eF-site ID
|
4c3h-ABCDEFGHIJKLMN |
PDB Code
|
4c3h |
Chain
|
A, B, C, D, E, F, G, H, I, J, K, L, M, N |
|
click to enlarge
|
|
Title
|
Structure of 14-subunit RNA polymerase I at 3.27 A resolution, crystal form C2-93 |
Classification
|
TRANSCRIPTION |
Compound
|
DNA-DIRECTED RNA POLYMERASE I SUBUNIT RPA190 |
Source
|
ORGANISM_COMMON: BAKER'S YEAST; ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE; |
|
Sequence
|
A: |
MDISKPVGSEITSVDFGILTAKEIRNLSAKQITNPTVLDN
LGHPVSGGLYDLALGAFLRNLCSTCGLDEKFCPGHQGHIE
LPVPCYNPLFFNQLYIYLRASCLFCHHFRLKSVEVHRYAC
KLRLLQYGLIDESYKLDEITLDISSTLLNELKSKRSEYVD
MAIAKALSDGRTTERGSFTATVNDERKKLVHEFHKKLLSR
GKCDNCGMFSPKFRKDGFTKIFETALNEKQITNNRVKGFI
RQDMISTYILSTEVKNILDTVFRKEQCVLQYVFHSRPNLS
RKLVKADSFFMDVLVVPPTRFRLPSKLGEEVHENSQNQLL
SKVLTTSLLIRDLNDDLSKLKVSLEDRRVIFSRLMNAFVT
IQNDVNAFIDSTKAQGRTVPIPGVKQALEKKEGLFRKHMM
GKRVNYAARSVISPDPNIETNEIGVPPVFAVKLTYPEPVT
AYNIAELRQAVINGPDKWPGATQIQNEDGSLVSLIGMSVE
QRKALANQLLTPSSNVSTHTLNKKVYRHIKNRDVVLMNRQ
PTLHKASMMGHKVRVLPNEKTLRLHYANTGAYNADFDGDE
MNMHFPQNENARAEALNLANTDSQYLTPTSGSPVRGLIQD
HISAGVWLTSKDSFFTREQYQQYIYGCIRPEDGHTTRSKI
VTLPPTIFKPYPLWTGKQIITTVLLNVTPPDMPGINLISK
NKIKNEYWGKGSLENEVLFKDGALLCGILDKSQYGASKYG
IVHSLHEVYGPEVAAKVLSVLGRLFTNYITATAFTCGMDD
LRLTAEGNKWRTDILKTSVDTGREAAAEVTNLDKDTPADD
PELLKRLQEILRDNNKSGILDAVTSSKVNAITSQVVSKCV
PDGTMKKFPCNSMQAMALSGAKGSNVNVSQIMCLLGQQAL
EGRRVPVMVSGKTLPSFKPYETDAMAGGYVKGRFYSGIKP
QEYYFHCMAGREGLIDTAVKTSRSGYLQRCLTKQLEGVHV
SYDNSIRDADGTLVQFMYGGDAIDITKESHMTQFEFCLDN
YYALLKKYNPSALIEHLDVESALKYSKKTLKYRKKHSKEP
HYKQSVKYDPVLAKYNPAKYLGSVSENFQDKLESFLDKNS
KGVNEKKFRALMQLKYMRSLINPGEAVGIIASQSVGEPST
QMTLNTFNVTLGIPRLREIVMTASAAIKTPQMTLPIWNDV
SDEQADTFCKSISKVLLSEVIDKVIVTETTGTARSYVIHM
RFFDNNEYSEEYDVSKEELQNVISNQFIHLLEAAIVKEIK
KQKRTTGPDIGVAVPRLQNSKRLEEDNDEEQSHKKTKQAV
SYDEPDEDEIETMREAENMNKVQRDRQSAIISHHRFITKY
NFDDESGKWCEFKLELAADTEKLLMVNIVEEICRKSIIRQ
IPHIDRCVHPEPENGKRVLVTEGVNFQAMWDQEAFIDVDG
ITSNDVAAVLKTYGVEAARNTIVNEINNVFSRYAISVSFR
HLDLIADMMTRQGTYLAFNRQGMETSTSSFMKMSYETTCQ
FLTKAVLDNEREQLDSPSARIVVGKLNNVGTGSFDVLAKV
PNA
|
B: |
RTADFRTLERESRFINPPKDKSAFPLLQEAVQPHIGSFNA
LTEGPDGGLLNLGVKDIGEKVIFDGKPLNSEEISNSGYLG
NKLSVSVEQVSIAKPMSNDSAVERKVYPSESRQRLTSYRG
KLLLKLKWSVNNGEENLFEVRDCGGLPVMLQSNRCHLNKM
SPYELVQHKEESDEIGGYFIVNGIEKLIRMLIVQRRNHPM
AIIRPSFANRGASYSHYGIQIRSVRPDQTSQTNVLHYLND
GQVTFRFSWRKNEYLVPVVMILKALCHTSDREIFDGIIGN
DVKDSFLTDRLELLLRGFKKRYPHLQNRTQVLQYLGDKFR
VVFQASPDQSDLEVGQEVLDRIVLVHLGKDGSQDKFRMLL
FMIRKLYSLVAGECSPDNPDATQHQEVLLGGFLYGMILKE
KIDEYLQNIIAQVRMDINRGMAINFKDKRYMSRVLMRVNE
NIGSKMQYFLSTGNLVSQSGLDLQQVSGYTVVAEKINFYR
FISHFRMVHRGSFFAQLKTTTVRKLLPESWGFLCPVHTPD
GSPCGLLNHFAHKCRISTQQSDVSRIPSILYSLGVAPASH
TFAAGPSLCCVQIDGKIIGWVSHEQGKIIADTLRYWKVEG
KTPGLPIDLEIGYVPPSTRGQYPGLYLFGGHSRMLRPVRY
LPLDKEDIVGPFEQVYMNIAVTPQEIQNNVHTHVEFTPTN
ILSILANLTPFSDFNQSPRNMYQCQMGKQTMGTPGVALCH
RSDNKLYRLQTGQTPIVKANLYDDYGMDNFPNGFNAVVAV
ISYTGYDMDDAMIINKSADERGFGYGTMYKTEKVDLALDP
ITQHFGFGNDEWPKEWLEKLDEDGLPYIGTYVEEGDPICA
YFDDTLNKTKIKTYHSSEPAYIEEVNLIGDESNKFQELQT
VSIKYRIRRTPQIGDKFSSRHGQKGVCSRKWPTIDMPFSE
TGIQPDIIINPHAFPSRMTIGMFVESLAGKAGALHGIAQD
STPWIFNEDDTPADYFGEQLAKAGYNYHGNEPMYSGATGE
ELRADIYVGVVYYQRLRHMVNDKFQVRSTGPVNSLTMQPV
KGRKRHGGIRVGEMERDALIGHGTSFLLQDRLLNSSDYTQ
ASVCRECGSILTTQQSVPRIGSISTVCCRRCSMRFEDAKK
GEKIFIDDSQIWEDGQGNKFVGGNETTTVAIPFVLKYLDS
ELSAMGIRLRYNVEPK
|
C: |
EWNVEKFKKDFEVNISSLDAREANFDLINIDTSIANAFRR
IMISEVPSVAAEYVYFFNNTSVIQDEVLAHRIGLVPLKVD
PDMLTWVDSNLPDDEKFTDENTIVLSLNVKCTRNPDAPST
DPKELYNNAHVYARDLKFEPQGRQSTTFADCPVVPADPDI
LLAKLRPGQEISLKAHCILGIGGDHAKFSPVSTASYRLLP
QINILQPIKGESARRFQKCFPPGVIGIDEGSDEAYVKDAR
KDTVSREVLRYEEFADKVKLGRVRNHFIFNVESAGAMTPE
EIFFKSVRILKNKAEYLKNCPITQ
|
D: |
SATTLNTPVVIHATQLPQHVSTDEVLQFLESFIDEKENTN
LSSSISQLKRIQRDFKGLP
|
E: |
MDQENERNISRLWRAFRTVKEMVKDRGYFITQEEVELPLE
DFKAKYCDSMGRPQRKMMSFQANPTEESISKFPDMGSLWV
EFCDEPSVGVKTMKTFVIHIQEKNFQTGIFVYQNNITPSA
MKLVPSIPPATIETFNEAALVVNITHHELVPKHIRLSSDE
KRELLKRYRLKESQLPRIQRADPVALYLGLKRGEVVKIIR
KSETSGRYASYRICM
|
F: |
PEDFQQHEQIRRKTLKEKAIPKDQRATTPYMTKYERARIL
GTRALQISMNAPVFVDLEGETDPLRIAMKELAEKKIPLVI
RRYLPDGSFEDWSVEELIVD
|
G: |
NENRETARFIKKHKKQVTNPIDEKNGTSNCIVRVPIALYV
SLAPMYLENPLQGVMKQHLNPLVMKYNNKVGGVVLGYEGL
KILDADPLDTSEKLIKITPDTPFGFTWCHVNLYVWQPQVG
DVLEGYIFIQSASHIGLLIHDAFNASIKKNNIPVDWTFVH
NDVELGHWVDSNGEPIDGKLRFTVRNVHTTGRVVSVDGTL
ISYNSSRSQAESLPIVSNKKIVFDDEVSIENKESHKELDL
PEVKEDNGSEIVYEENTSE
|
H: |
NTLFDDIFQVSEVDPGRYNKVCRIEAASTTQDQCKLTLDI
NVELFPVAAQDSLTVTIASSLNATRSWRPPQAGDRSLADD
YDYVMYGTAYKFEEVSKDLIAVYYSFGGLLMRLEGNYRNL
NNLKQENAYLLIRR
|
I: |
SVVGSLIFCLDCGDLLENPNAVLGSNVECSQCKAIYPKSQ
FSNLKVVTTTADDAFPSSLRAKKSVVKTSLKKNELKDGAT
IKEKCPQCGNEEMNYHTLQLRSADEGATVFYTCTSCGYKF
RTNN
|
J: |
MIVPVRCFSCGKVVGDKWESYLNLLQEDELDEGTALSRLG
LKRYCCRRMILTHVDLIEKFLRYNPLEKR
|
K: |
EEPDREKIKLLTQATSEDGTSASFQIVEEDHTLGNALRYV
IMKNPDVEFCGYSIPHPSENLLNIRIQTYGETTAVDALQK
GLKDLMDLCDVVESKFTEKIKSM
|
L: |
TLKYICAECSSKLSLSRTDAVRCKDCGHRILLKARTKRLV
QFEAR
|
M: |
SEIEIESVQDQPSVAVGSFFKGFRAPSDTTFDLYKKKEKD
EFVLHGENERLEYEGYTDSSSQASNQYVVGLFNPEKKSIQ
LYKAPVLVSKVVSKSSKNLRGPKIK
|
N: |
FSIPDGFKKCKHLKNFPLNGDNKQQQVWLIKFPSNVDISK
LKSLPVDFESSTTMTIDKHDYKIMDDTDNMTLLVPSESKE
SLKIASTAPLQFDKVFSVSETAKIPAIDYSKVRVPRKDVP
KVEGLKLEHFATGYDAEDF
|
|
Description
|
(1) |
DNA-DIRECTED RNA POLYMERASE I SUBUNIT RPA190 (E.C.2.7.7.6), DNA-DIRECTED RNA POLYMERASE I SUBUNIT RPA135 (E.C.2.7.7.6), DNA-DIRECTED RNA POLYMERASES I AND III SUBUNIT RPAC1, DNA-DIRECTED RNA POLYMERASE I SUBUNIT RPA14, 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 I SUBUNIT RPA43, DNA-DIRECTED RNA POLYMERASES I, II, AND III SUBUNIT RPABC 3, DNA-DIRECTED RNA POLYMERASE I SUBUNIT RPA12, 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 I SUBUNIT RPA49, DNA-DIRECTED RNA POLYMERASE I SUBUNIT RPA34
|
|
|
|
1)
|
chain |
A |
residue |
102 |
type |
|
sequence |
C
|
description |
BINDING SITE FOR RESIDUE ZN A 2664
|
source |
: AC1
|
|
2)
|
chain |
A |
residue |
105 |
type |
|
sequence |
C
|
description |
BINDING SITE FOR RESIDUE ZN A 2664
|
source |
: AC1
|
|
3)
|
chain |
A |
residue |
233 |
type |
|
sequence |
C
|
description |
BINDING SITE FOR RESIDUE ZN A 2664
|
source |
: AC1
|
|
4)
|
chain |
A |
residue |
236 |
type |
|
sequence |
C
|
description |
BINDING SITE FOR RESIDUE ZN A 2664
|
source |
: AC1
|
|
5)
|
chain |
A |
residue |
62 |
type |
|
sequence |
C
|
description |
BINDING SITE FOR RESIDUE ZN A 2665
|
source |
: AC2
|
|
6)
|
chain |
A |
residue |
65 |
type |
|
sequence |
C
|
description |
BINDING SITE FOR RESIDUE ZN A 2665
|
source |
: AC2
|
|
7)
|
chain |
A |
residue |
72 |
type |
|
sequence |
C
|
description |
BINDING SITE FOR RESIDUE ZN A 2665
|
source |
: AC2
|
|
8)
|
chain |
A |
residue |
75 |
type |
|
sequence |
H
|
description |
BINDING SITE FOR RESIDUE ZN A 2665
|
source |
: AC2
|
|
9)
|
chain |
B |
residue |
1104 |
type |
|
sequence |
C
|
description |
BINDING SITE FOR RESIDUE ZN B 2204
|
source |
: AC3
|
|
10)
|
chain |
B |
residue |
1107 |
type |
|
sequence |
C
|
description |
BINDING SITE FOR RESIDUE ZN B 2204
|
source |
: AC3
|
|
11)
|
chain |
B |
residue |
1128 |
type |
|
sequence |
C
|
description |
BINDING SITE FOR RESIDUE ZN B 2204
|
source |
: AC3
|
|
12)
|
chain |
B |
residue |
1131 |
type |
|
sequence |
C
|
description |
BINDING SITE FOR RESIDUE ZN B 2204
|
source |
: AC3
|
|
13)
|
chain |
L |
residue |
31 |
type |
|
sequence |
C
|
description |
BINDING SITE FOR RESIDUE ZN L 1071
|
source |
: AC4
|
|
14)
|
chain |
L |
residue |
34 |
type |
|
sequence |
C
|
description |
BINDING SITE FOR RESIDUE ZN L 1071
|
source |
: AC4
|
|
15)
|
chain |
L |
residue |
48 |
type |
|
sequence |
C
|
description |
BINDING SITE FOR RESIDUE ZN L 1071
|
source |
: AC4
|
|
16)
|
chain |
L |
residue |
51 |
type |
|
sequence |
C
|
description |
BINDING SITE FOR RESIDUE ZN L 1071
|
source |
: AC4
|
|
17)
|
chain |
J |
residue |
7 |
type |
|
sequence |
C
|
description |
BINDING SITE FOR RESIDUE ZN J 1070
|
source |
: AC5
|
|
18)
|
chain |
J |
residue |
10 |
type |
|
sequence |
C
|
description |
BINDING SITE FOR RESIDUE ZN J 1070
|
source |
: AC5
|
|
19)
|
chain |
J |
residue |
45 |
type |
|
sequence |
C
|
description |
BINDING SITE FOR RESIDUE ZN J 1070
|
source |
: AC5
|
|
20)
|
chain |
J |
residue |
46 |
type |
|
sequence |
C
|
description |
BINDING SITE FOR RESIDUE ZN J 1070
|
source |
: AC5
|
|
21)
|
chain |
I |
residue |
10 |
type |
|
sequence |
C
|
description |
BINDING SITE FOR RESIDUE ZN I 1126
|
source |
: AC6
|
|
22)
|
chain |
I |
residue |
13 |
type |
|
sequence |
C
|
description |
BINDING SITE FOR RESIDUE ZN I 1126
|
source |
: AC6
|
|
23)
|
chain |
I |
residue |
30 |
type |
|
sequence |
C
|
description |
BINDING SITE FOR RESIDUE ZN I 1126
|
source |
: AC6
|
|
24)
|
chain |
I |
residue |
33 |
type |
|
sequence |
C
|
description |
BINDING SITE FOR RESIDUE ZN I 1126
|
source |
: AC6
|
|
25)
|
chain |
I |
residue |
86 |
type |
|
sequence |
C
|
description |
BINDING SITE FOR RESIDUE ZN I 1127
|
source |
: AC7
|
|
26)
|
chain |
I |
residue |
89 |
type |
|
sequence |
C
|
description |
BINDING SITE FOR RESIDUE ZN I 1127
|
source |
: AC7
|
|
27)
|
chain |
I |
residue |
114 |
type |
|
sequence |
C
|
description |
BINDING SITE FOR RESIDUE ZN I 1127
|
source |
: AC7
|
|
28)
|
chain |
I |
residue |
117 |
type |
|
sequence |
C
|
description |
BINDING SITE FOR RESIDUE ZN I 1127
|
source |
: AC7
|
|
29)
|
chain |
J |
residue |
45 |
type |
MOD_RES |
sequence |
C
|
description |
Phosphoserine => ECO:0007744|PubMed:17330950, ECO:0007744|PubMed:19779198
|
source |
Swiss-Prot : SWS_FT_FI1
|
|
30)
|
chain |
J |
residue |
46 |
type |
MOD_RES |
sequence |
C
|
description |
Phosphoserine => ECO:0007744|PubMed:17330950, ECO:0007744|PubMed:19779198
|
source |
Swiss-Prot : SWS_FT_FI1
|
|
31)
|
chain |
A |
residue |
102 |
type |
MOD_RES |
sequence |
C
|
description |
Phosphoserine => ECO:0007744|PubMed:17330950, ECO:0007744|PubMed:19779198
|
source |
Swiss-Prot : SWS_FT_FI1
|
|
32)
|
chain |
A |
residue |
105 |
type |
MOD_RES |
sequence |
C
|
description |
Phosphoserine => ECO:0007744|PubMed:17330950, ECO:0007744|PubMed:19779198
|
source |
Swiss-Prot : SWS_FT_FI1
|
|
33)
|
chain |
A |
residue |
233 |
type |
MOD_RES |
sequence |
C
|
description |
Phosphoserine => ECO:0007744|PubMed:17330950, ECO:0007744|PubMed:19779198
|
source |
Swiss-Prot : SWS_FT_FI1
|
|
34)
|
chain |
A |
residue |
236 |
type |
MOD_RES |
sequence |
C
|
description |
Phosphoserine => ECO:0007744|PubMed:17330950, ECO:0007744|PubMed:19779198
|
source |
Swiss-Prot : SWS_FT_FI1
|
|
35)
|
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
|
|
36)
|
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
|
|
37)
|
chain |
B |
residue |
914-926 |
type |
prosite |
sequence |
GDKFSSRHGQKGV
|
description |
RNA_POL_BETA RNA polymerases beta chain signature. GdKFSSrHGQKGV
|
source |
prosite : PS01166
|
|
38)
|
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
|
|
39)
|
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
|
|
40)
|
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
|
|
41)
|
chain |
I |
residue |
86-121 |
type |
prosite |
sequence |
CPQCGNEEMNYHTLQLRSADEGATVFYTCTSCGYKF
|
description |
ZF_TFIIS_1 Zinc finger TFIIS-type signature. CpqCgneemnyhtLQLRSaDEGatvfytCts...CgykF
|
source |
prosite : PS00466
|
|
42)
|
chain |
I |
residue |
9-33 |
type |
prosite |
sequence |
FCLDCGDLLENPNAVLGSNVECSQC
|
description |
RNA_POL_M_15KD RNA polymerases M / 15 Kd subunits signature. FClDCGDLLenpnavlgsnve..CsqC
|
source |
prosite : PS01030
|
|
43)
|
chain |
L |
residue |
34 |
type |
MOD_RES |
sequence |
C
|
description |
Phosphoserine => ECO:0007744|PubMed:17330950, ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198
|
source |
Swiss-Prot : SWS_FT_FI2
|
|
44)
|
chain |
L |
residue |
48 |
type |
MOD_RES |
sequence |
C
|
description |
Phosphoserine => ECO:0007744|PubMed:17330950, ECO:0007744|PubMed:18407956, 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:18407956, ECO:0007744|PubMed:19779198
|
source |
Swiss-Prot : SWS_FT_FI2
|
|
46)
|
chain |
N |
residue |
60 |
type |
MOD_RES |
sequence |
S
|
description |
Phosphoserine => ECO:0007744|PubMed:18407956
|
source |
Swiss-Prot : SWS_FT_FI3
|
|
47)
|
chain |
I |
residue |
89 |
type |
MOD_RES |
sequence |
C
|
description |
Phosphoserine => ECO:0007744|PubMed:18407956
|
source |
Swiss-Prot : SWS_FT_FI3
|
|
48)
|
chain |
I |
residue |
114 |
type |
MOD_RES |
sequence |
C
|
description |
Phosphoserine => ECO:0007744|PubMed:18407956
|
source |
Swiss-Prot : SWS_FT_FI3
|
|
49)
|
chain |
I |
residue |
117 |
type |
MOD_RES |
sequence |
C
|
description |
Phosphoserine => ECO:0007744|PubMed:18407956
|
source |
Swiss-Prot : SWS_FT_FI3
|
|
50)
|
chain |
B |
residue |
1156 |
type |
MOD_RES |
sequence |
S
|
description |
Phosphoserine => ECO:0007744|PubMed:19779198
|
source |
Swiss-Prot : SWS_FT_FI4
|
|