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 27-MAR-2024, entry version 207. 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; Pseudomonadota; 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}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 EMDB; EMD-3198; -. DR EMDB; EMD-3201; -. DR EMDB; EMD-3202; -. DR EMDB; EMD-4141; -. 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; 511145-b0184; -. DR EnsemblBacteria; AAC73295; AAC73295; b0184. 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; DFCMDGR; -. DR OrthoDB; 9803237at2; -. DR PhylomeDB; P10443; -. DR BioCyc; EcoCyc:EG10238-MONOMER; -. DR BioCyc; MetaCyc:EG10238-MONOMER; -. 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; NAS:ComplexPortal. DR GO; GO:0044776; C:DNA polymerase III, core complex; IDA:EcoCyc. DR GO; GO:0030894; C:replisome; NAS: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; NAS:ComplexPortal. DR GO; GO:0006273; P:lagging strand elongation; IDA:ComplexPortal. DR GO; GO:0006272; P:leading strand elongation; IDA:ComplexPortal. DR CDD; cd04485; DnaE_OBF; 1. DR CDD; cd07433; PHP_PolIIIA_DnaE1; 1. DR Gene3D; 1.10.150.870; -; 1. DR Gene3D; 1.10.10.1600; Bacterial DNA polymerase III alpha subunit, thumb domain; 1. DR Gene3D; 3.20.20.140; Metal-dependent hydrolases; 1. DR Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 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; IPR048472; DNA_pol_IIIA_C. DR InterPro; IPR004805; DnaE2/DnaE/PolC. 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; IPR049821; PolIIIA_DnaE1_PHP. DR NCBIfam; TIGR00594; polc; 1. DR PANTHER; PTHR32294; DNA POLYMERASE III SUBUNIT ALPHA; 1. DR PANTHER; PTHR32294:SF0; DNA POLYMERASE III SUBUNIT ALPHA; 1. DR Pfam; PF07733; DNA_pol3_alpha; 1. DR Pfam; PF17657; DNA_pol3_finger; 1. DR Pfam; PF20914; DNA_pol_IIIA_C; 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; PHP domain-like; 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 //