eF-site ID 6eu2-ABCDEFGHIJKLMNOPQ PDB Code 6eu2 Chain A, B, C, D, E, F, G, H, I, J, K, L, M, N, O, P, Q Title Apo RNA Polymerase III - open conformation (oPOL3) Classification TRANSCRIPTION Compound DNA-directed RNA polymerase III subunit RPC1 Source ORGANISM_COMMON: Baker's yeast; ORGANISM_SCIENTIFIC: Saccharomyces cerevisiae (strain ATCC 204508 / S288c); Sequence A:  KEVVVSETPKRIKGLEFSALSAADIVAQSEVEVSTRDLFD LEKDRAPKANGALDPKMGVSSSSLECATCHGNLASCHGHF GHLKLALPVFHIGYFKATIQILQGICKNCSAILLSETDKR QFLHELRRPGVDNLRRMGILKKILDQCKKQRRCLHCGALN GVVKKAAALKIIHDTFRWVGKKSAPEKDIWVGEWKEVLAH NPELERYVKRCMDDLNPLKTLNLFKQIKSADCELLGIDAT VPSGRPETYIWRYLPAPPVCIRPSVMMQDSPASNEDDLTV KLTEIVWTSSLIKAGLDKGISINNMMEHWDYLQLTVAMYI NSGNLSGKRVDFSGRTVISPDPNLSIDEVAVPDRVAKVLT YPEKVTRYNRHKLQELIVNGPNVHPGANYLLKRNEDARRN LRYGDRMKLAKNLQIGDVVERHLEDGDVVLFNRQPSLHRL SILSHYAKIRPWRTFRLNECVCTPYNADFDGDEMNLHVPQ TEEARAEAINLMGVKNNLLTPKSGEPIIAATQDFITGSYL ISHKDSFYDRATLTQLLSMMSDGIEHFDIPPPAIMKPYYL WTGKQVFSLLIKPNHNSPVVINLDAKNKVFVPPKSKSLPN EMSQNDGFVIIRGSQILSGVMDKSVLGDGKKHSVFYTILR DYGPQEAANAMNRMAKLCARFLGNRGFSIGINDVTPADDL KQKKEELVEIAYHKCDELITLFNKGELETQPGCNEEQTLE AKIGGLLSKVREEVGDVCINELDNWNAPLIMATCGSKGST LNVSQMVAVVGQQIISGNRVPDGFQDRSLPHFPKNSKTPQ SKGFVRNSFFSGLSPPEFLFHAISGREGLVDTAVKTAETG YMSRRLMKSLEDLSCQYDNTVRTSANGIVQFTYGGDGLDP LEMEGNAQPVNFNRSWDHAYNITFNNQDKGLLPYAIMETA NEILGPLEERLVRYDNSGCLVKREDLNKAEYVDQYDAERD FYHSLREYINGKATALANLRKSRGMLGLLEPPAKELQGID PDETVPDNVKTSVSQLYRISEKSVRKFLEIALFKYRKARL EPGTAIGAIGAQSIGEPGTQMTLKTFHFAGVASMNVTLGV PRIKEIINASKVISTPIINAVLVNDNDERAARVVKGRVEK TLLSDVAFYVQDVYKDNLSFIQVRIDLGTIDKLQLELTIE DIAVAITRASKLKIQASDVNIIGKDRIAINVFPSENDVFY RMQQLRRALPDVVVKGLPDISRAVINIRDDGKRELLVEGY GLRDVMCTDGVIGSRTTTNHVLEVFSVLGIEAARYSIIRE INYTMSNHGMSVDPRHIQLLGDVMTYKGEVLGITRFGLSK MRDSVLQLASFEKTTDHLFDAAFYMKKDAVEGVSECIILG QTMSIGTGSFKVVKGTNISEKDLVPKRCLFESLSNEAALK AN 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 TPEESAWIWPKLYFDVNEKIRFRIEREVFVDVKPKSPKER ELEERAQEKPPAYALLGSCQTDGMGLVSWWE H:  MSNTLFDDIFQVSEVDPGRYNKVCRIEAASTTQDQCKLTL DINVELFPVAAQDSLTVTIASSLNLEDSATRSWRPPQAGD RSLADDYDYVMYGTAYKFEEVSKDLIAVYYSFGGLLMRLE GNYRNLNNLKQENAYLLIRR I:  MLSFCPSCNNMLLITSGDSGVYTLACRSCPYEFPIEGIEI YD J:  MIVPVRCFSCGKVVGDKWESYLNLLQEDELDEGTALSRLG LKRYCCRRMILTHVDLIEKFLRYNPLEK K:  PDREKIKLLTQATSEDGTSASFQIVEEDHTLGNALRYVIM KNPDVEFCGYSIPHPSENLLNIRIQTYGETTAVDALQKGL KDLMDLCDVVESKFTEKIKSM L:  TLKYICAECSSKLSLSRTDAVRCKDCGHRILLKARTKRLV QFEAR M:  IEEFPLKISGEEESLHVFQYANRPRLVGRKPAEHPFISAA RYKPKSHLWEIDIPLDEQAFYNKDKAESEWNGVNVQTLKG VGVENNGQYAAFVKDMQVYLVPIERVAQLKPFFKYIDDAN VTRKQEQNRLTGSLLAHKVADEEANIELTWAEGTFEQFKD TIVKE N:  KEAAAELELLNADHQHILRKLKKMNNKPERFMVFQLPTRL PAVGSIRVHKSGKLSVKIGNVVMDIGKGAETTFLQDVIAL SIADDASSAELLGRVDGKIVVTPQI O:  VMTISSLEQRTLNPDLFLYKELVKAHLGERAASVIGMLVA LGRLSVRELVEKIDGMDVDSVKTTLVSLTQLRCVKYLQET AISGKKTTYYYYNEEGIHILLYSGLIIDEIITQMRVNDEE EHKQLVAEIVQNVISLGSLTVEDYLSSVTSDSMKYTISSL FVQLCEMGYLIQISKLHYTPIEDLWQFLYEKHYKNIPRNS PLSDLKKRSQAKMNAKTDFAKIINKPNELSQILTVDPKTS LRIVKPTVSLTINLDRFMKGRRSKQLINLAKTRVGSVTAQ VYKIALRLTEQKSPKIRDPLTQTGLLQDLEEAKSFQDEAE LVEEKTPGLTFNAIDLARHLASLINSHLKILASSNFPFLN ETKPGVYYVPYSKLMPVLKSSVYEYVIASTLGPSAMRLSR CIRDNKLVSEKIINSTALMKEKDIRSTLASLIRYNSVEIQ EVPRTADRSASRAVFLFRCKETHSYNFMRQNLEWNMANLL FKKEKLKQENSTLLKKANRDDLLPSELNQLKMVNERELNV FARLSRLLSLWEVFQMA P:  DIEFINSLLTIVWRFISENTFPNGFKNFENGPKKNVFYAP NVKNYSTTQEILEFITAAQVANVELTPSNIRSLCEVLVYD DKLEKVTHDCYRVTLESILQMFNYFKMFPASKHDKEVVYF DEW Q:  EFPSIPLPINGPITNKERSLAVKYINFGKTVKDGPFYTGS Description 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 110 type sequence C description binding site for residue ZN A 2001 source : AC2 8) chain A residue 154 type sequence C description binding site for residue ZN A 2001 source : AC2 9) chain A residue 157 type sequence C description binding site for residue ZN A 2001 source : AC2 10) chain A residue 511 type sequence D description binding site for residue MG A 2002 source : AC3 11) chain A residue 513 type sequence D description binding site for residue MG A 2002 source : AC3 12) chain A residue 515 type sequence D description binding site for residue MG A 2002 source : AC3 13) chain B residue 1095 type sequence C description binding site for residue ZN B 1201 source : AC4 14) chain B residue 1097 type sequence K description binding site for residue ZN B 1201 source : AC4 15) chain B residue 1098 type sequence C description binding site for residue ZN B 1201 source : AC4 16) chain B residue 1107 type sequence C description binding site for residue ZN B 1201 source : AC4 17) chain I residue 5 type sequence C description binding site for residue ZN I 201 source : AC5 18) chain I residue 8 type sequence C description binding site for residue ZN I 201 source : AC5 19) chain I residue 29 type sequence C description binding site for residue ZN I 201 source : AC5 20) chain J residue 7 type sequence C description binding site for residue ZN J 101 source : AC6 21) chain J residue 10 type sequence C description binding site for residue ZN J 101 source : AC6 22) chain J residue 43 type sequence R description binding site for residue ZN J 101 source : AC6 23) chain J residue 45 type sequence C description binding site for residue ZN J 101 source : AC6 24) chain J residue 46 type sequence C description binding site for residue ZN J 101 source : AC6 25) chain L residue 31 type sequence C description binding site for residue ZN L 101 source : AC7 26) chain L residue 34 type sequence C description binding site for residue ZN L 101 source : AC7 27) chain L residue 48 type sequence C description binding site for residue ZN L 101 source : AC7 28) chain L residue 51 type sequence C description binding site for residue ZN L 101 source : AC7 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 Phosphoserine => ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198 source Swiss-Prot : SWS_FT_FI1 37) chain J residue 45 type MOD_RES sequence C description Phosphoserine => ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198 source Swiss-Prot : SWS_FT_FI1 38) chain J residue 46 type MOD_RES sequence C description Phosphoserine => ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198 source Swiss-Prot : SWS_FT_FI1 39) chain A residue 107 type MOD_RES sequence C description Phosphoserine => ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198 source Swiss-Prot : SWS_FT_FI1 40) chain A residue 110 type MOD_RES sequence C description Phosphoserine => ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198 source Swiss-Prot : SWS_FT_FI1 41) chain A residue 154 type MOD_RES sequence C description Phosphoserine => ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198 source Swiss-Prot : SWS_FT_FI1 42) chain A residue 511 type MOD_RES sequence D description Phosphoserine => ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198 source Swiss-Prot : SWS_FT_FI1 43) chain A residue 513 type MOD_RES sequence D description Phosphoserine => ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198 source Swiss-Prot : SWS_FT_FI1 44) chain L residue 48 type MOD_RES sequence C description Phosphoserine => ECO:0007744|PubMed:17330950, 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:17330950, 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, ECO:0007744|PubMed:17330950, ECO:0007744|PubMed:18407956 source Swiss-Prot : SWS_FT_FI3 47) chain I residue 26 type MOD_RES sequence C description Phosphoserine => ECO:0007744|PubMed:17287358, ECO:0007744|PubMed:17330950, ECO:0007744|PubMed:18407956 source Swiss-Prot : SWS_FT_FI3 48) chain I residue 29 type MOD_RES sequence C description Phosphoserine => ECO:0007744|PubMed:17287358, ECO:0007744|PubMed:17330950, ECO:0007744|PubMed:18407956 source Swiss-Prot : SWS_FT_FI3

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