|
eF-site ID
|
6drd-ABCDEFGHIJKLM |
PDB Code
|
6drd |
Chain
|
A, B, C, D, E, F, G, H, I, J, K, L, M |
|
|
|
Title
|
RNA Pol II(G) |
Classification
|
TRANSFERASE |
Compound
|
DNA-directed RNA polymerase II subunit RPB1 |
Source
|
ORGANISM_COMMON: Human; ORGANISM_SCIENTIFIC: Homo sapiens; |
|
Sequence
|
A: |
RTVITPDPNLSIDQVGVPRSIAANMTFAEIVTPFNIDRLQ
ELVRRGNSQYPGAKYIIRRIDLRFHPKPSDLHLQTGYKVE
RHMCDGDIVIFMGHRVRILPWSTFRLNLEMNLHLPQSLET
RAEIQELAMVPRMIVQDTLTAVRKFTKRDVFLERGEVMNL
LMFLSTWDGKVPQPAILKPRPLWTGKQIFSLIIPGHINCI
RTHSTHPDDEDSGPYKHISPGDTKVVVENGELIMGILCKK
SLGTSAGSLVHISYLEMGHDITRLFYSNIQTVINNWLLIE
GHTIGIGDSIADSKTYQDIQNTIKKAKQDVIEVIEKAHNN
ELEPTPGNTLRQTFENQVNRILNDARDKTGSSAQKSLSEY
NNFKSMVVSGAKGSKINISQVIAVVGQQNVEGKRIPFGFK
HRTLPHFIKDDYGPESRGFVENSYLAGLTPTEFFFHAMGG
REGLIDTAVKTAETGYIQRRLIKSMESVMVKYDATVRNSI
NQVVQLRYGEDGLAGESVEFQNLATLKPSNKAFEKKFRFD
YTNERALRRTLQEDLVKDVLSNAHIQNELEREFERMREDR
EVLRVIFPTGDSKVVLPCNLLRMIWNAQKIFHINPRLPSD
LHPIKVVEGVKELSKKLVIVNGDDPLSRQAQENATLLFNI
HLRSTLCSRRMAEEFRLSGEAFDWLLGEIESKFNQAIAHP
GEMVGALAAQSLGEPATQNVTLGVPRLKELINISKKPKTP
SLTVFLLGQSARDAERAKDILCRLEHTTLRKVTANTAIYY
DPNPQSTVVAEDQEWVNVYYEMPDFDVARISPWLLRVELD
RKHMTDRKLTMEQIAEKINAGFGDDLNCIFNDDNAEKLVL
RIRIMNKMDDDVFLRCIESNMLTDMTLQGIEQISKVYMHL
PQTDNKKKIIITEDGEFKALQEWILETDGVSLMRVLSEKD
VDPVRTTSNDIVEIFTVLGIEAVRKALERELYHVISFDGS
YVNYRHLALLCDTMTCRGHLMAITGCFDLLLDAEKCKYGM
|
B: |
EITPDLWQEACWIVISSYFDEKGLVRQQLDSFDEFIQMSV
QRIVEDAPPIDLQPPRYLLKFEQIYLSKPTHWERDGAPSP
MMPNEARLRNLTYSAPLYVDITKTVIKEGEEQLQTQHQKT
FIGKIPIMLRSTYCLLNGLTDRDLCELNECPLDPGGYFII
NGSEKVLIAQEKMATNTVYVFAKKDSKYAYTGECRSCLEN
SSRPTSTIWVSMLARGGQGAKKSAIGQRIVATLPYIKQEV
PIIIVFRALGFVSDRDILEHIIYDFEDPEMMEMVKPSLDE
AFVIQEQNVALNFIGSRGAKPGVTKEKRIKYAKEVLQKEM
LPHVGVSDFCETKKAYFLGYMVHRLLLAALGRRELDDRDH
YGNKRLDLAGPLLAFLFRGMFKNLLKEVRIYAQKFIDRGK
DFNLELAIKTRIISDGLKYSLATGNWGDQKKAHQARAGVS
QVLNRLTFASTLSHLRRLNSPIKPRQLHNTLWGMVCPAET
PEGHAVGLVKNLALMAYISVGSQPSPILEFLEEWSMENLE
EISPAAIADATKIFVNGCWVGIHKDPEQLMNTLRKLRRQM
DIIVSEVSMIRDIREREIRIYTDAGRICRPLLIVEKQKLL
LKKRHIDQLKEREYNNYSWQDLVASGVVEYIDTLEEETVM
LAMTPDDLQEKEVAYCSTYTHCEIHPSMILGVCASIIPFP
DHNQSPRNTYQSAMGKQAMGVYITNFHVRMDTLAHVLYYP
QKPLVTTRSMEYLRFRELPAGINSIVAIASYTGYNQEDSV
IMNRSAVDRGFFRSVFYRSYKEQESKKDQEEVFEKPTRET
CQGMRHAIYDKLDDDGLIAPGVRVSGDDVIIGKTVTLTKR
DCSTFLRTSETGIVDQVMVTLNQEGYKFCKIRVRSVRIPQ
IGDKFASRHGQKGTCGIQYRQEDMPFTCEGITPDIIINPH
AIPSRMTIGHLIECLQGKVSANKGEIGDATPFNDAVNVQK
ISNLLSDYGYHLRGNEVLYNGFTGRKITSQIFIGPTYYQR
LKHMVDDKI
|
C: |
PYANQPTVRITELTDENVKFIIENTDLAVANSIRRVFIAE
VPIIAIDWVQIDANSSVLHDEFIAHRLGLIPLISDDIVDK
LQYSRDCTCEEFCPECSVEFTLDVRCNEDQTRHVTSRDLI
SNSPRVIPVTSRNVEQDDILIVKLRKGQELRLRAYAKKGF
GKEHAKWNPTAGVAFEYDPDNALRHTVYPKPEEWPKSEYS
ELDEDESQAPYDPNGKPERFYYNVESCGSLRPETIVLSAL
SGLKKKLSDLQTQLSHEIQSDV
|
D: |
EEDASQLIFPKEFETAETLLNSEVHMLLEHRKQQNESAED
EQELSEVFMKTLNYTARFSRFKNRETIASVRSLLLQKKLH
KFELACLANLCPETAEESKALIPSLEGRFEDEELQQILDD
IQTKRSFQ
|
E: |
ETYRLWKIRKTIMQLCHDRGYLVTQDELDQTLEEFKAQTD
LTVLVAHNQMFVFFPEEPKVGIKTIKVYCQRMQEENITRA
LIVVQQGSAKQSLVDMAPKYILEQFLEQELLINITEHELV
PEHVVMTKEEVSELLARYKLRENQLPRIQAGDPVARYFGI
RRGQVVKIIRPSETAGRYITYRLVQ
|
F: |
RITTPYMTKYERARVLGTRALQIAMCAPVMPLLIAMKELK
ARKIPIIIRRYLPDGSYEDWGVDELIIT
|
G: |
MFYHISLEHEILLHPRYFLNTVKQKLFTEVEGTCTGKYGF
VIAVTTIDNIGAGVIQPGRGFVLYPVKYKAIVFRPFKGEV
VDAVVTQVNKVGLFTEIGPMSCFISRHSIPSEMEFDPNSN
PPCYKTMDEDIVIQQDDEIRLKIVGTRVDKNDIFAIGSLM
DDYLGLV
|
H: |
GILFEDIFDVKDIDPEGKKFDRVSRLHCESESFKMDLILD
VNIQIYPVDLGDKFRLVIASTLYEDGTLDDGEYNPTDDRP
SRADQFEYVMYGKVYRIEGDETSTEAATRLSAYVSYGGLL
MRLQGDANNLHGFEVDSRVYLLMKKL
|
I: |
VGIRFCQECNNMLYPKEDKENRILLYACRNCDYQQEADNS
CIYVNKITHEVDELTQIIADVSQDPTLPRTEDHPCQKCGH
KEAVFFQSHSDAMRLYYVCTAPHCGHRWTE
|
J: |
MIIPVRCFTCGKIVGNKWEAYLGLLQAEYTEGDALDALGL
KRYCCRRMLLAHVDLIEKLLNYAP
|
K: |
NAPPAFESFLLFEGEKKITINKDTKVPNACLFTINKEDHT
LGNIIKSQLLKDPQVLFAGYKVPHPLEHKIIIRVQTTPDY
SPQEAFTNAITDLISELSLLEERFRVAIKDK
|
L: |
MIYICGECHTENEICRECGYRIMYKKRTKRLVVFDAR
|
M: |
XXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXX
XXXXXPTQLLSIEESLALQKQQ
|
|
Description
|
(1) |
DNA-directed RNA polymerase II subunit RPB1 (E.C.2.7.7.6,2.7.7.48), DNA-directed RNA polymerase II subunit RPB2 (E.C.2.7.7.6), DNA-directed RNA polymerase II subunit RPB3, DNA-directed RNA polymerase II subunit RPB4, DNA-directed RNA polymerases I, II, and III subunit RPABC1, DNA-directed RNA polymerases I, II, and III subunit RPABC2, DNA-directed RNA polymerase II subunit RPB7, DNA-directed RNA polymerases I, II, and III subunit RPABC3, DNA-directed RNA polymerase II subunit RPB9, DNA-directed RNA polymerases I, II, and III subunit RPABC5, DNA-directed RNA polymerase II subunit RPB11-a, DNA-directed RNA polymerases I, II, and III subunit RPABC4, Gdown1,DNA-directed RNA polymerase II subunit GRINL1A
|
|
Functional site
|
|
1)
|
chain |
C |
residue |
88 |
type |
|
sequence |
C
|
description |
binding site for residue ZN C 301
|
source |
: AC1
|
|
2)
|
chain |
C |
residue |
90 |
type |
|
sequence |
C
|
description |
binding site for residue ZN C 301
|
source |
: AC1
|
|
3)
|
chain |
C |
residue |
93 |
type |
|
sequence |
F
|
description |
binding site for residue ZN C 301
|
source |
: AC1
|
|
4)
|
chain |
C |
residue |
94 |
type |
|
sequence |
C
|
description |
binding site for residue ZN C 301
|
source |
: AC1
|
|
5)
|
chain |
C |
residue |
97 |
type |
|
sequence |
C
|
description |
binding site for residue ZN C 301
|
source |
: AC1
|
|
6)
|
chain |
I |
residue |
17 |
type |
|
sequence |
C
|
description |
binding site for residue ZN I 201
|
source |
: AC2
|
|
7)
|
chain |
I |
residue |
20 |
type |
|
sequence |
C
|
description |
binding site for residue ZN I 201
|
source |
: AC2
|
|
8)
|
chain |
I |
residue |
39 |
type |
|
sequence |
C
|
description |
binding site for residue ZN I 201
|
source |
: AC2
|
|
9)
|
chain |
I |
residue |
42 |
type |
|
sequence |
C
|
description |
binding site for residue ZN I 201
|
source |
: AC2
|
|
10)
|
chain |
I |
residue |
86 |
type |
|
sequence |
C
|
description |
binding site for residue ZN I 202
|
source |
: AC3
|
|
11)
|
chain |
I |
residue |
89 |
type |
|
sequence |
C
|
description |
binding site for residue ZN I 202
|
source |
: AC3
|
|
12)
|
chain |
I |
residue |
114 |
type |
|
sequence |
C
|
description |
binding site for residue ZN I 202
|
source |
: AC3
|
|
13)
|
chain |
I |
residue |
119 |
type |
|
sequence |
C
|
description |
binding site for residue ZN I 202
|
source |
: AC3
|
|
14)
|
chain |
J |
residue |
7 |
type |
|
sequence |
C
|
description |
binding site for residue ZN J 101
|
source |
: AC4
|
|
15)
|
chain |
J |
residue |
10 |
type |
|
sequence |
C
|
description |
binding site for residue ZN J 101
|
source |
: AC4
|
|
16)
|
chain |
J |
residue |
44 |
type |
|
sequence |
C
|
description |
binding site for residue ZN J 101
|
source |
: AC4
|
|
17)
|
chain |
J |
residue |
45 |
type |
|
sequence |
C
|
description |
binding site for residue ZN J 101
|
source |
: AC4
|
|
18)
|
chain |
L |
residue |
19 |
type |
|
sequence |
C
|
description |
binding site for residue ZN L 101
|
source |
: AC5
|
|
19)
|
chain |
L |
residue |
21 |
type |
|
sequence |
E
|
description |
binding site for residue ZN L 101
|
source |
: AC5
|
|
20)
|
chain |
L |
residue |
22 |
type |
|
sequence |
C
|
description |
binding site for residue ZN L 101
|
source |
: AC5
|
|
21)
|
chain |
L |
residue |
39 |
type |
|
sequence |
C
|
description |
binding site for residue ZN L 101
|
source |
: AC5
|
|
22)
|
chain |
I |
residue |
112-118 |
type |
prosite |
sequence |
YVCTAPH
|
description |
IG_MHC Immunoglobulins and major histocompatibility complex proteins signature. YVCTAPH
|
source |
prosite : PS00290
|
|
23)
|
chain |
C |
residue |
32-72 |
type |
prosite |
sequence |
NSIRRVFIAEVPIIAIDWVQIDANSSVLHDEFIAHRLGLI
P
|
description |
RNA_POL_D_30KD RNA polymerases D / 30 to 40 Kd subunits signature. NSIRRvfiaevpiiAidwVqidaNsSvlhDEfIAhRLGLIP
|
source |
prosite : PS00446
|
|
24)
|
chain |
I |
residue |
86-123 |
type |
prosite |
sequence |
CQKCGHKEAVFFQSHSDAMRLYYVCTAPHCGHRW
|
description |
ZF_TFIIS_1 Zinc finger TFIIS-type signature. CqkCghkeavffqSHSARaEDAmrlyyvCtaph.CghrW
|
source |
prosite : PS00466
|
|
25)
|
chain |
I |
residue |
16-42 |
type |
prosite |
sequence |
FCQECNNMLYPKEDKENRILLYACRNC
|
description |
RNA_POL_M_15KD RNA polymerases M / 15 Kd subunits signature. FCQECNNMLypkedkenrillyaCrnC
|
source |
prosite : PS01030
|
|
26)
|
chain |
E |
residue |
142-155 |
type |
prosite |
sequence |
HELVPEHVVMTKEE
|
description |
RNA_POL_H_23KD RNA polymerases H / 23 Kd subunits signature. HELVPEHvvMtkEE
|
source |
prosite : PS01110
|
|
27)
|
chain |
F |
residue |
58-72 |
type |
prosite |
sequence |
TKYERARVLGTRALQ
|
description |
RNA_POL_K_14KD RNA polymerases K / 14 to 18 Kd subunits signature. TkYErARvLGtRAlQ
|
source |
prosite : PS01111
|
|
28)
|
chain |
J |
residue |
2-11 |
type |
prosite |
sequence |
IIPVRCFTCG
|
description |
RNA_POL_N_8KD RNA polymerases N / 8 Kd subunits signature. IIPVrCFTCG
|
source |
prosite : PS01112
|
|
29)
|
chain |
K |
residue |
35-66 |
type |
prosite |
sequence |
INKEDHTLGNIIKSQLLKDPQVLFAGYKVPHP
|
description |
RNA_POL_L_13KD RNA polymerases L / 13 to 16 Kd subunits signature. InkEdHTLgNiIksqLlkdpqVlfagYkvpHP
|
source |
prosite : PS01154
|
|
30)
|
chain |
B |
residue |
932-944 |
type |
prosite |
sequence |
GDKFASRHGQKGT
|
description |
RNA_POL_BETA RNA polymerases beta chain signature. GdKFASrHGQKGT
|
source |
prosite : PS01166
|
|
31)
|
chain |
L |
residue |
19-39 |
type |
ZN_FING |
sequence |
CGECHTENEICREC
|
description |
C4-type => ECO:0000269|PubMed:33558764, ECO:0000269|PubMed:33558766, ECO:0000269|PubMed:33674783, ECO:0000312|PDB:7DN3, ECO:0007744|PDB:7AE1, ECO:0007744|PDB:7D58
|
source |
Swiss-Prot : SWS_FT_FI1
|
|
32)
|
chain |
J |
residue |
10 |
type |
ZN_FING |
sequence |
C
|
description |
C4-type => ECO:0000269|PubMed:33558764, ECO:0000269|PubMed:33558766, ECO:0000269|PubMed:33674783, ECO:0000312|PDB:7DN3, ECO:0007744|PDB:7AE1, ECO:0007744|PDB:7D58
|
source |
Swiss-Prot : SWS_FT_FI1
|
|
33)
|
chain |
J |
residue |
44 |
type |
ZN_FING |
sequence |
C
|
description |
C4-type => ECO:0000269|PubMed:33558764, ECO:0000269|PubMed:33558766, ECO:0000269|PubMed:33674783, ECO:0000312|PDB:7DN3, ECO:0007744|PDB:7AE1, ECO:0007744|PDB:7D58
|
source |
Swiss-Prot : SWS_FT_FI1
|
|
34)
|
chain |
C |
residue |
97 |
type |
ZN_FING |
sequence |
C
|
description |
C4-type => ECO:0000269|PubMed:33558764, ECO:0000269|PubMed:33558766, ECO:0000269|PubMed:33674783, ECO:0000312|PDB:7DN3, ECO:0007744|PDB:7AE1, ECO:0007744|PDB:7D58
|
source |
Swiss-Prot : SWS_FT_FI1
|
|
35)
|
chain |
L |
residue |
19 |
type |
BINDING |
sequence |
C
|
description |
BINDING => ECO:0000269|PubMed:27193682, ECO:0000269|PubMed:33558764, ECO:0000269|PubMed:33558766, ECO:0000269|PubMed:33674783, ECO:0000312|PDB:7DN3, ECO:0007744|PDB:5IY6, ECO:0007744|PDB:7AE1, ECO:0007744|PDB:7D58
|
source |
Swiss-Prot : SWS_FT_FI2
|
|
36)
|
chain |
B |
residue |
792 |
type |
BINDING |
sequence |
D
|
description |
BINDING => ECO:0000269|PubMed:27193682, ECO:0000269|PubMed:33558764, ECO:0000269|PubMed:33558766, ECO:0000269|PubMed:33674783, ECO:0000312|PDB:7DN3, ECO:0007744|PDB:5IY6, ECO:0007744|PDB:7AE1, ECO:0007744|PDB:7D58
|
source |
Swiss-Prot : SWS_FT_FI2
|
|
37)
|
chain |
L |
residue |
22 |
type |
BINDING |
sequence |
C
|
description |
BINDING => ECO:0000269|PubMed:27193682, ECO:0000269|PubMed:33558764, ECO:0007744|PDB:5IY6, ECO:0007744|PDB:7AE1
|
source |
Swiss-Prot : SWS_FT_FI3
|
|
38)
|
chain |
I |
residue |
20 |
type |
BINDING |
sequence |
C
|
description |
BINDING => ECO:0000269|PubMed:27193682, ECO:0000269|PubMed:33558764, ECO:0007744|PDB:5IY6, ECO:0007744|PDB:7AE1
|
source |
Swiss-Prot : SWS_FT_FI3
|
|
39)
|
chain |
I |
residue |
39 |
type |
BINDING |
sequence |
C
|
description |
BINDING => ECO:0000269|PubMed:27193682, ECO:0000269|PubMed:33558764, ECO:0007744|PDB:5IY6, ECO:0007744|PDB:7AE1
|
source |
Swiss-Prot : SWS_FT_FI3
|
|
40)
|
chain |
I |
residue |
42 |
type |
BINDING |
sequence |
C
|
description |
BINDING => ECO:0000269|PubMed:27193682, ECO:0000269|PubMed:33558764, ECO:0007744|PDB:5IY6, ECO:0007744|PDB:7AE1
|
source |
Swiss-Prot : SWS_FT_FI3
|
|
41)
|
chain |
B |
residue |
942 |
type |
BINDING |
sequence |
K
|
description |
BINDING => ECO:0000269|PubMed:27193682, ECO:0000269|PubMed:33558764, ECO:0007744|PDB:5IY6, ECO:0007744|PDB:7AE1
|
source |
Swiss-Prot : SWS_FT_FI3
|
|
42)
|
chain |
L |
residue |
36 |
type |
BINDING |
sequence |
C
|
description |
BINDING => ECO:0000269|PubMed:27193682, ECO:0000269|PubMed:33558764, ECO:0000269|PubMed:33558766, ECO:0007744|PDB:5IY6, ECO:0007744|PDB:7AE1, ECO:0007744|PDB:7D58
|
source |
Swiss-Prot : SWS_FT_FI4
|
|
43)
|
chain |
I |
residue |
89 |
type |
BINDING |
sequence |
C
|
description |
BINDING => ECO:0000269|PubMed:27193682, ECO:0000269|PubMed:33558764, ECO:0000269|PubMed:33558766, ECO:0007744|PDB:5IY6, ECO:0007744|PDB:7AE1, ECO:0007744|PDB:7D58
|
source |
Swiss-Prot : SWS_FT_FI4
|
|
44)
|
chain |
I |
residue |
114 |
type |
BINDING |
sequence |
C
|
description |
BINDING => ECO:0000269|PubMed:27193682, ECO:0000269|PubMed:33558764, ECO:0000269|PubMed:33558766, ECO:0007744|PDB:5IY6, ECO:0007744|PDB:7AE1, ECO:0007744|PDB:7D58
|
source |
Swiss-Prot : SWS_FT_FI4
|
|
45)
|
chain |
I |
residue |
119 |
type |
BINDING |
sequence |
C
|
description |
BINDING => ECO:0000269|PubMed:27193682, ECO:0000269|PubMed:33558764, ECO:0000269|PubMed:33558766, ECO:0007744|PDB:5IY6, ECO:0007744|PDB:7AE1, ECO:0007744|PDB:7D58
|
source |
Swiss-Prot : SWS_FT_FI4
|
|
46)
|
chain |
L |
residue |
39 |
type |
BINDING |
sequence |
C
|
description |
BINDING => ECO:0000269|PubMed:27193682, ECO:0000269|PubMed:33558766, ECO:0000269|PubMed:33674783, ECO:0000312|PDB:7DN3, ECO:0007744|PDB:5IY6, ECO:0007744|PDB:7D58
|
source |
Swiss-Prot : SWS_FT_FI5
|
|
47)
|
chain |
B |
residue |
1052 |
type |
MOD_RES |
sequence |
K
|
description |
N6-methyllysine => ECO:0007744|PubMed:24129315
|
source |
Swiss-Prot : SWS_FT_FI6
|
|
|
|