eF-site ID
|
1wcm-ABCDEFGHIJKL |
PDB Code
|
1wcm |
Chain
|
A, B, C, D, E, F, G, H, I, J, K, L |
|
click to enlarge
|
|
Title
|
Complete 12-Subunit RNA Polymerase II at 3.8 Angstrom |
Classification
|
TRANSCRIPTION |
Compound
|
DNA-DIRECTED RNA POLYMERASE II LARGEST SUBUNIT |
Source
|
ORGANISM_COMMON: YEAST; ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE; |
|
Sequence
|
A: |
VGQQYSSAPLRTVKEVQFGLFSPEEVRAISVAKIRFPETM
DETQTRAKIGGLNDPRLGSIDRNLKCQTCQEGMNECPGHF
GHIDLAKPVFHVGFIAKIKKVCECVCMHCGKLLLDEHNEL
MRQALAIKDSKKRFAAIWTLCKTKMVCETDVPSEDDPTQL
VSRGGCGNTQPTIRKDGLKLVGSWKDEPELRVLSTEEILN
IFKHISVKDFTSLGFNEVFSRPEWMILTCLPVPPPPVRPS
ISFNESQRGEDDLTFKLADILKANISLETLEHNGAPHHAI
EEAESLLQFHVATYMDNDIAGQPQALQKSGRPVKSIRARL
KGKEGRIRGNLMGKRVDFSARTVISGDPNLELDQVGVPKS
IAKTLTYPEVVTPYNIDRLTQLVRNGPNEHPGAKYVIRDS
GDRIDLRYSKRAGDIQLQYGWKVERHIMDNDPVLFNRQPS
LHKMSMMAHRVKVIPYSTFRLNLSVTSPYNADFDGDEMNL
HVPQSEETRAELSQLCAVPLQIVSPQSNKPCMGIVQDTLC
GIRKLTLRDTFIELDQVLNMLYWVPDWDGVIPTPAIIKPK
PLWSGKQILSVAIPNGIHLQRFDEGTTLLSPKDNGMLIID
GQIIFGVVEKKTVGSSNGGLIHVVTREKGPQVCAKLFGNI
QKVVNFWLLHNGFSTGIGDTIADGPTMREITETIAEAKKK
VLDVTKEAQANLLTAKHGMTLRESFEDNVVRFLNEARDKA
GRLAEVNLKDLNNVKQMVMAGSKGSFINIAQMSACVGQQS
VEGKRIAFGFVDRTLPHFSKDDYSPESKGFVENSYLRGLT
PQEFFFHAMGGREGLIDTAVKTAETGYIQRRLVKALEDIM
VHYDNTTRNSLGNVIQFIYGEDGMDAAHIEKQSLDTIGGS
DAAFEKRYRVDLLNTDHTLDPSLLESGSEILGDLKLQVLL
DEEYKQLVKDRKFLREVFVDGEANWPLPVNIRRIIQNAQQ
TFHIDHTKPSDLTIKDIVLGVKDLQENLLVLRGKNEIIQN
AQRDAVTLFCCLLRSRLATRRVLQEYRLTKQAFDWVLSNI
EAQFLRSVVHPGEMVGVLAAQSIGEPATQMTLKKVTSGVP
RLKEILNVAKNMKTPSLTVYLEPGHAADQEQAKLIRSAIE
HTTLKSVTIASEIYYDPDPRSTVIPEDEEIIQLHFSLQQS
PWLLRLELDRAAMNDKDLTMGQVGERIKQTFKNDLFVIWS
EDNDEKLIIRCRVVAEEDHMLKKIENTMLENITLRGVENI
ERVVMMKYDRKVPSPTGEYVKEPEWVLETDGVNLSEVMTV
PGIDPTRIYTNSFIDIMEVLGIEAGRAALYKEVYNVIASD
GSYVNYRHMALLVDVMTTQGGLTSVTRHGFNRSNTGALMR
CSFEETVEILFEAGASAELDDCRGVSENVILGQMAPIGTG
AFDVMIDEESLVKYMP
|
B: |
DESAPITAEDSWAVISAFFREKGLVSQQLDSFNQFVDYTL
QDIICEDSTLIISFGKIYVTKPMVNESDGVTHALYPQEAR
LRNLTYSSGLFVDVKKKVFIGRLPIMLRSKNCYLSEATES
DLYKLKECPFDMGGYFIINGSEKVLIAQERSAGNIVQVFK
KAAPSPISHVAEIRSALEKGSRFISTLQVKLYGREGSSAR
TIKATLPYIKQDIPIVIIFRALGIIPDGEILEHICYDVND
WQMLEMLKPCVEDGFVIQDRETALDFIGKEKRIQYAKDIL
QKEFLPHITQLEGFESRKAFFLGYMINRLLLCALDRKDQD
DRDHFGKKRLDLAGPLLAQLFKTLFKKLTKDIFRYMQRTV
ELAINAKTITSGLKYALATGNWGAGVSQVLNRYTYSSTLS
HLRRTNTPIAKPRQLHNTHWGLVCPAETPEGQACGLVKNL
SLMSCISVGTDPMPIITFLSEWGMEPLEDYVPHQSPDATR
VFVNGVWHGVHRNPARLMETLRTLRRKGDINPEVSMIRDI
REKELKIFTDAGRVYRPLFIVEDDESLGHKELKVRKGHIA
KLMATEYQDEYTWSSLLNEGLVEYIDAEEEESILIAMQPE
DLEPAEADVDPAKRIRVSHHATTFTHCEIHPSMILGVAAS
IIPFPDHNQSPRNTYQSAMGKQAMGVFLTNYNVRMDTMAN
ILYYPQKPLGTTRAMEYLKFRELPAGQNAIVAIACYSGYN
QEDSMIMNQSSIDRGLFRSLFFRSYMDQEKKYGMSITETF
EKPQRTNTLRMKHGTYDKLDDDGLIAPGVRVSGEDVIIGK
TTPISSKRDASTPLRSTENGIVDQVLVTTNQDGLKFVKVR
VRTTKIPQIGDKFASRHGQKGTIGITYRREDMPFTAEGIV
PDLIINPHAIPSRMTVAHLIECLLSKVAALSGNEGDASPF
TDITVEGISKLLREHGYQSRGFEVMYNGHTGKKLMAQIFF
GPTYYQRLRHMVDDKIHARARGPMQVLTRQPVEGRSRDGG
LRFGEMERDCMIAHGAASFLKERLMEASDAFRVHICGICG
LMTVIAKLNHNQFECKGCDNKIDIYQIHIPYAAKLLFQEL
MAMNITPRLYTDRSRDF
|
C: |
EEGPQVKIREASKDNVDFILSNVDLAMANSLRRVMIAEIP
TLAIDSVEVETNTTVLADEFIAHRLGLIPLQSMDIEQLEY
SRDCFCEDHCDKCSVVLTLQAFGESESTTNVYSKDLVIVS
NLMGRNIGHPIIQDKEGNGVLICKLRKGQELKLTCVAKKG
IAKEHAKWGPAAAIEFEYDPWNKLKHTDYWYEQDSAKEWP
QSKNCEYEDPPNEGDPFDYKAQADTFYMNVESVGSIPVDQ
VVVRGIDTLQKKVASILLALTQMDQD
|
D: |
STSTFQTRRRRLKKVEEEENAATLQLGQEFQLKQINHQGE
EEELIALNLSEARLVIKEALVERRRAFKRSQKKTREKELE
SIDVLLEQTTGGNNKDLKNTMQYLTNFSRFRDQETVGAVI
QLLKSTGLHPFEVAQLGSLACDTADEAKTLIPSLNNKISD
DELERILKELSNLETLY
|
E: |
DQENERNISRLWRAFRTVKEMVKDRGYFITQEEVELPLED
FKAKYCDSMGRPQRKMMSFQANPTEESISKFPDMGSLWVE
FCDEPSVGVKTMKTFVIHIQEKNFQTGIFVYQNNITPSAM
KLVPSIPPATIETFNEAALVVNITHHELVPKHIRLSSDEK
RELLKRYRLKESQLPRIQRADPVALYLGLKRGEVVKIIRK
SETSGRYASYRICM
|
F: |
KAIPKDQRATTPYMTKYERARILGTRALQISMNAPVFVDL
EGETDPLRIAMKELAEKKIPLVIRRYLPDGSFEDWSVEEL
IVDL
|
G: |
MFFIKDLSLNITLHPSFFGPRMKQYLKTKLLEEVEGSCTG
KFGYILCVLDYDNIDIQRGRILPTDGSAEFNVKYRAVVFK
PFKGEVVDGTVVSCSQHGFEVQVGPMKVFVTKHLMPQDLT
FNAGSNPPSYQSSEDVITIKSRIRVKIEGCISQVSSIHAI
GSIKEDYLGAI
|
H: |
SNTLFDDIFQVSEVDPGRYNKVCRIEAASTTQDQCKLTLD
INVELFPVAAQDSLTVTIASSLTRSWRPPQAGDRSLADDY
DYVMYGTAYKFEEVSKDLIAVYYSFGGLLMRLEGNYRNLN
NLKQENAYLLIRR
|
I: |
TTFRFCRDCNNMLYPREDKENNRLLFECRTCSYVEEAGSP
LVYRHELITNIGETAGVVQDIGSDPTLPRSDRECPKCHSR
ENVFFQSQQRRKDTSMVLFFVCLSCSHIFTSDQKNKRTQ
|
J: |
MIVPVRCFSCGKVVGDKWESYLNLLQEDELDEGTALSRLG
LKRYCCRRMILTHVDLIEKFLRYNP
|
K: |
MNAPDRFELFLLGEGESKLKIDPDTKAPNAVVITFEKEDH
TLGNLIRAELLNDRKVLFAAYKVEHPFFARFKLRIQTTEG
YDPKDALKNACNSIINKLGALKTNFETEWNLQTLA
|
L: |
ATLKYICAECSSKLSLSRTDAVRCKDCGHRILLKARTKRL
VQFEAR
|
|
Description
|
(1) |
DNA-DIRECTED RNA POLYMERASE II LARGEST SUBUNIT (E.C.2.7.7.6), DNA-DIRECTED RNA POLYMERASE II SECOND LARGEST SUBUNIT (E.C.2.7.7.6), DNA-DIRECTED RNA POLYMERASE II 45 KDA POLYPEPTIDE (E.C.2.7.7.6), DNA-DIRECTED RNA POLYMERASE II 32 KDA POLYPEPTIDE (E.C.2.7.7.6), DNA-DIRECTED RNA POLYMERASES I, II, AND III 27 KDA POLYPEPTIDE (E.C.2.7.7.6), DNA-DIRECTED RNA POLYMERASES I, II, AND III 23 KDA POLYPEPTIDE (E.C.2.7.7.6), DNA-DIRECTED RNA POLYMERASE II 19 KD POLYPEPTIDE (E.C.2.7.7.6), DNA-DIRECTED RNA POLYMERASES I, II, AND III 14.5 KDA POLYPEPTIDE (E.C.2.7.7.6), DNA-DIRECTED RNA POLYMERASE II 14.2 KDA POLYPEPTIDE (E.C.2.7.7.6), DNA-DIRECTED RNA POLYMERASES I, II AND III 8.3 KDA POLYPEPTIDE (E.C.2.7.7.6), DNA-DIRECTED RNA POLYMERASE II 13.6 KDA POLYPEPTIDE (E.C.2.7.7.6), DNA-DIRECTED RNA POLYMERASES I, II, AND III 7.7 KDA POLYPEPTIDE (E.C.2.7.7.6)
|
|
|
|
1)
|
chain |
A |
residue |
108 |
type |
|
sequence |
M
|
description |
BINDING SITE FOR RESIDUE ZN A2456
|
source |
: AC1
|
|
2)
|
chain |
A |
residue |
110 |
type |
|
sequence |
C
|
description |
BINDING SITE FOR RESIDUE ZN A2456
|
source |
: AC1
|
|
3)
|
chain |
A |
residue |
148 |
type |
|
sequence |
C
|
description |
BINDING SITE FOR RESIDUE ZN A2456
|
source |
: AC1
|
|
4)
|
chain |
A |
residue |
167 |
type |
|
sequence |
C
|
description |
BINDING SITE FOR RESIDUE ZN A2456
|
source |
: AC1
|
|
5)
|
chain |
A |
residue |
67 |
type |
|
sequence |
C
|
description |
BINDING SITE FOR RESIDUE ZN A2457
|
source |
: AC2
|
|
6)
|
chain |
A |
residue |
70 |
type |
|
sequence |
C
|
description |
BINDING SITE FOR RESIDUE ZN A2457
|
source |
: AC2
|
|
7)
|
chain |
A |
residue |
77 |
type |
|
sequence |
C
|
description |
BINDING SITE FOR RESIDUE ZN A2457
|
source |
: AC2
|
|
8)
|
chain |
A |
residue |
80 |
type |
|
sequence |
H
|
description |
BINDING SITE FOR RESIDUE ZN A2457
|
source |
: AC2
|
|
9)
|
chain |
A |
residue |
481 |
type |
|
sequence |
D
|
description |
BINDING SITE FOR RESIDUE MG A2458
|
source |
: AC3
|
|
10)
|
chain |
A |
residue |
483 |
type |
|
sequence |
D
|
description |
BINDING SITE FOR RESIDUE MG A2458
|
source |
: AC3
|
|
11)
|
chain |
A |
residue |
485 |
type |
|
sequence |
D
|
description |
BINDING SITE FOR RESIDUE MG A2458
|
source |
: AC3
|
|
12)
|
chain |
B |
residue |
1163 |
type |
|
sequence |
C
|
description |
BINDING SITE FOR RESIDUE ZN B2225
|
source |
: AC4
|
|
13)
|
chain |
B |
residue |
1166 |
type |
|
sequence |
C
|
description |
BINDING SITE FOR RESIDUE ZN B2225
|
source |
: AC4
|
|
14)
|
chain |
B |
residue |
1182 |
type |
|
sequence |
C
|
description |
BINDING SITE FOR RESIDUE ZN B2225
|
source |
: AC4
|
|
15)
|
chain |
B |
residue |
1185 |
type |
|
sequence |
C
|
description |
BINDING SITE FOR RESIDUE ZN B2225
|
source |
: AC4
|
|
16)
|
chain |
C |
residue |
86 |
type |
|
sequence |
C
|
description |
BINDING SITE FOR RESIDUE ZN C1269
|
source |
: AC5
|
|
17)
|
chain |
C |
residue |
88 |
type |
|
sequence |
C
|
description |
BINDING SITE FOR RESIDUE ZN C1269
|
source |
: AC5
|
|
18)
|
chain |
C |
residue |
91 |
type |
|
sequence |
H
|
description |
BINDING SITE FOR RESIDUE ZN C1269
|
source |
: AC5
|
|
19)
|
chain |
C |
residue |
92 |
type |
|
sequence |
C
|
description |
BINDING SITE FOR RESIDUE ZN C1269
|
source |
: AC5
|
|
20)
|
chain |
C |
residue |
95 |
type |
|
sequence |
C
|
description |
BINDING SITE FOR RESIDUE ZN C1269
|
source |
: AC5
|
|
21)
|
chain |
I |
residue |
7 |
type |
|
sequence |
C
|
description |
BINDING SITE FOR RESIDUE ZN I1121
|
source |
: AC6
|
|
22)
|
chain |
I |
residue |
10 |
type |
|
sequence |
C
|
description |
BINDING SITE FOR RESIDUE ZN I1121
|
source |
: AC6
|
|
23)
|
chain |
I |
residue |
29 |
type |
|
sequence |
C
|
description |
BINDING SITE FOR RESIDUE ZN I1121
|
source |
: AC6
|
|
24)
|
chain |
I |
residue |
32 |
type |
|
sequence |
C
|
description |
BINDING SITE FOR RESIDUE ZN I1121
|
source |
: AC6
|
|
25)
|
chain |
I |
residue |
75 |
type |
|
sequence |
C
|
description |
BINDING SITE FOR RESIDUE ZN I1122
|
source |
: AC7
|
|
26)
|
chain |
I |
residue |
78 |
type |
|
sequence |
C
|
description |
BINDING SITE FOR RESIDUE ZN I1122
|
source |
: AC7
|
|
27)
|
chain |
I |
residue |
103 |
type |
|
sequence |
C
|
description |
BINDING SITE FOR RESIDUE ZN I1122
|
source |
: AC7
|
|
28)
|
chain |
I |
residue |
106 |
type |
|
sequence |
C
|
description |
BINDING SITE FOR RESIDUE ZN I1122
|
source |
: AC7
|
|
29)
|
chain |
J |
residue |
7 |
type |
|
sequence |
C
|
description |
BINDING SITE FOR RESIDUE ZN J1066
|
source |
: AC8
|
|
30)
|
chain |
J |
residue |
10 |
type |
|
sequence |
C
|
description |
BINDING SITE FOR RESIDUE ZN J1066
|
source |
: AC8
|
|
31)
|
chain |
J |
residue |
45 |
type |
|
sequence |
C
|
description |
BINDING SITE FOR RESIDUE ZN J1066
|
source |
: AC8
|
|
32)
|
chain |
J |
residue |
46 |
type |
|
sequence |
C
|
description |
BINDING SITE FOR RESIDUE ZN J1066
|
source |
: AC8
|
|
33)
|
chain |
L |
residue |
31 |
type |
|
sequence |
C
|
description |
BINDING SITE FOR RESIDUE ZN L1071
|
source |
: AC9
|
|
34)
|
chain |
L |
residue |
34 |
type |
|
sequence |
C
|
description |
BINDING SITE FOR RESIDUE ZN L1071
|
source |
: AC9
|
|
35)
|
chain |
L |
residue |
48 |
type |
|
sequence |
C
|
description |
BINDING SITE FOR RESIDUE ZN L1071
|
source |
: AC9
|
|
36)
|
chain |
L |
residue |
51 |
type |
|
sequence |
C
|
description |
BINDING SITE FOR RESIDUE ZN L1071
|
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 |
L |
residue |
31 |
type |
BINDING |
sequence |
C
|
description |
|
source |
Swiss-Prot : SWS_FT_FI2
|
|
41)
|
chain |
L |
residue |
34 |
type |
BINDING |
sequence |
C
|
description |
|
source |
Swiss-Prot : SWS_FT_FI2
|
|
42)
|
chain |
L |
residue |
48 |
type |
BINDING |
sequence |
C
|
description |
|
source |
Swiss-Prot : SWS_FT_FI2
|
|
43)
|
chain |
L |
residue |
51 |
type |
BINDING |
sequence |
C
|
description |
|
source |
Swiss-Prot : SWS_FT_FI2
|
|
44)
|
chain |
B |
residue |
1185 |
type |
BINDING |
sequence |
C
|
description |
|
source |
Swiss-Prot : SWS_FT_FI2
|
|
45)
|
chain |
I |
residue |
40 |
type |
MOD_RES |
sequence |
S
|
description |
Phosphoserine => ECO:0007744|PubMed:18407956
|
source |
Swiss-Prot : SWS_FT_FI5
|
|
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
|
|