eF-site ID 2r92-ABCDEFGHIJKL
PDB Code 2r92
Chain A, B, C, D, E, F, G, H, I, J, K, L
Title Elongation complex of RNA polymerase II with artificial RdRP scaffold
Classification Transferase/RNA
Compound RNA (5'-R(*UP*GP*CP*AP*UP*AP*AP*AP*GP*AP*CP*CP*AP*GP*GP*C)-3')
Source ORGANISM_COMMON: baker's yeast; ORGANISM_SCIENTIFIC: Saccharomyces cerevisiae;
Sequence A:  VGQQYSSAPLRTVKEVQFGLFSPEEVRAISVAKIRFPETM
DETQTRAKIGGLNDPRLGSIDRNLKCQTCQEGMNECPGHF
GHIDLAKPVFHVGFIAKIKKVCECVCMHCGKLLLDEHNEL
MRQALAIKDSKKRFAAIWTLCKTKMVCETDVPSEDDPTQL
VSRGGCGNTQPTIRKDGLKLVGSWKKDRDEPELRVLSTEE
ILNIFKHISVKDFTSLGFNEVFSRPEWMILTCLPVPPPPV
RPSISFNESQRGEDDLTFKLADILKANISLETLEHNGAPH
HAIEEAESLLQFHVATYMDNDIAGQPQALQKSGRPVKSIR
ARLKGKEGRIRGNLMGKRVDFSARTVISGDPNLELDQVGV
PKSIAKTLTYPEVVTPYNIDRLTQLVRNGPNEHPGAKYVI
RDSGDRIDLRYSKRAGDIQLQYGWKVERHIMDNDPVLFNR
QPSLHKMSMMAHRVKVIPYSTFRLNLSVTSPYNADFDGDE
MNLHVPQSEETRAELSQLCAVPLQIVSPQSNKPCMGIVQD
TLCGIRKLTLRDTFIELDQVLNMLYWVPDWDGVIPTPAII
KPKPLWSGKQILSVAIPNGIHLQRFDEGTTLLSPKDNGML
IIDGQIIFGVVEKKTVGSSNGGLIHVVTREKGPQVCAKLF
GNIQKVVNFWLLHNGFSTGIGDTIADGPTMREITETIAEA
KKKVLDVTKEAQANLLTAKHGMTLRESFEDNVVRFLNEAR
DKAGRLAEVNLKDLNNVKQMVMAGSKGSFINIAQMSACVG
QQSVEGKRIAFGFVDRTLPHFSKDDYSPESKGFVENSYLR
GLTPQEFFFHAMGGREGLIDTAVKTAETGYIQRRLVKALE
DIMVHYDNTTRNSLGNVIQFIYGEDGMDAAHIEKQSLDTI
GGSDAAFEKRYRVDLLNTDHTLDPSLLESGSEILGDLKLQ
VLLDEEYKQLVKDRKFLREVFVDGEANWPLPVNIRRIIQN
AQQTFHIDHTKPSDLTIKDIVLGVKDLQENLLVLRGKNEI
IQNAQRDAVTLFCCLLRSRLATRRVLQEYRLTKQAFDWVL
SNIEAQFLRSVVHPGEMVGVLAAQSIGEPATQMTLKKVTS
GVPRLKEILNVAKNMKTPSLTVYLEPGHAADQEQAKLIRS
AIEHTTLKSVTIASEIYYDPDPRSTVIPEDEEIIQLHFSL
LQQSPWLLRLELDRAAMNDKDLTMGQVGERIKQTFKNDLF
VIWSEDNDEKLIIRCRVVRPAEEDHMLKKIENTMLENITL
RGVENIERVVMMKYDRKVPSPTGEYVKEPEWVLETDGVNL
SEVMTVPGIDPTRIYTNSFIDIMEVLGIEAGRAALYKEVY
NVIASDGSYVNYRHMALLVDVMTTQGGLTSVTRHGFNRSN
TGALMRCSFEETVEILFEAGASAELDDCRGVSENVILGQM
APIGTGAFDVMIDEESLVKYMP
B:  EDESAPITAEDSWAVISAFFREKGLVSQQLDSFNQFVDYT
LQDIICEDSTLIISFGKIYVTKPMVNESDGVTHALYPQEA
RLRNLTYSSGLFVDVKKVFIGRLPIMLRSKNCYLSEATES
DLYKLKECPFDMGGYFIINGSEKVLIAQERSAGNIVQVFK
KAAPSPISHVAEIRSALEKGSRFISTLQVKLYGREGSSAR
TIKATLPYIKQDIPIVIIFRALGIIPDGEILEHICYDVND
WQMLEMLKPCVEDGFVIQDRETALDFIGRRGTALGIKKEK
RIQYAKDILQKEFLPHITQLEGFESRKAFFLGYMINRLLL
CALDRKDQDDRDHFGKKRLDLAGPLLAQLFKTLFKKLTKD
IFRYMQRTVELAINAKTITSGLKYALATGNWGEQKKAMSS
RAGVSQVLNRYTYSSTLSHLRRTNTPIKPRQLHNTHWGLV
CPAETPEGQACGLVKNLSLMSCISVGTDPMPIITFLSEWG
MEPLEDYVPHQSPDATRVFVNGVWHGVHRNPARLMETLRT
LRRKGDINPEVSMIRDIREKELKIFTDAGRVYRPLFIVED
DESLGHKELKVRKGHIAKLMATEYQDEYTWSSLLNEGLVE
YIDAEEEESILIAMQPEDLEPAEADVDPAKRIRVSHHATT
FTHCEIHPSMILGVAASIIPFPDHNQSPRNTYQSAMGKQA
MGVFLTNYNVRMDTMANILYYPQKPLGTTRAMEYLKFREL
PAGQNAIVAIACYSGYNQEDSMIMNQSSIDRGLFRSLFFR
SYMDQEKKYGMSITETFEKPQRTNTLRMKHGTYDKLDDDG
LIAPGVRVSGEDVIIGKTTPSKRDASTPLRSTENGIVDQV
LVTTNQDGLKFVKVRVRTTKIPQIGDKFASRHGQKGTIGI
TYRREDMPFTAEGIVPDLIINPHAIPSRMTVAHLIECLLS
KVAALSGNEGDASPFTDITVEGISKLLREHGYQSRGFEVM
YNGHTGKKLMAQIFFGPTYYQRLRHMVDDKIHARARGPMQ
VLTRQPVEGRSRDGGLRFGEMERDCMIAHGAASFLKERLM
EASDAFRVHICGICGLMTVIAKLNHNQFECKGCDNKIDIY
QIHIPYAAKLLFQELMAMNITPRLYTDRSRDF
C:  SEEGPQVKIREASKDNVDFILSNVDLAMANSLRRVMIAEI
PTLAIDSVEVETNTTVLADEFIAHRLGLIPLQSMDIEQLE
YSRDCFCEDHCDKCSVVLTLQAFGESESTTNVYSKDLVIV
SNLMGRNIGHPIIQDKEGNGVLICKLRKGQELKLTCVAKK
GIAKEHAKWGPAAAIEFEYDPWNKLKHTDYWYEQDSAKEW
PQSKNCEYEDPPNEGDPFDYKAQADTFYMNVESVGSIPVD
QVVVRGIDTLQKKVASILLALTQMDQD
D:  VSTSTFQTRRRRLKKVEEEENAATLQLGQEFQLKQINHQG
EEEELIALNLSEARLVIKEALVERRRAFKRSQKKTREKEL
ESIDVLLEQTTGGNNKDLKNTMQYLTNFSRFRDQETVGAV
IQLLKSTGLHPFEVAQLGSLACDTADEAKTLIPSLNNKIS
DDELERILKELSNLETLY
E:  DQENERNISRLWRAFRTVKEMVKDRGYFITQEEVELPLED
FKAKYCDSMGRPQRKMMSFQANPTEESISKFPDMGSLWVE
FCDEPSVGVKTMKTFVIHIQEKNFQTGIFVYQNNITPSAM
KLVPSIPPATIETFNEAALVVNITHHELVPKHIRLSSDEK
RELLKRYRLKESQLPRIQRADPVALYLGLKRGEVVKIIRK
SETSGRYASYRICM
F:  TLKEKAIPKDQRATTPYMTKYERARILGTRALQISMNAPV
FVDLEGETDPLRIAMKELAEKKIPLVIRRYLPDGSFEDWS
VEELIVDL
G:  MFFIKDLSLNITLHPSFFGPRMKQYLKTKLLEEVEGSCTG
KFGYILCVLDYDNIDIQRGRILPTDGSAEFNVKYRAVVFK
PFKGEVVDGTVVSCSQHGFEVQVGPMKVFVTKHLMPQDLT
FNAGSNPPSYQSSEDVITIKSRIRVKIEGCISQVSSIHAI
GSIKEDYLGAI
H:  SNTLFDDIFQVSEVDPGRYNKVCRIEAASTTQDQCKLTLD
INVELFPVAAQDSLTVTIASSLNLTRSWRPPQAGDRSLAD
DYDYVMYGTAYKFEEVSKDLIAVYYSFGGLLMRLEGNYRN
LNNLKQENAYLLIRR
I:  TTFRFCRDCNNMLYPREDKENNRLLFECRTCSYVEEAGSP
LVYRHELITNIGETAGVVQDIGSDPTLPRSDRECPKCHSR
ENVFFQSQQRRKDTSMVLFFVCLSCSHIFTSDQKNK
J:  MIVPVRCFSCGKVVGDKWESYLNLLQEDELDEGTALSRLG
LKRYCCRRMILTHVDLIEKFLRYNP
K:  MNAPDRFELFLLGEGESKLKIDPDTKAPNAVVITFEKEDH
TLGNLIRAELLNDRKVLFAAYKVEHPFFARFKLRIQTTEG
YDPKDALKNACNSIINKLGALKTNFETEWNLQ
L:  ATLKYICAECSSKLSLSRTDAVRCKDCGHRILLKARTKRL
VQFEAR
Description (1)  PROTEIN/RNA Complex


Functional site

1) chain B
residue 837
type catalytic
sequence D
description 788
source MCSA : MCSA1

2) chain A
residue 483
type catalytic
sequence D
description 788
source MCSA : MCSA1

3) chain A
residue 485
type catalytic
sequence D
description 788
source MCSA : MCSA1

4) 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

5) 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

6) 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

7) 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

8) 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

9) 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

10) 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

11) 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

12) chain I
residue 40
type MOD_RES
sequence S
description Phosphoserine => ECO:0007744|PubMed:18407956
source Swiss-Prot : SWS_FT_FI5

13) 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

14) 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

15) chain I
residue 75-110
type prosite
sequence CPKCHSRENVFFQSQQRRKDTSMVLFFVCLSCSHIF
description ZF_TFIIS_1 Zinc finger TFIIS-type signature. CpkChsrenvffqSQQRRkDTSmvlffvCls...CshiF
source prosite : PS00466

16) 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

17) 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

18) 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

19) 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

20) chain B
residue 977-989
type prosite
sequence GDKFASRHGQKGT
description RNA_POL_BETA RNA polymerases beta chain signature. GdKFASrHGQKGT
source prosite : PS01166

21) chain L
residue 31-51
type ZN_FING
sequence CAECSSKLSLSRTDAVRCKDC
description C4-type
source Swiss-Prot : SWS_FT_FI1

22) chain A
residue 483
type ZN_FING
sequence D
description C4-type
source Swiss-Prot : SWS_FT_FI1

23) chain A
residue 485
type ZN_FING
sequence D
description C4-type
source Swiss-Prot : SWS_FT_FI1

24) chain J
residue 10
type ZN_FING
sequence C
description C4-type
source Swiss-Prot : SWS_FT_FI1

25) chain J
residue 45
type ZN_FING
sequence C
description C4-type
source Swiss-Prot : SWS_FT_FI1

26) chain J
residue 46
type ZN_FING
sequence C
description C4-type
source Swiss-Prot : SWS_FT_FI1

27) chain A
residue 107
type ZN_FING
sequence C
description C4-type
source Swiss-Prot : SWS_FT_FI1

28) chain A
residue 110
type ZN_FING
sequence C
description C4-type
source Swiss-Prot : SWS_FT_FI1

29) chain A
residue 148
type ZN_FING
sequence C
description C4-type
source Swiss-Prot : SWS_FT_FI1

30) chain A
residue 167
type ZN_FING
sequence C
description C4-type
source Swiss-Prot : SWS_FT_FI1

31) chain A
residue 481
type ZN_FING
sequence D
description C4-type
source Swiss-Prot : SWS_FT_FI1

32) chain L
residue 31
type BINDING
sequence C
description
source Swiss-Prot : SWS_FT_FI2

33) chain L
residue 34
type BINDING
sequence C
description
source Swiss-Prot : SWS_FT_FI2

34) chain L
residue 48
type BINDING
sequence C
description
source Swiss-Prot : SWS_FT_FI2

35) chain L
residue 51
type BINDING
sequence C
description
source Swiss-Prot : SWS_FT_FI2

36) chain B
residue 1185
type BINDING
sequence C
description
source Swiss-Prot : SWS_FT_FI2


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