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eF-site ID
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1wcm-I |
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PDB Code
|
1wcm |
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Chain
|
I |
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click to enlarge
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Title
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Complete 12-Subunit RNA Polymerase II at 3.8 Angstrom |
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Classification
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TRANSCRIPTION |
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Compound
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DNA-DIRECTED RNA POLYMERASE II LARGEST SUBUNIT |
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Source
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ORGANISM_COMMON: YEAST; ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE; |
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Sequence
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I: |
TTFRFCRDCNNMLYPREDKENNRLLFECRTCSYVEEAGSP
LVYRHELITNIGETAGVVQDIGSDPTLPRSDRECPKCHSR
ENVFFQSQQRRKDTSMVLFFVCLSCSHIFTSDQKNKRTQ
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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
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1)
|
chain |
I |
| residue |
7 |
| type |
|
| sequence |
C
|
| description |
BINDING SITE FOR RESIDUE ZN I1121
|
| source |
: AC6
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2)
|
chain |
I |
| residue |
10 |
| type |
|
| sequence |
C
|
| description |
BINDING SITE FOR RESIDUE ZN I1121
|
| source |
: AC6
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|
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3)
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chain |
I |
| residue |
29 |
| type |
|
| sequence |
C
|
| description |
BINDING SITE FOR RESIDUE ZN I1121
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| source |
: AC6
|
|
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4)
|
chain |
I |
| residue |
32 |
| type |
|
| sequence |
C
|
| description |
BINDING SITE FOR RESIDUE ZN I1121
|
| source |
: AC6
|
|
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5)
|
chain |
I |
| residue |
75 |
| type |
|
| sequence |
C
|
| description |
BINDING SITE FOR RESIDUE ZN I1122
|
| source |
: AC7
|
|
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6)
|
chain |
I |
| residue |
78 |
| type |
|
| sequence |
C
|
| description |
BINDING SITE FOR RESIDUE ZN I1122
|
| source |
: AC7
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|
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7)
|
chain |
I |
| residue |
103 |
| type |
|
| sequence |
C
|
| description |
BINDING SITE FOR RESIDUE ZN I1122
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| source |
: AC7
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|
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8)
|
chain |
I |
| residue |
106 |
| type |
|
| sequence |
C
|
| description |
BINDING SITE FOR RESIDUE ZN I1122
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| source |
: AC7
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|
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9)
|
chain |
I |
| residue |
40 |
| type |
MOD_RES |
| sequence |
S
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| description |
Phosphoserine => ECO:0007744|PubMed:18407956
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| source |
Swiss-Prot : SWS_FT_FI5
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|
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10)
|
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
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|
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11)
|
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
|
|
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12)
|
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
|
|
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13)
|
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
|
|
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14)
|
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
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|
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15)
|
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
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|
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16)
|
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
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|
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17)
|
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
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18)
|
chain |
I |
| residue |
75-110 |
| type |
prosite |
| sequence |
CPKCHSRENVFFQSQQRRKDTSMVLFFVCLSCSHIF
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| description |
ZF_TFIIS_1 Zinc finger TFIIS-type signature. CpkChsrenvffqSQQRRkDTSmvlffvCls...CshiF
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| source |
prosite : PS00466
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19)
|
chain |
I |
| residue |
6-32 |
| type |
prosite |
| sequence |
FCRDCNNMLYPREDKENNRLLFECRTC
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| description |
RNA_POL_M_15KD RNA polymerases M / 15 Kd subunits signature. FCrDCNNMLypredkennrllfeCrtC
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| source |
prosite : PS01030
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