eF-site ID 1sfo-ABCEFHIJKL PDB Code 1sfo Chain A, B, C, E, F, H, I, J, K, L Title RNA POLYMERASE II STRAND SEPARATED ELONGATION COMPLEX Classification TRANSCRIPTION/DNA-RNA HYBRID Compound RNA STRAND Source ORGANISM_COMMON: baker's yeast; ORGANISM_SCIENTIFIC: Saccharomyces cerevisiae; Sequence A:  GQQYSSAPLRTVKEVQFGLFSPEEVRAISVAKIRFPETMD ETQTRAKIGGLNDPRLGSIDRNLKCQTCQEGMNECPGHFG HIDLAKPVFHVGFIAKIKKVCECVCMHCGKLLLDEHNELM RQALAIKDSKKRFAAIWTLCKTKMVCETDVPSLVSRGGCG NTQPTIRKDGLKLVGSWKLRVLSTEEILNIFKHISVKDFT SLGFNEVFSRPEWMILTCLPVPPPPVRPSISFNESQRGED DLTFKLADILKANISLETLEHNGAPHHAIEEAESLLQFHV ATYMDNDIAGQPQALQKSGRPVKSIRARLKGKEGRIRGNL MGKRVDFSARTVISGDPNLELDQVGVPKSIAKTLTYPEVV TPYNIDRLTQLVRNGPNEHPGAKYVIRDSGDRIDLRYSKR AGDIQLQYGWKVERHIMDNDPVLFNRQPSLHKMSMMAHRV KVIPYSTFRLNLSVTSPYNADFDGDEMNLHVPQSEETRAE LSQLCAVPLQIVSPQSNKPCMGIVQDTLCGIRKLTLRDTF IELDQVLNMLYWVPDWDGVIPTPAIIKPKPLWSGKQILSV AIPNGIHLQRFDEGTTLLSPKDNGMLIIDGQIIFGVVEKK TVGSSNGGLIHVVTREKGPQVCAKLFGNIQKVVNFWLLHN GFSTGIGDTIADGPTMREITETIAEAKKKVLDVTKEAQAN LLTAKHGMTLRESFEDNVVRFLNEARDKAGRLAEVNLKDL NNVKQMVMAGSKGSFINIAQMSACVGQQSVEGKRIAFGFV DRTLPHFSKDDYSPESKGFVENSYLRGLTPQEFFFHAMGG REGLIDTAVKTAETGYIQRRLVKALEDIMVHYDNTTRNSL GNVIQFIYGEDGMDAAHIEKQSLDTIGGSDAAFEKRYRVD LLNTDHTLDPSLLESGSEILGDLKLQVLLDEEYKQLVKDR KFLREVFVDGEANWPLPVNIRRIIQNAQQTFHIDHTKPSD LTIKDIVLGVKDLQENLLVLRGKNEIIQNAQRDAVTLFCC LLRSRLATRRVLQEYRLTKQAFDWVLSNIEAQFLRSVVHP GEMVGVLAAQSIGEPATQMTLKKVTSGVPRLKEILNVAKN MKTPSLTVYLEPGHAADQEQAKLIRSAIEHTTLKSVTIAS EIYYDPDPRSTVIPEDEEIIQLHFSLQQSPWLLRLELDRA AMNDKDLTMGQVGERIKQTFKNDLFVIWSEDNDEKLIIRC RVVAEEDHMLKKIENTMLENITLRGVENIERVVMMKYDRK VPSPTGEYVKEPEWVLETDGVNLSEVMTVPGIDPTRIYTN SFIDIMEVLGIEAGRAALYKEVYNVIASDGSYVNYRHMAL LVDVMTTQGGLTSVTRHGFNRSNTGALMRCSFEETVEILF EAGASAELDDCRGVSENVILGQMAPIGTGAFDVMI B:  DESAPITAEDSWAVISAFFREKGLVSQQLDSFNQFVDYTL QDIICEDSTLIISFGKIYVTKPMVNESDGVTHALYPQEAR LRNLTYSSGLFVDVKKKVFIGRLPIMLRSKNCYLSEATES DLYKLKECPFDMGGYFIINGSEKVLIAQERSAGNIVQVFK KAAPSPISHVAEIRSALEKGSRFISTLQVKLYGREGSSAR TIKATLPYIKQDIPIVIIFRALGIIPDGEILEHICYDVND WQMLEMLKPCVEDGFVIQDRETALDFIGKEKRIQYAKDIL QKEFLPHITQLEGFESRKAFFLGYMINRLLLCALDRKDQD DRDHFGKKRLDLAGPLLAQLFKTLFKKLTKDIFRYMQRTV ELAINAKTITSGLKYALATGNWGEQKKAMSSRAGVSQVLN RYTYSSTLSHLRRTNTPIAKPRQLHNTHWGLVCPAETPEG QACGLVKNLSLMSCISVGTDPMPIITFLSEWGMEPLEDYV PHQSPDATRVFVNGVWHGVHRNPARLMETLRTLRRKGDIN PEVSMIRDIREKELKIFTDAGRVYRPLFIVEDDESLGHKE LKVRKGHIAKLMATEYQDEYTWSSLLNEGLVEYIDAEEEE SILIAMQPEDLEPAEADVDPAKRIRVSHHATTFTHCEIHP SMILGVAASIIPFPDHNQSPRNTYQSAMGKQAMGVFLTNY NVRMDTMANILYYPQKPLGTTRAMEYLKFRELPAGQNAIV AIACYSGYNQEDSMIMNQSSIDRGLFRSLFFRSYMDQEKK YGMSITETFEKPQRTNTLRMKHGTYDKLDDDGLIAPGVRV SGEDVIIGKTTPISSKRDASTPLRSTENGIVDQVLVTTNQ DGLKFVKVRVRTTKIPQIGDKFASRHGQKGTIGITYRRED MPFTAEGIVPDLIINPHAIPSRMTVAHLIECLLSKVAALS GNEGDASPFTDITVEGISKLLREHGYQSRGFEVMYNGHTG KKLMAQIFFGPTYYQRLRHMVDDKIHARARGPMQVLTRQP VEGRSRDGGLRFGEMERDCMIAHGAASFLKERLMEASDAF RVHICGICGLMTVIAKLNHNQFECKGCDNKIDIYQIHIPY AAKLLFQELMAMNITPRLYTDRSRDF C:  EEGPQVKIREASKDNVDFILSNVDLAMANSLRRVMIAEIP TLAIDSVEVETNTTVLADEFIAHRLGLIPLQSMDIEQLEY SRDCFCEDHCDKCSVVLTLQAFGESESTTNVYSKDLVIVS NLMGRNIGHPIIQDKEGNGVLICKLRKGQELKLTCVAKKG IAKEHAKWGPAAAIEFEYDPWNKLKHTDYWYEQDSAKEWP QSKNCEYEDPPNEGDPFDYKAQADTFYMNVESVGSIPVDQ VVVRGIDTLQKKVASILLALTQMDQD E:  DQENERNISRLWRAFRTVKEMVKDRGYFITQEEVELPLED FKAKYCDSMGRPQRKMMSFQANPTEESISKFPDMGSLWVE FCDEPSVGVKTMKTFVIHIQEKNFQTGIFVYQNNITPSAM KLVPSIPPATIETFNEAALVVNITHHELVPKHIRLSSDEK RELLKRYRLKESQLPRIQRADPVALYLGLKRGEVVKIIRK SETSGRYASYRICM F:  KAIPKDQRATTPYMTKYERARILGTRALQISMNAPVFVDL EGETDPLRIAMKELAEKKIPLVIRRYLPDGSFEDWSVEEL IVDL H:  SNTLFDDIFQVSEVDPGRYNKVCRIEAASTTQDQCKLTLD INVELFPVAAQDSLTVTIASSLTRSWRPPQAGDRSLADDY DYVMYGTAYKFEEVSKDLIAVYYSFGGLLMRLEGNYRNLN NLKQENAYLLIRR 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 1734 source : AC1 2) chain A residue 108 type sequence M description BINDING SITE FOR RESIDUE ZN A 1734 source : AC1 3) chain A residue 110 type sequence C description BINDING SITE FOR RESIDUE ZN A 1734 source : AC1 4) chain A residue 148 type sequence C description BINDING SITE FOR RESIDUE ZN A 1734 source : AC1 5) chain A residue 167 type sequence C description BINDING SITE FOR RESIDUE ZN A 1734 source : AC1 6) chain A residue 67 type sequence C description BINDING SITE FOR RESIDUE ZN A 1735 source : AC2 7) chain A residue 68 type sequence Q description BINDING SITE FOR RESIDUE ZN A 1735 source : AC2 8) chain A residue 70 type sequence C description BINDING SITE FOR RESIDUE ZN A 1735 source : AC2 9) chain A residue 77 type sequence C description BINDING SITE FOR RESIDUE ZN A 1735 source : AC2 10) chain A residue 80 type sequence H description BINDING SITE FOR RESIDUE ZN A 1735 source : AC2 11) chain B residue 1163 type sequence C description BINDING SITE FOR RESIDUE ZN B 1307 source : AC3 12) chain B residue 1166 type sequence C description BINDING SITE FOR RESIDUE ZN B 1307 source : AC3 13) chain B residue 1182 type sequence C description BINDING SITE FOR RESIDUE ZN B 1307 source : AC3 14) chain C residue 86 type sequence C description BINDING SITE FOR RESIDUE ZN C 319 source : AC4 15) chain C residue 88 type sequence C description BINDING SITE FOR RESIDUE ZN C 319 source : AC4 16) chain C residue 91 type sequence H 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 203 source : AC5 20) chain I residue 8 type sequence R description BINDING SITE FOR RESIDUE ZN I 203 source : AC5 21) chain I residue 9 type sequence D description BINDING SITE FOR RESIDUE ZN I 203 source : AC5 22) chain I residue 10 type sequence C description BINDING SITE FOR RESIDUE ZN I 203 source : AC5 23) chain I residue 11 type sequence N description BINDING SITE FOR RESIDUE ZN I 203 source : AC5 24) chain I residue 29 type sequence C description BINDING SITE FOR RESIDUE ZN I 203 source : AC5 25) chain I residue 75 type sequence C description BINDING SITE FOR RESIDUE ZN I 204 source : AC6 26) chain I residue 78 type sequence C description BINDING SITE FOR RESIDUE ZN I 204 source : AC6 27) chain I residue 79 type sequence H description BINDING SITE FOR RESIDUE ZN I 204 source : AC6 28) chain I residue 80 type sequence S description BINDING SITE FOR RESIDUE ZN I 204 source : AC6 29) chain I residue 103 type sequence C description BINDING SITE FOR RESIDUE ZN I 204 source : AC6 30) chain J residue 7 type sequence C description BINDING SITE FOR RESIDUE ZN J 101 source : AC7 31) chain J residue 9 type sequence S description BINDING SITE FOR RESIDUE ZN J 101 source : AC7 32) chain J residue 10 type sequence C description BINDING SITE FOR RESIDUE ZN J 101 source : AC7 33) chain J residue 45 type sequence C description BINDING SITE FOR RESIDUE ZN J 101 source : AC7 34) chain J residue 46 type sequence C description BINDING SITE FOR RESIDUE ZN J 101 source : AC7 35) chain L residue 31 type sequence C description BINDING SITE FOR RESIDUE ZN L 105 source : AC8 36) chain L residue 34 type sequence C description BINDING SITE FOR RESIDUE ZN L 105 source : AC8 37) chain L residue 48 type sequence C description BINDING SITE FOR RESIDUE ZN L 105 source : AC8 38) chain L residue 51 type sequence C description BINDING SITE FOR RESIDUE ZN L 105 source : AC8 39) chain A residue 481 type sequence D description BINDING SITE FOR RESIDUE MG A 2000 source : AC9 40) chain A residue 483 type sequence D description BINDING SITE FOR RESIDUE MG A 2000 source : AC9 41) chain A residue 485 type sequence D description BINDING SITE FOR RESIDUE MG A 2000 source : AC9 42) chain B residue 837 type catalytic sequence D description 788 source MCSA : MCSA1 43) chain A residue 483 type catalytic sequence D description 788 source MCSA : MCSA1 44) chain A residue 485 type catalytic sequence D description 788 source MCSA : MCSA1 45) chain L residue 31 type BINDING sequence C description source Swiss-Prot : SWS_FT_FI2 46) chain L residue 34 type BINDING sequence C description source Swiss-Prot : SWS_FT_FI2 47) chain L residue 48 type BINDING sequence C description source Swiss-Prot : SWS_FT_FI2 48) chain L residue 51 type BINDING sequence C description source Swiss-Prot : SWS_FT_FI2 49) chain B residue 1185 type BINDING sequence C description source Swiss-Prot : SWS_FT_FI2 50) chain I residue 40 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:18407956 source Swiss-Prot : SWS_FT_FI5 51) chain L residue 31-51 type ZN_FING sequence CAECSSKLSLSRTDAVRCKDC description C4-type source Swiss-Prot : SWS_FT_FI1 52) chain A residue 483 type ZN_FING sequence D description C4-type source Swiss-Prot : SWS_FT_FI1 53) chain A residue 485 type ZN_FING sequence D description C4-type source Swiss-Prot : SWS_FT_FI1 54) chain C residue 88 type ZN_FING sequence C description C4-type source Swiss-Prot : SWS_FT_FI1 55) chain C residue 92 type ZN_FING sequence C description C4-type source Swiss-Prot : SWS_FT_FI1 56) chain C residue 95 type ZN_FING sequence C description C4-type source Swiss-Prot : SWS_FT_FI1 57) chain A residue 107 type ZN_FING sequence C description C4-type source Swiss-Prot : SWS_FT_FI1 58) chain A residue 110 type ZN_FING sequence C description C4-type source Swiss-Prot : SWS_FT_FI1 59) chain A residue 148 type ZN_FING sequence C description C4-type source Swiss-Prot : SWS_FT_FI1 60) chain A residue 167 type ZN_FING sequence C description C4-type source Swiss-Prot : SWS_FT_FI1 61) chain A residue 481 type ZN_FING sequence D description C4-type source Swiss-Prot : SWS_FT_FI1 62) 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 63) 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 64) chain I residue 75-110 type prosite sequence CPKCHSRENVFFQSQQRRKDTSMVLFFVCLSCSHIF description ZF_TFIIS_1 Zinc finger TFIIS-type signature. CpkChsrenvffqSQQRRkDTSmvlffvCls...CshiF source prosite : PS00466 65) 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 66) 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 67) 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 68) 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 69) chain B residue 977-989 type prosite sequence GDKFASRHGQKGT description RNA_POL_BETA RNA polymerases beta chain signature. GdKFASrHGQKGT source prosite : PS01166 70) chain B residue 919 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:17330950, ECO:0007744|PubMed:18407956 source Swiss-Prot : SWS_FT_FI3 71) chain I residue 10 type MOD_RES sequence C description Phosphoserine => ECO:0007744|PubMed:17330950, ECO:0007744|PubMed:18407956 source Swiss-Prot : SWS_FT_FI3 72) chain A residue 1350 type MOD_RES sequence K description Phosphoserine => ECO:0007744|PubMed:17330950, ECO:0007744|PubMed:18407956 source Swiss-Prot : SWS_FT_FI3 73) chain I residue 32 type MOD_RES sequence C description Phosphoserine => ECO:0007744|PubMed:17330950, ECO:0007744|PubMed:18407956 source Swiss-Prot : SWS_FT_FI3 74) chain I residue 78 type CROSSLNK sequence C description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000305|PubMed:32142654, ECO:0007744|PubMed:22106047 source Swiss-Prot : SWS_FT_FI4 75) chain I residue 103 type CROSSLNK sequence C description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000305|PubMed:32142654, ECO:0007744|PubMed:22106047 source Swiss-Prot : SWS_FT_FI4 76) chain I residue 106 type CROSSLNK sequence C description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000305|PubMed:32142654, ECO:0007744|PubMed:22106047 source Swiss-Prot : SWS_FT_FI4

Display surface Download Links