eF-site ID
|
5m3f-ABCDEFGHIJKLMN |
PDB Code
|
5m3f |
Chain
|
A, B, C, D, E, F, G, H, I, J, K, L, M, N |
|
|
|
Title
|
Yeast RNA polymerase I elongation complex at 3.8A |
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
KLRLLQYGLIDESYKLDEITLSSTLLNELKSKRSEYVDMA
IAKALSDGRTTERGSFTATVNDERKKLVHEFHKKLLSRGK
CDNCGMFSPKFRKDGFTKIFETALNEKQITNNRVKGSTYI
LSTEVKNILDTVFRKEQCVLQYVFHSRPNLSRKLVKADSF
FMDVLVVPPTRFRLPSKLGEEVHENSQNQLLSKVLTTSLL
IRDLNDDLSKLQKDKVSLEDRRVIFSRLMNAFVTIQNDVN
AFIDSTKAQGRTSGKVPIPGVKQALEKKEGLFRKHMMGKR
VNYAARSVISPDPNIETNEIGVPPVFAVKLTYPEPVTAYN
IAELRQAVINGPDKWPGATQIQNEDGSLVSLIGMSVEQRK
ALANQLLTPSSNVSTHTLNKKVYRHIKNRDVVLMNRQPTL
HKASMMGHKVRVLPNEKTLRLHYANTGAYNADFDGDEMNM
HFPQNENARAEALNLANTDSQYLTPTSGSPVRGLIQDHIS
AGVWLTSKDSFFTREQYQQYIYGCIRPEDGHTTRSKIVTL
PPTIFKPYPLWTGKQIITTVLLNVTPPDMPGINLISKNKI
KNEYWGKGSLENEVLFKDGALLCGILDKSQYGASKYGIVH
SLHEVYGPEVAAKVLSVLGRLFTNYITATAFTCGMDDLRL
TAEGNKWRTDILKTSVDTGREAAAEVTNLDKDTPADDPEL
LKRLQEILRDNNKSGILDAVTSSKVNAITSQVVSKCVPDG
TMKKFPCNSMQAMALSGAKGSNVNVSQIMCLLGQQALEGR
RVPVMVSGKTLPSFKPYETDAMAGGYVKGRFYSGIKPQEY
YFHCMAGREGLIDTAVKTSRSGYLQRCLTKQLEGVHVSYD
NSIRDADGTLVQFMYGGDAIDITKESHMTQFEFCLDNYYA
LLKKYNPSALIEHLDVESALKYSKKTLKYRKKHSKEPHYK
QSVKYDPVLAKYNPAKYLGSVSENFQDKLESFLDKNSKLF
KSSDGVNEKKFRALMQLKYMRSLINPGEAVGIIASQSVGE
PSTQMANVTLGIPRLREIVMTASAAIKTPQMTLPIWNDVS
DEQADTFCKSISKVLLSEVIDKVIVTERSYVIHMRFFDNN
EYSEEYDVSKEELQNVISNQFIHLLEAAIVKEIKKQKKVQ
RDRQSAIISHHRFITKYNFDDESGKWCEFKLELAADTEKL
LMVNIVEEICRKSIIRQIPHIDRCVHPEPENGKRVLVTEG
VNFQAMWDQEAFIDVDGITSNDVAAVLKTYGVEAARNTIV
NEINNVFSRYAISVSFRHLDLIADMMTRQGTYLAFNRQGM
ETSTSSFMKMSYETTCQFLTKAVLDNEREQLDSPSARIVV
GKLNNVGTGSFDVLAKVPN
|
B: |
TADFRTLERESRFINPPKDKSAFPLLQEAVQPHIGSFNAL
TEGPDGGLLNLGVKDIGEKVIFDGKPLNSNSGYLGNKLSV
SVEQVSIAKPMSNDGVSSAVERKVYPSESRQRLTSYRGKL
LLKLKWSVNNGEENLFEVRDCGGLPVMLQSNRCHLNKMSP
YELVQHKEESDEIGGYFIVNGIEKLIRMLIVQRRNHPMAI
IRPSFANRGASYSHYGIQIRSVRPDQTSQTNVLHYLNDGQ
VTFRFSWRKNEYLVPVVMILKALCHTSDREIFDGIIGNDV
KDSFLTDRLELLLRGFKKRYPHLQNRTQVLQYLGDKFRVV
FQASPDQSDLEVGQEVLDRIVLVHLGKDGSQDKFRMLLFM
IRKLYSLVAGECSPDNPDATQHQEVLLGGFLYGMILKEKI
DEYLQNIIAQVRMDINRGMAINFKDKRYMSRVLMRVNENI
GSKMQYFLSTGNLVSQSGLDLQQVSGYTVVAEKINFYRFI
SHFRMVHRGSFFAQLKTTTVRKLLPESWGFLCPVHTPDGS
PCGLLNHFAHKCRISTQQSDVSRIPSILYSLGVAPASHTF
AAGPSLCCVQIDGKIIGWVSHEQGKIIADTLRYWKVEGKT
PGLPIDLEIGYVPPSTRGQYPGLYLFGGHSRMLRPVRYLP
LDKEDIVGPFEQVYMNIAVTPQEIQNNVHTHVEFTPTNIL
SILANLTPFSDFNQSPRNMYQCQMGKQTMGTPGVALCHRS
DNKLYRLQTGQTPIVKANLYDDYGMDNFPNGFNAVVAVIS
YTGYDMDDAMIINKSADERGFGYGTMYKTEKVDLALNRNR
GDPITQHFGFGNDEWPKEWLEKLDEDGLPYIGTYVEEGDP
ICAYFDDTLNKTKIKTYHSSEPAYIEEVNLIGDESNKFQE
LQTVSIKYRIRRTPQIGDKFSSRHGQKGVCSRKWPTIDMP
FSETGIQPDIIINPHAFPSRMTIGMFVESLAGKAGALHGI
AQDSTPWIFNEDDTPADYFGEQLAKAGYNYHGNEPMYSGA
TGEELRADIYVGVVYYQRLRHMVNDKFQVRSTGPVNSLTM
QPVKGRKRHGGIRVGEMERDALIGHGTSFLLQDRLLNSSD
YTQASVCRECGSILTTQQSVPRIGSISTVCCRRCSMRFED
AKKLIFIDDSQIWEDGQGNKFVGGNETTTVAIPFVLKYLD
SELSAMGIRLRYNVEPK
|
C: |
WNVEKFKKDFEVNISSLDAREANFDLINIDTSIANAFRRI
MISEVPSVAAEYVYFFNNTSVIQDEVLAHRIGLVPLKVDP
DMLTWVDSNLPDDEKFTDENTIVLSLNVKCTRNPDAPKGS
TDPKELYNNAHVYARDLKFEPQGRQSTTFADCPVVPADPD
ILLAKLRPGQEISLKAHCILGIGGDHAKFSPVSTASYRLL
PQINILQPIKGESARRFQKCFPPGVIGIDEGSDEAYVKDA
RKDTVSREVLRYEEFADKVKLGRVRNHFIFNVESAGAMTP
EEIFFKSVRILKNKAEYLKNCPITQ
|
D: |
TATTLNTPVVIHATQLPQHVSTDEVLQFLESFIDEKETNL
SSSISQLKRIQRDF
|
E: |
ENERNISRLWRAFRTVKEMVKDRGYFITQEEVELPLEDFK
AKYCDSMGRPQRKMMSFQANPTEESISKFPDMGSLWVEFC
DEPSVGVKTMKTFVIHIQEKNFQTGIFVYQNNITPSAMKL
VPSIPPATIETFNEAALVVNITHHELVPKHIRLSSDEKRE
LLKRYRLKESQLPRIQRADPVALYLGLKRGEVVKIIRKSE
TSGRYASYRICM
|
F: |
PEDFQQHEQIRRKTLKEKAIPKDQRATTPYMTKYERARIL
GTRALQISMNAPVFVDLEGETDPLRIAMKELAEKKIPLVI
RRYLPDGSFEDWSVEELIVD
|
G: |
ARFIKKHKKQVTNPIDEKNGTSNCIVRVPIALYVSLAPMY
LENPLQGVMKQHLNPLVMKYNNKVGGVVLGYEGLKILDAD
PLSKEDTSEKLIKITPDTPFGFTWCHVNLYVWQPQVGDVL
EGYIFIQSASHIGLLIHDAFNASIKKNNIPVDWTFVHGHW
VDSNGEPIDGKLRFTVRNVHTTGRVVSVDGTLI
|
H: |
NTLFDDIFQVSEVDPGRYNKVCRIEAASTTQDQCKLTLDI
NVELFPVAAQDSLTVTIASSLNSWRPPQAGDRSLADDYDY
VMYGTAYKFEEVSKDLIAVYYSFGGLLMRLEGNYRNLNNL
KQENAYLLIRR
|
I: |
SVVGSLIFCLDCGDLLENPNAVLGSNVECSQCKAIYPKSQ
FSNLKVVTTTADDAFPSSLRAKK
|
J: |
MIVPVRCFSCGKVVGDKWESYLNLLQEDELDEGTALSRLG
LKRYCCRRMILTHVDLIEKFLRYNPLEKR
|
K: |
PDREKIKLLTQATSEDGTSASFQIVEEDHTLGNALRYVIM
KNPDVEFCGYSIPHPSENLLNIRIQTYGETTAVDALQKGL
KDLMDLCDVVESKFTEKIKSM
|
L: |
LKYICAECSSKLSLSRTDAVRCKDCGHRILLKARTKRLVQ
FEAR
|
M: |
SEIEIESVQDQPSVAVGSFFKGFRAPSDTTFDLYKKKKSE
KDEFVLHGENERLEYEGYTDSSSQASNQYVVGLFNPEKKS
IQLYKAPVLVSKVVSKSSKNLRGPKIKS
|
N: |
SIPDGFKKCKHLKNFPLNKQQQVWLIKFPSNVDISKLKSL
PVTTMTIDKHDYKIMDDTDIESSLTQDNLSNMTLLVPSES
KESLKIASTAKDNAPLQFDKVFSVSETAKIPAIDYSKVRV
PRKDVPKVEGLKLEHFATGYDAEDF
|
|
Description
|
(1) |
DNA-directed RNA polymerase I subunit RPA190, DNA-directed RNA polymerase I subunit RPA135, DNA-directed RNA polymerases I and III subunit RPAC1, DNA-directed RNA polymerases I, II, and III subunit RPABC1, DNA-directed RNA polymerases I, II, and III subunit RPABC2, DNA-directed RNA polymerases I, II, and III subunit RPABC3, DNA-directed RNA polymerase I subunit RPA12, 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 I subunit RPA49, DNA-directed RNA polymerase I subunit RPA34, DNA-directed RNA polymerase I subunit RPA14, DNA-directed RNA polymerase I subunit RPA43/DNA Complex
|
|
|
|
1)
|
chain |
A |
residue |
62 |
type |
|
sequence |
C
|
description |
binding site for residue ZN A 3001
|
source |
: AC1
|
|
2)
|
chain |
A |
residue |
65 |
type |
|
sequence |
C
|
description |
binding site for residue ZN A 3001
|
source |
: AC1
|
|
3)
|
chain |
A |
residue |
72 |
type |
|
sequence |
C
|
description |
binding site for residue ZN A 3001
|
source |
: AC1
|
|
4)
|
chain |
A |
residue |
75 |
type |
|
sequence |
H
|
description |
binding site for residue ZN A 3001
|
source |
: AC1
|
|
5)
|
chain |
A |
residue |
102 |
type |
|
sequence |
C
|
description |
binding site for residue ZN A 3002
|
source |
: AC2
|
|
6)
|
chain |
A |
residue |
105 |
type |
|
sequence |
C
|
description |
binding site for residue ZN A 3002
|
source |
: AC2
|
|
7)
|
chain |
A |
residue |
233 |
type |
|
sequence |
C
|
description |
binding site for residue ZN A 3002
|
source |
: AC2
|
|
8)
|
chain |
A |
residue |
236 |
type |
|
sequence |
C
|
description |
binding site for residue ZN A 3002
|
source |
: AC2
|
|
9)
|
chain |
A |
residue |
627 |
type |
|
sequence |
D
|
description |
binding site for residue MG A 3003
|
source |
: AC3
|
|
10)
|
chain |
A |
residue |
629 |
type |
|
sequence |
D
|
description |
binding site for residue MG A 3003
|
source |
: AC3
|
|
11)
|
chain |
A |
residue |
631 |
type |
|
sequence |
D
|
description |
binding site for residue MG A 3003
|
source |
: AC3
|
|
12)
|
chain |
B |
residue |
501 |
type |
|
sequence |
R
|
description |
binding site for residue SO4 B 1301
|
source |
: AC4
|
|
13)
|
chain |
B |
residue |
532 |
type |
|
sequence |
H
|
description |
binding site for residue SO4 B 1301
|
source |
: AC4
|
|
14)
|
chain |
B |
residue |
544 |
type |
|
sequence |
H
|
description |
binding site for residue SO4 B 1301
|
source |
: AC4
|
|
15)
|
chain |
B |
residue |
698 |
type |
|
sequence |
S
|
description |
binding site for residue SO4 B 1301
|
source |
: AC4
|
|
16)
|
chain |
B |
residue |
699 |
type |
|
sequence |
I
|
description |
binding site for residue SO4 B 1301
|
source |
: AC4
|
|
17)
|
chain |
B |
residue |
700 |
type |
|
sequence |
L
|
description |
binding site for residue SO4 B 1301
|
source |
: AC4
|
|
18)
|
chain |
B |
residue |
1104 |
type |
|
sequence |
C
|
description |
binding site for residue ZN B 1302
|
source |
: AC5
|
|
19)
|
chain |
B |
residue |
1107 |
type |
|
sequence |
C
|
description |
binding site for residue ZN B 1302
|
source |
: AC5
|
|
20)
|
chain |
B |
residue |
1128 |
type |
|
sequence |
C
|
description |
binding site for residue ZN B 1302
|
source |
: AC5
|
|
21)
|
chain |
B |
residue |
1131 |
type |
|
sequence |
C
|
description |
binding site for residue ZN B 1302
|
source |
: AC5
|
|
22)
|
chain |
I |
residue |
10 |
type |
|
sequence |
C
|
description |
binding site for residue ZN I 3001
|
source |
: AC6
|
|
23)
|
chain |
I |
residue |
13 |
type |
|
sequence |
C
|
description |
binding site for residue ZN I 3001
|
source |
: AC6
|
|
24)
|
chain |
I |
residue |
30 |
type |
|
sequence |
C
|
description |
binding site for residue ZN I 3001
|
source |
: AC6
|
|
25)
|
chain |
I |
residue |
33 |
type |
|
sequence |
C
|
description |
binding site for residue ZN I 3001
|
source |
: AC6
|
|
26)
|
chain |
J |
residue |
7 |
type |
|
sequence |
C
|
description |
binding site for residue ZN J 3001
|
source |
: AC7
|
|
27)
|
chain |
J |
residue |
10 |
type |
|
sequence |
C
|
description |
binding site for residue ZN J 3001
|
source |
: AC7
|
|
28)
|
chain |
J |
residue |
45 |
type |
|
sequence |
C
|
description |
binding site for residue ZN J 3001
|
source |
: AC7
|
|
29)
|
chain |
J |
residue |
46 |
type |
|
sequence |
C
|
description |
binding site for residue ZN J 3001
|
source |
: AC7
|
|
30)
|
chain |
L |
residue |
31 |
type |
|
sequence |
C
|
description |
binding site for residue ZN L 3001
|
source |
: AC8
|
|
31)
|
chain |
L |
residue |
34 |
type |
|
sequence |
C
|
description |
binding site for residue ZN L 3001
|
source |
: AC8
|
|
32)
|
chain |
L |
residue |
48 |
type |
|
sequence |
C
|
description |
binding site for residue ZN L 3001
|
source |
: AC8
|
|
33)
|
chain |
L |
residue |
51 |
type |
|
sequence |
C
|
description |
binding site for residue ZN L 3001
|
source |
: AC8
|
|
34)
|
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
|
|
35)
|
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
|
|
36)
|
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
|
|
37)
|
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
|
|
38)
|
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
|
|
39)
|
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
|
|
40)
|
chain |
B |
residue |
914-926 |
type |
prosite |
sequence |
GDKFSSRHGQKGV
|
description |
RNA_POL_BETA RNA polymerases beta chain signature. GdKFSSrHGQKGV
|
source |
prosite : PS01166
|
|
41)
|
chain |
G |
residue |
244 |
type |
MOD_RES |
sequence |
S
|
description |
Phosphoserine => ECO:0007744|PubMed:18407956
|
source |
Swiss-Prot : SWS_FT_FI1
|
|
42)
|
chain |
J |
residue |
46 |
type |
MOD_RES |
sequence |
C
|
description |
Phosphoserine => ECO:0007744|PubMed:18407956
|
source |
Swiss-Prot : SWS_FT_FI1
|
|
43)
|
chain |
A |
residue |
102 |
type |
MOD_RES |
sequence |
C
|
description |
Phosphoserine => ECO:0007744|PubMed:18407956
|
source |
Swiss-Prot : SWS_FT_FI1
|
|
44)
|
chain |
A |
residue |
105 |
type |
MOD_RES |
sequence |
C
|
description |
Phosphoserine => ECO:0007744|PubMed:18407956
|
source |
Swiss-Prot : SWS_FT_FI1
|
|
45)
|
chain |
A |
residue |
233 |
type |
MOD_RES |
sequence |
C
|
description |
Phosphoserine => ECO:0007744|PubMed:18407956
|
source |
Swiss-Prot : SWS_FT_FI1
|
|
46)
|
chain |
A |
residue |
236 |
type |
MOD_RES |
sequence |
C
|
description |
Phosphoserine => ECO:0007744|PubMed:18407956
|
source |
Swiss-Prot : SWS_FT_FI1
|
|
47)
|
chain |
L |
residue |
34 |
type |
MOD_RES |
sequence |
C
|
description |
Phosphoserine => ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198
|
source |
Swiss-Prot : SWS_FT_FI2
|
|
48)
|
chain |
L |
residue |
48 |
type |
MOD_RES |
sequence |
C
|
description |
Phosphoserine => ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198
|
source |
Swiss-Prot : SWS_FT_FI2
|
|
49)
|
chain |
L |
residue |
51 |
type |
MOD_RES |
sequence |
C
|
description |
Phosphoserine => ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198
|
source |
Swiss-Prot : SWS_FT_FI2
|
|
50)
|
chain |
I |
residue |
13 |
type |
MOD_RES |
sequence |
C
|
description |
Phosphoserine => ECO:0007744|PubMed:15665377, ECO:0007744|PubMed:17330950, ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198
|
source |
Swiss-Prot : SWS_FT_FI3
|
|
51)
|
chain |
I |
residue |
30 |
type |
MOD_RES |
sequence |
C
|
description |
Phosphoserine => ECO:0007744|PubMed:15665377, ECO:0007744|PubMed:17330950, ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198
|
source |
Swiss-Prot : SWS_FT_FI3
|
|
52)
|
chain |
I |
residue |
33 |
type |
MOD_RES |
sequence |
C
|
description |
Phosphoserine => ECO:0007744|PubMed:15665377, ECO:0007744|PubMed:17330950, ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198
|
source |
Swiss-Prot : SWS_FT_FI3
|
|