eF-site ID 3hov-ABCDEFGHIJKL PDB Code 3hov Chain A, B, C, D, E, F, G, H, I, J, K, L click to enlarge Title Complete RNA polymerase II elongation complex II Classification TRANSCRIPTION, TRANSFERASE/DNA/RNA Compound DNA-directed RNA polymerase II subunit RPB1 Source ORGANISM_COMMON: Baker's yeast; ORGANISM_SCIENTIFIC: Saccharomyces cerevisiae; Sequence A:  VGQQYSSAPLRTVKEVQFGLFSPEEVRAISVAKIRFPETM DETQTRAKIGGLNDPRLGSIDRNLKCQTCQEGMNECPGHF GHIDLAKPVFHVGFIAKIKKVCECVCMHCGKLLLDEHNEL MRQALAIKDSKKRFAAIWTLCKTKMVCETDVPSEDDPTQL VSRGGCGNTQPTIRKDGLKLVGSWKDEPELRVLSTEEILN IFKHISVKDFTSLGFNEVFSRPEWMILTCLPVPPPPVRPS ISFNESQRGEDDLTFKLADILKANISLETLEHNGAPHHAI EEAESLLQFHVATYMDNDIAGQPQALQKSGRPVKSIRARL KGKEGRIRGNLMGKRVDFSARTVISGDPNLELDQVGVPKS IAKTLTYPEVVTPYNIDRLTQLVRNGPNEHPGAKYVIRDS GDRIDLRYSKRAGDIQLQYGWKVERHIMDNDPVLFNRQPS LHKMSMMAHRVKVIPYSTFRLNLSVTSPYNADFDGDEMNL HVPQSEETRAELSQLCAVPLQIVSPQSNKPCMGIVQDTLC GIRKLTLRDTFIELDQVLNMLYWVPDWDGVIPTPAIIKPK PLWSGKQILSVAIPNGIHLQRFDEGTTLLSPKDNGMLIID GQIIFGVVEKKTVGSSNGGLIHVVTREKGPQVCAKLFGNI QKVVNFWLLHNGFSTGIGDTIADGPTMREITETIAEAKKK VLDVTKEAQANLLTAKHGMTLRESFEDNVVRFLNEARDKA GRLAEVNLKDLNNVKQMVMAGSKGSFINIAQMSACVGQQS VEGKRIAFGFVDRTLPHFSKDDYSPESKGFVENSYLRGLT PQEFFFHAMGGREGLIDTAVKTAETGYIQRRLVKALEDIM VHYDNTTRNSLGNVIQFIYGEDGMDAAHIEKQSLDTIGGS DAAFEKRYRVDLLNTDHTLDPSLLESGSEILGDLKLQVLL DEEYKQLVKDRKFLREVFVDGEANWPLPVNIRRIIQNAQQ TFHIDHTKPSDLTIKDIVLGVKDLQENLLVLRGKNEIIQN AQRDAVTLFCCLLRSRLATRRVLQEYRLTKQAFDWVLSNI EAQFLRSVVHPGEMVGVLAAQSIGEPATQMTLKKVTSGVP RLKEILNVAKNMKTPSLTVYLEPGHAADQEQAKLIRSAIE HTTLKSVTIASEIYYDPDPRSTVIPEDEEIIQLHFSQQSP WLLRLELDRAAMNDKDLTMGQVGERIKQTFKNDLFVIWSE DNDEKLIIRCRVVRAEEDHMLKKIENTMLENITLRGVENI ERVVMMKYDRKVPSPTGEYVKEPEWVLETDGVNLSEVMTV PGIDPTRIYTNSFIDIMEVLGIEAGRAALYKEVYNVIASD GSYVNYRHMALLVDVMTTQGGLTSVTRHGFNRSNTGALMR CSFEETVEILFEAGASAELDDCRGVSENVILGQMAPIGTG AFDVMIDEESLVKYMP B:  DESAPITAEDSWAVISAFFREKGLVSQQLDSFNQFVDYTL QDIICEDSTLIISFGKIYVTKPMVNESDGVTHALYPQEAR LRNLTYSSGLFVDVKKKVFIGRLPIMLRSKNCYLSEATES DLYKLKECPFDMGGYFIINGSEKVLIAQERSAGNIVQVFK KAAPSPISHVAEIRSALEKGSRFISTLQVKLYGREGSSAR TIKATLPYIKQDIPIVIIFRALGIIPDGEILEHICYDVND WQMLEMLKPCVEDGFVIQDRETALDFIGRKEKRIQYAKDI LQKEFLPHITQLEGFESRKAFFLGYMINRLLLCALDRKDQ DDRDHFGKKRLDLAGPLLAQLFKTLFKKLTKDIFRYMQRT VELAINAKTITSGLKYALATGNWGEQKAMSSRAGVSQVLN RYTYSSTLSHLRRTNTPILAKPRQLHNTHWGLVCPAETPE GQACGLVKNLSLMSCISVGTDPMPIITFLSEWGMEPLEDY VPHQSPDATRVFVNGVWHGVHRNPARLMETLRTLRRKGDI NPEVSMIRDIREKELKIFTDAGRVYRPLFIVEDDESLGHK ELKVRKGHIAKLMATEYQDEYTWSSLLNEGLVEYIDAEEE ESILIAMQPEDLEPAEADVDPAKRIRVSHHATTFTHCEIH PSMILGVAASIIPFPDHNQSPRNTYQSAMGKQAMGVFLTN YNVRMDTMANILYYPQKPLGTTRAMEYLKFRELPAGQNAI VAIACYSGYNQEDSMIMNQSSIDRGLFRSLFFRSYMDQEK KYGMSITETFEKPQRTRMKHGTYDKLDDDGLIAPGVRVSG EDVIIGKTTPISSKRDASTPLRSTENGIVDQVLVTTNQDG LKFVKVRVRTTKIPQIGDKFASRHGQKGTIGITYRREDMP FTAEGIVPDLIINPHAIPSRMTVAHLIECLLSKVAALSGN EGDASPFTDITVEGISKLLREHGYQSRGFEVMYNGHTGKK LMAQIFFGPTYYQRLRHMVDDKIHARARGPMQVLTRQPVE GRSRDGGLRFGEMERDCMIAHGAASFLKERLMEASDAFRV HICGICGLMTVIAKLNHNQFECKGCDNKIDIYQIHIPYAA KLLFQELMAMNITPRLYTDRSRDF C:  EEGPQVKIREASKDNVDFILSNVDLAMANSLRRVMIAEIP TLAIDSVEVETNTTVLADEFIAHRLGLIPLQSMDIEQLEY SRDCFCEDHCDKCSVVLTLQAFGESESTTNVYSKDLVIVS NLMGRNIGHPIIQDKEGNGVLICKLRKGQELKLTCVAKKG IAKEHAKWGPAAAIEFEYDPWNKLKHTDYWYEQDSAKEWP QSKNCEYEDPPNEGDPFDYKAQADTFYMNVESVGSIPVDQ VVVRGIDTLQKKVASILLALTQMDQD D:  VSTSTFQTRRRRLKKVEEEENAATLQLGQEFQLKQINHQG EEEELIALNLSEARLVIKEALVERRRAFKRSQKKTREKEL ESIDVLLEQTTGGNNKDLKNTMQYLTNFSRFRDQETVGAV IQLLKSTGLHPFEVAQLGSLACDTADEAKTLIPSLNNKIS DDELERILKELSNLETLY E:  DQENERNISRLWRAFRTVKEMVKDRGYFITQEEVELPLED FKAKYCDSMGRPQRKMMSFQANPTEESISKFPDMGSLWVE FCDEPSVGVKTMKTFVIHIQEKNFQTGIFVYQNNITPSAM KLVPSIPPATIETFNEAALVVNITHHELVPKHIRLSSDEK RELLKRYRLKESQLPRIQRADPVALYLGLKRGEVVKIIRK SETSGRYASYRICM F:  LKEKAIPKDQRATTPYMTKYERARILGTRALQISMNAPVF VDLEGETDPLRIAMKELAEKKIPLVIRRYLPDGSFEDWSV EELIVDL G:  MFFIKDLSLNITLHPSFFGPRMKQYLKTKLLEEVEGSCTG KFGYILCVLDYDNIDIQRGRILPTDGSAEFNVKYRAVVFK PFKGEVVDGTVVSCSQHGFEVQVGPMKVFVTKHLMPQDLT FNAGSNPPSYQSSEDVITIKSRIRVKIEGCISQVSSIHAI GSIKEDYLGAI H:  SNTLFDDIFQVSEVDPGRYNKVCRIEAASTTQDQCKLTLD INVELFPVAAQDSLTVTIASSLNTRSWRPPQAGDRSLADD YDYVMYGTAYKFEEVSKDLIAVYYSFGGLLMRLEGNYRNL NNLKQENAYLLIRR I:  TTFRFCRDCNNMLYPREDKENNRLLFECRTCSYVEEAGSP LVYRHELITNIGETAGVVQDIGSDPTLPRSDRECPKCHSR ENVFFQSQQRRKDTSMVLFFVCLSCSHIFTSDQKNKRTQ J:  MIVPVRCFSCGKVVGDKWESYLNLLQEDELDEGTALSRLG LKRYCCRRMILTHVDLIEKFLRYNP K:  MNAPDRFELFLLGEGESKLKIDPDTKAPNAVVITFEKEDH TLGNLIRAELLNDRKVLFAAYKVEHPFFARFKLRIQTTEG YDPKDALKNACNSIINKLGALKTNFETEWNLQTL L:  ATLKYICAECSSKLSLSRTDAVRCKDCGHRILLKARTKRL VQFEAR Description Functional site 1) chain A residue 107 type sequence C description BINDING SITE FOR RESIDUE ZN A 2456 source : AC1 2) chain A residue 110 type sequence C description BINDING SITE FOR RESIDUE ZN A 2456 source : AC1 3) chain A residue 148 type sequence C description BINDING SITE FOR RESIDUE ZN A 2456 source : AC1 4) chain A residue 167 type sequence C description BINDING SITE FOR RESIDUE ZN A 2456 source : AC1 5) chain A residue 67 type sequence C description BINDING SITE FOR RESIDUE ZN A 2457 source : AC2 6) chain A residue 70 type sequence C description BINDING SITE FOR RESIDUE ZN A 2457 source : AC2 7) chain A residue 77 type sequence C description BINDING SITE FOR RESIDUE ZN A 2457 source : AC2 8) chain A residue 80 type sequence H description BINDING SITE FOR RESIDUE ZN A 2457 source : AC2 9) chain A residue 481 type sequence D description BINDING SITE FOR RESIDUE MG A 2458 source : AC3 10) chain A residue 483 type sequence D description BINDING SITE FOR RESIDUE MG A 2458 source : AC3 11) chain A residue 485 type sequence D description BINDING SITE FOR RESIDUE MG A 2458 source : AC3 12) chain B residue 1163 type sequence C description BINDING SITE FOR RESIDUE ZN B 2225 source : AC4 13) chain B residue 1166 type sequence C description BINDING SITE FOR RESIDUE ZN B 2225 source : AC4 14) chain B residue 1182 type sequence C description BINDING SITE FOR RESIDUE ZN B 2225 source : AC4 15) chain B residue 1185 type sequence C description BINDING SITE FOR RESIDUE ZN B 2225 source : AC4 16) chain C residue 86 type sequence C description BINDING SITE FOR RESIDUE ZN C 1269 source : AC5 17) chain C residue 88 type sequence C description BINDING SITE FOR RESIDUE ZN C 1269 source : AC5 18) chain C residue 91 type sequence H description BINDING SITE FOR RESIDUE ZN C 1269 source : AC5 19) chain C residue 92 type sequence C description BINDING SITE FOR RESIDUE ZN C 1269 source : AC5 20) chain C residue 95 type sequence C description BINDING SITE FOR RESIDUE ZN C 1269 source : AC5 21) chain I residue 7 type sequence C description BINDING SITE FOR RESIDUE ZN I 1121 source : AC6 22) chain I residue 10 type sequence C description BINDING SITE FOR RESIDUE ZN I 1121 source : AC6 23) chain I residue 29 type sequence C description BINDING SITE FOR RESIDUE ZN I 1121 source : AC6 24) chain I residue 32 type sequence C description BINDING SITE FOR RESIDUE ZN I 1121 source : AC6 25) chain I residue 75 type sequence C description BINDING SITE FOR RESIDUE ZN I 1122 source : AC7 26) chain I residue 78 type sequence C description BINDING SITE FOR RESIDUE ZN I 1122 source : AC7 27) chain I residue 103 type sequence C description BINDING SITE FOR RESIDUE ZN I 1122 source : AC7 28) chain I residue 106 type sequence C description BINDING SITE FOR RESIDUE ZN I 1122 source : AC7 29) chain I residue 108 type sequence H description BINDING SITE FOR RESIDUE ZN I 1122 source : AC7 30) chain J residue 7 type sequence C description BINDING SITE FOR RESIDUE ZN J 1066 source : AC8 31) chain J residue 10 type sequence C description BINDING SITE FOR RESIDUE ZN J 1066 source : AC8 32) chain J residue 45 type sequence C description BINDING SITE FOR RESIDUE ZN J 1066 source : AC8 33) chain J residue 46 type sequence C description BINDING SITE FOR RESIDUE ZN J 1066 source : AC8 34) chain L residue 31 type sequence C description BINDING SITE FOR RESIDUE ZN L 1071 source : AC9 35) chain L residue 34 type sequence C description BINDING SITE FOR RESIDUE ZN L 1071 source : AC9 36) chain L residue 48 type sequence C description BINDING SITE FOR RESIDUE ZN L 1071 source : AC9 37) chain L residue 51 type sequence C description BINDING SITE FOR RESIDUE ZN L 1071 source : AC9 38) 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 39) chain B residue 977-989 type prosite sequence GDKFASRHGQKGT description RNA_POL_BETA RNA polymerases beta chain signature. GdKFASrHGQKGT source prosite : PS01166 40) 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 41) chain K residue 35-66 type prosite sequence FEKEDHTLGNLIRAELLNDRKVLFAAYKVEHP description RNA_POL_L_13KD RNA polymerases L / 13 to 16 Kd subunits signature. FekEdHTLgNlIraeLlndrkVlfaaYkveHP source prosite : PS01154 42) chain C residue 31-71 type prosite sequence NSLRRVMIAEIPTLAIDSVEVETNTTVLADEFIAHRLGLI P description RNA_POL_D_30KD RNA polymerases D / 30 to 40 Kd subunits signature. NSLRRvmiaeiptlAidsVevetNtTvlaDEfIAhRLGLIP source prosite : PS00446 43) 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 44) chain I residue 75-110 type prosite sequence CPKCHSRENVFFQSQQRRKDTSMVLFFVCLSCSHIF description ZF_TFIIS_1 Zinc finger TFIIS-type signature. CpkChsrenvffqSQQRRkDTSmvlffvCls...CshiF source prosite : PS00466 45) chain I residue 6-32 type prosite sequence FCRDCNNMLYPREDKENNRLLFECRTC description RNA_POL_M_15KD RNA polymerases M / 15 Kd subunits signature. FCrDCNNMLypredkennrllfeCrtC source prosite : PS01030 46) chain B residue 837 type catalytic sequence D description 788 source MCSA : MCSA1 47) chain A residue 483 type catalytic sequence D description 788 source MCSA : MCSA1 48) chain A residue 485 type catalytic sequence D description 788 source MCSA : MCSA1 49) chain I residue 29 type BINDING sequence C description BINDING => ECO:0000269|PubMed:11313498, ECO:0000269|PubMed:11805306, ECO:0000269|PubMed:15537538, ECO:0000305|PubMed:11313499 source Swiss-Prot : SWS_FT_FI3 50) chain I residue 32 type BINDING sequence C description BINDING => ECO:0000269|PubMed:11313498, ECO:0000269|PubMed:11805306, ECO:0000269|PubMed:15537538, ECO:0000305|PubMed:11313499 source Swiss-Prot : SWS_FT_FI3 51) chain I residue 10 type BINDING sequence C description BINDING => ECO:0000269|PubMed:11313498, ECO:0000269|PubMed:11805306, ECO:0000269|PubMed:15537538, ECO:0000305|PubMed:11313499 source Swiss-Prot : SWS_FT_FI3 52) chain I residue 7 type BINDING sequence C description BINDING => ECO:0000269|PubMed:11313498, ECO:0000269|PubMed:11805306, ECO:0000269|PubMed:15537538, ECO:0000305|PubMed:11313499 source Swiss-Prot : SWS_FT_FI3 53) chain I residue 75 type BINDING sequence C description BINDING => ECO:0000255|PROSITE-ProRule:PRU00472, ECO:0000269|PubMed:11313498, ECO:0000269|PubMed:11805306, ECO:0000269|PubMed:15537538, ECO:0000305|PubMed:11313499 source Swiss-Prot : SWS_FT_FI4 54) chain I residue 78 type BINDING sequence C description BINDING => ECO:0000255|PROSITE-ProRule:PRU00472, ECO:0000269|PubMed:11313498, ECO:0000269|PubMed:11805306, ECO:0000269|PubMed:15537538, ECO:0000305|PubMed:11313499 source Swiss-Prot : SWS_FT_FI4 55) chain I residue 103 type BINDING sequence C description BINDING => ECO:0000255|PROSITE-ProRule:PRU00472, ECO:0000269|PubMed:11313498, ECO:0000269|PubMed:11805306, ECO:0000269|PubMed:15537538, ECO:0000305|PubMed:11313499 source Swiss-Prot : SWS_FT_FI4 56) chain I residue 106 type BINDING sequence C description BINDING => ECO:0000255|PROSITE-ProRule:PRU00472, ECO:0000269|PubMed:11313498, ECO:0000269|PubMed:11805306, ECO:0000269|PubMed:15537538, ECO:0000305|PubMed:11313499 source Swiss-Prot : SWS_FT_FI4 57) chain I residue 40 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:18407956 source Swiss-Prot : SWS_FT_FI5 58) chain J residue 46 type ZN_FING sequence C description C4-type source Swiss-Prot : SWS_FT_FI1 59) chain J residue 45 type ZN_FING sequence C description C4-type source Swiss-Prot : SWS_FT_FI1 60) chain A residue 483 type ZN_FING sequence D description C4-type source Swiss-Prot : SWS_FT_FI1 61) chain A residue 485 type ZN_FING sequence D description C4-type source Swiss-Prot : SWS_FT_FI1 62) chain A residue 107 type ZN_FING sequence C description C4-type source Swiss-Prot : SWS_FT_FI1 63) chain A residue 110 type ZN_FING sequence C description C4-type source Swiss-Prot : SWS_FT_FI1 64) chain A residue 148 type ZN_FING sequence C description C4-type source Swiss-Prot : SWS_FT_FI1 65) chain A residue 167 type ZN_FING sequence C description C4-type source Swiss-Prot : SWS_FT_FI1 66) chain A residue 481 type ZN_FING sequence D description C4-type source Swiss-Prot : SWS_FT_FI1 67) chain L residue 31-51 type ZN_FING sequence CAECSSKLSLSRTDAVRCKDC description C4-type source Swiss-Prot : SWS_FT_FI1 68) chain J residue 10 type ZN_FING sequence C description C4-type source Swiss-Prot : SWS_FT_FI1 69) chain L residue 51 type BINDING sequence C description source Swiss-Prot : SWS_FT_FI2 70) chain B residue 1185 type BINDING sequence C description source Swiss-Prot : SWS_FT_FI2 71) chain L residue 31 type BINDING sequence C description source Swiss-Prot : SWS_FT_FI2 72) chain L residue 34 type BINDING sequence C description source Swiss-Prot : SWS_FT_FI2 73) chain L residue 48 type BINDING sequence C description source Swiss-Prot : SWS_FT_FI2

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