eF-site ID 5m3m-ABCDEFGHIJKLMN PDB Code 5m3m Chain A, B, C, D, E, F, G, H, I, J, K, L, M, N Title Free monomeric RNA polymerase I at 4.0A resolution Classification TRANSCRIPTION Compound DNA-directed RNA polymerase I subunit RPA190 Source ORGANISM_COMMON: Baker's yeast; ORGANISM_SCIENTIFIC: Saccharomyces cerevisiae (strain ATCC 204508 / S288c); Sequence A:  MDISKPVGSEITSVDFGILTAKEIRNLSAKQITNPTVLDN LGHPVSGGLYDLALGAFLRNLCSTCGLDEKFCPGHQGHIE LPVPCYNPLFFNQLYIYLRASCLFCHHFRLKSVEVHRYAC KLRLLQYGLIDESYKLDEITLSSTLLNELKSKRSEYVDMA IAKALSDGRTTERGSFTATVNDERKKLVHEFHKKLLSRGK CDNCGMFSPKFRKDGFTKIFETALNEKQITNNRVKGFIRQ DSTYILSTEVKNILDTVFRKEQCVLQYVFHSRPNLSRKLV KADSFFMDVLVVPPTRFRLPSKLGEEVHENSQNQLLSKVL TTSLLIRDLNDDLSKLQKDKVSLEDRRVIFSRLMNAFVTI QNDVNAFIDSTKAQGRTSGKVPIPGVKQALEKKEGLFRKH MMGKRVNYAARSVISPDPNIETNEIGVPPVFAVKLTYPEP VTAYNIAELRQAVINGPDKWPGATQIQNEDGSLVSLIGMS VEQRKALANQLLTPSSNVSTHTLNKKVYRHIKNRDVVLMN RQPTLHKASMMGHKVRVLPNEKTLRLHYANTGAYNADFDG DEMNMHFPQNENARAEALNLANTDSQYLTPTSGSPVRGLI QDHISAGVWLTSKDSFFTREQYQQYIYGCIRPEDGHTTRS KIVTLPPTIFKPYPLWTGKQIITTVLLNVTPPDMPGINLI SKNKIKNEYWGKGSLENEVLFKDGALLCGILDKSQYGASK YGIVHSLHEVYGPEVAAKVLSVLGRLFTNYITATAFTCGM DDLRLTAEGNKWRTDILKTSVDTGREAAAEVTNLDKDTPA DDPELLKRLQEILRDNNKSGILDAVTSSKVNAITSQVVSK CVPDGTMKKFPCNSMQAMALSGAKGSNVNVSQIMCLLGQQ ALEGRRVPVMVSGKTLPSFKPYETDAMAGGYVKGRFYSGI KPQEYYFHCMAGREGLIDTAGYLQRCLTKQLEGVHVSYDN SIRDADGTLVQFMYGGDAIDITKESHMTQFEFCLDNYYAL LKKYNPSALIEHLDVESALKYSKKTLKYRKKHSKEPHYKQ SVKYDPVLAKYNPAKYLGSVSENFQDKLESFLDKNSKLFK SSDGVNEKKFRALMQLKYMRSLINPGEAVGIIASQSVGEP STQMTLNTFANVTLGIPRLREIVMTASAAIKTPQMTLPIW NDVSDEQADTFCKSISKVLLSEVIDKVIVTETTAARSYVI HMRFFDNNEYSEEYDVSKEELQNVISNQFIHLLEAAIVKE IKKQKKVQRDRQSAIISHHRFITKYNFDDESGKWCEFKLE LAADTEKLLMVNIVEEICRKSIIRQIPHIDRCVHPEPENG KRVLVTEGVNFQAMWDQEAFIDVDGITSNDVAAVLKTYGV EAARNTIVNEINNVFSRYAISVSFRHLDLIADMMTRQGTY LAFNRQGMETSTSSFMKMSYETTCQFLTKAVLDNEREQLD SPSARIVVGKLNNVGTGSFDVL B:  TADFRTLERESRFINPPKDKSAFPLLQEAVQPHIGSFNAL TEGPDGGLLNLGVKDIGEKVIFDGKPLNSGYLGNKLSVSV EQVSIAKPMSNDGVSSAVERKVYPSESRQRLTSYRGKLLL KLKWSVNNGEENLFEVRDCGGLPVMLQSNRCHLNKMSPYE LVQHKEESDEIGGYFIVNGIEKLIRMLIVQRRNHPMAIIR PSFANRGASYSHYGIQIRSVRPDQTSQTNVLHYLNDGQVT FRFSWRKNEYLVPVVMILKALCHTSDREIFDGIIGNDVKD SFLTDRLELLLRGFKKRYPHLQNRTQVLQYLGDKFRVVFQ ASPDQSDLEVGQEVLDRIVLVHLGKDGSQDKFRMLLFMIR KLYSLVAGECSPDNPDATQHQEVLLGGFLYGMILKEKIDE YLQNIIAQVRMDINRGMAINFKDKRYMSRVLMRVNENIGS KMQYFLSTGNLVSQSGLDLQQVSGYTVVAEKINFYRFISH FRMVHRGSFFAQLKTTTVRKLLPESWGFLCPVHTPDGSPC GLLNHFAHKCRISTQQSDVSRIPSILYSLGVAPASHTFAA GPSLCCVQIDGKIIGWVSHEQGKIIADTLRYWKVEGKTPG LPIDLEIGYVPPSTRGQYPGLYLFGGHSRMLRPVRYLPLD KEDIVGPFEQVYMNIAVTPQEIQNNVHTHVEFTPTNILSI LANLTPFSDFNQSPRNMYQCQMGKQTMGTPGVALCHRSDN KLYRLQTGQTPIVKANLYDDYGMDNFPNGFNAVVAVISYT GYDMDDAMIINKSADERGFGYGTMYKTEKVDLALNRNRGD PITQHFGFGNDEWPKEWLEKLDEDGLPYIGTYVEEGDPIC AYFDDTLNKTKIKTYHSSEPAYIEEVNLIGDESNKFQELQ TVSIKYRIRRTPQIGDKFSSRHGQKGVCSRKWPTIDMPFS ETGIQPDIIINPHAFPSRMTIGMFVESLAGKAGALHGIAQ DSTPWIFNEDDTPADYFGEQLAKAGYNYHGNEPMYSGATG EELRADIYVGVVYYQRLRHMVNDKFQVRSTGPVNSLTMQP VKIRVGEMERDALIGHGTSFLLQDRLLNSSDYTQASVCRE CGSILTTQQSVPRIGSISTVCCRRCSMRFEDAKIFIDDSQ IWEDGQGNKFVGGNETTTVAIPFVLKYLDSELSAMGIRLR YNVEPK C:  WNVEKFKKDFEVNISSLDAREANFDLINIDTSIANAFRRI MISEVPSVAAEYVYFFNNTSVIQDEVLAHRIGLVPLKVDP DMLTWVDSNLPDDEKFTDENTIVLSLNVKCTRNPDAPKGS TDPKELYNNAHVYARDLKFEPQGRQSTTFADCPVVPADPD ILLAKLRPGQEISLKAHCILGIGGDHAKFSPVSTASYRLL PQINILQPIKGESARRFQKCFPPGVIGIDEGSDEAYVKDA RKDTVSREVLRYEEFADKVKLGRVRNHFIFNVESAGAMTP EEIFFKSVRILKNKAEYLKNCPITQ D:  TATTLNTPVVIHATQLPQHVSTDEVLQFLESFIDEKETNL SSSISQLKRIQRDFKGLP E:  ENERNISRLWRAFRTVKEMVKDRGYFITQEEVELPLEDFK AKYCDSMGRPQRKMMSFQANPTEESISKFPDMGSLWVEFC DEPSVGVKTMKTFVIHIQEKNFQTGIFVYQNNITPSAMKL VPSIPPATIETFNEAALVVNITHHELVPKHIRLSSDEKRE LLKRYRLKESQLPRIQRADPVALYLGLKRGEVVKIIRKSE TSGRYASYRICM F:  DFQQHEQIRRKTLKEKAIPKDQRATTPYMTKYERARILGT RALQISMNAPVFVDLEGETDPLRIAMKELAEKKIPLVIRR YLPDGSFEDWSVEELIVD G:  ARFIKKHKKQVTNPIDEKNGTSNCIVRVPIALYVSLAPMY ENPLQGVMKQHLNPLVMKYNNKVGGVVLGYEGLKILDADP LSKEDTSEKLIKITPDTPFGFTWCHVNLYVWQPQVGDVLE GYIFIQSASHIGLLIHDAFNASIKKNNIPVDWTFVHGHWV DSNGEPIDGKLRFTVRNVHTTGRVVSVDGTLI H:  NTLFDDIFQVSEVDPGRYNKVCRIEAASTTQDQCKLTLDI NVELFPVAAQDSLTVTIASSLNSWRPPQAGDRSLADDYDY VMYGTAYKFEEVSKDLIAVYYSFGGLLMRLEGNYRNLNNL KQENAYLLIRR I:  SVVGSLIFCLDCGDLLENPNAVLGSNVECSQCKAIYPKSQ FSNLKVVTTTADDAFPSSLRAKKSVVKTSLKKNELKDGAT IKEKCPQCGNEEMNYHTLATVFYTCTSCGYKFRTNN J:  MIVPVRCFSCGKVVGDKWESYLNLLQEDELDEGTALSRLG LKRYCCRRMILTHVDLIEKFLRYNPLEKR K:  PDREKIKLLTQATSEDGTSASFQIVEEDHTLGNALRYVIM KNPDVEFCGYSIPHPSENLLNIRIQTYGETTAVDALQKGL KDLMDLCDVVESKFTEKIKSM L:  LKYICAECSSKLSLSRTDAVRCKDCGHRILLKARTKRLVQ FEAR M:  SEIEIESVQDQPSVAVGSFFKGFRAPSDTTFDLYKKKKSE KDEFVLHGENERLEYEGYTDSSSQASNQYVVGLFNPEKKS IQLYKAPVLVSKVVSKS N:  SIPDGFKKCKHLKNFPLNKQQQVWLIKFPSNVDISKLKSL PVTTMTIDKHDYKIMDDTDIESSLTQDNLSNMTLLVPSES KESLKIASTAKDNAPLQFDKVFSVSETAKIPAIDYSKVRV PRKDVPKVEGL Description (1)  DNA-directed RNA polymerase I subunit RPA190 (E.C.2.7.7.6), DNA-directed RNA polymerase I subunit RPA135 (E.C.2.7.7.6), DNA-directed RNA polymerases I and III subunit RPAC1, DNA-directed RNA polymerases I, II, and III subunit RPABC1, DNA-directed RNA polymerases I, II, and III subunit RPABC2, DNA-directed RNA polymerases I, II, and III subunit RPABC3, DNA-directed RNA polymerase I subunit RPA12, DNA-directed RNA polymerases I, II, and III subunit RPABC5, DNA-directed RNA polymerases I and III subunit RPAC2, DNA-directed RNA polymerases I, II, and III subunit RPABC4, DNA-directed RNA polymerase I subunit RPA49, DNA-directed RNA polymerase I subunit RPA34, DNA-directed RNA polymerase I subunit RPA14, DNA-directed RNA polymerase I subunit RPA43 Functional site 1) chain A residue 65 type sequence C description binding site for residue ZN A 3001 source : AC1 2) chain A residue 67 type sequence L description binding site for residue ZN A 3001 source : AC1 3) chain A residue 71 type sequence F description binding site for residue ZN A 3001 source : AC1 4) chain A residue 72 type sequence C description binding site for residue ZN A 3001 source : AC1 5) chain A residue 73 type sequence P description binding site for residue ZN A 3001 source : AC1 6) chain A residue 102 type sequence C description binding site for residue ZN A 3002 source : AC2 7) chain A residue 103 type sequence L description binding site for residue ZN A 3002 source : AC2 8) chain A residue 104 type sequence F description binding site for residue ZN A 3002 source : AC2 9) chain A residue 105 type sequence C description binding site for residue ZN A 3002 source : AC2 10) chain A residue 106 type sequence H description binding site for residue ZN A 3002 source : AC2 11) chain B residue 532 type sequence H description binding site for residue SO4 B 1301 source : AC3 12) chain B residue 698 type sequence S description binding site for residue SO4 B 1301 source : AC3 13) chain B residue 699 type sequence I description binding site for residue SO4 B 1301 source : AC3 14) chain B residue 700 type sequence L description binding site for residue SO4 B 1301 source : AC3 15) chain B residue 701 type sequence A description binding site for residue SO4 B 1301 source : AC3 16) chain B residue 1104 type sequence C description binding site for residue ZN B 1302 source : AC4 17) chain B residue 1105 type sequence R description binding site for residue ZN B 1302 source : AC4 18) chain B residue 1106 type sequence E description binding site for residue ZN B 1302 source : AC4 19) chain B residue 1107 type sequence C description binding site for residue ZN B 1302 source : AC4 20) chain B residue 1172 type sequence E description binding site for residue ZN B 1302 source : AC4 21) chain I residue 10 type sequence C description binding site for residue ZN I 3001 source : AC5 22) chain I residue 11 type sequence L description binding site for residue ZN I 3001 source : AC5 23) chain I residue 12 type sequence D description binding site for residue ZN I 3001 source : AC5 24) chain I residue 13 type sequence C description binding site for residue ZN I 3001 source : AC5 25) chain I residue 86 type sequence C description binding site for residue ZN I 3002 source : AC6 26) chain I residue 94 type sequence M description binding site for residue ZN I 3002 source : AC6 27) chain I residue 114 type sequence C description binding site for residue ZN I 3002 source : AC6 28) chain I residue 117 type sequence C description binding site for residue ZN I 3002 source : AC6 29) chain I residue 119 type sequence Y description binding site for residue ZN I 3002 source : AC6 30) chain J residue 7 type sequence C description binding site for residue ZN J 3001 source : AC7 31) chain J residue 10 type sequence C description binding site for residue ZN J 3001 source : AC7 32) chain J residue 45 type sequence C description binding site for residue ZN J 3001 source : AC7 33) chain J residue 46 type sequence C description binding site for residue ZN J 3001 source : AC7 34) chain L residue 31 type sequence C description binding site for residue ZN L 3001 source : AC8 35) chain L residue 34 type sequence C description binding site for residue ZN L 3001 source : AC8 36) chain L residue 48 type sequence C description binding site for residue ZN L 3001 source : AC8 37) chain L residue 51 type sequence C description binding site for residue ZN L 3001 source : AC8 38) 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 39) 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 40) chain B residue 914-926 type prosite sequence GDKFSSRHGQKGV description RNA_POL_BETA RNA polymerases beta chain signature. GdKFSSrHGQKGV source prosite : PS01166 41) 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 42) 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 43) chain I residue 86-121 type prosite sequence CPQCGNEEMNYHTLATVFYTCTSCGYKF description ZF_TFIIS_1 Zinc finger TFIIS-type signature. CpqCgneemnyhtLQLRSaDEGatvfytCts...CgykF source prosite : PS00466 44) chain I residue 9-33 type prosite sequence FCLDCGDLLENPNAVLGSNVECSQC description RNA_POL_M_15KD RNA polymerases M / 15 Kd subunits signature. FClDCGDLLenpnavlgsnve..CsqC source prosite : PS01030 45) 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 46) chain A residue 102 type MOD_RES sequence C description Phosphoserine => ECO:0007744|PubMed:18407956 source Swiss-Prot : SWS_FT_FI1 47) chain A residue 105 type MOD_RES sequence C description Phosphoserine => ECO:0007744|PubMed:18407956 source Swiss-Prot : SWS_FT_FI1 48) chain A residue 233 type MOD_RES sequence C description Phosphoserine => ECO:0007744|PubMed:18407956 source Swiss-Prot : SWS_FT_FI1 49) chain A residue 236 type MOD_RES sequence C description Phosphoserine => ECO:0007744|PubMed:18407956 source Swiss-Prot : SWS_FT_FI1 50) chain J residue 46 type MOD_RES sequence C description Phosphoserine => ECO:0007744|PubMed:18407956 source Swiss-Prot : SWS_FT_FI1 51) chain G residue 244 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:18407956 source Swiss-Prot : SWS_FT_FI1 52) chain L residue 34 type MOD_RES sequence C description Phosphoserine => ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198 source Swiss-Prot : SWS_FT_FI2 53) chain L residue 48 type MOD_RES sequence C description Phosphoserine => ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198 source Swiss-Prot : SWS_FT_FI2 54) chain L residue 51 type MOD_RES sequence C description Phosphoserine => ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198 source Swiss-Prot : SWS_FT_FI2 55) chain I residue 89 type MOD_RES sequence C description Phosphoserine => ECO:0007744|PubMed:15665377, ECO:0007744|PubMed:17330950, ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198 source Swiss-Prot : SWS_FT_FI3 56) chain I residue 114 type MOD_RES sequence C description Phosphoserine => ECO:0007744|PubMed:15665377, ECO:0007744|PubMed:17330950, ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198 source Swiss-Prot : SWS_FT_FI3 57) chain I residue 117 type MOD_RES sequence C description Phosphoserine => ECO:0007744|PubMed:15665377, ECO:0007744|PubMed:17330950, ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198 source Swiss-Prot : SWS_FT_FI3 58) chain B residue 1156 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:19779198 source Swiss-Prot : SWS_FT_FI4

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