|
eF-site ID
|
1wcm-I |
PDB Code
|
1wcm |
Chain
|
I |
|
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
|
I: |
TTFRFCRDCNNMLYPREDKENNRLLFECRTCSYVEEAGSP
LVYRHELITNIGETAGVVQDIGSDPTLPRSDRECPKCHSR
ENVFFQSQQRRKDTSMVLFFVCLSCSHIFTSDQKNKRTQ
|
|
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)
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|
Functional site
|
|
1)
|
chain |
I |
residue |
7 |
type |
|
sequence |
C
|
description |
BINDING SITE FOR RESIDUE ZN I1121
|
source |
: AC6
|
|
2)
|
chain |
I |
residue |
10 |
type |
|
sequence |
C
|
description |
BINDING SITE FOR RESIDUE ZN I1121
|
source |
: AC6
|
|
3)
|
chain |
I |
residue |
29 |
type |
|
sequence |
C
|
description |
BINDING SITE FOR RESIDUE ZN I1121
|
source |
: AC6
|
|
4)
|
chain |
I |
residue |
32 |
type |
|
sequence |
C
|
description |
BINDING SITE FOR RESIDUE ZN I1121
|
source |
: AC6
|
|
5)
|
chain |
I |
residue |
75 |
type |
|
sequence |
C
|
description |
BINDING SITE FOR RESIDUE ZN I1122
|
source |
: AC7
|
|
6)
|
chain |
I |
residue |
78 |
type |
|
sequence |
C
|
description |
BINDING SITE FOR RESIDUE ZN I1122
|
source |
: AC7
|
|
7)
|
chain |
I |
residue |
103 |
type |
|
sequence |
C
|
description |
BINDING SITE FOR RESIDUE ZN I1122
|
source |
: AC7
|
|
8)
|
chain |
I |
residue |
106 |
type |
|
sequence |
C
|
description |
BINDING SITE FOR RESIDUE ZN I1122
|
source |
: AC7
|
|
9)
|
chain |
I |
residue |
75-110 |
type |
prosite |
sequence |
CPKCHSRENVFFQSQQRRKDTSMVLFFVCLSCSHIF
|
description |
ZF_TFIIS_1 Zinc finger TFIIS-type signature. CpkChsrenvffqSQQRRkDTSmvlffvCls...CshiF
|
source |
prosite : PS00466
|
|
10)
|
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
|
|
11)
|
chain |
I |
residue |
7 |
type |
BINDING |
sequence |
C
|
description |
BINDING => ECO:0000255|PROSITE-ProRule:PRU10145, ECO:0000269|PubMed:11313498, ECO:0000269|PubMed:11805306, ECO:0000269|PubMed:15537538, ECO:0000305|PubMed:11313499
|
source |
Swiss-Prot : SWS_FT_FI3
|
|
12)
|
chain |
I |
residue |
10 |
type |
BINDING |
sequence |
C
|
description |
BINDING => ECO:0000255|PROSITE-ProRule:PRU10145, ECO:0000269|PubMed:11313498, ECO:0000269|PubMed:11805306, ECO:0000269|PubMed:15537538, ECO:0000305|PubMed:11313499
|
source |
Swiss-Prot : SWS_FT_FI3
|
|
13)
|
chain |
I |
residue |
29 |
type |
BINDING |
sequence |
C
|
description |
BINDING => ECO:0000255|PROSITE-ProRule:PRU10145, ECO:0000269|PubMed:11313498, ECO:0000269|PubMed:11805306, ECO:0000269|PubMed:15537538, ECO:0000305|PubMed:11313499
|
source |
Swiss-Prot : SWS_FT_FI3
|
|
14)
|
chain |
I |
residue |
32 |
type |
BINDING |
sequence |
C
|
description |
BINDING => ECO:0000255|PROSITE-ProRule:PRU10145, ECO:0000269|PubMed:11313498, ECO:0000269|PubMed:11805306, ECO:0000269|PubMed:15537538, ECO:0000305|PubMed:11313499
|
source |
Swiss-Prot : SWS_FT_FI3
|
|
15)
|
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
|
|
16)
|
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
|
|
17)
|
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
|
|
18)
|
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
|
|
19)
|
chain |
I |
residue |
40 |
type |
MOD_RES |
sequence |
S
|
description |
Phosphoserine => ECO:0007744|PubMed:18407956
|
source |
Swiss-Prot : SWS_FT_FI5
|
|
|
|