eF-site ID
|
6eu2-ABCDEFGHIJKLMNOPQ |
PDB Code
|
6eu2 |
Chain
|
A, B, C, D, E, F, G, H, I, J, K, L, M, N, O, P, Q |
|
|
|
Title
|
Apo RNA Polymerase III - open conformation (oPOL3) |
Classification
|
TRANSCRIPTION |
Compound
|
DNA-directed RNA polymerase III subunit RPC1 |
Source
|
ORGANISM_COMMON: Baker's yeast; ORGANISM_SCIENTIFIC: Saccharomyces cerevisiae (strain ATCC 204508 / S288c); |
|
Sequence
|
A: |
KEVVVSETPKRIKGLEFSALSAADIVAQSEVEVSTRDLFD
LEKDRAPKANGALDPKMGVSSSSLECATCHGNLASCHGHF
GHLKLALPVFHIGYFKATIQILQGICKNCSAILLSETDKR
QFLHELRRPGVDNLRRMGILKKILDQCKKQRRCLHCGALN
GVVKKAAALKIIHDTFRWVGKKSAPEKDIWVGEWKEVLAH
NPELERYVKRCMDDLNPLKTLNLFKQIKSADCELLGIDAT
VPSGRPETYIWRYLPAPPVCIRPSVMMQDSPASNEDDLTV
KLTEIVWTSSLIKAGLDKGISINNMMEHWDYLQLTVAMYI
NSGNLSGKRVDFSGRTVISPDPNLSIDEVAVPDRVAKVLT
YPEKVTRYNRHKLQELIVNGPNVHPGANYLLKRNEDARRN
LRYGDRMKLAKNLQIGDVVERHLEDGDVVLFNRQPSLHRL
SILSHYAKIRPWRTFRLNECVCTPYNADFDGDEMNLHVPQ
TEEARAEAINLMGVKNNLLTPKSGEPIIAATQDFITGSYL
ISHKDSFYDRATLTQLLSMMSDGIEHFDIPPPAIMKPYYL
WTGKQVFSLLIKPNHNSPVVINLDAKNKVFVPPKSKSLPN
EMSQNDGFVIIRGSQILSGVMDKSVLGDGKKHSVFYTILR
DYGPQEAANAMNRMAKLCARFLGNRGFSIGINDVTPADDL
KQKKEELVEIAYHKCDELITLFNKGELETQPGCNEEQTLE
AKIGGLLSKVREEVGDVCINELDNWNAPLIMATCGSKGST
LNVSQMVAVVGQQIISGNRVPDGFQDRSLPHFPKNSKTPQ
SKGFVRNSFFSGLSPPEFLFHAISGREGLVDTAVKTAETG
YMSRRLMKSLEDLSCQYDNTVRTSANGIVQFTYGGDGLDP
LEMEGNAQPVNFNRSWDHAYNITFNNQDKGLLPYAIMETA
NEILGPLEERLVRYDNSGCLVKREDLNKAEYVDQYDAERD
FYHSLREYINGKATALANLRKSRGMLGLLEPPAKELQGID
PDETVPDNVKTSVSQLYRISEKSVRKFLEIALFKYRKARL
EPGTAIGAIGAQSIGEPGTQMTLKTFHFAGVASMNVTLGV
PRIKEIINASKVISTPIINAVLVNDNDERAARVVKGRVEK
TLLSDVAFYVQDVYKDNLSFIQVRIDLGTIDKLQLELTIE
DIAVAITRASKLKIQASDVNIIGKDRIAINVFPSENDVFY
RMQQLRRALPDVVVKGLPDISRAVINIRDDGKRELLVEGY
GLRDVMCTDGVIGSRTTTNHVLEVFSVLGIEAARYSIIRE
INYTMSNHGMSVDPRHIQLLGDVMTYKGEVLGITRFGLSK
MRDSVLQLASFEKTTDHLFDAAFYMKKDAVEGVSECIILG
QTMSIGTGSFKVVKGTNISEKDLVPKRCLFESLSNEAALK
AN
|
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
TPEESAWIWPKLYFDVNEKIRFRIEREVFVDVKPKSPKER
ELEERAQEKPPAYALLGSCQTDGMGLVSWWE
|
H: |
MSNTLFDDIFQVSEVDPGRYNKVCRIEAASTTQDQCKLTL
DINVELFPVAAQDSLTVTIASSLNLEDSATRSWRPPQAGD
RSLADDYDYVMYGTAYKFEEVSKDLIAVYYSFGGLLMRLE
GNYRNLNNLKQENAYLLIRR
|
I: |
MLSFCPSCNNMLLITSGDSGVYTLACRSCPYEFPIEGIEI
YD
|
J: |
MIVPVRCFSCGKVVGDKWESYLNLLQEDELDEGTALSRLG
LKRYCCRRMILTHVDLIEKFLRYNPLEK
|
K: |
PDREKIKLLTQATSEDGTSASFQIVEEDHTLGNALRYVIM
KNPDVEFCGYSIPHPSENLLNIRIQTYGETTAVDALQKGL
KDLMDLCDVVESKFTEKIKSM
|
L: |
TLKYICAECSSKLSLSRTDAVRCKDCGHRILLKARTKRLV
QFEAR
|
M: |
IEEFPLKISGEEESLHVFQYANRPRLVGRKPAEHPFISAA
RYKPKSHLWEIDIPLDEQAFYNKDKAESEWNGVNVQTLKG
VGVENNGQYAAFVKDMQVYLVPIERVAQLKPFFKYIDDAN
VTRKQEQNRLTGSLLAHKVADEEANIELTWAEGTFEQFKD
TIVKE
|
N: |
KEAAAELELLNADHQHILRKLKKMNNKPERFMVFQLPTRL
PAVGSIRVHKSGKLSVKIGNVVMDIGKGAETTFLQDVIAL
SIADDASSAELLGRVDGKIVVTPQI
|
O: |
VMTISSLEQRTLNPDLFLYKELVKAHLGERAASVIGMLVA
LGRLSVRELVEKIDGMDVDSVKTTLVSLTQLRCVKYLQET
AISGKKTTYYYYNEEGIHILLYSGLIIDEIITQMRVNDEE
EHKQLVAEIVQNVISLGSLTVEDYLSSVTSDSMKYTISSL
FVQLCEMGYLIQISKLHYTPIEDLWQFLYEKHYKNIPRNS
PLSDLKKRSQAKMNAKTDFAKIINKPNELSQILTVDPKTS
LRIVKPTVSLTINLDRFMKGRRSKQLINLAKTRVGSVTAQ
VYKIALRLTEQKSPKIRDPLTQTGLLQDLEEAKSFQDEAE
LVEEKTPGLTFNAIDLARHLASLINSHLKILASSNFPFLN
ETKPGVYYVPYSKLMPVLKSSVYEYVIASTLGPSAMRLSR
CIRDNKLVSEKIINSTALMKEKDIRSTLASLIRYNSVEIQ
EVPRTADRSASRAVFLFRCKETHSYNFMRQNLEWNMANLL
FKKEKLKQENSTLLKKANRDDLLPSELNQLKMVNERELNV
FARLSRLLSLWEVFQMA
|
P: |
DIEFINSLLTIVWRFISENTFPNGFKNFENGPKKNVFYAP
NVKNYSTTQEILEFITAAQVANVELTPSNIRSLCEVLVYD
DKLEKVTHDCYRVTLESILQMFNYFKMFPASKHDKEVVYF
DEW
|
Q: |
EFPSIPLPINGPITNKERSLAVKYINFGKTVKDGPFYTGS
|
|
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 RPABC1, DNA-directed RNA polymerases I, II, and III subunit RPABC2, DNA-directed RNA polymerase III subunit RPC8, DNA-directed RNA polymerases I, II, and III subunit RPABC3, DNA-directed RNA polymerase III subunit RPC10, DNA-directed RNA polymerases I, II, and III subunit RPABC5, DNA-directed RNA polymerases I and III subunit RPAC2, DNA-directed RNA polymerases I, II, and III subunit RPABC4, 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
|
|
|
|
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 |
110 |
type |
|
sequence |
C
|
description |
binding site for residue ZN A 2001
|
source |
: AC2
|
|
8)
|
chain |
A |
residue |
154 |
type |
|
sequence |
C
|
description |
binding site for residue ZN A 2001
|
source |
: AC2
|
|
9)
|
chain |
A |
residue |
157 |
type |
|
sequence |
C
|
description |
binding site for residue ZN A 2001
|
source |
: AC2
|
|
10)
|
chain |
A |
residue |
511 |
type |
|
sequence |
D
|
description |
binding site for residue MG A 2002
|
source |
: AC3
|
|
11)
|
chain |
A |
residue |
513 |
type |
|
sequence |
D
|
description |
binding site for residue MG A 2002
|
source |
: AC3
|
|
12)
|
chain |
A |
residue |
515 |
type |
|
sequence |
D
|
description |
binding site for residue MG A 2002
|
source |
: AC3
|
|
13)
|
chain |
B |
residue |
1095 |
type |
|
sequence |
C
|
description |
binding site for residue ZN B 1201
|
source |
: AC4
|
|
14)
|
chain |
B |
residue |
1097 |
type |
|
sequence |
K
|
description |
binding site for residue ZN B 1201
|
source |
: AC4
|
|
15)
|
chain |
B |
residue |
1098 |
type |
|
sequence |
C
|
description |
binding site for residue ZN B 1201
|
source |
: AC4
|
|
16)
|
chain |
B |
residue |
1107 |
type |
|
sequence |
C
|
description |
binding site for residue ZN B 1201
|
source |
: AC4
|
|
17)
|
chain |
I |
residue |
5 |
type |
|
sequence |
C
|
description |
binding site for residue ZN I 201
|
source |
: AC5
|
|
18)
|
chain |
I |
residue |
8 |
type |
|
sequence |
C
|
description |
binding site for residue ZN I 201
|
source |
: AC5
|
|
19)
|
chain |
I |
residue |
29 |
type |
|
sequence |
C
|
description |
binding site for residue ZN I 201
|
source |
: AC5
|
|
20)
|
chain |
J |
residue |
7 |
type |
|
sequence |
C
|
description |
binding site for residue ZN J 101
|
source |
: AC6
|
|
21)
|
chain |
J |
residue |
10 |
type |
|
sequence |
C
|
description |
binding site for residue ZN J 101
|
source |
: AC6
|
|
22)
|
chain |
J |
residue |
43 |
type |
|
sequence |
R
|
description |
binding site for residue ZN J 101
|
source |
: AC6
|
|
23)
|
chain |
J |
residue |
45 |
type |
|
sequence |
C
|
description |
binding site for residue ZN J 101
|
source |
: AC6
|
|
24)
|
chain |
J |
residue |
46 |
type |
|
sequence |
C
|
description |
binding site for residue ZN J 101
|
source |
: AC6
|
|
25)
|
chain |
L |
residue |
31 |
type |
|
sequence |
C
|
description |
binding site for residue ZN L 101
|
source |
: AC7
|
|
26)
|
chain |
L |
residue |
34 |
type |
|
sequence |
C
|
description |
binding site for residue ZN L 101
|
source |
: AC7
|
|
27)
|
chain |
L |
residue |
48 |
type |
|
sequence |
C
|
description |
binding site for residue ZN L 101
|
source |
: AC7
|
|
28)
|
chain |
L |
residue |
51 |
type |
|
sequence |
C
|
description |
binding site for residue ZN L 101
|
source |
: AC7
|
|
29)
|
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
|
|
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 |
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
|
|
32)
|
chain |
B |
residue |
909-921 |
type |
prosite |
sequence |
GDKFSSRHGQKGV
|
description |
RNA_POL_BETA RNA polymerases beta chain signature. GdKFSSrHGQKGV
|
source |
prosite : PS01166
|
|
33)
|
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
|
|
34)
|
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
|
|
35)
|
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
|
|
36)
|
chain |
A |
residue |
515 |
type |
MOD_RES |
sequence |
D
|
description |
Phosphoserine => ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198
|
source |
Swiss-Prot : SWS_FT_FI1
|
|
37)
|
chain |
J |
residue |
45 |
type |
MOD_RES |
sequence |
C
|
description |
Phosphoserine => ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198
|
source |
Swiss-Prot : SWS_FT_FI1
|
|
38)
|
chain |
J |
residue |
46 |
type |
MOD_RES |
sequence |
C
|
description |
Phosphoserine => ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198
|
source |
Swiss-Prot : SWS_FT_FI1
|
|
39)
|
chain |
A |
residue |
107 |
type |
MOD_RES |
sequence |
C
|
description |
Phosphoserine => ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198
|
source |
Swiss-Prot : SWS_FT_FI1
|
|
40)
|
chain |
A |
residue |
110 |
type |
MOD_RES |
sequence |
C
|
description |
Phosphoserine => ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198
|
source |
Swiss-Prot : SWS_FT_FI1
|
|
41)
|
chain |
A |
residue |
154 |
type |
MOD_RES |
sequence |
C
|
description |
Phosphoserine => ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198
|
source |
Swiss-Prot : SWS_FT_FI1
|
|
42)
|
chain |
A |
residue |
511 |
type |
MOD_RES |
sequence |
D
|
description |
Phosphoserine => ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198
|
source |
Swiss-Prot : SWS_FT_FI1
|
|
43)
|
chain |
A |
residue |
513 |
type |
MOD_RES |
sequence |
D
|
description |
Phosphoserine => ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198
|
source |
Swiss-Prot : SWS_FT_FI1
|
|
44)
|
chain |
L |
residue |
48 |
type |
MOD_RES |
sequence |
C
|
description |
Phosphoserine => ECO:0007744|PubMed:17330950, 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:17330950, ECO:0007744|PubMed:19779198
|
source |
Swiss-Prot : SWS_FT_FI2
|
|