eF-site ID 5fja-ABCDEFGHIJKLMNOPQ
PDB Code 5fja
Chain A, B, C, D, E, F, G, H, I, J, K, L, M, N, O, P, Q
Title Cryo-EM structure of yeast RNA polymerase III at 4.7 A
Classification TRANSCRIPTION
Compound DNA-DIRECTED RNA POLYMERASE III SUBUNIT RPC1
Source ORGANISM_COMMON: BAKER'S YEAST; ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;
Sequence A:  KEVVVSETPKRIKGLEFSALSAADIVAQSEVEVSTRDLFD
LEKDRAPKANGALDPKMGVSSSSLECATCHGNLASCHGHF
GHLKLALPVFHIGYFKATIQILQGICKNCSAILLSETDKR
QFLHELRRPGVDNLRRMGILKKILDQCKKQRRCLHCGALN
GVVKKAAALKIIHDTFRWVGKKSAPEKDIWVGEWKEVLAH
NPELERYVKRCMDDLNPLKTLNLFKQIKSADCELLGIDAT
VPSGRPETYIWRYLPAPPVCIRPSVMMQDSPASNEDDLTV
KLTEIVWTSSLIKAGLDKGISINNMMEHWDYLQLTVAMYI
NKPIRGFCQRLKGKQGRFRGNLSGKRVDFSGRTVISPDPN
LSIDEVAVPDRVAKVLTYPEKVTRYNRHKLQELIVNGPNV
HPGANYLLKRNEDARRNLRYGDRMKLAKNLQIGDVVERHL
EDGDVVLFNRQPSLHRLSILSHYAKIRPWRTFRLNECVCT
PYNADFDGDEMNLHVPQTEEARAEAINLMGVKNNLLTPKS
GEPIIAATQDFITGSYLISHKDSFYDRATLTQLLSMMSDG
IEHFDIPPPAIMKPYYLWTGKQVFSLLIKPNHNSPVVINL
DAKNKVFVPPKSKSLPNEMSQNDGFVIIRGSQILSGVMDK
SVLGDGKKHSVFYTILRDYGPQEAANAMNRMAKLCARFLG
NRGFSIGINDVTPADDLKQKKEELVEIAYHKCDELITLFN
KGELETQPGCNEEQTLEAKIGGLLSKVREEVGDVCINELD
NWNAPLIMATCGSKGSTLNVSQMVAVVGQQIISGNRVPDG
FQDRSLPHFPKNSKTPQSKGFVRNSFFSGLSPPEFLFHAI
SGREGLVDTAVKTAETGYMSRRLMKSLEDLSCQYDNTVRT
SANGIVQFTYGGDGLDPLEMEGNAQPVNFNRSWDHAYNIT
FNNQDKGLLPYAIMETANEILGPLEERLVRYDNSGCLVKR
EDLNKAEYVDQYDAERDFYHSLREYINGKATALANLRKSR
GMLGLLEPPAKELQGIDPDETVPDNVKTSVSQLYRISEKS
VRKFLEIALFKYRKARLEPGTAIGAIGAQSIGEPMNVTLG
VPRIKEIINASKVISTPIINAVLVNDNDERAARVVKGRVE
KTLLSDVAFYVQDVYKDNLSFIQVRIDLGTIDKLQLELTI
EDIAVAITRASKLKIQASDVNIIGKDRIAINVFPSENDVF
YRMQQLRRALPDVVVKGLPDISRAVINIRDDGKRELLVEG
YGLRDVMCTDGVIGSRTTTNHVLEVFSVLGIEAARYSIIR
EINYTMSNHGMSVDPRHIQLLGDVMTYKGEVLGITRFGLS
KMRDSVLQLASFEKTTDHLFDAAFYMKKDAVEGVSECIIL
GQTMSIGTGSFKVVKGTNISEKDLVPKRCLFESLSNEAAL
KAN
B:  DEINTAQDKWHLLPAFLKVKGLVKQHLDSFNYFVDTDLKK
IIKANQLILSDVDPEFYLKYVDIRVGKKSSSSTKDYLTPP
HECRLRDMTYSAPIYVDIEYTRGRNIIMHKDVEIGRMPIM
LRSNKCILYDADESKMAKLNECPLDPGGYFIVNGTEKVIL
VQEQLSKNRIIVEADEKKGIVQASVTSSTHERKSKTYVIT
KNGKIYLKHNSIAEEIPIAIVLKACGILSDLEIMQLVCGN
DSSYQDIFAVNLEESSKLDIYTQQQALEYIGAKVKTMRRQ
KLTILQEGIEAIATTVIAHLTVEALDFREKALYIAMMTRR
VVMAMYNPKMIDDRDYVGNKRLELAGQLISLLFEDLFKKF
NNDFKLSIDKVLKKPNRAMEYDALLSINVHSNNITSGLNR
AISTGNWSLKRFKMERAGVTHVLSRLSYISALGMMTRISS
QFEKSRKVSGPRALQPSQFGMLCTADTPEGEACGLVKNLA
LMTHITTDDEEEPIKKLCYVLGVEDITLIDSASLHLNYGV
YLNGTLIGSIRFPTKFVTQFRHLRRTGKVSEFISIYSNSH
QMAVHIATDGGRICRPLIIVSDGQSRVKDIHLRKLLDGEL
DFDDFLKLGLVEYLDVNEENDSYIALYEKDIVPSMTHLEI
EPFTILGAVAGLIPYPHHNQSPRNTYQCAMGKQAIGAIAY
NQFKRIDTLLYLMTYPQQPMVKTKTIELIDYDKLPAGQNA
TVAVMSYSGYDIEDALVLNKSSIDRGFGRCETRRKTTTVL
KRYANHTQDIIGGMRVDENGDPIWQHQSLGPDGLGEVGMK
VQSGQIYINKSVPTNSADAPNPNNVNVQTQYREAPVIYRG
PEPSHIDQVMMSVSDNDQALIKVLLRQNRRPELGDKFSSR
HGQKGVCGIIVKQEDMPFNDQGIVPDIIMNPHGFPSRMTV
GKMIELISGKAGVLNGTLEYGTCFGGSKLEDMSKILVDQG
FNYSGKDMLYSGITGECLQAYIFFGPIYYQKLKHMVLDKM
HARARGPRAVLTRQPTEGRSRDGGLRLGEMERDCVIAYGA
SQLLLERLMISSDAFEVDVCDKCGLMGYSGWCTTCKSAEN
IIKMTIPYAAKLLFQELLSMNIAPRLRLEDIFQQ
C:  MSNIVGIEYNRVTNTTSTDFPGFSKDAENEWNVEKFKKDF
EVNISSLDAREANFDLINIDTSIANAFRRIMISEVPSVAA
EYVYFFNNTSVIQDEVLAHRIGLVPLKVDPDMLTWVDSNL
PDDEKFTDENTIVLSLNVKCTRNPDAPKGSTDPKELYNNA
HVYARDLKFEPQGRQSTTFADCPVVPADPDILLAKLRPGQ
EISLKAHCILGIGGDHAKFSPVSTASYRLLPQINILQPIK
GESARRFQKCFPPGVIGIDEGSDEAYVKDARKDTVSREVL
RYEEFADKVKLGRVRNHFIFNVESAGAMTPEEIFFKSVRI
LKNKAEYLKNCPITQ
D:  MKVLEERNAFLSDYEVLKFLTDLEKKHLWDQKSLAPELQG
ITRNVVNYLSINKNFMSDESFAELMTKLNSFKLFKAEKLQ
IVNQLPANMVHLYSIVEECDARFDEKTIEEMLEIISGYA
E:  MDQENERNISRLWRAFRTVKEMVKDRGYFITQEEVELPLE
DFKAKYCDSMGRPQRKMMSFQANPTEESISKFPDMGSLWV
EFCDEPSVGVKTMKTFVIHIQEKNFQTGIFVYQNNITPSA
MKLVPSIPPATIETFNEAALVVNITHHELVPKHIRLSSDE
KRELLKRYRLKESQLPRIQRADPVALYLGLKRGEVVKIIR
KSETSGRYASYRICM
F:  EKAIPKDQRATTPYMTKYERARILGTRALQISMNAPVFVD
LEGETDPLRIAMKELAEKKIPLVIRRYLPDGSFEDWSVEE
LIV
G:  FILSKIADLVRIPPDQFHRDTISAITHQLNNKFANKIIPN
VGLCITIYDLLTVEEGQLKPGDGSSYINVTFRAVVFKPFL
GEIVTGWISKCTAEGIKVSLLGIFDDIFIPQNMLFEGCYY
TPEESAWIWPKLYFDVNEKIRFRIEREVFVDVKPKSPKEK
PPAYALLGSCQTDGMGLVSWWE
H:  MSNTLFDDIFQVSEVDPGRYNKVCRIEAASTTQDQCKLTL
DINVELFPVAAQDSLTVTIASSLNLEDSATRSWRPPQAGD
RSLADDYDYVMYGTAYKFEEVSKDLIAVYYSFGGLLMRLE
GNYRNLNNLKQENAYLLIRR
I:  MLSFCPSCNNMLLITSGDSGVYTLACRSCPYEFPIEGIEI
YDNVDQTKTQCPNYDTCGGESAYFFQLQIRSADEPMTTFY
KCVNCGHRWKEN
J:  MIVPVRCFSCGKVVGDKWESYLNLLQEDELDEGTALSRLG
LKRYCCRRMILTHVDLIEKFLRYNPLE
K:  PDREKIKLLTQATSEDGTSASFQIVEEDHTLGNALRYVIM
KNPDVEFCGYSIPHPSENLLNIRIQTYGETTAVDALQKGL
KDLMDLCDVVESKFTEKIKSM
L:  TLKYICAECSSKLSLSRTDAVRCKDCGHRILLKARTKRLV
QFEAR
M:  IEEFPLKISGEEESLHVFQYANRPRLVGRKPAEHPFISAA
RYKPKSHLWEIDIPLDEQAFYNKDKAESEWNGVNVQTLKG
VGVENNGQYAAFVKDMQVYLVPIERVAQLKPFFKYIDDAN
VTRKQENRLTGSLLAHKVADEEANIELTWAEGTFEQFKDT
IVKE
N:  KEAAAELELLNADHQHILRKLKKMNNKPERFMVFQLPTRL
PAFERPAVGSIRVHKSGKLSVKIGNVVMDIGKGAETTFLQ
DVIALSIADDASSAELLGRVDGKIVVTPQI
O:  VMTISSLEQRTLNPDLFLYKELVKAHLGERAASVIGMLVA
LGRLSVRELVEKIDGMDVDSVKTTLVSLTQLRCVKYLQET
AISGKKTTYYYYNEEGIHILLYSGLIIDEIITQMRVNDEE
EHKQLVAEIVQNVISLGSLTVEDYLSSVTSDSMKYTISSL
FVQLCEMGYLIQISKLHYTPIEDLWQFLYEKHYKNIPRNS
PLSDLKKRSQAKMNAKTDFAKIINKPNELSQILTVDPKTS
LRIVKPTVSLTINLDRFMKGRRSKQLINLAKTRVGSVTAQ
VYKIALRLTEQKSPKIRDPLTQTGLLQDLEEAKSFQDEAE
LVEEKTPGLTFNAIDLARHLPSASLINSHLKILASSNFPF
LNETKPGVYYVPYSKLMPVLKSSVYEYVIASTLGPSAMRL
SRCIRDNKLVSEKIINSTALMKEKDIRSTLASLIRYNSVE
IQEVPRTADRSASRAVFLFRCKETHSYNFMRQNLEWNMAN
LLFKKEKLKQENSTLLKKANRDDLLPSELNQLKMVNEREL
NVFARLSRLLSLWEVFQMA
P:  DIEFINSLLTIVWRFISENYSTTQEILEFITAAQVANVEL
TPSNIRSLCEVLVYDDKLEKVTHDCYRVTLESILQMSKHD
KEVVYFDEW
Q:  PINGPITNKERSLAVKYINFGKTVKDGPXXXXXXXXXXXX
XXXXXXX
Description (1)  DNA-DIRECTED RNA POLYMERASE III SUBUNIT RPC1 (E.C.2.7.7.6), DNA-DIRECTED RNA POLYMERASE III SUBUNIT RPC2 (E.C.2.7.7.6), DNA-DIRECTED RNA POLYMERASES I AND III SUBUNIT RPAC1, DNA-DIRECTED RNA POLYMERASE III SUBUNIT RPC9, DNA-DIRECTED RNA POLYMERASES I, II, AND III SUBUNIT RPABC 1, DNA-DIRECTED RNA POLYMERASES I, II, AND III SUBUNIT RPABC 2, DNA-DIRECTED RNA POLYMERASE III SUBUNIT RPC8, DNA-DIRECTED RNA POLYMERASES I, II, AND III SUBUNIT RPABC 3, DNA-DIRECTED RNA POLYMERASE III SUBUNIT RPC10, DNA-DIRECTED RNA POLYMERASES I, II, AND III SUBUNIT RPABC 5, DNA-DIRECTED RNA POLYMERASES I AND III SUBUNIT RPAC2, DNA-DIRECTED RNA POLYMERASES I, II, AND III SUBUNIT RPABC 4, DNA-DIRECTED RNA POLYMERASE III SUBUNIT RPC5, DNA-DIRECTED RNA POLYMERASE III SUBUNIT RPC4, DNA-DIRECTED RNA POLYMERASE III SUBUNIT RPC3, DNA-DIRECTED RNA POLYMERASE III SUBUNIT RPC6, DNA-DIRECTED RNA POLYMERASE III SUBUNIT RPC7


Functional site

1) chain A
residue 67
type
sequence C
description BINDING SITE FOR RESIDUE ZN A 2000
source : AC1

2) chain A
residue 69
type
sequence T
description BINDING SITE FOR RESIDUE ZN A 2000
source : AC1

3) chain A
residue 70
type
sequence C
description BINDING SITE FOR RESIDUE ZN A 2000
source : AC1

4) chain A
residue 77
type
sequence C
description BINDING SITE FOR RESIDUE ZN A 2000
source : AC1

5) chain A
residue 80
type
sequence H
description BINDING SITE FOR RESIDUE ZN A 2000
source : AC1

6) chain A
residue 107
type
sequence C
description BINDING SITE FOR RESIDUE ZN A 2001
source : AC2

7) chain A
residue 109
type
sequence N
description BINDING SITE FOR RESIDUE ZN A 2001
source : AC2

8) chain A
residue 110
type
sequence C
description BINDING SITE FOR RESIDUE ZN A 2001
source : AC2

9) chain A
residue 154
type
sequence C
description BINDING SITE FOR RESIDUE ZN A 2001
source : AC2

10) chain A
residue 156
type
sequence H
description BINDING SITE FOR RESIDUE ZN A 2001
source : AC2

11) chain A
residue 157
type
sequence C
description BINDING SITE FOR RESIDUE ZN A 2001
source : AC2

12) chain B
residue 1095
type
sequence C
description BINDING SITE FOR RESIDUE ZN B 2000
source : AC3

13) chain B
residue 1097
type
sequence K
description BINDING SITE FOR RESIDUE ZN B 2000
source : AC3

14) chain B
residue 1098
type
sequence C
description BINDING SITE FOR RESIDUE ZN B 2000
source : AC3

15) chain B
residue 1107
type
sequence C
description BINDING SITE FOR RESIDUE ZN B 2000
source : AC3

16) chain B
residue 1110
type
sequence C
description BINDING SITE FOR RESIDUE ZN B 2000
source : AC3

17) chain I
residue 5
type
sequence C
description BINDING SITE FOR RESIDUE ZN I 2000
source : AC4

18) chain I
residue 8
type
sequence C
description BINDING SITE FOR RESIDUE ZN I 2000
source : AC4

19) chain I
residue 26
type
sequence C
description BINDING SITE FOR RESIDUE ZN I 2000
source : AC4

20) chain I
residue 29
type
sequence C
description BINDING SITE FOR RESIDUE ZN I 2000
source : AC4

21) chain J
residue 7
type
sequence C
description BINDING SITE FOR RESIDUE ZN J 2000
source : AC5

22) chain J
residue 10
type
sequence C
description BINDING SITE FOR RESIDUE ZN J 2000
source : AC5

23) chain J
residue 45
type
sequence C
description BINDING SITE FOR RESIDUE ZN J 2000
source : AC5

24) chain J
residue 46
type
sequence C
description BINDING SITE FOR RESIDUE ZN J 2000
source : AC5

25) chain L
residue 31
type
sequence C
description BINDING SITE FOR RESIDUE ZN L 2000
source : AC6

26) chain L
residue 34
type
sequence C
description BINDING SITE FOR RESIDUE ZN L 2000
source : AC6

27) chain L
residue 48
type
sequence C
description BINDING SITE FOR RESIDUE ZN L 2000
source : AC6

28) chain L
residue 51
type
sequence C
description BINDING SITE FOR RESIDUE ZN L 2000
source : AC6

29) chain C
residue 65-105
type prosite
sequence NAFRRIMISEVPSVAAEYVYFFNNTSVIQDEVLAHRIGLV
P
description RNA_POL_D_30KD RNA polymerases D / 30 to 40 Kd subunits signature. NAFRRimisevpsvAaeyVyffnNtSviqDEvLAhRIGLVP
source prosite : PS00446

30) chain I
residue 4-29
type prosite
sequence FCPSCNNMLLITSGDSGVYTLACRSC
description RNA_POL_M_15KD RNA polymerases M / 15 Kd subunits signature. FCPSCNNMLlitsgdsgvytla.CrsC
source prosite : PS01030

31) 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

32) 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

33) 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

34) chain K
residue 65-96
type prosite
sequence IVEEDHTLGNALRYVIMKNPDVEFCGYSIPHP
description RNA_POL_L_13KD RNA polymerases L / 13 to 16 Kd subunits signature. IveEdHTLgNaLryvImknpdVefcgYsipHP
source prosite : PS01154

35) chain B
residue 909-921
type prosite
sequence GDKFSSRHGQKGV
description RNA_POL_BETA RNA polymerases beta chain signature. GdKFSSrHGQKGV
source prosite : PS01166

36) chain A
residue 515
type MOD_RES
sequence D
description Phosphothreonine => ECO:0007744|PubMed:18407956
source Swiss-Prot : SWS_FT_FI1

37) chain J
residue 45
type MOD_RES
sequence C
description Phosphothreonine => ECO:0007744|PubMed:18407956
source Swiss-Prot : SWS_FT_FI1

38) chain J
residue 46
type MOD_RES
sequence C
description Phosphothreonine => ECO:0007744|PubMed:18407956
source Swiss-Prot : SWS_FT_FI1

39) chain A
residue 107
type MOD_RES
sequence C
description Phosphothreonine => ECO:0007744|PubMed:18407956
source Swiss-Prot : SWS_FT_FI1

40) chain A
residue 110
type MOD_RES
sequence C
description Phosphothreonine => ECO:0007744|PubMed:18407956
source Swiss-Prot : SWS_FT_FI1

41) chain A
residue 154
type MOD_RES
sequence C
description Phosphothreonine => ECO:0007744|PubMed:18407956
source Swiss-Prot : SWS_FT_FI1

42) chain A
residue 511
type MOD_RES
sequence D
description Phosphothreonine => ECO:0007744|PubMed:18407956
source Swiss-Prot : SWS_FT_FI1

43) chain A
residue 513
type MOD_RES
sequence D
description Phosphothreonine => ECO:0007744|PubMed:18407956
source Swiss-Prot : SWS_FT_FI1

44) chain L
residue 48
type MOD_RES
sequence C
description Phosphoserine => ECO:0007744|PubMed:19779198
source Swiss-Prot : SWS_FT_FI2

45) chain L
residue 51
type MOD_RES
sequence C
description Phosphoserine => ECO:0007744|PubMed:19779198
source Swiss-Prot : SWS_FT_FI2

46) chain I
residue 8
type MOD_RES
sequence C
description Phosphoserine => ECO:0007744|PubMed:17287358
source Swiss-Prot : SWS_FT_FI3

47) chain I
residue 26
type MOD_RES
sequence C
description Phosphoserine => ECO:0007744|PubMed:17287358
source Swiss-Prot : SWS_FT_FI3

48) chain I
residue 29
type MOD_RES
sequence C
description Phosphoserine => ECO:0007744|PubMed:17287358
source Swiss-Prot : SWS_FT_FI3

49) chain I
residue 100
type MOD_RES
sequence C
description Phosphothreonine => ECO:0007744|PubMed:17287358, ECO:0007744|PubMed:17330950
source Swiss-Prot : SWS_FT_FI4

50) chain I
residue 103
type MOD_RES
sequence C
description Phosphothreonine => ECO:0007744|PubMed:17287358, ECO:0007744|PubMed:17330950
source Swiss-Prot : SWS_FT_FI4


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