DPO3A_ECOLI
ID DPO3A_ECOLI Reviewed; 1160 AA.
AC P10443;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1989, sequence version 1.
DT 03-AUG-2022, entry version 200.
DE RecName: Full=DNA polymerase III subunit alpha;
DE EC=2.7.7.7 {ECO:0000269|PubMed:2932432};
GN Name=dnaE; Synonyms=polC; OrderedLocusNames=b0184, JW0179;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3316192; DOI=10.1128/jb.169.12.5735-5744.1987;
RA Tomasiewicz H.G., McHenry C.S.;
RT "Sequence analysis of the Escherichia coli dnaE gene.";
RL J. Bacteriol. 169:5735-5744(1987).
RN [2]
RP ERRATUM OF PUBMED:3316192.
RX PubMed=2066347; DOI=10.1128/jb.173.14.4549-4549.1991;
RA Tomasiewicz H.G., McHenry C.S.;
RL J. Bacteriol. 173:4549-4549(1991).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RA Takemoto K., Mori H., Murayama N., Kataoka K., Yano M., Itoh T.,
RA Yamamoto Y., Inokuchi H., Miki T., Hatada E., Fukuda R., Ichihara S.,
RA Mizuno T., Makino K., Nakata A., Yura T., Sampei G., Mizobuchi K.;
RT "Systematic sequencing of the Escherichia coli genome: analysis of the 4.0
RT - 6.0 min (189,987 - 281,416bp) region.";
RL Submitted (FEB-1996) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RA Chung E., Allen E., Araujo R., Aparicio A.M., Davis K., Duncan M.,
RA Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., Lew H., Lin D.,
RA Namath A., Oefner P., Roberts D., Schramm S., Davis R.W.;
RT "Sequence of minutes 4-25 of Escherichia coli.";
RL Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [7]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1065-1160, AND NUCLEOTIDE SEQUENCE
RP [MRNA] OF 1070-1160.
RX PubMed=7678242; DOI=10.1128/jb.175.2.332-340.1993;
RA Li S.-J., Cronan J.E. Jr.;
RT "Growth rate regulation of Escherichia coli acetyl coenzyme A carboxylase,
RT which catalyzes the first committed step of lipid biosynthesis.";
RL J. Bacteriol. 175:332-340(1993).
RN [8]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1137-1160.
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RA Yamamoto Y.;
RL Submitted (DEC-1995) to the EMBL/GenBank/DDBJ databases.
RN [9]
RP IDENTIFICATION OF DNAE AS THE ALPHA SUBUNIT.
RC STRAIN=K12 / CS520;
RX PubMed=6288664; DOI=10.1128/jb.152.1.351-356.1982;
RA Welch M.M., McHenry C.S.;
RT "Cloning and identification of the product of the dnaE gene of Escherichia
RT coli.";
RL J. Bacteriol. 152:351-356(1982).
RN [10]
RP FUNCTION AND HIGH PROCESSIVITY.
RX PubMed=2413035; DOI=10.1016/s0021-9258(17)38959-7;
RA O'Donnell M.E., Kornberg A.;
RT "Dynamics of DNA polymerase III holoenzyme of Escherichia coli in
RT replication of a multiprimed template.";
RL J. Biol. Chem. 260:12875-12883(1985).
RN [11]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=2932432; DOI=10.1016/s0021-9258(17)38824-5;
RA Maki H., Horiuchi T., Kornberg A.;
RT "The polymerase subunit of DNA polymerase III of Escherichia coli. I.
RT Amplification of the dnaE gene product and polymerase activity of the alpha
RT subunit.";
RL J. Biol. Chem. 260:12982-12986(1985).
RN [12]
RP FUNCTION, SUBUNIT, AND INTERACTION WITH DNAN AND DNAQ.
RX PubMed=2040637; DOI=10.1016/s0021-9258(18)99166-0;
RA Stukenberg P.T., Studwell-Vaughan P.S., O'Donnell M.;
RT "Mechanism of the sliding beta-clamp of DNA polymerase III holoenzyme.";
RL J. Biol. Chem. 266:11328-11334(1991).
RN [13]
RP INTERACTION WITH DNAN, AND MUTAGENESIS OF 920-GLN--PHE-924 AND
RP 923-MET-PHE-924.
RC STRAIN=K12 / XL1-Blue;
RX PubMed=11573000; DOI=10.1073/pnas.191384398;
RA Dalrymple B.P., Kongsuwan K., Wijffels G., Dixon N.E., Jennings P.A.;
RT "A universal protein-protein interaction motif in the eubacterial DNA
RT replication and repair systems.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:11627-11632(2001).
RN [14]
RP REPLISOME COMPLEX, AND SUBUNIT.
RX PubMed=20413500; DOI=10.1126/science.1185757;
RA Reyes-Lamothe R., Sherratt D.J., Leake M.C.;
RT "Stoichiometry and architecture of active DNA replication machinery in
RT Escherichia coli.";
RL Science 328:498-501(2010).
RN [15]
RP REPLISOME COMPLEX, AND SUBUNIT.
RX PubMed=22157955; DOI=10.1038/nsmb.2179;
RA Georgescu R.E., Kurth I., O'Donnell M.E.;
RT "Single-molecule studies reveal the function of a third polymerase in the
RT replisome.";
RL Nat. Struct. Mol. Biol. 19:113-116(2011).
RN [16] {ECO:0007744|PDB:5FKU, ECO:0007744|PDB:5FKV, ECO:0007744|PDB:5FKW}
RP STRUCTURE BY ELECTRON MICROSCOPY (7.30 ANGSTROMS) OF DNAE; DNAN; DNAQ; DNAX
RP WITH AND WITHOUT DNA, SUBUNIT, MUTAGENESIS OF 921-ALA--MET-923, AND
RP DNA-BINDING.
RX PubMed=26499492; DOI=10.7554/elife.11134;
RA Fernandez-Leiro R., Conrad J., Scheres S.H., Lamers M.H.;
RT "cryo-EM structures of the E. coli replicative DNA polymerase reveal its
RT dynamic interactions with the DNA sliding clamp, exonuclease and tau.";
RL Elife 4:0-0(2015).
RN [17]
RP REVIEW.
RX PubMed=1575709; DOI=10.1002/bies.950140206;
RA O'Donnell M.;
RT "Accessory protein function in the DNA polymerase III holoenzyme from E.
RT coli.";
RL Bioessays 14:105-111(1992).
RN [18]
RP MUTAGENESIS.
RX PubMed=8375647; DOI=10.1093/genetics/134.4.1039;
RA Fijalkowska I.J., Schaaper R.M.;
RT "Antimutator mutations in the alpha subunit of Escherichia coli DNA
RT polymerase III: identification of the responsible mutations and alignment
RT with other DNA polymerases.";
RL Genetics 134:1039-1044(1993).
CC -!- FUNCTION: DNA polymerase III is a complex, multichain enzyme
CC responsible for most of the replicative synthesis in bacteria
CC (PubMed:2932432). This DNA polymerase also exhibits 3' to 5'
CC exonuclease activity. The alpha chain is the DNA polymerase catalytic
CC subunit (PubMed:2932432). It is tethered to replicating DNA by the beta
CC sliding clamp (dnaN), which confers extremely high processivity to the
CC catalytic subunit, copying a 5.4 kb genome in 11 seconds, a speed of at
CC least 500 nucleotides/second at 30 degrees Celsius (PubMed:2413035).
CC {ECO:0000269|PubMed:2413035, ECO:0000269|PubMed:2932432}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) =
CC diphosphate + DNA(n+1); Xref=Rhea:RHEA:22508, Rhea:RHEA-COMP:17339,
CC Rhea:RHEA-COMP:17340, ChEBI:CHEBI:33019, ChEBI:CHEBI:61560,
CC ChEBI:CHEBI:173112; EC=2.7.7.7;
CC Evidence={ECO:0000269|PubMed:2932432};
CC -!- SUBUNIT: The DNA polymerase III holoenzyme complex contains at least 10
CC different subunits organized into 3 functionally essential
CC subassemblies: the Pol III core, the beta sliding clamp processivity
CC factor and the clamp-loading complex. The Pol III core (subunits alpha,
CC epsilon and theta) contains the polymerase and the 3'-5' exonuclease
CC proofreading activities (PubMed:2040637). The polymerase is tethered to
CC the template via the dimeric beta sliding clamp processivity factor.
CC The clamp loader (also called gamma complex) assembles the beta sliding
CC clamp onto the primed template and plays a central role in the
CC organization and communication at the replication fork. The clamp-
CC loading complex contains delta, delta', psi and chi, and 3 copies of
CC either or both of two different DnaX proteins, gamma and tau. The DNA
CC replisome complex has a single clamp loader (3 tau and 1 each of delta,
CC delta', psi and chi subunits) which binds 3 Pol III cores (1 core on
CC the leading strand and 2 on the lagging strand) each with a beta
CC sliding clamp dimer. Additional proteins in the replisome are other
CC copies of gamma, psi and chi, Ssb, DNA helicase and RNA primase
CC (PubMed:20413500, PubMed:22157955). Interacts with the beta sliding-
CC clamp subunit via the peptide Gln-Ala-Asp-Met-Phe (residues 920-924)
CC (PubMed:11573000). {ECO:0000269|PubMed:11573000,
CC ECO:0000269|PubMed:2040637, ECO:0000269|PubMed:20413500,
CC ECO:0000269|PubMed:22157955}.
CC -!- INTERACTION:
CC P10443; P0A988: dnaN; NbExp=19; IntAct=EBI-549111, EBI-542385;
CC P10443; P03007: dnaQ; NbExp=25; IntAct=EBI-549111, EBI-549131;
CC P10443; P06710: dnaX; NbExp=12; IntAct=EBI-549111, EBI-549140;
CC P10443; P28630: holA; NbExp=5; IntAct=EBI-549111, EBI-549153;
CC P10443; P0A7K2: rplL; NbExp=3; IntAct=EBI-549111, EBI-543702;
CC P10443; P77806: ybdL; NbExp=3; IntAct=EBI-549111, EBI-543661;
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- SIMILARITY: Belongs to the DNA polymerase type-C family. DnaE
CC subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA70369.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; M19334; AAC36920.1; -; Genomic_DNA.
DR EMBL; U70214; AAB08613.1; -; Genomic_DNA.
DR EMBL; U00096; AAC73295.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA77859.1; -; Genomic_DNA.
DR EMBL; S52931; AAB24889.1; -; mRNA.
DR EMBL; M96394; AAA70369.1; ALT_INIT; Genomic_DNA.
DR EMBL; D49445; BAA08424.1; -; Genomic_DNA.
DR PIR; C28390; DJEC3A.
DR RefSeq; NP_414726.1; NC_000913.3.
DR RefSeq; WP_001294757.1; NZ_STEB01000032.1.
DR PDB; 2HNH; X-ray; 2.30 A; A=1-910.
DR PDB; 2HQA; X-ray; 2.60 A; A=1-917.
DR PDB; 4GX8; X-ray; 1.70 A; A/B/C/D=1-270.
DR PDB; 4GX9; X-ray; 2.15 A; A/B/C/D=1-270.
DR PDB; 4JOM; X-ray; 2.90 A; A=1-917.
DR PDB; 5FKU; EM; 8.34 A; A=1-1160.
DR PDB; 5FKV; EM; 8.00 A; A=1-1160.
DR PDB; 5FKW; EM; 7.30 A; A=1-1160.
DR PDB; 5M1S; EM; 6.70 A; A=1-927.
DR PDBsum; 2HNH; -.
DR PDBsum; 2HQA; -.
DR PDBsum; 4GX8; -.
DR PDBsum; 4GX9; -.
DR PDBsum; 4JOM; -.
DR PDBsum; 5FKU; -.
DR PDBsum; 5FKV; -.
DR PDBsum; 5FKW; -.
DR PDBsum; 5M1S; -.
DR AlphaFoldDB; P10443; -.
DR SMR; P10443; -.
DR BioGRID; 4262228; 218.
DR BioGRID; 849277; 5.
DR ComplexPortal; CPX-1925; DNA polymerase III core complex.
DR DIP; DIP-9458N; -.
DR IntAct; P10443; 70.
DR MINT; P10443; -.
DR STRING; 511145.b0184; -.
DR BindingDB; P10443; -.
DR ChEMBL; CHEMBL4621; -.
DR jPOST; P10443; -.
DR PaxDb; P10443; -.
DR PRIDE; P10443; -.
DR EnsemblBacteria; AAC73295; AAC73295; b0184.
DR EnsemblBacteria; BAA77859; BAA77859; BAA77859.
DR GeneID; 66671528; -.
DR GeneID; 944877; -.
DR KEGG; ecj:JW0179; -.
DR KEGG; eco:b0184; -.
DR PATRIC; fig|1411691.4.peg.2095; -.
DR EchoBASE; EB0234; -.
DR eggNOG; COG0587; Bacteria.
DR HOGENOM; CLU_001600_0_2_6; -.
DR InParanoid; P10443; -.
DR OMA; NECRRMG; -.
DR PhylomeDB; P10443; -.
DR BioCyc; EcoCyc:EG10238-MON; -.
DR BioCyc; MetaCyc:EG10238-MON; -.
DR EvolutionaryTrace; P10443; -.
DR PRO; PR:P10443; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IDA:EcoliWiki.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:0009360; C:DNA polymerase III complex; IC:ComplexPortal.
DR GO; GO:0044776; C:DNA polymerase III, core complex; IDA:EcoCyc.
DR GO; GO:0030894; C:replisome; IC:ComplexPortal.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003887; F:DNA-directed DNA polymerase activity; IDA:EcoliWiki.
DR GO; GO:0006261; P:DNA-templated DNA replication; IC:ComplexPortal.
DR GO; GO:0006273; P:lagging strand elongation; IDA:ComplexPortal.
DR GO; GO:0006272; P:leading strand elongation; IDA:ComplexPortal.
DR Gene3D; 1.10.10.1600; -; 1.
DR Gene3D; 2.40.50.140; -; 1.
DR InterPro; IPR011708; DNA_pol3_alpha_NTPase_dom.
DR InterPro; IPR041931; DNA_pol3_alpha_thumb_dom.
DR InterPro; IPR040982; DNA_pol3_finger.
DR InterPro; IPR029460; DNAPol_HHH.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR004365; NA-bd_OB_tRNA.
DR InterPro; IPR004013; PHP_dom.
DR InterPro; IPR003141; Pol/His_phosphatase_N.
DR InterPro; IPR016195; Pol/histidinol_Pase-like.
DR InterPro; IPR004805; PolC_alpha.
DR PANTHER; PTHR32294; PTHR32294; 1.
DR Pfam; PF07733; DNA_pol3_alpha; 1.
DR Pfam; PF17657; DNA_pol3_finger; 1.
DR Pfam; PF14579; HHH_6; 1.
DR Pfam; PF02811; PHP; 1.
DR Pfam; PF01336; tRNA_anti-codon; 1.
DR SMART; SM00481; POLIIIAc; 1.
DR SUPFAM; SSF89550; SSF89550; 1.
DR TIGRFAMs; TIGR00594; polc; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; DNA replication; DNA-binding;
KW DNA-directed DNA polymerase; Nucleotidyltransferase; Reference proteome;
KW Transferase.
FT CHAIN 1..1160
FT /note="DNA polymerase III subunit alpha"
FT /id="PRO_0000103321"
FT MUTAGEN 920..924
FT /note="QADMF->PADMP: Loss of interaction with beta sliding
FT clamp (dnaN)."
FT /evidence="ECO:0000269|PubMed:11573000"
FT MUTAGEN 921..923
FT /note="ADM->LDL: Increases binding to beta sliding clamp
FT (dnaN), increases stability of enzyme complex."
FT /evidence="ECO:0000269|PubMed:26499492"
FT MUTAGEN 923..924
FT /note="MF->KK: Loss of interaction with beta sliding clamp
FT (dnaN)."
FT /evidence="ECO:0000269|PubMed:11573000"
FT TURN 14..17
FT /evidence="ECO:0007829|PDB:4GX8"
FT STRAND 18..20
FT /evidence="ECO:0007829|PDB:4GX8"
FT HELIX 25..33
FT /evidence="ECO:0007829|PDB:4GX8"
FT STRAND 37..44
FT /evidence="ECO:0007829|PDB:4GX8"
FT HELIX 50..59
FT /evidence="ECO:0007829|PDB:4GX8"
FT STRAND 63..73
FT /evidence="ECO:0007829|PDB:4GX8"
FT HELIX 75..77
FT /evidence="ECO:0007829|PDB:4GX8"
FT STRAND 82..88
FT /evidence="ECO:0007829|PDB:4GX8"
FT HELIX 91..106
FT /evidence="ECO:0007829|PDB:4GX8"
FT HELIX 120..124
FT /evidence="ECO:0007829|PDB:4GX8"
FT STRAND 128..131
FT /evidence="ECO:0007829|PDB:4GX8"
FT HELIX 134..136
FT /evidence="ECO:0007829|PDB:4GX8"
FT HELIX 138..145
FT /evidence="ECO:0007829|PDB:4GX8"
FT HELIX 148..161
FT /evidence="ECO:0007829|PDB:4GX8"
FT STRAND 166..170
FT /evidence="ECO:0007829|PDB:4GX8"
FT HELIX 178..192
FT /evidence="ECO:0007829|PDB:4GX8"
FT STRAND 196..198
FT /evidence="ECO:0007829|PDB:4GX8"
FT STRAND 204..206
FT /evidence="ECO:0007829|PDB:4GX8"
FT HELIX 207..209
FT /evidence="ECO:0007829|PDB:4GX8"
FT HELIX 210..221
FT /evidence="ECO:0007829|PDB:4GX8"
FT HELIX 243..249
FT /evidence="ECO:0007829|PDB:4GX8"
FT TURN 250..252
FT /evidence="ECO:0007829|PDB:4GX8"
FT HELIX 254..266
FT /evidence="ECO:0007829|PDB:4GX8"
FT STRAND 284..286
FT /evidence="ECO:0007829|PDB:2HQA"
FT HELIX 288..307
FT /evidence="ECO:0007829|PDB:2HNH"
FT HELIX 311..317
FT /evidence="ECO:0007829|PDB:2HNH"
FT HELIX 319..334
FT /evidence="ECO:0007829|PDB:2HNH"
FT HELIX 338..353
FT /evidence="ECO:0007829|PDB:2HNH"
FT HELIX 365..367
FT /evidence="ECO:0007829|PDB:2HNH"
FT HELIX 369..373
FT /evidence="ECO:0007829|PDB:2HNH"
FT TURN 381..385
FT /evidence="ECO:0007829|PDB:2HNH"
FT HELIX 388..390
FT /evidence="ECO:0007829|PDB:2HNH"
FT STRAND 405..407
FT /evidence="ECO:0007829|PDB:4JOM"
FT HELIX 408..410
FT /evidence="ECO:0007829|PDB:2HNH"
FT HELIX 411..422
FT /evidence="ECO:0007829|PDB:2HNH"
FT HELIX 424..426
FT /evidence="ECO:0007829|PDB:2HNH"
FT STRAND 427..430
FT /evidence="ECO:0007829|PDB:2HNH"
FT STRAND 433..435
FT /evidence="ECO:0007829|PDB:2HNH"
FT HELIX 438..448
FT /evidence="ECO:0007829|PDB:2HNH"
FT HELIX 453..460
FT /evidence="ECO:0007829|PDB:2HNH"
FT HELIX 471..477
FT /evidence="ECO:0007829|PDB:2HNH"
FT HELIX 480..487
FT /evidence="ECO:0007829|PDB:2HNH"
FT HELIX 489..501
FT /evidence="ECO:0007829|PDB:2HNH"
FT STRAND 505..508
FT /evidence="ECO:0007829|PDB:2HNH"
FT STRAND 514..517
FT /evidence="ECO:0007829|PDB:2HNH"
FT HELIX 522..524
FT /evidence="ECO:0007829|PDB:2HNH"
FT STRAND 538..541
FT /evidence="ECO:0007829|PDB:2HNH"
FT HELIX 543..548
FT /evidence="ECO:0007829|PDB:2HNH"
FT STRAND 552..556
FT /evidence="ECO:0007829|PDB:2HNH"
FT HELIX 561..574
FT /evidence="ECO:0007829|PDB:2HNH"
FT TURN 575..580
FT /evidence="ECO:0007829|PDB:2HNH"
FT HELIX 586..588
FT /evidence="ECO:0007829|PDB:2HNH"
FT HELIX 594..601
FT /evidence="ECO:0007829|PDB:2HNH"
FT STRAND 608..610
FT /evidence="ECO:0007829|PDB:2HQA"
FT HELIX 614..623
FT /evidence="ECO:0007829|PDB:2HNH"
FT HELIX 628..637
FT /evidence="ECO:0007829|PDB:2HNH"
FT HELIX 640..643
FT /evidence="ECO:0007829|PDB:2HNH"
FT HELIX 647..655
FT /evidence="ECO:0007829|PDB:2HNH"
FT STRAND 657..659
FT /evidence="ECO:0007829|PDB:2HQA"
FT STRAND 666..669
FT /evidence="ECO:0007829|PDB:2HNH"
FT HELIX 671..673
FT /evidence="ECO:0007829|PDB:2HNH"
FT HELIX 674..677
FT /evidence="ECO:0007829|PDB:2HNH"
FT HELIX 678..680
FT /evidence="ECO:0007829|PDB:2HNH"
FT HELIX 687..698
FT /evidence="ECO:0007829|PDB:2HNH"
FT HELIX 702..714
FT /evidence="ECO:0007829|PDB:2HNH"
FT HELIX 717..733
FT /evidence="ECO:0007829|PDB:2HNH"
FT HELIX 738..752
FT /evidence="ECO:0007829|PDB:2HNH"
FT HELIX 758..777
FT /evidence="ECO:0007829|PDB:2HNH"
FT HELIX 779..789
FT /evidence="ECO:0007829|PDB:2HNH"
FT TURN 790..792
FT /evidence="ECO:0007829|PDB:2HNH"
FT HELIX 794..806
FT /evidence="ECO:0007829|PDB:2HNH"
FT TURN 816..818
FT /evidence="ECO:0007829|PDB:2HNH"
FT STRAND 820..822
FT /evidence="ECO:0007829|PDB:2HNH"
FT HELIX 835..837
FT /evidence="ECO:0007829|PDB:2HNH"
FT HELIX 843..854
FT /evidence="ECO:0007829|PDB:2HNH"
FT STRAND 855..857
FT /evidence="ECO:0007829|PDB:4JOM"
FT HELIX 862..865
FT /evidence="ECO:0007829|PDB:2HNH"
FT STRAND 871..874
FT /evidence="ECO:0007829|PDB:2HNH"
FT HELIX 876..884
FT /evidence="ECO:0007829|PDB:2HNH"
FT TURN 885..891
FT /evidence="ECO:0007829|PDB:2HNH"
FT HELIX 895..899
FT /evidence="ECO:0007829|PDB:2HNH"
FT STRAND 902..905
FT /evidence="ECO:0007829|PDB:2HNH"
FT HELIX 906..909
FT /evidence="ECO:0007829|PDB:2HNH"
SQ SEQUENCE 1160 AA; 129905 MW; 1A4F75F373841716 CRC64;
MSEPRFVHLR VHSDYSMIDG LAKTAPLVKK AAALGMPALA ITDFTNLCGL VKFYGAGHGA
GIKPIVGADF NVQCDLLGDE LTHLTVLAAN NTGYQNLTLL ISKAYQRGYG AAGPIIDRDW
LIELNEGLIL LSGGRMGDVG RSLLRGNSAL VDECVAFYEE HFPDRYFLEL IRTGRPDEES
YLHAAVELAE ARGLPVVATN DVRFIDSSDF DAHEIRVAIH DGFTLDDPKR PRNYSPQQYM
RSEEEMCELF ADIPEALANT VEIAKRCNVT VRLGEYFLPQ FPTGDMSTED YLVKRAKEGL
EERLAFLFPD EEERLKRRPE YDERLETELQ VINQMGFPGY FLIVMEFIQW SKDNGVPVGP
GRGSGAGSLV AYALKITDLD PLEFDLLFER FLNPERVSMP DFDVDFCMEK RDQVIEHVAD
MYGRDAVSQI ITFGTMAAKA VIRDVGRVLG HPYGFVDRIS KLIPPDPGMT LAKAFEAEPQ
LPEIYEADEE VKALIDMARK LEGVTRNAGK HAGGVVIAPT KITDFAPLYC DEEGKHPVTQ
FDKSDVEYAG LVKFDFLGLR TLTIINWALE MINKRRAKNG EPPLDIAAIP LDDKKSFDML
QRSETTAVFQ LESRGMKDLI KRLQPDCFED MIALVALFRP GPLQSGMVDN FIDRKHGREE
ISYPDVQWQH ESLKPVLEPT YGIILYQEQV MQIAQVLSGY TLGGADMLRR AMGKKKPEEM
AKQRSVFAEG AEKNGINAEL AMKIFDLVEK FAGYGFNKSH SAAYALVSYQ TLWLKAHYPA
EFMAAVMTAD MDNTEKVVGL VDECWRMGLK ILPPDINSGL YHFHVNDDGE IVYGIGAIKG
VGEGPIEAII EARNKGGYFR ELFDLCARTD TKKLNRRVLE KLIMSGAFDR LGPHRAALMN
SLGDALKAAD QHAKAEAIGQ ADMFGVLAEE PEQIEQSYAS CQPWPEQVVL DGERETLGLY
LTGHPINQYL KEIERYVGGV RLKDMHPTER GKVITAAGLV VAARVMVTKR GNRIGICTLD
DRSGRLEVML FTDALDKYQQ LLEKDRILIV SGQVSFDDFS GGLKMTAREV MDIDEAREKY
ARGLAISLTD RQIDDQLLNR LRQSLEPHRS GTIPVHLYYQ RADARARLRF GATWRVSPSD
RLLNDLRGLI GSEQVELEFD
