eF-site ID
|
4v1m-ABCEFHIJKLNPT |
PDB Code
|
4v1m |
Chain
|
A, B, C, E, F, H, I, J, K, L, N, P, T |
|
|
|
Title
|
Architecture of the RNA polymerase II-Mediator core transcription initiation complex |
Classification
|
TRANSCRIPTION |
Compound
|
DNA-DIRECTED RNA POLYMERASE II SUBUNIT RPB1 |
Source
|
ORGANISM_COMMON: BAKER'S YEAST; ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE; |
|
Sequence
|
A: |
GQQYSSAPLRTVKEVQFGLFSPEEVRAISVAKIRFPETMD
ETQTRAKIGGLNDPRLGSIDRNLKCQTCQEGMNECPGHFG
HIDLAKPVFHVGFIAKIKKVCECVCMHCGKLLLDEHNELM
RQALAIKDSKKRFAAIWTLCKTKMVCETDVPSEDDPTQLV
SRGGCGNTQPTIRKDGLKLVGSWKKDRATGDADEPELRVL
STEEILNIFKHISVKDFTSLGFNEVFSRPEWMILTCLPVP
PPPVRPSISFNESQRGEDDLTFKLADILKANISLETLEHN
GAPHHAIEEAESLLQFHVATYMDNDIAGQPQALQKSGRPV
KSIRARLKGKEGRIRGNLMGKRVDFSARTVISGDPNLELD
QVGVPKSIAKTLTYPEVVTPYNIDRLTQLVRNGPNEHPGA
KYVIRDSGDRIDLRYSKRAGDIQLQYGWKVERHIMDNDPV
LFNRQPSLHKMSMMAHRVKVIPYSTFRLNLSVTSPYNADF
DGDEMNLHVPQSEETRAELSQLCAVPLQIVSPQSNKPCMG
IVQDTLCGIRKLTLRDTFIELDQVLNMLYWVPDWDGVIPT
PAIIKPKPLWSGKQILSVAIPNGIHLQRFDEGTTLLSPKD
NGMLIIDGQIIFGVVEKKTVGSSNGGLIHVVTREKGPQVC
AKLFGNIQKVVNFWLLHNGFSTGIGDTIADGPTMREITET
IAEAKKKVLDVTKEAQANLLTAKHGMTLRESFEDNVVRFL
NEARDKAGRLAEVNLKDLNNVKQMVMAGSKGSFINIAQMS
ACVGQQSVEGKRIAFGFVDRTLPHFSKDDYSPESKGFVEN
SYLRGLTPQEFFFHAMGGREGLIDTAVKTAETGYIQRRLV
KALEDIMVHYDNTTRNSLGNVIQFIYGEDGMDAAHIEKQS
LDTIGGSDAAFEKRYRVDLLNTDHTLDPSLLESGSEILGD
LKLQVLLDEEYKQLVKDRKFLREVFVDGEANWPLPVNIRR
IIQNAQQTFHIDHTKPSDLTIKDIVLGVKDLQENLLVLRG
KNEIIQNAQRDAVTLFCCLLRSRLATRRVLQEYRLTKQAF
DWVLSNIEAQFLRSVVHPGEMVGVLAAQSIGEPATQMTKK
VTSGVPRLKEILNVAKNMKTPSLTVYLEPGHAADQEQAKL
IRSAIEHTTLKSVTIASEIYYDPDPRSTVIPEDEEIIQLH
FSLQQSPWLLRLELDRAAMNDKDLTMGQVGERIKQTFKND
LFVIWSEDNDEKLIIRCRVVAEEDHMLKKIENTMLENITL
RGVENIERVVMMKYDRKVPSPTGEYVKEPEWVLETDGVNL
SEVMTVPGIDPTRIYTNSFIDIMEVLGIEAGRAALYKEVY
NVIASDGSYVNYRHMALLVDVMTTQGGLTSVTRHGFNRSN
TGALMRCSFEETVEILFEAGASAELDDCRGVSENVILGQM
APIGTGAFDVMIDEESLVKYMP
|
B: |
DESAPITAEDSWAVISAFFREKGLVSQQLDSFNQFVDYTL
QDIICEDSTLILEQLAQHTTESDNISRKYEISFGKIYVTK
PMVNESDGVTHALYPQEARLRNLTYSSGLFVDVKKRTYEA
IDELKYELGKVFIGRLPIMLRSKNCYLSEATESDLYKLKE
CPFDMGGYFIINGSEKVLIAQERSAGNIVQVFKKAAPSPI
SHVAEIRSALEKGSRFISTLQVKLYGREGSSARTIKATLP
YIKQDIPIVIIFRALGIIPDGEILEHICYDVNDWQMLEML
KPCVEDGFVIQDRETALDFIGRRGTALGIKKEKRIQYAKD
ILQKEFLPHITQLEGFESRKAFFLGYMINRLLLCALDRKD
QDDRDHFGKKRLDLAGPLLAQLFKTLFKKLTKDIFRYMQR
TVEEAHDFNMKLAINAKTITSGLKYALATGNWGEQKKAMS
SRAGVSQVLNRYTYSSTLSHLRRTNTPIAKPRQLHNTHWG
LVCPAETPEGQACGLVKNLSLMSCISVGTDPMPIITFLSE
WGMEPLEDYVPHQSPDATRVFVNGVWHGVHRNPARLMETL
RTLRRKGDINPEVSMIRDIREKELKIFTDAGRVYRPLFIV
EDDESLGHKELKVRKGHIAKLMATEYQDEYTWSSLLNEGL
VEYIDAEEEESILIAMQPEDLEPAEADVDPAKRIRVSHHA
TTFTHCEIHPSMILGVAASIIPFPDHNQSPRNTYQSAMGK
QAMGVFLTNYNVRMDTMANILYYPQKPLGTTRAMEYLKFR
ELPAGQNAIVAIACYSGYNQEDSMIMNQSSIDRGLFRSLF
FRSYMDQEKKYGMSITETFEKPQRTNTLRMKHGTYDKLDD
DGLIAPGVRVSGEDVIIGKTTPISSKRDASTPLRSTENGI
VDQVLVTTNQDGLKFVKVRVRTTKIPQIGDKFASRHGQKG
TIGITYRREDMPFTAEGIVPDLIINPHAIPSRMTVAHLIE
CLLSKVAALSGNEGDASPFTDITVEGISKLLREHGYQSRG
FEVMYNGHTGKKLMAQIFFGPTYYQRLRHMVDDKIHARAR
GPMQVLTRQPVEGRSRDGGLRFGEMERDCMIAHGAASFLK
ERLMEASDAFRVHICGICGLMTVIAKLNHNQFECKGCDNK
IDIYQIHIPYAAKLLFQELMAMNITPRLYTDRSRDF
|
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: |
TTFRFCRDCNNMLYPREDKENNRLLFECRTCSYVEEAGSP
LVYRHELITNIGETAGVVQDIGSDPTLPRSDRECPKCHSR
ENVFFQSQQRRKDTSMVLFFVCLSCSHIFTSDQKNKRTQ
|
J: |
MIVPVRCFSCGKVVGDKWESYLNLLQEDELDEGTALSRLG
LKRYCCRRMILTHVDLIEKFLRYNP
|
K: |
MNAPDRFELFLLGEGESKLKIDPDTKAPNAVVITFEKEDH
TLGNLIRAELLNDRKVLFAAYKVEHPFFARFKLRIQTTEG
YDPKDALKNACNSIINKLGALKTNFETEWNLQTLA
|
L: |
ATLKYICAECSSKLSLSRTDAVRCKDCGHRILLKARTKRL
VQFEAR
|
N: |
AAGTACTTGA
|
P: |
CCAGGA
|
T: |
TCAAGTACTTTTTCCXGGTC
|
|
Description
|
(1) |
DNA-DIRECTED RNA POLYMERASE II SUBUNIT RPB1 (E.C.2.7.7.6), DNA-DIRECTED RNA POLYMERASE II SUBUNIT RPB2 (E.C.2.7.7.6), DNA-DIRECTED RNA POLYMERASE II SUBUNIT RPB3, 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 POLYMERASES I, II, AND III SUBUNIT RPABC 3, DNA-DIRECTED RNA POLYMERASE II SUBUNIT RPB9, DNA-DIRECTED RNA POLYMERASES I, II, AND III SUBUNIT RPABC 5, DNA-DIRECTED RNA POLYMERASE II SUBUNIT RPB11, DNA-DIRECTED RNA POLYMERASES I, II, AND III SUBUNIT RPABC 4 (E.C.2.7.7.6)
|
|
|
|
1)
|
chain |
A |
residue |
107 |
type |
|
sequence |
C
|
description |
BINDING SITE FOR RESIDUE ZN A 2456
|
source |
: AC1
|
|
2)
|
chain |
A |
residue |
110 |
type |
|
sequence |
C
|
description |
BINDING SITE FOR RESIDUE ZN A 2456
|
source |
: AC1
|
|
3)
|
chain |
A |
residue |
148 |
type |
|
sequence |
C
|
description |
BINDING SITE FOR RESIDUE ZN A 2456
|
source |
: AC1
|
|
4)
|
chain |
A |
residue |
167 |
type |
|
sequence |
C
|
description |
BINDING SITE FOR RESIDUE ZN A 2456
|
source |
: AC1
|
|
5)
|
chain |
A |
residue |
67 |
type |
|
sequence |
C
|
description |
BINDING SITE FOR RESIDUE ZN A 2457
|
source |
: AC2
|
|
6)
|
chain |
A |
residue |
70 |
type |
|
sequence |
C
|
description |
BINDING SITE FOR RESIDUE ZN A 2457
|
source |
: AC2
|
|
7)
|
chain |
A |
residue |
77 |
type |
|
sequence |
C
|
description |
BINDING SITE FOR RESIDUE ZN A 2457
|
source |
: AC2
|
|
8)
|
chain |
A |
residue |
80 |
type |
|
sequence |
H
|
description |
BINDING SITE FOR RESIDUE ZN A 2457
|
source |
: AC2
|
|
9)
|
chain |
A |
residue |
481 |
type |
|
sequence |
D
|
description |
BINDING SITE FOR RESIDUE MG A 2458
|
source |
: AC3
|
|
10)
|
chain |
A |
residue |
483 |
type |
|
sequence |
D
|
description |
BINDING SITE FOR RESIDUE MG A 2458
|
source |
: AC3
|
|
11)
|
chain |
A |
residue |
485 |
type |
|
sequence |
D
|
description |
BINDING SITE FOR RESIDUE MG A 2458
|
source |
: AC3
|
|
12)
|
chain |
P |
residue |
10 |
type |
|
sequence |
A
|
description |
BINDING SITE FOR RESIDUE MG A 2458
|
source |
: AC3
|
|
13)
|
chain |
B |
residue |
1163 |
type |
|
sequence |
C
|
description |
BINDING SITE FOR RESIDUE ZN B 2225
|
source |
: AC4
|
|
14)
|
chain |
B |
residue |
1166 |
type |
|
sequence |
C
|
description |
BINDING SITE FOR RESIDUE ZN B 2225
|
source |
: AC4
|
|
15)
|
chain |
B |
residue |
1182 |
type |
|
sequence |
C
|
description |
BINDING SITE FOR RESIDUE ZN B 2225
|
source |
: AC4
|
|
16)
|
chain |
B |
residue |
1185 |
type |
|
sequence |
C
|
description |
BINDING SITE FOR RESIDUE ZN B 2225
|
source |
: AC4
|
|
17)
|
chain |
C |
residue |
86 |
type |
|
sequence |
C
|
description |
BINDING SITE FOR RESIDUE ZN C 1269
|
source |
: AC5
|
|
18)
|
chain |
C |
residue |
88 |
type |
|
sequence |
C
|
description |
BINDING SITE FOR RESIDUE ZN C 1269
|
source |
: AC5
|
|
19)
|
chain |
C |
residue |
92 |
type |
|
sequence |
C
|
description |
BINDING SITE FOR RESIDUE ZN C 1269
|
source |
: AC5
|
|
20)
|
chain |
C |
residue |
95 |
type |
|
sequence |
C
|
description |
BINDING SITE FOR RESIDUE ZN C 1269
|
source |
: AC5
|
|
21)
|
chain |
I |
residue |
7 |
type |
|
sequence |
C
|
description |
BINDING SITE FOR RESIDUE ZN I 1121
|
source |
: AC6
|
|
22)
|
chain |
I |
residue |
10 |
type |
|
sequence |
C
|
description |
BINDING SITE FOR RESIDUE ZN I 1121
|
source |
: AC6
|
|
23)
|
chain |
I |
residue |
29 |
type |
|
sequence |
C
|
description |
BINDING SITE FOR RESIDUE ZN I 1121
|
source |
: AC6
|
|
24)
|
chain |
I |
residue |
32 |
type |
|
sequence |
C
|
description |
BINDING SITE FOR RESIDUE ZN I 1121
|
source |
: AC6
|
|
25)
|
chain |
I |
residue |
75 |
type |
|
sequence |
C
|
description |
BINDING SITE FOR RESIDUE ZN I 1122
|
source |
: AC7
|
|
26)
|
chain |
I |
residue |
78 |
type |
|
sequence |
C
|
description |
BINDING SITE FOR RESIDUE ZN I 1122
|
source |
: AC7
|
|
27)
|
chain |
I |
residue |
103 |
type |
|
sequence |
C
|
description |
BINDING SITE FOR RESIDUE ZN I 1122
|
source |
: AC7
|
|
28)
|
chain |
I |
residue |
106 |
type |
|
sequence |
C
|
description |
BINDING SITE FOR RESIDUE ZN I 1122
|
source |
: AC7
|
|
29)
|
chain |
J |
residue |
7 |
type |
|
sequence |
C
|
description |
BINDING SITE FOR RESIDUE ZN J 1066
|
source |
: AC8
|
|
30)
|
chain |
J |
residue |
10 |
type |
|
sequence |
C
|
description |
BINDING SITE FOR RESIDUE ZN J 1066
|
source |
: AC8
|
|
31)
|
chain |
J |
residue |
45 |
type |
|
sequence |
C
|
description |
BINDING SITE FOR RESIDUE ZN J 1066
|
source |
: AC8
|
|
32)
|
chain |
J |
residue |
46 |
type |
|
sequence |
C
|
description |
BINDING SITE FOR RESIDUE ZN J 1066
|
source |
: AC8
|
|
33)
|
chain |
L |
residue |
31 |
type |
|
sequence |
C
|
description |
BINDING SITE FOR RESIDUE ZN L 1071
|
source |
: AC9
|
|
34)
|
chain |
L |
residue |
34 |
type |
|
sequence |
C
|
description |
BINDING SITE FOR RESIDUE ZN L 1071
|
source |
: AC9
|
|
35)
|
chain |
L |
residue |
48 |
type |
|
sequence |
C
|
description |
BINDING SITE FOR RESIDUE ZN L 1071
|
source |
: AC9
|
|
36)
|
chain |
L |
residue |
51 |
type |
|
sequence |
C
|
description |
BINDING SITE FOR RESIDUE ZN L 1071
|
source |
: AC9
|
|
37)
|
chain |
B |
residue |
837 |
type |
catalytic |
sequence |
D
|
description |
788
|
source |
MCSA : MCSA1
|
|
38)
|
chain |
A |
residue |
483 |
type |
catalytic |
sequence |
D
|
description |
788
|
source |
MCSA : MCSA1
|
|
39)
|
chain |
A |
residue |
485 |
type |
catalytic |
sequence |
D
|
description |
788
|
source |
MCSA : MCSA1
|
|
40)
|
chain |
I |
residue |
40 |
type |
MOD_RES |
sequence |
S
|
description |
Phosphoserine => ECO:0007744|PubMed:18407956
|
source |
Swiss-Prot : SWS_FT_FI5
|
|
41)
|
chain |
L |
residue |
31 |
type |
BINDING |
sequence |
C
|
description |
|
source |
Swiss-Prot : SWS_FT_FI2
|
|
42)
|
chain |
L |
residue |
34 |
type |
BINDING |
sequence |
C
|
description |
|
source |
Swiss-Prot : SWS_FT_FI2
|
|
43)
|
chain |
L |
residue |
48 |
type |
BINDING |
sequence |
C
|
description |
|
source |
Swiss-Prot : SWS_FT_FI2
|
|
44)
|
chain |
L |
residue |
51 |
type |
BINDING |
sequence |
C
|
description |
|
source |
Swiss-Prot : SWS_FT_FI2
|
|
45)
|
chain |
B |
residue |
1185 |
type |
BINDING |
sequence |
C
|
description |
|
source |
Swiss-Prot : SWS_FT_FI2
|
|
46)
|
chain |
I |
residue |
7 |
type |
BINDING |
sequence |
C
|
description |
BINDING => ECO:0000269|PubMed:11313498, ECO:0000269|PubMed:11805306, ECO:0000269|PubMed:15537538, ECO:0000305|PubMed:11313499
|
source |
Swiss-Prot : SWS_FT_FI3
|
|
47)
|
chain |
I |
residue |
10 |
type |
BINDING |
sequence |
C
|
description |
BINDING => ECO:0000269|PubMed:11313498, ECO:0000269|PubMed:11805306, ECO:0000269|PubMed:15537538, ECO:0000305|PubMed:11313499
|
source |
Swiss-Prot : SWS_FT_FI3
|
|
48)
|
chain |
I |
residue |
29 |
type |
BINDING |
sequence |
C
|
description |
BINDING => ECO:0000269|PubMed:11313498, ECO:0000269|PubMed:11805306, ECO:0000269|PubMed:15537538, ECO:0000305|PubMed:11313499
|
source |
Swiss-Prot : SWS_FT_FI3
|
|
49)
|
chain |
I |
residue |
32 |
type |
BINDING |
sequence |
C
|
description |
BINDING => ECO:0000269|PubMed:11313498, ECO:0000269|PubMed:11805306, ECO:0000269|PubMed:15537538, ECO:0000305|PubMed:11313499
|
source |
Swiss-Prot : SWS_FT_FI3
|
|
50)
|
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
|
|
51)
|
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
|
|
52)
|
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
|
|
53)
|
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
|
|
54)
|
chain |
L |
residue |
31-51 |
type |
ZN_FING |
sequence |
CAECSSKLSLSRTDAVRCKDC
|
description |
C4-type
|
source |
Swiss-Prot : SWS_FT_FI1
|
|
55)
|
chain |
A |
residue |
483 |
type |
ZN_FING |
sequence |
D
|
description |
C4-type
|
source |
Swiss-Prot : SWS_FT_FI1
|
|
56)
|
chain |
A |
residue |
485 |
type |
ZN_FING |
sequence |
D
|
description |
C4-type
|
source |
Swiss-Prot : SWS_FT_FI1
|
|
57)
|
chain |
J |
residue |
10 |
type |
ZN_FING |
sequence |
C
|
description |
C4-type
|
source |
Swiss-Prot : SWS_FT_FI1
|
|
58)
|
chain |
J |
residue |
45 |
type |
ZN_FING |
sequence |
C
|
description |
C4-type
|
source |
Swiss-Prot : SWS_FT_FI1
|
|
59)
|
chain |
J |
residue |
46 |
type |
ZN_FING |
sequence |
C
|
description |
C4-type
|
source |
Swiss-Prot : SWS_FT_FI1
|
|
60)
|
chain |
A |
residue |
107 |
type |
ZN_FING |
sequence |
C
|
description |
C4-type
|
source |
Swiss-Prot : SWS_FT_FI1
|
|
61)
|
chain |
A |
residue |
110 |
type |
ZN_FING |
sequence |
C
|
description |
C4-type
|
source |
Swiss-Prot : SWS_FT_FI1
|
|
62)
|
chain |
A |
residue |
148 |
type |
ZN_FING |
sequence |
C
|
description |
C4-type
|
source |
Swiss-Prot : SWS_FT_FI1
|
|
63)
|
chain |
A |
residue |
167 |
type |
ZN_FING |
sequence |
C
|
description |
C4-type
|
source |
Swiss-Prot : SWS_FT_FI1
|
|
64)
|
chain |
A |
residue |
481 |
type |
ZN_FING |
sequence |
D
|
description |
C4-type
|
source |
Swiss-Prot : SWS_FT_FI1
|
|
65)
|
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
|
|
66)
|
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
|
|
67)
|
chain |
I |
residue |
75-110 |
type |
prosite |
sequence |
CPKCHSRENVFFQSQQRRKDTSMVLFFVCLSCSHIF
|
description |
ZF_TFIIS_1 Zinc finger TFIIS-type signature. CpkChsrenvffqSQQRRkDTSmvlffvCls...CshiF
|
source |
prosite : PS00466
|
|
68)
|
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
|
|
69)
|
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
|
|
70)
|
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
|
|
71)
|
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
|
|
72)
|
chain |
B |
residue |
977-989 |
type |
prosite |
sequence |
GDKFASRHGQKGT
|
description |
RNA_POL_BETA RNA polymerases beta chain signature. GdKFASrHGQKGT
|
source |
prosite : PS01166
|
|