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DNA polymerase III subunit tau (EC 2.7.7.7) (DNA polymerase III subunit gamma)

 DPO3X_ECOLI             Reviewed;         643 AA.
P06710; Q2MBV7; Q47721;
01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
01-JAN-1988, sequence version 1.
20-JUN-2018, entry version 178.
RecName: Full=DNA polymerase III subunit tau;
EC=2.7.7.7;
AltName: Full=DNA polymerase III subunit gamma;
Name=dnaX; Synonyms=dnaZ, dnaZX; OrderedLocusNames=b0470, JW0459;
Escherichia coli (strain K12).
Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
Enterobacteriaceae; Escherichia.
NCBI_TaxID=83333;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=K12 / JM109 / ATCC 53323;
PubMed=3534795; DOI=10.1093/nar/14.20.8091;
Flower A.M., McHenry C.S.;
"The adjacent dnaZ and dnaX genes of Escherichia coli are contained
within one continuous open reading frame.";
Nucleic Acids Res. 14:8091-8101(1986).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=3018672; DOI=10.1093/nar/14.16.6541;
Yin K.-C., Blinkowa A.L., Walker J.R.;
"Nucleotide sequence of the Escherichia coli replication gene dnaZX.";
Nucleic Acids Res. 14:6541-6549(1986).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / MG1655 / ATCC 47076;
Chung E., Allen E., Araujo R., Aparicio A.M., Davis K., Duncan M.,
Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., Lew H., Lin D.,
Namath A., Oefner P., Roberts D., Schramm S., Davis R.W.;
"Sequence of minutes 4-25 of Escherichia coli.";
Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / MG1655 / ATCC 47076;
PubMed=9278503; DOI=10.1126/science.277.5331.1453;
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J.,
Mau B., Shao Y.;
"The complete genome sequence of Escherichia coli K-12.";
Science 277:1453-1462(1997).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
PubMed=16738553; DOI=10.1038/msb4100049;
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
"Highly accurate genome sequences of Escherichia coli K-12 strains
MG1655 and W3110.";
Mol. Syst. Biol. 2:E1-E5(2006).
[6]
PROTEIN SEQUENCE OF 1-13.
STRAIN=ATCC 33694 / HB101;
PubMed=3283125;
Maki S., Kornberg A.;
"DNA polymerase III holoenzyme of Escherichia coli. I. Purification
and distinctive functions of subunits tau and gamma, the dnaZX gene
products.";
J. Biol. Chem. 263:6547-6554(1988).
[7]
PROBABLE FUNCTION OF TAU IN DIMERIZATION OF DNA POLYMERASE.
STRAIN=HMS 83;
PubMed=7037770;
McHenry C.S.;
"Purification and characterization of DNA polymerase III'.
Identification of tau as a subunit of the DNA polymerase III
holoenzyme.";
J. Biol. Chem. 257:2657-2663(1982).
[8]
RIBOSOMAL FRAMESHIFT, ISOFORMS TAU AND GAMMA, AND PROTEIN SEQUENCE OF
428-431 (ISOFORM GAMMA).
PubMed=2181440; DOI=10.1073/pnas.87.7.2516;
Tsuchihashi Z., Kornberg A.;
"Translational frameshifting generates the gamma subunit of DNA
polymerase III holoenzyme.";
Proc. Natl. Acad. Sci. U.S.A. 87:2516-2520(1990).
[9]
RIBOSOMAL FRAMESHIFT, AND ISOFORMS TAU AND GAMMA.
STRAIN=K12 / JM103Y;
PubMed=2186364; DOI=10.1093/nar/18.7.1725;
Blinkowa A.L., Walker J.R.;
"Programmed ribosomal frameshifting generates the Escherichia coli DNA
polymerase III gamma subunit from within the tau subunit reading
frame.";
Nucleic Acids Res. 18:1725-1729(1990).
[10]
RIBOSOMAL FRAMESHIFT, AND ISOFORMS TAU AND GAMMA.
STRAIN=K12;
PubMed=2187190; DOI=10.1073/pnas.87.10.3713;
Flower A.M., McHenry C.S.;
"The gamma subunit of DNA polymerase III holoenzyme of Escherichia
coli is produced by ribosomal frameshifting.";
Proc. Natl. Acad. Sci. U.S.A. 87:3713-3717(1990).
[11]
FUNCTION, AND SUBUNIT.
PubMed=2040637;
Stukenberg P.T., Studwell-Vaughan P.S., O'Donnell M.;
"Mechanism of the sliding beta-clamp of DNA polymerase III
holoenzyme.";
J. Biol. Chem. 266:11328-11334(1991).
[12]
REVIEW.
PubMed=1575709; DOI=10.1002/bies.950140206;
O'Donnell M.;
"Accessory protein function in the DNA polymerase III holoenzyme from
E. coli.";
Bioessays 14:105-111(1992).
[13]
IDENTIFICATION BY 2D-GEL.
PubMed=9298644; DOI=10.1002/elps.1150180805;
VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R.,
Neidhardt F.C.;
"Escherichia coli proteome analysis using the gene-protein database.";
Electrophoresis 18:1243-1251(1997).
[14]
IDENTIFICATION OF TEMPERATURE-SENSITIVE ALLELES, FUNCTION, AND
MUTAGENESIS OF GLY-118 AND GLU-601.
STRAIN=K12;
PubMed=8376347; DOI=10.1128/jb.175.18.6018-6027.1993;
Blinkova A., Hervas C., Stukenberg P.T., Onrust R., O'Donnell M.E.,
Walker J.R.;
"The Escherichia coli DNA polymerase III holoenzyme contains both
products of the dnaX gene, tau and gamma, but only tau is essential.";
J. Bacteriol. 175:6018-6027(1993).
[15]
FUNCTION OF GAMMA, AND SUBUNIT.
PubMed=9927437; DOI=10.1093/emboj/18.3.771;
Turner J., Hingorani M.M., Kelman Z., O'Donnell M.;
"The internal workings of a DNA polymerase clamp-loading machine.";
EMBO J. 18:771-783(1999).
[16]
REPLISOME COMPLEX, AND SUBUNIT.
PubMed=20413500; DOI=10.1126/science.1185757;
Reyes-Lamothe R., Sherratt D.J., Leake M.C.;
"Stoichiometry and architecture of active DNA replication machinery in
Escherichia coli.";
Science 328:498-501(2010).
[17]
REPLISOME COMPLEX, AND SUBUNIT.
PubMed=22157955; DOI=10.1038/nsmb.2179;
Georgescu R.E., Kurth I., O'Donnell M.E.;
"Single-molecule studies reveal the function of a third polymerase in
the replisome.";
Nat. Struct. Mol. Biol. 19:113-116(2011).
[18] {ECO:0000244|PDB:1JR3}
X-RAY CRYSTALLOGRAPHY (2.70 ANGSTROMS) OF 1-373 (GAMMA) IN COMPLEX
WITH HOLA AND HOLB.
PubMed=11525729; DOI=10.1016/S0092-8674(01)00463-9;
Jeruzalmi D., O'Donnell M., Kuriyan J.;
"Crystal structure of the processivity clamp loader gamma (gamma)
complex of E. coli DNA polymerase III.";
Cell 106:429-441(2001).
[19] {ECO:0000244|PDB:5FKU, ECO:0000244|PDB:5FKV}
STRUCTURE BY ELECTRON MICROSCOPY (8.00 ANGSTROMS) OF 500-643 OF DNAE;
DNAN; DNAQ; DNAX WITH AND WITHOUT DNA, AND SUBUNIT.
PubMed=26499492; DOI=10.7554/eLife.11134;
Fernandez-Leiro R., Conrad J., Scheres S.H., Lamers M.H.;
"cryo-EM structures of the E. coli replicative DNA polymerase reveal
its dynamic interactions with the DNA sliding clamp, exonuclease and
tau.";
Elife 4:0-0(2015).
-!- FUNCTION: Part of the beta sliding clamp loading complex, which
hydrolyzes ATP to load the beta clamp onto primed DNA to form the
DNA replication pre-initiation complex (PubMed:2040637). DNA
polymerase III is a complex, multichain enzyme responsible for
most of the replicative synthesis in bacteria. This DNA polymerase
also exhibits 3'-5' exonuclease activity. The gamma complex
(gamma(3),delta,delta') is thought to load beta dimers onto DNA by
binding ATP which alters the complex's conformation so it can bind
beta sliding clamp dimers and open them at one interface. Primed
DNA is recognized, ATP is hydrolyzed releasing the gamma complex
and closing the beta sliding clamp ring around the primed DNA
(PubMed:9927437). {ECO:0000269|PubMed:2040637}.
-!- FUNCTION: Isoform tau: serves as a scaffold to trimerize the core
complex (PubMed:7037770). {ECO:0000305|PubMed:7037770}.
-!- FUNCTION: Isoform gamma: interacts with the delta and delta'
subunits to transfer the beta subunit on the DNA (PubMed:9927437).
Interacts with ATP, drives ATP-induced conformational changes in
the gamma complex that opens the beta sliding clamp ring. After
loading of primed DNA ATP is hydrolyzed and the beta sliding clamp
ring closes (PubMed:9927437). {ECO:0000269|PubMed:9927437}.
-!- CATALYTIC ACTIVITY: Deoxynucleoside triphosphate + DNA(n) =
diphosphate + DNA(n+1).
-!- SUBUNIT: The DNA polymerase III holoenzyme complex contains at
least 10 different subunits organized into 3 functionally
essential subassemblies: the Pol III core, the beta sliding clamp
processivity factor and the clamp-loading complex. The Pol III
core (subunits alpha, epsilon and theta) contains the polymerase
and the 3'-5' exonuclease proofreading activities
(PubMed:2040637). The polymerase is tethered to the template via
the dimeric beta sliding clamp processivity factor. The clamp-
loading complex (also called gamma complex) assembles the beta
sliding clamp onto the primed template and plays a central role in
the organization and communication at the replication fork. The
clamp-loading complex contains delta, delta', psi and chi, and 3
copies of either or both of two different DnaX proteins, gamma and
tau. The DNA replisome complex has a single clamp loader (3 tau
and 1 each of delta, delta', psi and chi subunits) which binds 3
Pol III cores (1 core on the leading strand and 2 on the lagging
strand) each with a beta sliding clamp dimer. Additional proteins
in the replisome are other copies of gamma, psi and chi, Ssb, DNA
helicase and RNA primase (PubMed:20413500, PubMed:22157955). The
clamp loader hydrolyzes ATP to assemble the beta processivity
factor onto the primed template (PubMed:2040637, PubMed:9927437)
and plays a central role in the organization and communication at
the replication fork; the minimal complex to load the beta sliding
clamp on DNA is delta, delta', gamma (PubMed:9927437).
{ECO:0000269|PubMed:11525729, ECO:0000269|PubMed:2040637,
ECO:0000269|PubMed:20413500, ECO:0000269|PubMed:22157955,
ECO:0000269|PubMed:9927437}.
-!- INTERACTION:
Self; NbExp=9; IntAct=EBI-549140, EBI-549140;
P11989:bglG; NbExp=3; IntAct=EBI-549140, EBI-545674;
P0ACB0:dnaB; NbExp=2; IntAct=EBI-549140, EBI-548978;
P10443:dnaE; NbExp=11; IntAct=EBI-549140, EBI-549111;
P0A988:dnaN; NbExp=4; IntAct=EBI-549140, EBI-542385;
P03007:dnaQ; NbExp=6; IntAct=EBI-549140, EBI-549131;
P20605:fic; NbExp=2; IntAct=EBI-549140, EBI-1132602;
P28630:holA; NbExp=19; IntAct=EBI-549140, EBI-549153;
P28631:holB; NbExp=26; IntAct=EBI-549140, EBI-549161;
P28905:holC; NbExp=20; IntAct=EBI-549140, EBI-549169;
P28632:holD; NbExp=26; IntAct=EBI-549140, EBI-549176;
P23367:mutL; NbExp=2; IntAct=EBI-2604194, EBI-554913;
P0A7L0:rplA; NbExp=2; IntAct=EBI-549140, EBI-543771;
P0AGE0:ssb; NbExp=2; IntAct=EBI-549140, EBI-1118620;
-!- ALTERNATIVE PRODUCTS:
Event=Ribosomal frameshifting; Named isoforms=2;
Comment=The production of the two protein products from this
region is due to programmed ribosomal frameshifting.
Frameshifting is about 40% efficient.
{ECO:0000269|PubMed:2181440, ECO:0000269|PubMed:2186364,
ECO:0000269|PubMed:2187190};
Name=tau;
IsoId=P06710-1; Sequence=Displayed;
Note=Produced by full-length translation of the dnaX gene. This
isoform is essential, constructs that express only the gamma
isoform are not viable (Ref.14). {ECO:0000269|PubMed:8376347};
Name=gamma;
IsoId=P06710-2; Sequence=VSP_042848, VSP_042849;
Note=Formed by programmed ribosomal frameshifting to a premature
stop codon in the -1 frame at codon 430, the last residue is
thus Glu and not Ser. Mutants which remove the frameshift are
viable, suggesting strongly that gamma is not essential for
viability (Ref.14). {ECO:0000269|PubMed:2181440,
ECO:0000269|PubMed:2186364, ECO:0000269|PubMed:2187190,
ECO:0000269|PubMed:8376347};
-!- SIMILARITY: Belongs to the DnaX/STICHEL family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=CAA28175.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
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EMBL; X04487; CAA28174.1; -; Genomic_DNA.
EMBL; X04487; CAA28175.1; ALT_INIT; Genomic_DNA.
EMBL; X04275; CAA27827.1; -; Genomic_DNA.
EMBL; U82664; AAB40224.1; -; Genomic_DNA.
EMBL; U00096; AAC73572.1; -; Genomic_DNA.
EMBL; AP009048; BAE76249.1; -; Genomic_DNA.
EMBL; M38777; AAA23457.1; -; Genomic_DNA.
PIR; A25549; DJEC3G.
RefSeq; NP_415003.1; NC_000913.3.
RefSeq; WP_000122013.1; NZ_LN832404.1.
PDB; 1JR3; X-ray; 2.70 A; A/B/C=1-373.
PDB; 1NJF; X-ray; 2.30 A; A/B/C/D=1-243.
PDB; 1NJG; X-ray; 2.20 A; A/B=1-243.
PDB; 1XXH; X-ray; 3.45 A; B/C/D/G/H/I=1-373.
PDB; 1XXI; X-ray; 4.10 A; B/C/D/G/H/I=1-368.
PDB; 2AYA; NMR; -; A=499-625.
PDB; 3GLF; X-ray; 3.39 A; B/C/D/G/H/I=1-373.
PDB; 3GLG; X-ray; 3.25 A; B/C/D/G/H/I=1-373.
PDB; 3GLH; X-ray; 3.89 A; B/C/D/G/H/I/L/M/N=1-373.
PDB; 3GLI; X-ray; 3.50 A; B/C/D/G/H/I=1-373.
PDB; 5FKU; EM; 8.34 A; E=500-643.
PDB; 5FKV; EM; 8.00 A; E=500-643.
PDBsum; 1JR3; -.
PDBsum; 1NJF; -.
PDBsum; 1NJG; -.
PDBsum; 1XXH; -.
PDBsum; 1XXI; -.
PDBsum; 2AYA; -.
PDBsum; 3GLF; -.
PDBsum; 3GLG; -.
PDBsum; 3GLH; -.
PDBsum; 3GLI; -.
PDBsum; 5FKU; -.
PDBsum; 5FKV; -.
ProteinModelPortal; P06710; -.
SMR; P06710; -.
BioGrid; 4259846; 140.
ComplexPortal; CPX-1926; DNA polymerase III clamp loader complex. [P06710-1]
DIP; DIP-9464N; -.
IntAct; P06710; 33.
STRING; 316385.ECDH10B_0426; -.
BindingDB; P06710; -.
DrugBank; DB02930; Phosphothiophosphoric Acid-Adenylate Ester.
EPD; P06710; -.
PaxDb; P06710; -.
PRIDE; P06710; -.
EnsemblBacteria; AAC73572; AAC73572; b0470.
EnsemblBacteria; BAE76249; BAE76249; BAE76249.
GeneID; 945105; -.
KEGG; ecj:JW0459; -.
KEGG; eco:b0470; -.
PATRIC; fig|1411691.4.peg.1806; -.
EchoBASE; EB0241; -.
EcoGene; EG10245; dnaX.
eggNOG; ENOG4107QMP; Bacteria.
eggNOG; COG2812; LUCA.
HOGENOM; HOG000083934; -.
InParanoid; P06710; -.
KO; K02343; -.
OMA; FFYQVIV; -.
PhylomeDB; P06710; -.
BioCyc; MetaCyc:EG10245-MONOMER; -.
BioCyc; MetaCyc:MONOMER0-2383; -.
EvolutionaryTrace; P06710; -.
PRO; PR:P06710; -.
Proteomes; UP000000318; Chromosome.
Proteomes; UP000000625; Chromosome.
GO; GO:0043846; C:DNA polymerase III, clamp loader complex; IDA:EcoliWiki.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0016887; F:ATPase activity; IDA:EcoliWiki.
GO; GO:0003677; F:DNA binding; IEA:InterPro.
GO; GO:0030337; F:DNA polymerase processivity factor activity; IDA:EcoliWiki.
GO; GO:0003887; F:DNA-directed DNA polymerase activity; IEA:UniProtKB-KW.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0017111; F:nucleoside-triphosphatase activity; IDA:EcoliWiki.
GO; GO:0006260; P:DNA replication; IMP:EcoliWiki.
GO; GO:0006261; P:DNA-dependent DNA replication; IBA:GO_Central.
Gene3D; 3.30.300.150; -; 1.
InterPro; IPR003593; AAA+_ATPase.
InterPro; IPR001270; ClpA/B.
InterPro; IPR008921; DNA_pol3_clamp-load_cplx_C.
InterPro; IPR022001; DNA_pol3_tau_IV.
InterPro; IPR022754; DNA_pol_III_gamma-3.
InterPro; IPR012763; DNA_pol_III_sug/sutau.
InterPro; IPR021029; DNA_pol_III_tau_dom-5.
InterPro; IPR027417; P-loop_NTPase.
InterPro; IPR038249; PolIII_tau_C_sf.
Pfam; PF12169; DNA_pol3_gamma3; 1.
Pfam; PF12168; DNA_pol3_tau_4; 1.
Pfam; PF12170; DNA_pol3_tau_5; 1.
PRINTS; PR00300; CLPPROTEASEA.
SMART; SM00382; AAA; 1.
SUPFAM; SSF48019; SSF48019; 1.
SUPFAM; SSF52540; SSF52540; 1.
TIGRFAMs; TIGR02397; dnaX_nterm; 1.
1: Evidence at protein level;
3D-structure; ATP-binding; Complete proteome;
Direct protein sequencing; DNA replication;
DNA-directed DNA polymerase; Nucleotide-binding;
Nucleotidyltransferase; Reference proteome; Ribosomal frameshifting;
Transferase.
INIT_MET 1 1 Removed.
CHAIN 2 643 DNA polymerase III subunit tau.
/FTId=PRO_0000007360.
NP_BIND 45 52 ATP. {ECO:0000255}.
VAR_SEQ 431 431 S -> E (in isoform gamma). {ECO:0000305}.
/FTId=VSP_042848.
VAR_SEQ 432 643 Missing (in isoform gamma).
{ECO:0000305}.
/FTId=VSP_042849.
MUTAGEN 118 118 G->D: In dnaX2016(Ts); present in both
isoforms, unable to grow at 42 degrees
Celsius. {ECO:0000269|PubMed:8376347}.
MUTAGEN 601 601 E->K: In dnaX36(Ts); present only in
isoform tau, unable to grow at 42 degrees
Celsius. {ECO:0000269|PubMed:8376347}.
HELIX 6 9 {ECO:0000244|PDB:1NJG}.
HELIX 15 17 {ECO:0000244|PDB:1NJG}.
HELIX 22 34 {ECO:0000244|PDB:1NJG}.
STRAND 39 44 {ECO:0000244|PDB:1NJG}.
STRAND 46 50 {ECO:0000244|PDB:3GLF}.
HELIX 51 63 {ECO:0000244|PDB:1NJG}.
HELIX 77 83 {ECO:0000244|PDB:1NJG}.
STRAND 88 94 {ECO:0000244|PDB:1NJG}.
TURN 95 97 {ECO:0000244|PDB:3GLG}.
HELIX 98 100 {ECO:0000244|PDB:1NJG}.
HELIX 101 109 {ECO:0000244|PDB:1NJG}.
STRAND 111 113 {ECO:0000244|PDB:3GLG}.
STRAND 116 126 {ECO:0000244|PDB:1NJG}.
HELIX 128 130 {ECO:0000244|PDB:1NJG}.
HELIX 133 144 {ECO:0000244|PDB:1NJG}.
STRAND 150 157 {ECO:0000244|PDB:1NJG}.
HELIX 159 161 {ECO:0000244|PDB:1NJG}.
HELIX 164 167 {ECO:0000244|PDB:1NJG}.
STRAND 170 174 {ECO:0000244|PDB:1NJG}.
HELIX 180 193 {ECO:0000244|PDB:1NJG}.
HELIX 200 210 {ECO:0000244|PDB:1NJG}.
HELIX 214 225 {ECO:0000244|PDB:1NJG}.
TURN 226 229 {ECO:0000244|PDB:1NJG}.
STRAND 230 232 {ECO:0000244|PDB:1NJG}.
HELIX 234 240 {ECO:0000244|PDB:1NJG}.
HELIX 248 257 {ECO:0000244|PDB:3GLG}.
HELIX 261 274 {ECO:0000244|PDB:3GLG}.
HELIX 278 294 {ECO:0000244|PDB:3GLG}.
TURN 295 297 {ECO:0000244|PDB:3GLG}.
HELIX 299 301 {ECO:0000244|PDB:3GLG}.
TURN 304 306 {ECO:0000244|PDB:3GLF}.
HELIX 307 318 {ECO:0000244|PDB:3GLG}.
HELIX 322 338 {ECO:0000244|PDB:3GLG}.
TURN 339 341 {ECO:0000244|PDB:3GLG}.
STRAND 342 344 {ECO:0000244|PDB:3GLG}.
HELIX 345 358 {ECO:0000244|PDB:3GLG}.
STRAND 361 363 {ECO:0000244|PDB:3GLG}.
HELIX 507 520 {ECO:0000244|PDB:2AYA}.
HELIX 522 530 {ECO:0000244|PDB:2AYA}.
HELIX 535 541 {ECO:0000244|PDB:2AYA}.
STRAND 543 547 {ECO:0000244|PDB:2AYA}.
STRAND 549 556 {ECO:0000244|PDB:2AYA}.
HELIX 558 560 {ECO:0000244|PDB:2AYA}.
TURN 561 563 {ECO:0000244|PDB:2AYA}.
HELIX 566 580 {ECO:0000244|PDB:2AYA}.
STRAND 585 590 {ECO:0000244|PDB:2AYA}.
HELIX 599 620 {ECO:0000244|PDB:2AYA}.
SEQUENCE 643 AA; 71138 MW; D2028BD99E375150 CRC64;
MSYQVLARKW RPQTFADVVG QEHVLTALAN GLSLGRIHHA YLFSGTRGVG KTSIARLLAK
GLNCETGITA TPCGVCDNCR EIEQGRFVDL IEIDAASRTK VEDTRDLLDN VQYAPARGRF
KVYLIDEVHM LSRHSFNALL KTLEEPPEHV KFLLATTDPQ KLPVTILSRC LQFHLKALDV
EQIRHQLEHI LNEEHIAHEP RALQLLARAA EGSLRDALSL TDQAIASGDG QVSTQAVSAM
LGTLDDDQAL SLVEAMVEAN GERVMALINE AAARGIEWEA LLVEMLGLLH RIAMVQLSPA
ALGNDMAAIE LRMRELARTI PPTDIQLYYQ TLLIGRKELP YAPDRRMGVE MTLLRALAFH
PRMPLPEPEV PRQSFAPVAP TAVMTPTQVP PQPQSAPQQA PTVPLPETTS QVLAARQQLQ
RVQGATKAKK SEPAAATRAR PVNNAALERL ASVTDRVQAR PVPSALEKAP AKKEAYRWKA
TTPVMQQKEV VATPKALKKA LEHEKTPELA AKLAAEAIER DPWAAQVSQL SLPKLVEQVA
LNAWKEESDN AVCLHLRSSQ RHLNNRGAQQ KLAEALSMLK GSTVELTIVE DDNPAVRTPL
EWRQAIYEEK LAQARESIIA DNNIQTLRRF FDAELDEESI RPI


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EIAAB35787 DNA-directed RNA polymerase II subunit J-1,DNA-directed RNA polymerase II subunit RPB11-a,Homo sapiens,Human,POLR2J,POLR2J1,RNA polymerase II 13.3 kDa subunit,RNA polymerase II subunit B11-a,RPB11a
EIAAB35827 DNA-directed RNA polymerase III subunit G,DNA-directed RNA polymerase III subunit RPC7,Homo sapiens,Human,POLR3G,RNA polymerase III 32 kDa subunit,RNA polymerase III subunit C7,RPC32
EIAAB35815 DNA-directed RNA polymerase III subunit C,DNA-directed RNA polymerase III subunit RPC3,Homo sapiens,Human,POLR3C,RNA polymerase III 62 kDa subunit,RNA polymerase III subunit C3,RPC62
EIAAB35796 DNA-directed RNA polymerase II subunit D,DNA-directed RNA polymerase II subunit RPB4,Homo sapiens,Human,POLR2D,RNA polymerase II 16 kDa subunit,RNA polymerase II subunit B4,RPB16
EIAAB35786 DNA-directed RNA polymerase II subunit J,DNA-directed RNA polymerase II subunit RPB11,Mouse,Mus musculus,Polr2j,RNA polymerase II 13.3 kDa subunit,RNA polymerase II subunit B11,RPB14,Rpo2-4
EIAAB35802 DNA-directed RNA polymerase II subunit I,DNA-directed RNA polymerase II subunit RPB9,Homo sapiens,Human,POLR2I,RNA polymerase II 14.5 kDa subunit,RNA polymerase II subunit B9,RPB14.5
EIAAB35825 DNA-directed RNA polymerase III subunit F,DNA-directed RNA polymerase III subunit RPC6,Homo sapiens,Human,POLR3F,RNA polymerase III 39 kDa subunit,RNA polymerase III subunit C6,RPC39
EIAAB35750 DNA-directed RNA polymerase I subunit E,DNA-directed RNA polymerase I subunit RPA49,Homo sapiens,Human,PAF53,POLR1E,PRAF1,RNA polymerase I subunit A49,RNA polymerase I-associated factor 1,RNA polymera
EIAAB11819 DNA polymerase gamma accessory 55 kDa subunit,DNA polymerase subunit gamma-2, mitochondrial,Homo sapiens,Human,Mitochondrial DNA polymerase accessory subunit,MtPolB,MTPOLB,p55,POLG2,PolG-beta
EIAAB35749 DNA-directed RNA polymerase I subunit E,DNA-directed RNA polymerase I subunit RPA49,Mouse,Mus musculus,Paf53,Polr1e,Praf1,RNA polymerase I subunit A49,RNA polymerase I-associated factor 1,RNA polymera
EIAAB35785 DNA-directed RNA polymerase II subunit A,DNA-directed RNA polymerase II subunit RPB1,DNA-directed RNA polymerase III largest subunit,Mouse,Mus musculus,Polr2a,RNA polymerase II subunit B1,Rpii215,Rpo2
EIAAB35736 A190,DNA-directed RNA polymerase I largest subunit,DNA-directed RNA polymerase I subunit A,DNA-directed RNA polymerase I subunit RPA1,Homo sapiens,Human,POLR1A,RNA polymerase I 194 kDa subunit,RNA pol
EIAAB35784 DNA-directed RNA polymerase II subunit A,DNA-directed RNA polymerase II subunit RPB1,DNA-directed RNA polymerase III largest subunit,Homo sapiens,Human,POLR2,POLR2A,RNA polymerase II subunit B1,RNA-di
EIAAB35810 Bos taurus,Bovine,DNA-directed RNA polymerase III subunit K,DNA-directed RNA polymerase III subunit RPC10,POLR3K,RNA polymerase III subunit C10,RNA polymerase III subunit C11,RPC11
EIAAB35811 DNA-directed RNA polymerase III subunit K,DNA-directed RNA polymerase III subunit RPC10,Mouse,Mus musculus,Polr3k,RNA polymerase III subunit C10,RNA polymerase III subunit C11,RPC11
EIAAB35804 DNA-directed RNA polymerase II subunit I,DNA-directed RNA polymerase II subunit RPB9,Mouse,Mus musculus,Polr2i,RNA polymerase II 14.5 kDa subunit,RNA polymerase II subunit B9,RPB14.5
EIAAB35820 BN51,BN51T,DNA-directed RNA polymerase III subunit D,DNA-directed RNA polymerase III subunit RPC4,Homo sapiens,Human,POLR3D,Protein BN51,RNA polymerase III 47 kDa subunit,RNA polymerase III subunit C4
EIAAB11821 DNA polymerase gamma accessory 55 kDa subunit,DNA polymerase subunit gamma-2, mitochondrial,Mitochondrial DNA polymerase accessory subunit,Mouse,MtPolB,Mtpolb,Mus musculus,p55,Polg2,PolG-beta
EIAAB35821 DNA-directed RNA polymerase III subunit RPC5,Mouse,Mus musculus,Polr3e,RNA polymerase III subunit 5,RNA polymerase III subunit C5,Sex-lethal interactor homolog,Sin
EIAAB35735 A194,DNA-directed RNA polymerase I largest subunit,DNA-directed RNA polymerase I subunit A,DNA-directed RNA polymerase I subunit RPA1,Polr1a,Rat,Rattus norvegicus,RNA polymerase I 194 kDa subunit,RNA
EIAAB35737 DNA-directed RNA polymerase I largest subunit,DNA-directed RNA polymerase I subunit A,DNA-directed RNA polymerase I subunit RPA1,Mouse,Mus musculus,Polr1a,RNA polymerase I 194 kDa subunit,RNA polymera
EIAAB35808 DNA-directed RNA polymerase III largest subunit,DNA-directed RNA polymerase III subunit A,DNA-directed RNA polymerase III subunit RPC1,Homo sapiens,Human,POLR3A,RNA polymerase III 155 kDa subunit,RNA
EIAAB35805 DNA-directed RNA polymerase II subunit I,DNA-directed RNA polymerase II subunit RPB9,Pig,POLR2I,RNA polymerase II 14.5 kDa subunit,RNA polymerase II subunit B9,RPB14.5,Sus scrofa


 

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