eF-site ID 2b8k-ABCDEFGHIJKL PDB Code 2b8k Chain A, B, C, D, E, F, G, H, I, J, K, L click to enlarge Title 12-subunit RNA Polymerase II Classification TRANSFERASE Compound DNA-directed RNA polymerase II largest subunit 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 HTTLKSVTIASEIYYDPDPRSTVIPEDEEIIQLHFSLQQS PWLLRLELDRAAMNDKDLTMGQVGERIKQTFKNDLFVIWS EDNDEKLIIRCRVVAEEDHMLKKIENTMLENITLRGVENI ERVVMMKYDRKVPSPTGEYVKEPEWVLETDGVNLSEVMTV PGIDPTRIYTNSFIDIMEVLGIEAGRAALYKEVYNVIASD GSYVNYRHMALLVDVMTTQGGLTSVTRHGFNRSNTGALMR CSFEETVEILFEAGASAELDDCRGVSENVILGQMAPIGTG AFDVMIDEESLVKYMP B:  DESAPITAEDSWAVISAFFREKGLVSQQLDSFNQFVDYTL QDIICEDSTLIISFGKIYVTKPMVNESDGVTHALYPQEAR LRNLTYSSGLFVDVKKKVFIGRLPIMLRSKNCYLSEATES DLYKLKECPFDMGGYFIINGSEKVLIAQERSAGNIVQVFK KAAPSPISHVAEIRSALEKGSRFISTLQVKLYGREGSSAR TIKATLPYIKQDIPIVIIFRALGIIPDGEILEHICYDVND WQMLEMLKPCVEDGFVIQDRETALDFIGKEKRIQYAKDIL QKEFLPHITQLEGFESRKAFFLGYMINRLLLCALDRKDQD DRDHFGKKRLDLAGPLLAQLFKTLFKKLTKDIFRYMQRTV EEAHDFNMKLAINAKTITSGLKYALATGNWGEQKKAMSSR AGVSQVLNRYTYSSTLSHLRRTNTPIAKPRQLHNTHWGLV CPAETPEGQACGLVKNLSLMSCISVGTDPMPIITFLSEWG MEPLEDYVPHQSPDATRVFVNGVWHGVHRNPARLMETLRT LRRKGDINPEVSMIRDIREKELKIFTDAGRVYRPLFIVED DESLGHKELKVRKGHIAKLMATEYQDEYTWSSLLNEGLVE YIDAEEEESILIAMQPEDLEPAEADVDPAKRIRVSHHATT FTHCEIHPSMILGVAASIIPFPDHNQSPRNTYQSAMGKQA MGVFLTNYNVRMDTMANILYYPQKPLGTTRAMEYLKFREL PAGQNAIVAIACYSGYNQEDSMIMNQSSIDRGLFRSLFFR SYMDQEKKYGMSITETFEKPQRTNTLRMKHGTYDKLDDDG LIAPGVRVSGEDVIIGKTTPISSKRDASTPLRSTENGIVD QVLVTTNQDGLKFVKVRVRTTKIPQIGDKFASRHGQKGTI GITYRREDMPFTAEGIVPDLIINPHAIPSRMTVAHLIECL LSKVAALSGNEGDASPFTDITVEGISKLLREHGYQSRGFE VMYNGHTGKKLMAQIFFGPTYYQRLRHMVDDKIHARARGP MQVLTRQPVEGRSRDGGLRFGEMERDCMIAHGAASFLKER LMEASDAFRVHICGICGLMTVIAKLNHNQFECKGCDNKID IYQIHIPYAAKLLFQELMAMNITPRLYTDRSRDF C:  EEGPQVKIREASKDNVDFILSNVDLAMANSLRRVMIAEIP TLAIDSVEVETNTTVLADEFIAHRLGLIPLQSMDIEQLEY SRDCFCEDHCDKCSVVLTLQAFGESESTTNVYSKDLVIVS NLMGRNIGHPIIQDKEGNGVLICKLRKGQELKLTCVAKKG IAKEHAKWGPAAAIEFEYDPWNKLKHTDYWYEQDSAKEWP QSKNCEYEDPPNEGDPFDYKAQADTFYMNVESVGSIPVDQ VVVRGIDTLQKKVASILLALTQMDQD D:  STSTFQTRRRRLKKVEEEENAATLQLGQEFQLKQINHQGE EEELIALNLSEARLVIKEALVERRRAFKRSQKKFMHSETR EKELESIDVLLEQTTGGNNKDLKNTMQYLTNFSRFRDQET VGAVIQLLKSTGLHPFEVAQLGSLACDTADEAKTLIPSLN NKISDDELERILKELSNLETLY E:  DQENERNISRLWRAFRTVKEMVKDRGYFITQEEVELPLED FKAKYCDSMGRPQRKMMSFQANPTEESISKFPDMGSLWVE FCDEPSVGVKTMKTFVIHIQEKNFQTGIFVYQNNITPSAM KLVPSIPPATIETFNEAALVVNITHHELVPKHIRLSSDEK RELLKRYRLKESQLPRIQRADPVALYLGLKRGEVVKIIRK SETSGRYASYRICM F:  KAIPKDQRATTPYMTKYERARILGTRALQISMNAPVFVDL EGETDPLRIAMKELAEKKIPLVIRRYLPDGSFEDWSVEEL IVDL G:  MFFIKDLSLNITLHPSFFGPRMKQYLKTKLLEEVEGSCTG KFGYILCVLDYDNIDIQRGRILPTDGSAEFNVKYRAVVFK PFKGEVVDGTVVSCSQHGFEVQVGPMKVFVTKHLMPQDLT FNAGSNPPSYQSSEDVITIKSRIRVKIEGCISQVSSIHAI GSIKEDYLGAI H:  SNTLFDDIFQVSEVDPGRYNKVCRIEAASTTQDQCKLTLD INVELFPVAAQDSLTVTIASSLTRSWRPPQAGDRSLADDY DYVMYGTAYKFEEVSKDLIAVYYSFGGLLMRLEGNYRNLN NLKQENAYLLIRR I:  TTFRFCRDCNNMLYPREDKENNRLLFECRTCSYVEEAGSP LVYRHELITNIGETAGVVQDIGSDPTLPRSDRECPKCHSR ENVFFQSQQRRKDTSMVLFFVCLSCSHIFTSDQKNKRTQ J:  MIVPVRCFSCGKVVGDKWESYLNLLQEDELDEGTALSRLG LKRYCCRRMILTHVDLIEKFLRYNP K:  MNAPDRFELFLLGEGESKLKIDPDTKAPNAVVITFEKEDH TLGNLIRAELLNDRKVLFAAYKVEHPFFARFKLRIQTTEG YDPKDALKNACNSIINKLGALKTNFETEWNLQTLA L:  ATLKYICAECSSKLSLSRTDAVRCKDCGHRILLKARTKRL VQFEAR Description (1)  DNA-directed RNA polymerase II largest subunit (E.C.2.7.7.6), DNA-directed RNA polymerase II 140 kDa polypeptide (E.C.2.7.7.6), DNA-directed RNA polymerase II 45 kDa polypeptide (E.C.2.7.7.6), DNA-directed RNA polymerase II 32 kDa polypeptide (E.C.2.7.7.6), DNA-directed RNA polymerases I, II, and III 27 kDa polypeptide (E.C.2.7.7.6), DNA-directed RNA polymerases I, II, and III 23 kDa polypeptide (E.C.2.7.7.6), DNA-directed RNA polymerase II 19 kDa polypeptide (E.C.2.7.7.6), DNA-directed RNA polymerases I, II, and III 14.5 kDa polypeptide (E.C.2.7.7.6), DNA-directed RNA polymerase II subunit 9 (E.C.2.7.7.6), DNA-directed RNA polymerases I/II/III subunit 10 (E.C.2.7.7.6), DNA-directed RNA polymerase II 13.6 kDa polypeptide (E.C.2.7.7.6), DNA-directed RNA polymerases I, II, and III 7.7 kDa polypeptide (E.C.2.7.7.6) Functional site 1) chain A residue 108 type sequence M description BINDING SITE FOR RESIDUE ZN A 1734 source : AC1 2) chain A residue 110 type sequence C description BINDING SITE FOR RESIDUE ZN A 1734 source : AC1 3) chain A residue 148 type sequence C description BINDING SITE FOR RESIDUE ZN A 1734 source : AC1 4) chain A residue 167 type sequence C description BINDING SITE FOR RESIDUE ZN A 1734 source : AC1 5) chain A residue 67 type sequence C description BINDING SITE FOR RESIDUE ZN A 1735 source : AC2 6) chain A residue 68 type sequence Q description BINDING SITE FOR RESIDUE ZN A 1735 source : AC2 7) chain A residue 70 type sequence C description BINDING SITE FOR RESIDUE ZN A 1735 source : AC2 8) chain A residue 77 type sequence C description BINDING SITE FOR RESIDUE ZN A 1735 source : AC2 9) chain A residue 80 type sequence H description BINDING SITE FOR RESIDUE ZN A 1735 source : AC2 10) chain B residue 1163 type sequence C description BINDING SITE FOR RESIDUE ZN B 1225 source : AC3 11) chain B residue 1166 type sequence C description BINDING SITE FOR RESIDUE ZN B 1225 source : AC3 12) chain B residue 1170 type sequence T description BINDING SITE FOR RESIDUE ZN B 1225 source : AC3 13) chain B residue 1182 type sequence C description BINDING SITE FOR RESIDUE ZN B 1225 source : AC3 14) chain B residue 1185 type sequence C description BINDING SITE FOR RESIDUE ZN B 1225 source : AC3 15) chain C residue 86 type sequence C description BINDING SITE FOR RESIDUE ZN C 319 source : AC4 16) chain C residue 88 type sequence C description BINDING SITE FOR RESIDUE ZN C 319 source : AC4 17) chain C residue 92 type sequence C description BINDING SITE FOR RESIDUE ZN C 319 source : AC4 18) chain C residue 95 type sequence C description BINDING SITE FOR RESIDUE ZN C 319 source : AC4 19) chain I residue 7 type sequence C description BINDING SITE FOR RESIDUE ZN I 123 source : AC5 20) chain I residue 10 type sequence C description BINDING SITE FOR RESIDUE ZN I 123 source : AC5 21) chain I residue 29 type sequence C description BINDING SITE FOR RESIDUE ZN I 123 source : AC5 22) chain I residue 32 type sequence C description BINDING SITE FOR RESIDUE ZN I 123 source : AC5 23) chain I residue 75 type sequence C description BINDING SITE FOR RESIDUE ZN I 124 source : AC6 24) chain I residue 78 type sequence C description BINDING SITE FOR RESIDUE ZN I 124 source : AC6 25) chain I residue 106 type sequence C description BINDING SITE FOR RESIDUE ZN I 124 source : AC6 26) chain I residue 108 type sequence H description BINDING SITE FOR RESIDUE ZN I 124 source : AC6 27) chain J residue 7 type sequence C description BINDING SITE FOR RESIDUE ZN J 71 source : AC7 28) chain J residue 10 type sequence C description BINDING SITE FOR RESIDUE ZN J 71 source : AC7 29) chain J residue 45 type sequence C description BINDING SITE FOR RESIDUE ZN J 71 source : AC7 30) chain J residue 46 type sequence C description BINDING SITE FOR RESIDUE ZN J 71 source : AC7 31) chain L residue 31 type sequence C description BINDING SITE FOR RESIDUE ZN L 71 source : AC8 32) chain L residue 34 type sequence C description BINDING SITE FOR RESIDUE ZN L 71 source : AC8 33) chain L residue 48 type sequence C description BINDING SITE FOR RESIDUE ZN L 71 source : AC8 34) chain L residue 51 type sequence C description BINDING SITE FOR RESIDUE ZN L 71 source : AC8 35) chain B residue 837 type catalytic sequence D description 788 source MCSA : MCSA1 36) chain A residue 483 type catalytic sequence D description 788 source MCSA : MCSA1 37) chain A residue 485 type catalytic sequence D description 788 source MCSA : MCSA1 38) chain I residue 40 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:18407956 source Swiss-Prot : SWS_FT_FI5 39) chain L residue 31-51 type ZN_FING sequence CAECSSKLSLSRTDAVRCKDC description C4-type source Swiss-Prot : SWS_FT_FI1 40) chain A residue 483 type ZN_FING sequence D description C4-type source Swiss-Prot : SWS_FT_FI1 41) chain A residue 485 type ZN_FING sequence D description C4-type source Swiss-Prot : SWS_FT_FI1 42) chain J residue 10 type ZN_FING sequence C description C4-type source Swiss-Prot : SWS_FT_FI1 43) chain J residue 45 type ZN_FING sequence C description C4-type source Swiss-Prot : SWS_FT_FI1 44) chain J residue 46 type ZN_FING sequence C description C4-type source Swiss-Prot : SWS_FT_FI1 45) chain A residue 107 type ZN_FING sequence C description C4-type source Swiss-Prot : SWS_FT_FI1 46) chain A residue 110 type ZN_FING sequence C description C4-type source Swiss-Prot : SWS_FT_FI1 47) chain A residue 148 type ZN_FING sequence C description C4-type source Swiss-Prot : SWS_FT_FI1 48) chain A residue 167 type ZN_FING sequence C description C4-type source Swiss-Prot : SWS_FT_FI1 49) chain A residue 481 type ZN_FING sequence D description C4-type source Swiss-Prot : SWS_FT_FI1 50) 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 51) 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 52) chain I residue 75-110 type prosite sequence CPKCHSRENVFFQSQQRRKDTSMVLFFVCLSCSHIF description ZF_TFIIS_1 Zinc finger TFIIS-type signature. CpkChsrenvffqSQQRRkDTSmvlffvCls...CshiF source prosite : PS00466 53) 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 54) 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 55) 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 56) 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 57) chain B residue 977-989 type prosite sequence GDKFASRHGQKGT description RNA_POL_BETA RNA polymerases beta chain signature. GdKFASrHGQKGT source prosite : PS01166 58) chain L residue 31 type BINDING sequence C description source Swiss-Prot : SWS_FT_FI2 59) chain L residue 34 type BINDING sequence C description source Swiss-Prot : SWS_FT_FI2 60) chain L residue 48 type BINDING sequence C description source Swiss-Prot : SWS_FT_FI2 61) chain L residue 51 type BINDING sequence C description source Swiss-Prot : SWS_FT_FI2 62) chain B residue 1185 type BINDING sequence C description source Swiss-Prot : SWS_FT_FI2 63) 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 64) 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 65) 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 66) 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 67) 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 68) 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 69) 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 70) 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

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