eF-site ID 6h67-ABCDEFGHIJKLMN PDB Code 6h67 Chain A, B, C, D, E, F, G, H, I, J, K, L, M, N Title Yeast RNA polymerase I elongation complex stalled by cyclobutane pyrimidine dimer (CPD) Classification TRANSCRIPTION Compound DNA-directed RNA polymerase I subunit RPA190 Source ORGANISM_SCIENTIFIC: Saccharomyces cerevisiae (strain ATCC 204508 / S288c); Sequence A:  MDISKPVGSEITSVDFGILTAKEIRNLSAKQITNPTVLDN LGHPVSGGLYDLALGAFLRNLCSTCGLDEKFCPGHQGHIE LPVPCYNPLFFNQLYIYLRASCLFCHHFRLKSVEVHRYAC KLRLLQYGLIDESYKLDEITLSSTLLNELKSKRSEYVDMA IAKALSDGRTTERGSFTATVNDERKKLVHEFHKKLLSRGK CDNCGMFSPKFRKDGFTKIFETALNEKQITNNRVKGSTYI LSTEVKNILDTVFRKEQCVLQYVFHSRPNLSRKLVKADSF FMDVLVVPPTRFRLPSKVHENSQNQLLSKVLTTSLLIRDL NDDLSKLQKDKVSLEDRRVIFSRLMNAFVTIQNDVNAFID STKAQGRTSGKVPIPGVKQALEKKEGLFRKHMMGKRVNYA ARSVISPDPNIETNEIGVPPVFAVKLTYPEPVTAYNIAEL RQAVINGPDKWPGATQIQNEDGSLVSLIGMSVEQRKALAN QLLTPSSNVSTHTLNKKVYRHIKNRDVVLMNRQPTLHKAS MMGHKVRVLPNEKTLRLHYANTGAYNADFDGDEMNMHFPQ NENARAEALNLANTDSQYLTPTSGSPVRGLIQDHISAGVW LTSKDSFFTREQYQQYIYGCIRPEDGHTTRSKIVTLPPTI FKPYPLWTGKQIITTVLLNVTPPDMPGINLISKNKIKNEY WGKGSLENEVLFKDGALLCGILDKSQYGASKYGIVHSLHE VYGPEVAAKVLSVLGRLFTNYITATAFTCGMDDLRLTAEG NKWRTDILKTSVDTGREAAAEVTNLDKDTPADDPELLKRL QEILRDNNKSGILDAVTSSKVNAITSQVVSKCVPDGTMKK FPCNSMQAMALSGAKGSNVNVSQIMCLLGQQALEGRRVPV MVSGKTLPSFKPYETDAMAGGYVKGRFYSGIKPQEYYFHC MAGREGLIDTAVKTSRSGYLQRCLTKQLEGVHVSYDNSIR DADGTLVQFMYGGDAIDITKESHMTQFEFCLDNYYALLKK YNPSALIEHLDVESALKYSKKTLKYRKKHSKEPHYKQSVK YDPVLAKYNPAKYLGSVSENFQDKLESFLDKNSKLFKSSD GVNEKKFRALMQLKYMRSLINPGEAVGIIASQSVGEPSTQ MTLNTFHFAANVTLGIPRLREIVMTASAAIKTPQMTLPIW NDVSDEQADTFCKSISKVLLSEVIDKVIVTERSYVIHMRF FDNNEYSEEYDVSKEELQNVISNQFIHLLEAAIVKEIKKQ KKVQRDRQSAIISHHRFITKYNFDDESGKWCEFKLELAAD TEKLLMVNIVEEICRKSIIRQIPHIDRCVHPEPENGKRVL VTEGVNFQAMWDQEAFIDVDGITSNDVAAVLKTYGVEAAR NTIVNEINNVFSRYAISVSFRHLDLIADMMTRQGTYLAFN RQGMETSTSSFMKMSYETTCQFLTKAVLDNEREQLDSPSA RIVVGKLNNVGTGSFDVLAKVPN B:  ARTADFRTLERESRFINPPKDKSAFPLLQEAVQPHIGSFN ALTEGPDGGLLNLGVKDIGEKVIFDGKPGYLGNKLSVSVE QVSIAKPMSNDGVSSAVERKVYPSESRQRLTSYRGKLLLK LKWSVNNGEENLFEVRDCGGLPVMLQSNRCHLNKMSPYEL VQHKEESDEIGGYFIVNGIEKLIRMLIVQRRNHPMAIIRP SFANRGASYSHYGIQIRSVRPDQTSQTNVLHYLNDGQVTF RFSWRKNEYLVPVVMILKALCHTSDREIFDGIIGNDVKDS FLTDRLELLLRGFKKRYPHLQNRTQVLQYLGDKFRVVFQA SPDQSDLEVGQEVLDRIVLVHLGKDGSQDKFRMLLFMIRK LYSLVAGECSPDNPDATQHQEVLLGGFLYGMILKEKIDEY LQNIIAQVRMDINRGMAINFKDKRYMSRVLMRVNENIGSK MQYFLSTGNLVSQSGLDLQQVSGYTVVAEKINFYRFISHF RMVHRGSFFAQLKTTTVRKLLPESWGFLCPVHTPDGSPCG LLNHFAHKCRISTQQSDVSRIPSILYSLGVAPASHTFAAG PSLCCVQIDGKIIGWVSHEQGKIIADTLRYWKVEGKTPGL PIDLEIGYVPPSTRGQYPGLYLFGGHSRMLRPVRYLPLDK EDIVGPFEQVYMNIAVTPQEIQNNVHTHVEFTPTNILSIL ANLTPFSDFNQSPRNMYQCQMGKQTMGTPGVALCHRSDNK LYRLQTGQTPIVKANLYDDYGMDNFPNGFNAVVAVISYTG YDMDDAMIINKSADERGFGYGTMYKTEKVDLALNRNRGDP ITQHFGFGNDEWPKEWLEKLDEDGLPYIGTYVEEGDPICA YFDDTLNKTKIKTYHSSEPAYIEEVNLIGDESNKFQELQT VSIKYRIRRTPQIGDKFSSRHGQKGVCSRKWPTIDMPFSE TGIQPDIIINPHAFPSRMTIGMFVESLAGKAGALHGIAQD STPWIFNEDDTPADYFGEQLAKAGYNYHGNEPMYSGATGE ELRADIYVGVVYYQRLRHMVNDKFQVRSTGPVNSLTMQPV KGRKRHGGIRVGEMERDALIGHGTSFLLQDRLLNSSDYTQ ASVCRECGSILTTQQSVPRIGSISTVCCRRCSMRFEDAKK LIFIDDSQIWEDGQGNKFVGGNETTTVAIPFVLKYLDSEL SAMGIRLRYNVEPK C:  EWNVEKFKKDFEVNISSLDAREANFDLINIDTSIANAFRR IMISEVPSVAAEYVYFFNNTSVIQDEVLAHRIGLVPLKVD PDMLTWVDSNLPDDEKFTDENTIVLSLNVKCTRNPDAPKG STDPKELYNNAHVYARDLKFEPQGRQSTTFADCPVVPADP DILLAKLRPGQEISLKAHCILGIGGDHAKFSPVSTASYRL LPQINILQPIKGESARRFQKCFPPGVIGIDEGSDEAYVKD ARKDTVSREVLRYEEFADKVKLGRVRNHFIFNVESAGAMT PEEIFFKSVRILKNKAEYLKNCPITQ D:  TATTLNTPVVIHATQLPQHVSTDEVLQFLESFIDEKETNL SSSISQLKRIQRDF E:  ENERNISRLWRAFRTVKEMVKDRGYFITQEEVELPLEDFK AKYCDSMGRPQRKMMSFQANPTEESISKFPDMGSLWVEFC DEPSVGVKTMKTFVIHIQEKNFQTGIFVYQNNITPSAMKL VPSIPPATIETFNEAALVVNITHHELVPKHIRLSSDEKRE LLKRYRLKESQLPRIQRADPVALYLGLKRGEVVKIIRKSE TSGRYASYRICM F:  PEDFQQHEQIRRKTLKEKAIPKDQRATTPYMTKYERARIL GTRALQISMNAPVFVDLEGETDPLRIAMKELAEKKIPLVI RRYLPDGSFEDWSVEELIVD G:  NCIVRVPIALYVSLAPMYLENPLQGVMKQHLNPLVMKYNN KVGGVVLGYEGLKILDADPLSKEDTSEKLIKITPDTPFGF TWCHVNLYVWQPQVGDVLEGYIFIQSASHIGLLIHDAFNA SIKKNNIPVDWTFVHGHWVDSNGEPIDGKLRFTVRNVHTT GRVVSVDGTLI H:  NTLFDDIFQVSEVDPGRYNKVCRIEAASTTQDQCKLTLDI NVELFPVAAQDSLTVTIASSLNSWRPPQAGDRSLADDYDY VMYGTAYKFEEVSKDLIAVYYSFGGLLMRLEGNYRNLNNL KQENAYLLIRR I:  SVVGSLIFCLDCGDLLENPNAVLGSNVECSQCKAIYPKSQ FSNLKVVTTTADDAFPSSLRAKK J:  MIVPVRCFSCGKVVGDKWESYLNLLQEDELDEGTALSRLG LKRYCCRRMILTHVDLIEKFLRYNPLEKR K:  PDREKIKLLTQATSEDGTSASFQIVEEDHTLGNALRYVIM KNPDVEFCGYSIPHPSENLLNIRIQTYGETTAVDALQKGL KDLMDLCDVVESKFTEKIKSM L:  LKYICAECSSKLSLSRTDAVRCKDCGHRILLKARTKRLVQ FEAR M:  SEIEIESVQDQPSVAVGSFFKGFRAPSDTTFDLYKKKKSE KDEFVLHGENERLEYEGYTDSSSQASNQYVVGLFNPEKKS IQLYKAPVLVSKVVSKSSKNLRGPKIKS N:  SIPDGFKKCKHLKNFPLNQQQVWLIKFPSNVDISKLKSLP VTTMTIDKHDYKIMDDTDIESSLTQDNLSNMTLLVPSESK ESLKIASTAKDNAPLQFDKVFSVSETAKIPAIDYSKVRVP RKDVPKVEGLKLEHFATGYDAEDF 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 polymerase I subunit RPA14, DNA-directed RNA polymerases I, II, and III subunit RPABC1, DNA-directed RNA polymerases I, II, and III subunit RPABC2, DNA-directed RNA polymerase I subunit RPA43, 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/RNA 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 B residue 1104 type sequence C description binding site for residue ZN B 3001 source : AC4 13) chain B residue 1107 type sequence C description binding site for residue ZN B 3001 source : AC4 14) chain B residue 1128 type sequence C description binding site for residue ZN B 3001 source : AC4 15) chain B residue 1131 type sequence C description binding site for residue ZN B 3001 source : AC4 16) chain I residue 10 type sequence C description binding site for residue ZN I 3001 source : AC5 17) chain I residue 13 type sequence C description binding site for residue ZN I 3001 source : AC5 18) chain I residue 30 type sequence C description binding site for residue ZN I 3001 source : AC5 19) chain I residue 33 type sequence C description binding site for residue ZN I 3001 source : AC5 20) chain J residue 7 type sequence C description binding site for residue ZN J 3001 source : AC6 21) chain J residue 10 type sequence C description binding site for residue ZN J 3001 source : AC6 22) chain J residue 45 type sequence C description binding site for residue ZN J 3001 source : AC6 23) chain J residue 46 type sequence C description binding site for residue ZN J 3001 source : AC6 24) chain L residue 31 type sequence C description binding site for residue ZN L 3001 source : AC7 25) chain L residue 34 type sequence C description binding site for residue ZN L 3001 source : AC7 26) chain L residue 48 type sequence C description binding site for residue ZN L 3001 source : AC7 27) chain L residue 51 type sequence C description binding site for residue ZN L 3001 source : AC7 28) 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 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 B residue 914-926 type prosite sequence GDKFSSRHGQKGV description RNA_POL_BETA RNA polymerases beta chain signature. GdKFSSrHGQKGV source prosite : PS01166 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 J residue 2-11 type prosite sequence IVPVRCFSCG description RNA_POL_N_8KD RNA polymerases N / 8 Kd subunits signature. IVPVrCFSCG source prosite : PS01112 33) 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 34) 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 35) chain A residue 102 type MOD_RES sequence C description Phosphoserine => ECO:0007744|PubMed:17330950, ECO:0007744|PubMed:19779198 source Swiss-Prot : SWS_FT_FI1 36) chain A residue 105 type MOD_RES sequence C description Phosphoserine => ECO:0007744|PubMed:17330950, ECO:0007744|PubMed:19779198 source Swiss-Prot : SWS_FT_FI1 37) chain A residue 233 type MOD_RES sequence C description Phosphoserine => ECO:0007744|PubMed:17330950, ECO:0007744|PubMed:19779198 source Swiss-Prot : SWS_FT_FI1 38) chain A residue 236 type MOD_RES sequence C description Phosphoserine => ECO:0007744|PubMed:17330950, ECO:0007744|PubMed:19779198 source Swiss-Prot : SWS_FT_FI1 39) chain J residue 45 type MOD_RES sequence C description Phosphoserine => ECO:0007744|PubMed:17330950, ECO:0007744|PubMed:19779198 source Swiss-Prot : SWS_FT_FI1 40) chain J residue 46 type MOD_RES sequence C description Phosphoserine => ECO:0007744|PubMed:17330950, ECO:0007744|PubMed:19779198 source Swiss-Prot : SWS_FT_FI1 41) chain L residue 34 type MOD_RES sequence C description Phosphoserine => ECO:0007744|PubMed:17330950, ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198 source Swiss-Prot : SWS_FT_FI2 42) chain L residue 48 type MOD_RES sequence C description Phosphoserine => ECO:0007744|PubMed:17330950, ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198 source Swiss-Prot : SWS_FT_FI2 43) chain L residue 51 type MOD_RES sequence C description Phosphoserine => ECO:0007744|PubMed:17330950, ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198 source Swiss-Prot : SWS_FT_FI2 44) chain N residue 60 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:18407956 source Swiss-Prot : SWS_FT_FI3 45) 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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