eF-site ID 1r5u-ABCEFHIJKLM
PDB Code 1r5u
Chain A, B, C, E, F, H, I, J, K, L, M
Title RNA POLYMERASE II TFIIB COMPLEX
Classification TRANSCRIPTION
Compound DNA-directed RNA polymerase II largest subunit
Source ORGANISM_COMMON: baker's yeast; ORGANISM_SCIENTIFIC: Saccharomyces cerevisiae;
Sequence A:  VGQQYSSAPLRTVKEVQFGLFSPEEVRAISVAKIRFPETM
DETQTRAKIGGLNDPRLGSIDRNLKCQTCQEGMNECPGHF
GHIDLAKPVFHVGFIAKIKKVCECVCMHCGKLLLDEHNEL
MRQALAIKDSKKRFAAIWTLCKTKMVCETDVPSLVSRGGC
GNTQPTIRKDGLKLVGSWKLRVLSTEEILNIFKHISVKDF
TSLGFNEVFSRPEWMILTCLPVPPPPVRPSEDDLTFKLAD
ILKANISLETLEHNGAPHHAIEEAESLLQFHVATYMDNDI
AGQPQAPVKSIRARLKGKEGRIRGNLMGKRVDFSARTVIS
GDPNLELDQVGVPKSIAKTLTYPEVVTPYNIDRLTQLVRN
GPNEHPGAKYVIRDSGDRIDLRYSKRAGDIQLQYGWKVER
HIMDNDPVLFNRQPSLHKMSMMAHRVKVIPYSTFRLNLSV
TSPYNADFDGDEMNLHVPQSEETRAELSQLCAVPLQIVSP
QSNKPCMGIVQDTLCGIRKLTLRDTFIELDQVLNMLYWVP
DWDGVIPTPAIIKPKPLWSGKQILSVAIPNGIHLQRFDEG
TTLLSPKDNGMLIIDGQIIFGVVEKKTVGSSNGGLIHVVT
REKGPQVCAKLFGNIQKVVNFWLLHNGFSTGIGDTIADGP
TMREITETIAEAKKKVLDVTKEAQANLLTAKHGMTLRESF
EDNVVRFLNEARDKAGRLAEVNLKDLNNVKQMVMAGSKGS
FINIAQMSACVGQQSVEGKRIAFGFVDRTLPHFSKDDYSP
ESKGFVENSYLRGLPQEFFFHAMGGREGLIDTAVKTAETG
YIQRRLVKALEDIMVHYDNTTRNSLGNVIQFIYGEDGMDA
AHIEKQSLDTIGGSDAAFEKRYRVDLLNTDHTLDPSLLES
GSEILGDLKLQVLLDEEYKQLVKDRKFLREVFVDGEANWP
LPVNIRRIIQNAQQTFHIDHTKPSDLTIKDIVLGVKDLQE
NLLVLRGKNEIIQNAQRDAVTLFCCLLRSRLATRRVLQEY
RLTKQAFDWVLSNIEAQFLRSVVHPGEMVGVLAAQSIGEP
ATQMTLKKVTSGVPRLKEILNVAKNMKTPSLTVYLEPGHA
ADQEQAKLIRSAIEHTTLKSVTIASEIYYDPDPRSTVIPE
DEEIIQLHFSLQQSPWLLRLELDRAAMNDKDLTMGQVGER
IKQTFKNDLFVIWSEDNDEKLIIRCRVVAEEDHMLKKIEN
TMLENITLRGVENIERVVMMKYDRKVPSPTGEYVKEPEWV
LETDGVNLSEVMTVPGIDPTRIYTNSFIDIMEVLGIEAGR
AALYKEVYNVIASDGSYVNYRHMALLVDVMTTQGGLTSVT
RHGFNRSNTGALMRCSFEETVEILFEAGASAELDDCRGVS
ENVILGQMAPIGTGAFDVMI
B:  DESAPITAEDSWAVISAFFREKGLVSQQLDSFNQFVDYTL
QDIICEDSTLIISFGKIYVTKPMVNESDGVTHALYPQEAR
LRNLTYSSGLFVDVKKKVFIGRLPIMLRSKNCYLSEATES
DLYKLKECPFDMGGYFIINGSEKVLIAQERSAGNIVQVFK
KAAPSPISHVAEIRSALEKGSRFISTLQVKLYGREGSSAR
TIKATLPYIKQDIPIVIIFRALGIIPDGEILEHICYDVND
WQMLEMLKPCVEDGFVIQDRETALDFIGKEKRIQYAKDIL
QKEFLPHITQLEGFESRKAFFLGYMINRLLLCALDRKDQD
DRDHFGKKRLDLAGPLLAQLFKTLFKKLTKDIFRYMQRTV
ELAINAKTITSGLKYALATGNWGAGVSQVLNRYTYSSTLS
HLRRTNTPIAKPRQLHNTHWGLVCPAETPEGQACGLVKNL
SLMSCISVGTDPMPIITFLSEWGMEPLEDYVPHQSPDATR
VFVNGVWHGVHRNPARLMETLRTLRRKGDINPEVSMIRDI
REKELKIFTDAGRVYRPLFIVEDDESLGHKELKVRKGHIA
KLMATEYQDEYTWSSLLNEGLVEYIDAEEEESILIAMQPE
DLEPAEADVDPAKRIRVSHHATTFTHCEIHPSMILGVAAS
IIPFPDHNQSPRNTYQSAMGKQAMGVFLTNYNVRMDTMAN
ILYYPQKPLGTTRAMEYLKFRELPAGQNAIVAIACYSGYN
QEDSMIMNQSSIDRGLFRSLFFRSYMDQEKKYGMSITETF
EKPQRTNTLRMKHGTYDKLDDDGLIAPGVRVSGEDVIIGK
TTPISSKRDASTPLRSTENGIVDQVLVTTNQDGLKFVKVR
VRTTKIPQIGDKFASRHGQKGTIGITYRREDMPFTAEGIV
PDLIINPHAIPSRMTVAHLIECLLSKVAALSGNEGDASPF
TDITVEGISKLLREHGYQSRGFEVMYNGHTGKKLMAQIFF
GPTYYQRLRHMVDDKIHARARGPMQVLTRQPVEGRSRDGG
LRFGEMERDCMIAHGAASFLKERLMEASDAFRVHICGICG
LMTVIAKLNHNQFECKGCDNKIDIYQIHIPYAAKLLFQEL
MAMNITPRLYTDRSRDF
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:  TTFRFCRDCNNMLYPREDKENNRLLFECRTCSYVEEASPL
VYRHELITNIGETAGVVQDIGSDPTLPRSDRECPKCHSRE
NVFFQSQQRRKDTSMVLFFVCLSCSHIFTSDQKNKRTQ
J:  MIVPVRCFSCGKVVGDKWESYLNLLQEDELDEGTALSRLG
LKRYCCRRMILTHVDLIEKFLRYNP
K:  MNAPDRFELFLLGEGESKLKIDPDTKAPNAVVITFEKEDH
TLGNLIRAELLNDRKVLFAAYKVEHPFFARFKLRIQTTEG
YDPKDALKNACNSIINKLGALKTNFETEWNLQTL
L:  ATLKYICAECSSKLSLSRTDAVRCKDCGHRILLKARTKRL
VQFEAR
M:  XXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXX
XXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXX
XXXXXX
Description


Functional site
1) chain A
residue 110
type
sequence C
description BINDING SITE FOR RESIDUE ZN A 1734
source : AC1
2) chain A
residue 148
type
sequence C
description BINDING SITE FOR RESIDUE ZN A 1734
source : AC1
3) chain A
residue 167
type
sequence C
description BINDING SITE FOR RESIDUE ZN A 1734
source : AC1
4) chain A
residue 67
type
sequence C
description BINDING SITE FOR RESIDUE ZN A 1735
source : AC2
5) chain A
residue 70
type
sequence C
description BINDING SITE FOR RESIDUE ZN A 1735
source : AC2
6) chain A
residue 77
type
sequence C
description BINDING SITE FOR RESIDUE ZN A 1735
source : AC2
7) chain A
residue 80
type
sequence H
description BINDING SITE FOR RESIDUE ZN A 1735
source : AC2
8) chain B
residue 1163
type
sequence C
description BINDING SITE FOR RESIDUE ZN B 1307
source : AC3
9) chain B
residue 1166
type
sequence C
description BINDING SITE FOR RESIDUE ZN B 1307
source : AC3
10) chain B
residue 1182
type
sequence C
description BINDING SITE FOR RESIDUE ZN B 1307
source : AC3
11) chain B
residue 1185
type
sequence C
description BINDING SITE FOR RESIDUE ZN B 1307
source : AC3
12) chain C
residue 86
type
sequence C
description BINDING SITE FOR RESIDUE ZN C 319
source : AC4
13) chain C
residue 88
type
sequence C
description BINDING SITE FOR RESIDUE ZN C 319
source : AC4
14) chain C
residue 92
type
sequence C
description BINDING SITE FOR RESIDUE ZN C 319
source : AC4
15) chain C
residue 95
type
sequence C
description BINDING SITE FOR RESIDUE ZN C 319
source : AC4
16) chain I
residue 7
type
sequence C
description BINDING SITE FOR RESIDUE ZN I 203
source : AC5
17) chain I
residue 8
type
sequence R
description BINDING SITE FOR RESIDUE ZN I 203
source : AC5
18) chain I
residue 29
type
sequence C
description BINDING SITE FOR RESIDUE ZN I 203
source : AC5
19) chain I
residue 34
type
sequence Y
description BINDING SITE FOR RESIDUE ZN I 203
source : AC5
20) chain I
residue 75
type
sequence C
description BINDING SITE FOR RESIDUE ZN I 204
source : AC6
21) chain I
residue 78
type
sequence C
description BINDING SITE FOR RESIDUE ZN I 204
source : AC6
22) chain I
residue 103
type
sequence C
description BINDING SITE FOR RESIDUE ZN I 204
source : AC6
23) chain I
residue 106
type
sequence C
description BINDING SITE FOR RESIDUE ZN I 204
source : AC6
24) chain J
residue 7
type
sequence C
description BINDING SITE FOR RESIDUE ZN J 101
source : AC7
25) chain J
residue 10
type
sequence C
description BINDING SITE FOR RESIDUE ZN J 101
source : AC7
26) chain J
residue 45
type
sequence C
description BINDING SITE FOR RESIDUE ZN J 101
source : AC7
27) chain J
residue 46
type
sequence C
description BINDING SITE FOR RESIDUE ZN J 101
source : AC7
28) chain L
residue 31
type
sequence C
description BINDING SITE FOR RESIDUE ZN L 105
source : AC8
29) chain L
residue 34
type
sequence C
description BINDING SITE FOR RESIDUE ZN L 105
source : AC8
30) chain L
residue 48
type
sequence C
description BINDING SITE FOR RESIDUE ZN L 105
source : AC8
31) chain L
residue 51
type
sequence C
description BINDING SITE FOR RESIDUE ZN L 105
source : AC8
32) chain M
residue 48
type
sequence X
description BINDING SITE FOR RESIDUE ZN M 209
source : AC9
33) chain A
residue 481
type
sequence D
description BINDING SITE FOR RESIDUE MG A 1736
source : BC1
34) chain A
residue 483
type
sequence D
description BINDING SITE FOR RESIDUE MG A 1736
source : BC1
35) chain A
residue 485
type
sequence D
description BINDING SITE FOR RESIDUE MG A 1736
source : BC1
36) chain B
residue 837
type catalytic
sequence D
description 788
source MCSA : MCSA1
37) chain A
residue 483
type catalytic
sequence D
description 788
source MCSA : MCSA1
38) chain A
residue 485
type catalytic
sequence D
description 788
source MCSA : MCSA1
39) 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
40) chain I
residue 75-110
type prosite
sequence CPKCHSRENVFFQSQQRRKDTSMVLFFVCLSCSHIF
description ZF_TFIIS_1 Zinc finger TFIIS-type signature. CpkChsrenvffqSQQRRkDTSmvlffvCls...CshiF
source prosite : PS00466
41) 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
42) 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
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 J
residue 2-11
type prosite
sequence IVPVRCFSCG
description RNA_POL_N_8KD RNA polymerases N / 8 Kd subunits signature. IVPVrCFSCG
source prosite : PS01112
45) 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
46) chain B
residue 977-989
type prosite
sequence GDKFASRHGQKGT
description RNA_POL_BETA RNA polymerases beta chain signature. GdKFASrHGQKGT
source prosite : PS01166
47) chain L
residue 31-51
type ZN_FING
sequence CAECSSKLSLSRTDAVRCKDC
description C4-type
source Swiss-Prot : SWS_FT_FI1
48) chain A
residue 483
type ZN_FING
sequence D
description C4-type
source Swiss-Prot : SWS_FT_FI1
49) chain A
residue 485
type ZN_FING
sequence D
description C4-type
source Swiss-Prot : SWS_FT_FI1
50) chain J
residue 10
type ZN_FING
sequence C
description C4-type
source Swiss-Prot : SWS_FT_FI1
51) chain J
residue 45
type ZN_FING
sequence C
description C4-type
source Swiss-Prot : SWS_FT_FI1
52) chain J
residue 46
type ZN_FING
sequence C
description C4-type
source Swiss-Prot : SWS_FT_FI1
53) chain A
residue 107
type ZN_FING
sequence C
description C4-type
source Swiss-Prot : SWS_FT_FI1
54) chain A
residue 110
type ZN_FING
sequence C
description C4-type
source Swiss-Prot : SWS_FT_FI1
55) chain A
residue 148
type ZN_FING
sequence C
description C4-type
source Swiss-Prot : SWS_FT_FI1
56) chain A
residue 167
type ZN_FING
sequence C
description C4-type
source Swiss-Prot : SWS_FT_FI1
57) chain A
residue 481
type ZN_FING
sequence D
description C4-type
source Swiss-Prot : SWS_FT_FI1
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:0000255|PROSITE-ProRule:PRU10145, 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:0000255|PROSITE-ProRule:PRU10145, 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:0000255|PROSITE-ProRule:PRU10145, 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:0000255|PROSITE-ProRule:PRU10145, 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
71) chain I
residue 40
type MOD_RES
sequence S
description Phosphoserine => ECO:0007744|PubMed:18407956
source Swiss-Prot : SWS_FT_FI5

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