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DNA-directed RNA polymerase subunit alpha (RNAP subunit alpha) (EC 2.7.7.6) (RNA polymerase subunit alpha) (Transcriptase subunit alpha)

 RPOA_ECOLI              Reviewed;         329 AA.
P0A7Z4; P00574; Q2M6W0;
21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
21-JUL-1986, sequence version 1.
10-OCT-2018, entry version 134.
RecName: Full=DNA-directed RNA polymerase subunit alpha;
Short=RNAP subunit alpha;
EC=2.7.7.6;
AltName: Full=RNA polymerase subunit alpha;
AltName: Full=Transcriptase subunit alpha;
Name=rpoA; Synonyms=pez, phs, sez; OrderedLocusNames=b3295, JW3257;
Escherichia coli (strain K12).
Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
Enterobacteriaceae; Escherichia.
NCBI_TaxID=83333;
[1]
PROTEIN SEQUENCE.
PubMed=323055; DOI=10.1016/0014-5793(77)80131-2;
Ovchinnikov Y.A., Lipkin V.M., Modyanov N.N., Chertov O.Y.,
Smirnov Y.V.;
"Primary structure of alpha-subunit of DNA-dependent RNA polymerase
from Escherichia coli.";
FEBS Lett. 76:108-111(1977).
[2]
PROTEIN SEQUENCE.
Modyanov N.N., Lipkin V.M., Smirnov Y.V., Shuvaeva T.M.,
Kocherginskaya S.A.;
"The primary structure of alpha-subunit of DNA-dependent RNA
polymerase from E. coli. V. The cyanogen bromide peptides.";
Bioorg. Khim. 4:437-449(1978).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=6379605; DOI=10.1093/nar/12.14.5813;
Meek D.W., Hayward R.S.;
"Nucleotide sequence of the rpoA-rplQ DNA of Escherichia coli: a
second regulatory binding site for protein S4?";
Nucleic Acids Res. 12:5813-5821(1984).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=K12;
PubMed=2989779; DOI=10.1093/nar/13.11.3891;
Bedwell D.M., Davis G.R., Gosink M., Post L.E., Nomura M., Kestler H.,
Zengel J.M., Lindahl L.;
"Nucleotide sequence of the alpha ribosomal protein operon of
Escherichia coli.";
Nucleic Acids Res. 13:3891-3903(1985).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], DOMAIN, SUBUNIT, AND MUTAGENESIS OF
ARG-45 AND ARG-191.
STRAIN=K12;
PubMed=2235479; DOI=10.1093/nar/18.20.5945;
Igarashi K., Fujita N., Ishihama A.;
"Sequence analysis of two temperature-sensitive mutations in the alpha
subunit gene (rpoA) of Escherichia coli RNA polymerase.";
Nucleic Acids Res. 18:5945-5948(1990).
[6]
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).
[7]
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).
[8]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-159.
PubMed=387752;
Post L.E., Nomura M.;
"Nucleotide sequence of the intercistronic region preceding the gene
for RNA polymerase subunit alpha in Escherichia coli.";
J. Biol. Chem. 254:10604-10606(1979).
[9]
PROTEIN SEQUENCE OF 1-19.
STRAIN=K12 / EMG2;
PubMed=9298646; DOI=10.1002/elps.1150180807;
Link A.J., Robison K., Church G.M.;
"Comparing the predicted and observed properties of proteins encoded
in the genome of Escherichia coli K-12.";
Electrophoresis 18:1259-1313(1997).
[10]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-12.
STRAIN=K12;
PubMed=3894886; DOI=10.1007/BF00330268;
Schnier J., Isono S., Cumberlidge A.G., Isono K.;
"Unstable mutations caused by regional tandem multiplications in the
gene for ribosomal protein S4 show thermosensitivity in Escherichia
coli.";
Mol. Gen. Genet. 199:265-270(1985).
[11]
PROTEIN SEQUENCE OF 1-4.
STRAIN=K12;
PubMed=1095419; DOI=10.1016/0014-5793(75)81001-5;
Fujiki H., Zurek G.;
"The subunits of DNA-dependent RNA polymerase from E. coli: I. Amino
acid analysis and primary structure of the N-terminal regions.";
FEBS Lett. 55:242-244(1975).
[12]
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).
[13]
FUNCTION IN TRANSCRIPTION, PROBABLE INTERACTION WITH CRP, SUBUNIT, AND
DOMAIN.
PubMed=1646077; DOI=10.1016/0092-8674(91)90553-B;
Igarashi K., Ishihama A.;
"Bipartite functional map of the E. coli RNA polymerase alpha subunit:
involvement of the C-terminal region in transcription activation by
cAMP-CRP.";
Cell 65:1015-1022(1991).
[14]
INTERACTION WITH CRP, AND MUTAGENESIS OF 162-GLU--GLU-165 AND GLU-165.
PubMed=8978616; DOI=10.1016/S0092-8674(00)81806-1;
Niu W., Kim Y., Tau G., Heyduk T., Ebright R.H.;
"Transcription activation at class II CAP-dependent promoters: two
interactions between CAP and RNA polymerase.";
Cell 87:1123-1134(1996).
[15]
ACETYLATION AT LYS-297 AND LYS-298.
PubMed=21696463; DOI=10.1111/j.1365-2958.2011.07742.x;
Lima B.P., Antelmann H., Gronau K., Chi B.K., Becher D.,
Brinsmade S.R., Wolfe A.J.;
"Involvement of protein acetylation in glucose-induced transcription
of a stress-responsive promoter.";
Mol. Microbiol. 81:1190-1204(2011).
[16]
STRUCTURE BY NMR OF 233-349.
PubMed=7491496; DOI=10.1126/science.270.5241.1495;
Jeon Y.H., Negishi T., Shirakawa M., Yamazaki T., Fujita N.,
Ishihama A., Kyogoku Y.;
"Solution structure of the activator contact domain of the RNA
polymerase alpha subunit.";
Science 270:1495-1497(1995).
[17]
X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 1-235.
PubMed=9657722; DOI=10.1126/science.281.5374.262;
Zhang G., Darst S.A.;
"Structure of the Escherichia coli RNA polymerase alpha subunit amino-
terminal domain.";
Science 281:262-266(1998).
[18]
X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS) OF 246-329 IN COMPLEX WITH DNA
AND CRP, INTERACTION WITH CRP, DNA-BINDING, AND SUBUNIT.
PubMed=12202833; DOI=10.1126/science.1076376;
Benoff B., Yang H., Lawson C.L., Parkinson G., Liu J., Blatter E.,
Ebright Y.W., Berman H.M., Ebright R.H.;
"Structural basis of transcription activation: the CAP-alpha CTD-DNA
complex.";
Science 297:1562-1566(2002).
[19]
STRUCTURE BY ELECTRON MICROSCOPY (19.80 ANGSTROMS) IN COMPLEX WITH
RPOB; RPOC; RPOD; RPOZ CRP AND DNA, INTERACTION WITH CRP, DNA-BINDING,
AND SUBUNIT.
PubMed=19903881; DOI=10.1073/pnas.0908782106;
Hudson B.P., Quispe J., Lara-Gonzalez S., Kim Y., Berman H.M.,
Arnold E., Ebright R.H., Lawson C.L.;
"Three-dimensional EM structure of an intact activator-dependent
transcription initiation complex.";
Proc. Natl. Acad. Sci. U.S.A. 106:19830-19835(2009).
-!- FUNCTION: DNA-dependent RNA polymerase (RNAP) catalyzes the
transcription of DNA into RNA using the four ribonucleoside
triphosphates as substrates. This subunit plays an important role
in subunit assembly since its dimerization is the first step in
the sequential assembly of subunits to form the holoenzyme.
{ECO:0000269|PubMed:1646077}.
-!- CATALYTIC ACTIVITY: Nucleoside triphosphate + RNA(n) = diphosphate
+ RNA(n+1).
-!- SUBUNIT: Homodimer. The RNAP catalytic core consists of 2 alpha, 1
beta, 1 beta' and 1 omega subunit. When a sigma factor is
associated with the core the holoenzyme is formed, which can
initiate transcription. Both the N- and C-terminus interact with
different regions of transcriptional regulator CRP.
{ECO:0000269|PubMed:12202833, ECO:0000269|PubMed:1646077,
ECO:0000269|PubMed:19903881, ECO:0000269|PubMed:2235479}.
-!- INTERACTION:
P0ABQ0:coaBC; NbExp=2; IntAct=EBI-544985, EBI-548929;
P0AFF6:nusA; NbExp=7; IntAct=EBI-544985, EBI-551571;
P60422:rplB; NbExp=6; IntAct=EBI-544985, EBI-543515;
-!- DOMAIN: The N-terminal domain is essential for RNAP assembly and
basal transcription, whereas the C-terminal domain is involved in
interaction with transcriptional regulators (such as CRP) and with
upstream promoter elements. {ECO:0000269|PubMed:1646077,
ECO:0000269|PubMed:2235479}.
-!- PTM: Acetylated on Lys-297 and Lys-298 in the presence of glucose.
Pka controls acetylation of Lys-298 but not of Lys-297.
{ECO:0000269|PubMed:21696463}.
-!- SIMILARITY: Belongs to the RNA polymerase alpha chain family.
{ECO:0000305}.
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EMBL; J01685; AAA24577.1; -; Genomic_DNA.
EMBL; X00766; CAA25337.1; -; Genomic_DNA.
EMBL; X02543; CAA26395.1; -; Genomic_DNA.
EMBL; U18997; AAA58092.1; -; Genomic_DNA.
EMBL; X53843; CAA37838.1; -; Genomic_DNA.
EMBL; X53844; CAA37839.1; -; Genomic_DNA.
EMBL; U00096; AAC76320.1; -; Genomic_DNA.
EMBL; AP009048; BAE77996.1; -; Genomic_DNA.
EMBL; V00353; CAA23646.1; -; Genomic_DNA.
EMBL; M29822; AAA24590.1; -; Genomic_DNA.
EMBL; M29823; AAA24592.1; -; Genomic_DNA.
EMBL; M29824; AAA24594.1; -; Genomic_DNA.
PIR; A22884; RNECA.
RefSeq; NP_417754.1; NC_000913.3.
RefSeq; WP_001162094.1; NZ_LN832404.1.
PDB; 1BDF; X-ray; 2.50 A; A/B/C/D=1-235.
PDB; 1COO; NMR; -; A=233-329.
PDB; 1LB2; X-ray; 3.10 A; B/E=246-329.
PDB; 1XS9; NMR; -; D=249-329.
PDB; 3IYD; EM; -; A/B=1-329.
PDB; 3K4G; X-ray; 2.05 A; A/B/C/D/E/F/G/H=245-329.
PDB; 3LU0; EM; -; A/B=1-329.
PDB; 3N4M; X-ray; 2.99 A; B/C=246-329.
PDB; 3N97; X-ray; 3.25 A; B/C=246-329.
PDB; 4JK1; X-ray; 3.90 A; A/B/F/G=1-329.
PDB; 4JK2; X-ray; 4.20 A; A/B/F/G=1-329.
PDB; 4KMU; X-ray; 3.85 A; A/B/F/G=1-329.
PDB; 4KN4; X-ray; 3.96 A; A/B/F/G=1-329.
PDB; 4KN7; X-ray; 3.69 A; A/B/F/G=1-329.
PDB; 4MEX; X-ray; 3.90 A; A/B/G/H=1-329.
PDB; 4MEY; X-ray; 3.95 A; A/B/G/H=1-329.
PDB; 4S20; X-ray; 4.70 A; A/B/F/G=1-329.
PDB; 4XSX; X-ray; 3.71 A; A/B/G/H=1-234.
PDB; 4XSY; X-ray; 4.01 A; A/B/G/H=1-234.
PDB; 4XSZ; X-ray; 3.68 A; A/B/G/H=1-234.
PDB; 4YG2; X-ray; 3.70 A; A/B/G/H=1-329.
PDB; 4YLN; X-ray; 5.50 A; A/B/G/H/M/N=1-235.
PDB; 4YLO; X-ray; 6.00 A; A/B/G/H/M/N=1-235.
PDB; 4YLP; X-ray; 5.50 A; A/B/G/H/M/N=1-235.
PDB; 4ZH2; X-ray; 4.20 A; A/B/G/H=2-329.
PDB; 4ZH3; X-ray; 4.08 A; A/B/G/H=2-329.
PDB; 4ZH4; X-ray; 3.99 A; A/B/G/H=2-329.
PDB; 5BYH; X-ray; 3.76 A; A/B=1-329.
PDB; 5CIZ; X-ray; 5.01 A; B=246-329.
PDB; 5EZK; X-ray; 8.50 A; A/B=1-329.
PDB; 5IPL; X-ray; 3.60 A; A/B=1-235.
PDB; 5IPM; X-ray; 4.20 A; A/B=1-235.
PDB; 5IPN; X-ray; 4.61 A; A/B=1-235.
PDB; 5MS0; EM; 9.80 A; A/B=1-329.
PDB; 5MY1; EM; 7.60 A; V/W=1-329.
PDB; 5NSR; EM; 3.80 A; A/B=1-329.
PDB; 5NSS; EM; 5.80 A; A/B=1-329.
PDB; 5NWT; X-ray; 3.76 A; A/B=1-329.
PDB; 5UAC; X-ray; 3.80 A; A/B/G/H=1-329.
PDB; 5UAG; X-ray; 3.40 A; A/B/G/H=1-320.
PDB; 5UAH; X-ray; 4.10 A; A/B/G/H=1-329.
PDB; 5UAJ; X-ray; 3.92 A; A/B/G/H=1-329.
PDB; 5UAL; X-ray; 3.89 A; A/B/G/H=1-329.
PDB; 5UAQ; X-ray; 3.60 A; A/B/G/H=1-329.
PDB; 5VSW; X-ray; 4.29 A; A/B/G/H=1-329.
PDB; 5VT0; EM; 3.78 A; G/H=1-234.
PDB; 5W1S; X-ray; 3.81 A; A/B/G/H=1-329.
PDB; 5W1T; X-ray; 4.50 A; A/B/G/H=1-329.
PDB; 6ALF; EM; 4.10 A; G/H=1-234.
PDB; 6ALG; EM; 3.70 A; G/H=1-234.
PDB; 6ALH; EM; 4.40 A; G/H=1-234.
PDB; 6ASX; EM; 3.80 A; G/H=1-234.
PDB; 6BJS; EM; 5.50 A; G/H=1-234.
PDB; 6BYU; X-ray; 3.60 A; A/B/G/H=1-329.
PDB; 6C6S; EM; 3.70 A; G/H=1-234.
PDB; 6C6T; EM; 3.50 A; G/H=1-234.
PDB; 6C6U; EM; 3.70 A; G/H=1-234.
PDB; 6C9Y; EM; 4.25 A; A/B=1-329.
PDB; 6CA0; EM; 5.75 A; A/B=1-329.
PDB; 6CUX; X-ray; 4.10 A; A/B/G/H=1-329.
PDB; 6FLP; EM; 4.10 A; A/B=1-329.
PDB; 6FLQ; EM; 4.10 A; A/B=1-329.
PDB; 6GFW; EM; 3.70 A; A/B=1-329.
PDB; 6GH5; EM; 3.40 A; A/B=1-329.
PDB; 6GH6; EM; 4.10 A; A/B=1-329.
PDBsum; 1BDF; -.
PDBsum; 1COO; -.
PDBsum; 1LB2; -.
PDBsum; 1XS9; -.
PDBsum; 3IYD; -.
PDBsum; 3K4G; -.
PDBsum; 3LU0; -.
PDBsum; 3N4M; -.
PDBsum; 3N97; -.
PDBsum; 4JK1; -.
PDBsum; 4JK2; -.
PDBsum; 4KMU; -.
PDBsum; 4KN4; -.
PDBsum; 4KN7; -.
PDBsum; 4MEX; -.
PDBsum; 4MEY; -.
PDBsum; 4S20; -.
PDBsum; 4XSX; -.
PDBsum; 4XSY; -.
PDBsum; 4XSZ; -.
PDBsum; 4YG2; -.
PDBsum; 4YLN; -.
PDBsum; 4YLO; -.
PDBsum; 4YLP; -.
PDBsum; 4ZH2; -.
PDBsum; 4ZH3; -.
PDBsum; 4ZH4; -.
PDBsum; 5BYH; -.
PDBsum; 5CIZ; -.
PDBsum; 5EZK; -.
PDBsum; 5IPL; -.
PDBsum; 5IPM; -.
PDBsum; 5IPN; -.
PDBsum; 5MS0; -.
PDBsum; 5MY1; -.
PDBsum; 5NSR; -.
PDBsum; 5NSS; -.
PDBsum; 5NWT; -.
PDBsum; 5UAC; -.
PDBsum; 5UAG; -.
PDBsum; 5UAH; -.
PDBsum; 5UAJ; -.
PDBsum; 5UAL; -.
PDBsum; 5UAQ; -.
PDBsum; 5VSW; -.
PDBsum; 5VT0; -.
PDBsum; 5W1S; -.
PDBsum; 5W1T; -.
PDBsum; 6ALF; -.
PDBsum; 6ALG; -.
PDBsum; 6ALH; -.
PDBsum; 6ASX; -.
PDBsum; 6BJS; -.
PDBsum; 6BYU; -.
PDBsum; 6C6S; -.
PDBsum; 6C6T; -.
PDBsum; 6C6U; -.
PDBsum; 6C9Y; -.
PDBsum; 6CA0; -.
PDBsum; 6CUX; -.
PDBsum; 6FLP; -.
PDBsum; 6FLQ; -.
PDBsum; 6GFW; -.
PDBsum; 6GH5; -.
PDBsum; 6GH6; -.
ProteinModelPortal; P0A7Z4; -.
SMR; P0A7Z4; -.
BioGrid; 4263398; 114.
BioGrid; 852106; 1.
DIP; DIP-35879N; -.
IntAct; P0A7Z4; 91.
MINT; P0A7Z4; -.
STRING; 316385.ECDH10B_3470; -.
BindingDB; P0A7Z4; -.
ChEMBL; CHEMBL2364672; -.
DrugBank; DB00615; Rifabutin.
iPTMnet; P0A7Z4; -.
SWISS-2DPAGE; P0A7Z4; -.
EPD; P0A7Z4; -.
PaxDb; P0A7Z4; -.
PRIDE; P0A7Z4; -.
EnsemblBacteria; AAC76320; AAC76320; b3295.
EnsemblBacteria; BAE77996; BAE77996; BAE77996.
GeneID; 947794; -.
KEGG; ecj:JW3257; -.
KEGG; eco:b3295; -.
PATRIC; fig|1411691.4.peg.3436; -.
EchoBASE; EB0886; -.
EcoGene; EG10893; rpoA.
eggNOG; COG0202; LUCA.
HOGENOM; HOG000218481; -.
InParanoid; P0A7Z4; -.
KO; K03040; -.
OMA; LMKFRNF; -.
PhylomeDB; P0A7Z4; -.
BioCyc; EcoCyc:EG10893-MONOMER; -.
BioCyc; MetaCyc:EG10893-MONOMER; -.
EvolutionaryTrace; P0A7Z4; -.
PRO; PR:P0A7Z4; -.
Proteomes; UP000000318; Chromosome.
Proteomes; UP000000625; Chromosome.
GO; GO:0005737; C:cytoplasm; HDA:UniProtKB.
GO; GO:0005829; C:cytosol; IDA:EcoCyc.
GO; GO:0016020; C:membrane; HDA:UniProtKB.
GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
GO; GO:0003899; F:DNA-directed 5'-3' RNA polymerase activity; IBA:GO_Central.
GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
GO; GO:0008270; F:zinc ion binding; IDA:EcoliWiki.
GO; GO:0006354; P:DNA-templated transcription, elongation; IBA:GO_Central.
Gene3D; 2.170.120.12; -; 1.
Gene3D; 3.30.1360.10; -; 2.
HAMAP; MF_00059; RNApol_bact_RpoA; 1.
InterPro; IPR011262; DNA-dir_RNA_pol_insert.
InterPro; IPR011263; DNA-dir_RNA_pol_RpoA/D/Rpb3.
InterPro; IPR011773; DNA-dir_RpoA.
InterPro; IPR036603; RBP11-like.
InterPro; IPR011260; RNAP_asu_C.
InterPro; IPR036643; RNApol_insert_sf.
PANTHER; PTHR32108; PTHR32108; 1.
Pfam; PF01000; RNA_pol_A_bac; 1.
Pfam; PF03118; RNA_pol_A_CTD; 1.
Pfam; PF01193; RNA_pol_L; 1.
ProDom; PD001179; RNAP_asu_C; 1.
SMART; SM00662; RPOLD; 1.
SUPFAM; SSF55257; SSF55257; 2.
SUPFAM; SSF56553; SSF56553; 1.
TIGRFAMs; TIGR02027; rpoA; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Complete proteome;
Direct protein sequencing; DNA-directed RNA polymerase;
Nucleotidyltransferase; Reference proteome; Transcription;
Transferase.
CHAIN 1 329 DNA-directed RNA polymerase subunit
alpha.
/FTId=PRO_0000175304.
REGION 1 235 Alpha N-terminal domain (alpha-NTD).
REGION 162 165 Required for interaction with Crp at
class II promoters.
REGION 249 329 Alpha C-terminal domain (alpha-CTD); not
required for RNAP assembly or function.
MOD_RES 297 297 N6-acetyllysine.
{ECO:0000269|PubMed:21696463}.
MOD_RES 298 298 N6-acetyllysine; by Pka.
{ECO:0000269|PubMed:21696463}.
MUTAGEN 45 45 R->C: In rpoA112; temperature-sensitive,
blocks RNA polymerase assembly.
{ECO:0000269|PubMed:2235479}.
MUTAGEN 162 165 EEDE->AAAA: 5-fold decrease in CRP-class
II promoter-dependent transcription.
{ECO:0000269|PubMed:8978616}.
MUTAGEN 165 165 E->K: 5-fold decrease in CRP-class II
promoter-dependent transcription.
{ECO:0000269|PubMed:8978616}.
MUTAGEN 191 191 R->C: In rpoA101; temperature-sensitive.
{ECO:0000269|PubMed:2235479}.
CONFLICT 4 4 S -> N (in Ref. 11; AA sequence).
{ECO:0000305}.
CONFLICT 208 208 N -> T (in Ref. 4; CAA26395).
{ECO:0000305}.
STRAND 13 32 {ECO:0000244|PDB:1BDF}.
HELIX 35 47 {ECO:0000244|PDB:1BDF}.
STRAND 54 61 {ECO:0000244|PDB:1BDF}.
STRAND 74 76 {ECO:0000244|PDB:1BDF}.
HELIX 78 86 {ECO:0000244|PDB:1BDF}.
STRAND 96 111 {ECO:0000244|PDB:1BDF}.
HELIX 112 114 {ECO:0000244|PDB:1BDF}.
STRAND 122 124 {ECO:0000244|PDB:1BDF}.
STRAND 129 133 {ECO:0000244|PDB:1BDF}.
STRAND 139 148 {ECO:0000244|PDB:1BDF}.
STRAND 151 153 {ECO:0000244|PDB:1BDF}.
HELIX 155 157 {ECO:0000244|PDB:1BDF}.
STRAND 170 172 {ECO:0000244|PDB:5UAG}.
STRAND 179 186 {ECO:0000244|PDB:1BDF}.
STRAND 196 207 {ECO:0000244|PDB:1BDF}.
STRAND 209 211 {ECO:0000244|PDB:1BDF}.
HELIX 213 227 {ECO:0000244|PDB:1BDF}.
HELIX 228 231 {ECO:0000244|PDB:1BDF}.
HELIX 251 254 {ECO:0000244|PDB:3K4G}.
HELIX 257 260 {ECO:0000244|PDB:3K4G}.
HELIX 264 270 {ECO:0000244|PDB:3K4G}.
TURN 271 274 {ECO:0000244|PDB:3N4M}.
HELIX 278 283 {ECO:0000244|PDB:3K4G}.
HELIX 286 290 {ECO:0000244|PDB:3K4G}.
STRAND 292 294 {ECO:0000244|PDB:1XS9}.
HELIX 297 299 {ECO:0000244|PDB:1XS9}.
HELIX 300 303 {ECO:0000244|PDB:3K4G}.
HELIX 308 310 {ECO:0000244|PDB:3K4G}.
STRAND 318 322 {ECO:0000244|PDB:3K4G}.
SEQUENCE 329 AA; 36512 MW; 12A14B75A3CAEA19 CRC64;
MQGSVTEFLK PRLVDIEQVS STHAKVTLEP LERGFGHTLG NALRRILLSS MPGCAVTEVE
IDGVLHEYST KEGVQEDILE ILLNLKGLAV RVQGKDEVIL TLNKSGIGPV TAADITHDGD
VEIVKPQHVI CHLTDENASI SMRIKVQRGR GYVPASTRIH SEEDERPIGR LLVDACYSPV
ERIAYNVEAA RVEQRTDLDK LVIEMETNGT IDPEEAIRRA ATILAEQLEA FVDLRDVRQP
EVKEEKPEFD PILLRPVDDL ELTVRSANCL KAEAIHYIGD LVQRTEVELL KTPNLGKKSL
TEIKDVLASR GLSLGMRLEN WPPASIADE


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