE FOR RESIDUE ZN A 2000 source : AC1 3) chain A residue 70 type sequence C description BINDING SITE FOR RESIDUE ZN A 2000 source : AC1 4) chain A residue 77 type sequence C description BINDING SITE FOR RESIDUE ZN A 2000 source : AC1 5) chain A residue 80 type sequence H description BINDING SITE FOR RESIDUE ZN A 2000 source : AC1 6) chain A residue 107 type sequence C description BINDING SITE FOR RESIDUE ZN A 2001 source : AC2 7) chain A residue 109 type sequence N description BINDING SITE FOR RESIDUE ZN A 2001 source : AC2 8) chain A residue 110 type sequence C description BINDING SITE FOR RESIDUE ZN A 2001 source : AC2 9) chain A residue 154 type sequence C description BINDING SITE FOR RESIDUE ZN A 2001 source : AC2 10) chain A residue 156 type sequence H description BINDING SITE FOR RESIDUE ZN A 2001 source : AC2 11) chain A residue 157 type sequence C description BINDING SITE FOR RESIDUE ZN A 2001 source : AC2 12) chain B residue 1095 type sequence C description BINDING SITE FOR RESIDUE ZN B 2000 source : AC3 13) chain B residue 1097 type sequence K description BINDING SITE FOR RESIDUE ZN B 2000 source : AC3 14) chain B residue 1098 type sequence C description BINDING SITE FOR RESIDUE ZN B 2000 source : AC3 15) chain B residue 1107 type sequence C description BINDING SITE FOR RESIDUE ZN B 2000 source : AC3 16) chain B residue 1110 type sequence C description BINDING SITE FOR RESIDUE ZN B 2000 source : AC3 17) chain I residue 5 type sequence C description BINDING SITE FOR RESIDUE ZN I 2000 source : AC4 18) chain I residue 8 type sequence C description BINDING SITE FOR RESIDUE ZN I 2000 source : AC4 19) chain I residue 26 type sequence C description BINDING SITE FOR RESIDUE ZN I 2000 source : AC4 20) chain I residue 29 type sequence C description BINDING SITE FOR RESIDUE ZN I 2000 source : AC4 21) chain J residue 7 type sequence C description BINDING SITE FOR RESIDUE ZN J 2000 source : AC5 22) chain J residue 10 type sequence C description BINDING SITE FOR RESIDUE ZN J 2000 source : AC5 23) chain J residue 45 type sequence C description BINDING SITE FOR RESIDUE ZN J 2000 source : AC5 24) chain J residue 46 type sequence C description BINDING SITE FOR RESIDUE ZN J 2000 source : AC5 25) chain L residue 31 type sequence C description BINDING SITE FOR RESIDUE ZN L 2000 source : AC6 26) chain L residue 34 type sequence C description BINDING SITE FOR RESIDUE ZN L 2000 source : AC6 27) chain L residue 48 type sequence C description BINDING SITE FOR RESIDUE ZN L 2000 source : AC6 28) chain L residue 51 type sequence C description BINDING SITE FOR RESIDUE ZN L 2000 source : AC6 29) chain C residue 65-105 type prosite sequence NAFRRIMISEVPSVAAEYVYFFNNTSVIQDEVLAHRIGLV P description RNA_POL_D_30KD RNA polymerases D / 30 to 40 Kd subunits signature. NAFRRimisevpsvAaeyVyffnNtSviqDEvLAhRIGLVP source prosite : PS00446 30) chain I residue 4-29 type prosite sequence FCPSCNNMLLITSGDSGVYTLACRSC description RNA_POL_M_15KD RNA polymerases M / 15 Kd subunits signature. FCPSCNNMLlitsgdsgvytla.CrsC source prosite : PS01030 31) chain E residue 147-160 type prosite sequence HELVPKHIRLSSDE description RNA_POL_H_23KD RNA polymerases H / 23 Kd subunits signature. HELVPKHirLssDE source prosite : PS01110 32) chain F residue 86-100 type prosite sequence TKYERARILGTRALQ description RNA_POL_K_14KD RNA polymerases K / 14 to 18 Kd subunits signature. TkYErARiLGtRAlQ source prosite : PS01111 33) chain J residue 2-11 type prosite sequence IVPVRCFSCG description RNA_POL_N_8KD RNA polymerases N / 8 Kd subunits signature. IVPVrCFSCG source prosite : PS01112 34) chain K residue 65-96 type prosite sequence IVEEDHTLGNALRYVIMKNPDVEFCGYSIPHP description RNA_POL_L_13KD RNA polymerases L / 13 to 16 Kd subunits signature. IveEdHTLgNaLryvImknpdVefcgYsipHP source prosite : PS01154 35) chain B residue 909-921 type prosite sequence GDKFSSRHGQKGV description RNA_POL_BETA RNA polymerases beta chain signature. GdKFSSrHGQKGV source prosite : PS01166 36) chain A residue 515 type MOD_RES sequence D description Phosphothreonine => ECO:0007744|PubMed:18407956 source Swiss-Prot : SWS_FT_FI1 37) chain J residue 45 type MOD_RES sequence C description Phosphothreonine => ECO:0007744|PubMed:18407956 source Swiss-Prot : SWS_FT_FI1 38) chain J residue 46 type MOD_RES sequence C description Phosphothreonine => ECO:0007744|PubMed:18407956 source Swiss-Prot : SWS_FT_FI1 39) chain A residue 107 type MOD_RES sequence C description Phosphothreonine => ECO:0007744|PubMed:18407956 source Swiss-Prot : SWS_FT_FI1 40) chain A residue 110 type MOD_RES sequence C description Phosphothreonine => ECO:0007744|PubMed:18407956 source Swiss-Prot : SWS_FT_FI1 41) chain A residue 154 type MOD_RES sequence C description Phosphothreonine => ECO:0007744|PubMed:18407956 source Swiss-Prot : SWS_FT_FI1 42) chain A residue 511 type MOD_RES sequence D description Phosphothreonine => ECO:0007744|PubMed:18407956 source Swiss-Prot : SWS_FT_FI1 43) chain A residue 513 type MOD_RES sequence D description Phosphothreonine => ECO:0007744|PubMed:18407956 source Swiss-Prot : SWS_FT_FI1 44) chain L residue 48 type MOD_RES sequence C description Phosphoserine => ECO:0007744|PubMed:19779198 source Swiss-Prot : SWS_FT_FI2 45) chain L residue 51 type MOD_RES sequence C description Phosphoserine => ECO:0007744|PubMed:19779198 source Swiss-Prot : SWS_FT_FI2 46) chain I residue 8 type MOD_RES sequence C description Phosphoserine => ECO:0007744|PubMed:17287358 source Swiss-Prot : SWS_FT_FI3 47) chain I residue 26 type MOD_RES sequence C description Phosphoserine => ECO:0007744|PubMed:17287358 source Swiss-Prot : SWS_FT_FI3 48) chain I residue 29 type MOD_RES sequence C description Phosphoserine => ECO:0007744|PubMed:17287358 source Swiss-Prot : SWS_FT_FI3 49) chain I residue 100 type MOD_RES sequence C description Phosphothreonine => ECO:0007744|PubMed:17287358, ECO:0007744|PubMed:17330950 source Swiss-Prot : SWS_FT_FI4 50) chain I residue 103 type MOD_RES sequence C description Phosphothreonine => ECO:0007744|PubMed:17287358, ECO:0007744|PubMed:17330950 source Swiss-Prot : SWS_FT_FI4

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