eF-site ID 5m3f-ABCDEFGHIJKLMNRTU PDB Code 5m3f Chain A, B, C, D, E, F, G, H, I, J, K, L, M, N, R, T, U Title Yeast RNA polymerase I elongation complex at 3.8A Classification TRANSCRIPTION Compound DNA-directed RNA polymerase I subunit RPA190 Source ORGANISM_COMMON: Baker's yeast; ORGANISM_SCIENTIFIC: Saccharomyces cerevisiae; Sequence A:  MDISKPVGSEITSVDFGILTAKEIRNLSAKQITNPTVLDN LGHPVSGGLYDLALGAFLRNLCSTCGLDEKFCPGHQGHIE LPVPCYNPLFFNQLYIYLRASCLFCHHFRLKSVEVHRYAC KLRLLQYGLIDESYKLDEITLSSTLLNELKSKRSEYVDMA IAKALSDGRTTERGSFTATVNDERKKLVHEFHKKLLSRGK CDNCGMFSPKFRKDGFTKIFETALNEKQITNNRVKGSTYI LSTEVKNILDTVFRKEQCVLQYVFHSRPNLSRKLVKADSF FMDVLVVPPTRFRLPSKLGEEVHENSQNQLLSKVLTTSLL IRDLNDDLSKLQKDKVSLEDRRVIFSRLMNAFVTIQNDVN AFIDSTKAQGRTSGKVPIPGVKQALEKKEGLFRKHMMGKR VNYAARSVISPDPNIETNEIGVPPVFAVKLTYPEPVTAYN IAELRQAVINGPDKWPGATQIQNEDGSLVSLIGMSVEQRK ALANQLLTPSSNVSTHTLNKKVYRHIKNRDVVLMNRQPTL HKASMMGHKVRVLPNEKTLRLHYANTGAYNADFDGDEMNM HFPQNENARAEALNLANTDSQYLTPTSGSPVRGLIQDHIS AGVWLTSKDSFFTREQYQQYIYGCIRPEDGHTTRSKIVTL PPTIFKPYPLWTGKQIITTVLLNVTPPDMPGINLISKNKI KNEYWGKGSLENEVLFKDGALLCGILDKSQYGASKYGIVH SLHEVYGPEVAAKVLSVLGRLFTNYITATAFTCGMDDLRL TAEGNKWRTDILKTSVDTGREAAAEVTNLDKDTPADDPEL LKRLQEILRDNNKSGILDAVTSSKVNAITSQVVSKCVPDG TMKKFPCNSMQAMALSGAKGSNVNVSQIMCLLGQQALEGR RVPVMVSGKTLPSFKPYETDAMAGGYVKGRFYSGIKPQEY YFHCMAGREGLIDTAVKTSRSGYLQRCLTKQLEGVHVSYD NSIRDADGTLVQFMYGGDAIDITKESHMTQFEFCLDNYYA LLKKYNPSALIEHLDVESALKYSKKTLKYRKKHSKEPHYK QSVKYDPVLAKYNPAKYLGSVSENFQDKLESFLDKNSKLF KSSDGVNEKKFRALMQLKYMRSLINPGEAVGIIASQSVGE PSTQMANVTLGIPRLREIVMTASAAIKTPQMTLPIWNDVS DEQADTFCKSISKVLLSEVIDKVIVTERSYVIHMRFFDNN EYSEEYDVSKEELQNVISNQFIHLLEAAIVKEIKKQKKVQ RDRQSAIISHHRFITKYNFDDESGKWCEFKLELAADTEKL LMVNIVEEICRKSIIRQIPHIDRCVHPEPENGKRVLVTEG VNFQAMWDQEAFIDVDGITSNDVAAVLKTYGVEAARNTIV NEINNVFSRYAISVSFRHLDLIADMMTRQGTYLAFNRQGM ETSTSSFMKMSYETTCQFLTKAVLDNEREQLDSPSARIVV GKLNNVGTGSFDVLAKVPN B:  TADFRTLERESRFINPPKDKSAFPLLQEAVQPHIGSFNAL TEGPDGGLLNLGVKDIGEKVIFDGKPLNSNSGYLGNKLSV SVEQVSIAKPMSNDGVSSAVERKVYPSESRQRLTSYRGKL LLKLKWSVNNGEENLFEVRDCGGLPVMLQSNRCHLNKMSP YELVQHKEESDEIGGYFIVNGIEKLIRMLIVQRRNHPMAI IRPSFANRGASYSHYGIQIRSVRPDQTSQTNVLHYLNDGQ VTFRFSWRKNEYLVPVVMILKALCHTSDREIFDGIIGNDV KDSFLTDRLELLLRGFKKRYPHLQNRTQVLQYLGDKFRVV FQASPDQSDLEVGQEVLDRIVLVHLGKDGSQDKFRMLLFM IRKLYSLVAGECSPDNPDATQHQEVLLGGFLYGMILKEKI DEYLQNIIAQVRMDINRGMAINFKDKRYMSRVLMRVNENI GSKMQYFLSTGNLVSQSGLDLQQVSGYTVVAEKINFYRFI SHFRMVHRGSFFAQLKTTTVRKLLPESWGFLCPVHTPDGS PCGLLNHFAHKCRISTQQSDVSRIPSILYSLGVAPASHTF AAGPSLCCVQIDGKIIGWVSHEQGKIIADTLRYWKVEGKT PGLPIDLEIGYVPPSTRGQYPGLYLFGGHSRMLRPVRYLP LDKEDIVGPFEQVYMNIAVTPQEIQNNVHTHVEFTPTNIL SILANLTPFSDFNQSPRNMYQCQMGKQTMGTPGVALCHRS DNKLYRLQTGQTPIVKANLYDDYGMDNFPNGFNAVVAVIS YTGYDMDDAMIINKSADERGFGYGTMYKTEKVDLALNRNR GDPITQHFGFGNDEWPKEWLEKLDEDGLPYIGTYVEEGDP ICAYFDDTLNKTKIKTYHSSEPAYIEEVNLIGDESNKFQE LQTVSIKYRIRRTPQIGDKFSSRHGQKGVCSRKWPTIDMP FSETGIQPDIIINPHAFPSRMTIGMFVESLAGKAGALHGI AQDSTPWIFNEDDTPADYFGEQLAKAGYNYHGNEPMYSGA TGEELRADIYVGVVYYQRLRHMVNDKFQVRSTGPVNSLTM QPVKGRKRHGGIRVGEMERDALIGHGTSFLLQDRLLNSSD YTQASVCRECGSILTTQQSVPRIGSISTVCCRRCSMRFED AKKLIFIDDSQIWEDGQGNKFVGGNETTTVAIPFVLKYLD SELSAMGIRLRYNVEPK C:  WNVEKFKKDFEVNISSLDAREANFDLINIDTSIANAFRRI MISEVPSVAAEYVYFFNNTSVIQDEVLAHRIGLVPLKVDP DMLTWVDSNLPDDEKFTDENTIVLSLNVKCTRNPDAPKGS TDPKELYNNAHVYARDLKFEPQGRQSTTFADCPVVPADPD ILLAKLRPGQEISLKAHCILGIGGDHAKFSPVSTASYRLL PQINILQPIKGESARRFQKCFPPGVIGIDEGSDEAYVKDA RKDTVSREVLRYEEFADKVKLGRVRNHFIFNVESAGAMTP EEIFFKSVRILKNKAEYLKNCPITQ D:  TATTLNTPVVIHATQLPQHVSTDEVLQFLESFIDEKETNL SSSISQLKRIQRDF E:  ENERNISRLWRAFRTVKEMVKDRGYFITQEEVELPLEDFK AKYCDSMGRPQRKMMSFQANPTEESISKFPDMGSLWVEFC DEPSVGVKTMKTFVIHIQEKNFQTGIFVYQNNITPSAMKL VPSIPPATIETFNEAALVVNITHHELVPKHIRLSSDEKRE LLKRYRLKESQLPRIQRADPVALYLGLKRGEVVKIIRKSE TSGRYASYRICM F:  PEDFQQHEQIRRKTLKEKAIPKDQRATTPYMTKYERARIL GTRALQISMNAPVFVDLEGETDPLRIAMKELAEKKIPLVI RRYLPDGSFEDWSVEELIVD G:  ARFIKKHKKQVTNPIDEKNGTSNCIVRVPIALYVSLAPMY LENPLQGVMKQHLNPLVMKYNNKVGGVVLGYEGLKILDAD PLSKEDTSEKLIKITPDTPFGFTWCHVNLYVWQPQVGDVL EGYIFIQSASHIGLLIHDAFNASIKKNNIPVDWTFVHGHW VDSNGEPIDGKLRFTVRNVHTTGRVVSVDGTLI H:  NTLFDDIFQVSEVDPGRYNKVCRIEAASTTQDQCKLTLDI NVELFPVAAQDSLTVTIASSLNSWRPPQAGDRSLADDYDY VMYGTAYKFEEVSKDLIAVYYSFGGLLMRLEGNYRNLNNL KQENAYLLIRR I:  SVVGSLIFCLDCGDLLENPNAVLGSNVECSQCKAIYPKSQ FSNLKVVTTTADDAFPSSLRAKK J:  MIVPVRCFSCGKVVGDKWESYLNLLQEDELDEGTALSRLG LKRYCCRRMILTHVDLIEKFLRYNPLEKR K:  PDREKIKLLTQATSEDGTSASFQIVEEDHTLGNALRYVIM KNPDVEFCGYSIPHPSENLLNIRIQTYGETTAVDALQKGL KDLMDLCDVVESKFTEKIKSM L:  LKYICAECSSKLSLSRTDAVRCKDCGHRILLKARTKRLVQ FEAR M:  SEIEIESVQDQPSVAVGSFFKGFRAPSDTTFDLYKKKKSE KDEFVLHGENERLEYEGYTDSSSQASNQYVVGLFNPEKKS IQLYKAPVLVSKVVSKSSKNLRGPKIKS N:  SIPDGFKKCKHLKNFPLNKQQQVWLIKFPSNVDISKLKSL PVTTMTIDKHDYKIMDDTDIESSLTQDNLSNMTLLVPSES KESLKIASTAKDNAPLQFDKVFSVSETAKIPAIDYSKVRV PRKDVPKVEGLKLEHFATGYDAEDF R:  GACCAGGC T:  AAGCTCAAGTACTTAAGCCTGGTCA U:  AAGTACTTGAGCTT Description (1)  DNA-directed RNA polymerase I subunit RPA190, DNA-directed RNA polymerase I subunit RPA135, 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/DNA Complex Functional site 1) chain A residue 62 type sequence C description binding site for residue ZN A 3001 source : AC1 2) chain A residue 65 type sequence C description binding site for residue ZN A 3001 source : AC1 3) chain A residue 72 type sequence C description binding site for residue ZN A 3001 source : AC1 4) chain A residue 75 type sequence H description binding site for residue ZN A 3001 source : AC1 5) chain A residue 102 type sequence C description binding site for residue ZN A 3002 source : AC2 6) chain A residue 105 type sequence C description binding site for residue ZN A 3002 source : AC2 7) chain A residue 233 type sequence C description binding site for residue ZN A 3002 source : AC2 8) chain A residue 236 type sequence C description binding site for residue ZN A 3002 source : AC2 9) chain A residue 627 type sequence D description binding site for residue MG A 3003 source : AC3 10) chain A residue 629 type sequence D description binding site for residue MG A 3003 source : AC3 11) chain A residue 631 type sequence D description binding site for residue MG A 3003 source : AC3 12) chain R residue 20 type sequence C description binding site for residue MG A 3003 source : AC3 13) chain B residue 501 type sequence R description binding site for residue SO4 B 1301 source : AC4 14) chain B residue 532 type sequence H description binding site for residue SO4 B 1301 source : AC4 15) chain B residue 544 type sequence H description binding site for residue SO4 B 1301 source : AC4 16) chain B residue 698 type sequence S description binding site for residue SO4 B 1301 source : AC4 17) chain B residue 699 type sequence I description binding site for residue SO4 B 1301 source : AC4 18) chain B residue 700 type sequence L description binding site for residue SO4 B 1301 source : AC4 19) chain B residue 1104 type sequence C description binding site for residue ZN B 1302 source : AC5 20) chain B residue 1107 type sequence C description binding site for residue ZN B 1302 source : AC5 21) chain B residue 1128 type sequence C description binding site for residue ZN B 1302 source : AC5 22) chain B residue 1131 type sequence C description binding site for residue ZN B 1302 source : AC5 23) chain I residue 10 type sequence C description binding site for residue ZN I 3001 source : AC6 24) chain I residue 13 type sequence C description binding site for residue ZN I 3001 source : AC6 25) chain I residue 30 type sequence C description binding site for residue ZN I 3001 source : AC6 26) chain I residue 33 type sequence C description binding site for residue ZN I 3001 source : AC6 27) chain J residue 7 type sequence C description binding site for residue ZN J 3001 source : AC7 28) chain J residue 10 type sequence C description binding site for residue ZN J 3001 source : AC7 29) chain J residue 45 type sequence C description binding site for residue ZN J 3001 source : AC7 30) chain J residue 46 type sequence C description binding site for residue ZN J 3001 source : AC7 31) chain L residue 31 type sequence C description binding site for residue ZN L 3001 source : AC8 32) chain L residue 34 type sequence C description binding site for residue ZN L 3001 source : AC8 33) chain L residue 48 type sequence C description binding site for residue ZN L 3001 source : AC8 34) chain L residue 51 type sequence C description binding site for residue ZN L 3001 source : AC8 35) 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 36) 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 37) chain B residue 914-926 type prosite sequence GDKFSSRHGQKGV description RNA_POL_BETA RNA polymerases beta chain signature. GdKFSSrHGQKGV source prosite : PS01166 38) 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 39) 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 40) 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 41) 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 42) chain A residue 102 type MOD_RES sequence C description Phosphoserine => ECO:0007744|PubMed:18407956 source Swiss-Prot : SWS_FT_FI1 43) chain A residue 105 type MOD_RES sequence C description Phosphoserine => ECO:0007744|PubMed:18407956 source Swiss-Prot : SWS_FT_FI1 44) chain A residue 233 type MOD_RES sequence C description Phosphoserine => ECO:0007744|PubMed:18407956 source Swiss-Prot : SWS_FT_FI1 45) chain A residue 236 type MOD_RES sequence C description Phosphoserine => ECO:0007744|PubMed:18407956 source Swiss-Prot : SWS_FT_FI1 46) chain J residue 46 type MOD_RES sequence C description Phosphoserine => ECO:0007744|PubMed:18407956 source Swiss-Prot : SWS_FT_FI1 47) chain G residue 244 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:18407956 source Swiss-Prot : SWS_FT_FI1 48) 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 49) 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 50) 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 51) 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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