ID TOP1_ECOLI Reviewed; 865 AA. AC P06612; DT 01-JAN-1988, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1995, sequence version 2. DT 14-DEC-2022, entry version 207. DE RecName: Full=DNA topoisomerase 1 {ECO:0000255|HAMAP-Rule:MF_00952}; DE EC=5.6.2.1 {ECO:0000255|HAMAP-Rule:MF_00952, ECO:0000269|PubMed:10681504, ECO:0000269|PubMed:14604525, ECO:0000269|PubMed:21482796, ECO:0000269|PubMed:9497321}; DE AltName: Full=DNA topoisomerase I {ECO:0000255|HAMAP-Rule:MF_00952}; DE AltName: Full=Omega-protein; DE AltName: Full=Relaxing enzyme; DE AltName: Full=Swivelase; DE AltName: Full=Untwisting enzyme; GN Name=topA {ECO:0000255|HAMAP-Rule:MF_00952}; Synonyms=supX; GN OrderedLocusNames=b1274, JW1266; 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=3029379; DOI=10.1016/0022-2836(86)90129-4; RA Tse-Dinh Y.-C., Wang J.C.; RT "Complete nucleotide sequence of the topA gene encoding Escherichia coli RT DNA topoisomerase I."; RL J. Mol. Biol. 191:321-331(1986). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND SEQUENCE REVISION. RA Lynch D.A., Wang J.C.; RL Submitted (SEP-1991) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911; RX PubMed=9097039; DOI=10.1093/dnares/3.6.363; RA Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K., Itoh T., RA Kasai H., Kashimoto K., Kimura S., Kitakawa M., Kitagawa M., Makino K., RA Miki T., Mizobuchi K., Mori H., Mori T., Motomura K., Nakade S., RA Nakamura Y., Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G., RA Seki Y., Sivasundaram S., Tagami H., Takeda J., Takemoto K., Takeuchi Y., RA Wada C., Yamamoto Y., Horiuchi T.; RT "A 570-kb DNA sequence of the Escherichia coli K-12 genome corresponding to RT the 28.0-40.1 min region on the linkage map."; RL DNA Res. 3:363-377(1996). RN [4] 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 [5] 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 [6] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 698-865. RX PubMed=3032952; DOI=10.1016/s0021-9258(18)45528-7; RA Ostrowski J., Jagura-Burdzy G., Kredich N.M.; RT "DNA sequences of the cysB regions of Salmonella typhimurium and RT Escherichia coli."; RL J. Biol. Chem. 262:5999-6005(1987). RN [7] RP IDENTIFICATION BY 2D-GEL. RX PubMed=9298644; DOI=10.1002/elps.1150180805; RA VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C.; RT "Escherichia coli proteome analysis using the gene-protein database."; RL Electrophoresis 18:1243-1251(1997). RN [8] RP MUTAGENESIS OF GLU-9; TYR-319; ARG-321; HIS-365 AND THR-496, CATALYTIC RP ACTIVITY, FUNCTION, AND ACTIVE SITE. RX PubMed=9497321; DOI=10.1074/jbc.273.11.6050; RA Chen S.J., Wang J.C.; RT "Identification of active site residues in Escherichia coli DNA RT topoisomerase I."; RL J. Biol. Chem. 273:6050-6056(1998). RN [9] RP MUTAGENESIS OF ASP-111; ASP-113 AND GLU-115, COFACTOR, FUNCTION, ENZYME RP MECHANISM, METAL-BINDING SITES, AND CATALYTIC ACTIVITY. RX PubMed=10681504; DOI=10.1074/jbc.275.8.5318; RA Zhu C.X., Tse-Dinh Y.C.; RT "The acidic triad conserved in type IA DNA topoisomerases is required for RT binding of Mg(II) and subsequent conformational change."; RL J. Biol. Chem. 275:5318-5322(2000). RN [10] RP INDUCTION BY 2,4,6-TRINITROTOLUENE, AND BIOTECHNOLOGY. RC STRAIN=K12 / MG1655 / ATCC 47076; RX PubMed=25561288; DOI=10.1007/s12013-014-0481-8; RA Tan J., Kan N., Wang W., Ling J., Qu G., Jin J., Shao Y., Liu G., Chen H.; RT "Construction of 2,4,6-trinitrotoluene biosensors with novel sensing RT elements from Escherichia coli K-12 MG1655."; RL Cell Biochem. Biophys. 72:417-428(2015). RN [11] RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 1-597, PUTATIVE METAL-BINDING RP SITES, AND ACTIVE SITE. RX PubMed=8114910; DOI=10.1038/367138a0; RA Lima C.D., Wang J.C., Mondragon A.; RT "Three-dimensional structure of the 67K N-terminal fragment of E. coli DNA RT topoisomerase I."; RL Nature 367:138-146(1994). RN [12] RP STRUCTURE BY NMR OF 745-865. RX PubMed=7779808; DOI=10.1021/bi00023a008; RA Yu L., Zhu C.-X., Tse-Dinh Y.-C., Fesik S.W.; RT "Solution structure of the C-terminal single-stranded DNA-binding domain of RT Escherichia coli topoisomerase I."; RL Biochemistry 34:7622-7628(1995). RN [13] RP X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 214-477. RX PubMed=10504724; DOI=10.1038/13283; RA Feinberg H., Lima C.D., Mondragon A.; RT "Conformational changes in E. coli DNA topoisomerase I."; RL Nat. Struct. Biol. 6:918-922(1999). RN [14] RP X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 1-597 IN COMPLEXES WITH RP NUCLEOTIDES. RX PubMed=10504732; DOI=10.1038/13333; RA Feinberg H., Changela A., Mondragon A.; RT "Protein-nucleotide interactions in E. coli DNA topoisomerase I."; RL Nat. Struct. Biol. 6:961-968(1999). RN [15] RP X-RAY CRYSTALLOGRAPHY (1.67 ANGSTROMS) OF 1-592 OF MUTANT ARG-365 IN RP COMPLEX WITH SINGLE-STRANDED DNA, MUTAGENESIS OF HIS-365, AND CATALYTIC RP ACTIVITY. RX PubMed=14604525; DOI=10.1016/j.str.2003.09.013; RA Perry K., Mondragon A.; RT "Structure of a complex between E. coli DNA topoisomerase I and single- RT stranded DNA."; RL Structure 11:1349-1358(2003). RN [16] RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 1-596 OF MUTANT ASN-111 IN COMPLEX RP WITH DNA, FUNCTION, CATALYTIC ACTIVITY, ACTIVE SITE, COFACTOR, MUTAGENESIS RP OF ARG-168 AND ASP-172, DNA-BINDING SITES, AND ENZYME MECHANISM. RX PubMed=21482796; DOI=10.1073/pnas.1100300108; RA Zhang Z., Cheng B., Tse-Dinh Y.C.; RT "Crystal structure of a covalent intermediate in DNA cleavage and rejoining RT by Escherichia coli DNA topoisomerase I."; RL Proc. Natl. Acad. Sci. U.S.A. 108:6939-6944(2011). CC -!- FUNCTION: Releases the supercoiling and torsional tension of DNA, which CC is introduced during the DNA replication and transcription, by CC transiently cleaving and rejoining one strand of the DNA duplex. CC Introduces a single-strand break via transesterification at a target CC site in duplex DNA. The scissile phosphodiester is attacked by the CC catalytic tyrosine of the enzyme, resulting in the formation of a DNA- CC (5'-phosphotyrosyl)-enzyme intermediate and the expulsion of a 3'-OH CC DNA strand. The free DNA strand then undergoes passage around the CC unbroken strand, thus removing DNA supercoils. Finally, in the CC religation step, the DNA 3'-OH attacks the covalent intermediate to CC expel the active-site tyrosine and restore the DNA phosphodiester CC backbone. {ECO:0000255|HAMAP-Rule:MF_00952, CC ECO:0000269|PubMed:10681504, ECO:0000269|PubMed:21482796, CC ECO:0000269|PubMed:9497321}. CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP-independent breakage of single-stranded DNA, followed by CC passage and rejoining.; EC=5.6.2.1; Evidence={ECO:0000255|HAMAP- CC Rule:MF_00952, ECO:0000269|PubMed:10681504, CC ECO:0000269|PubMed:14604525, ECO:0000269|PubMed:21482796, CC ECO:0000269|PubMed:9497321}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000269|PubMed:10681504, ECO:0000269|PubMed:21482796}; CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; CC Evidence={ECO:0000269|PubMed:10681504, ECO:0000269|PubMed:21482796}; CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108; CC Evidence={ECO:0000269|PubMed:10681504, ECO:0000269|PubMed:21482796}; CC Note=Binds two Mg(2+) ions per subunit. The magnesium ions form salt CC bridges with both the protein and the DNA. Can also accept other CC divalent metal cations, such as Mn(2+) or Ca(2+). CC {ECO:0000269|PubMed:10681504, ECO:0000269|PubMed:21482796}; CC -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_00952, CC ECO:0000269|PubMed:14604525, ECO:0000269|PubMed:21482796}. CC -!- INTERACTION: CC P06612; P27862: yigZ; NbExp=3; IntAct=EBI-544172, EBI-561235; CC -!- INDUCTION: Transcription is increased specifically in response to CC 2,4,6-trinitrotoluene (TNT) and its indicator compounds 1,3-DNB, 2,4- CC DNT, and 2,6-DNT. {ECO:0000269|PubMed:25561288}. CC -!- BIOTECHNOLOGY: Has been used to construct a 2,4,6-trinitrotoluene (TNT) CC biosensor strain. {ECO:0000269|PubMed:25561288}. CC -!- SIMILARITY: Belongs to the type IA topoisomerase family. CC {ECO:0000255|HAMAP-Rule:MF_00952}. 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; X04475; CAA28164.1; -; Genomic_DNA. DR EMBL; M15041; AAA23641.1; -; Genomic_DNA. DR EMBL; U00096; AAC74356.1; -; Genomic_DNA. DR EMBL; AP009048; BAA14811.1; -; Genomic_DNA. DR PIR; E64875; ISECTP. DR RefSeq; NP_415790.1; NC_000913.3. DR RefSeq; WP_001297122.1; NZ_SSZK01000031.1. DR PDB; 1CY0; X-ray; 2.45 A; A=1-597. DR PDB; 1CY1; X-ray; 2.30 A; A=1-597. DR PDB; 1CY2; X-ray; 2.30 A; A=1-597. DR PDB; 1CY4; X-ray; 2.55 A; A=1-597. DR PDB; 1CY6; X-ray; 2.50 A; A=1-597. DR PDB; 1CY7; X-ray; 2.40 A; A=1-597. DR PDB; 1CY8; X-ray; 2.45 A; A=1-597. DR PDB; 1CY9; X-ray; 1.80 A; A/B=214-477. DR PDB; 1CYY; X-ray; 2.15 A; A/B=214-477. DR PDB; 1ECL; X-ray; 1.90 A; A=1-597. DR PDB; 1MW8; X-ray; 1.90 A; X=1-592. DR PDB; 1MW9; X-ray; 1.67 A; X=1-592. DR PDB; 1YUA; NMR; -; A=745-865. DR PDB; 3PWT; X-ray; 1.90 A; A=1-596. DR PDB; 3PX7; X-ray; 2.30 A; A=1-595. DR PDB; 4RUL; X-ray; 2.90 A; A=2-865. DR PDBsum; 1CY0; -. DR PDBsum; 1CY1; -. DR PDBsum; 1CY2; -. DR PDBsum; 1CY4; -. DR PDBsum; 1CY6; -. DR PDBsum; 1CY7; -. DR PDBsum; 1CY8; -. DR PDBsum; 1CY9; -. DR PDBsum; 1CYY; -. DR PDBsum; 1ECL; -. DR PDBsum; 1MW8; -. DR PDBsum; 1MW9; -. DR PDBsum; 1YUA; -. DR PDBsum; 3PWT; -. DR PDBsum; 3PX7; -. DR PDBsum; 4RUL; -. DR AlphaFoldDB; P06612; -. DR BMRB; P06612; -. DR SMR; P06612; -. DR BioGRID; 4259579; 153. DR BioGRID; 850229; 5. DR DIP; DIP-11011N; -. DR IntAct; P06612; 69. DR STRING; 511145.b1274; -. DR BindingDB; P06612; -. DR ChEMBL; CHEMBL3259513; -. DR DrugBank; DB01812; Adenosine 3',5'-diphosphate. DR DrugBank; DB01643; Thymidine monophosphate. DR DrugBank; DB04205; Thymidine-3',5'-Diphosphate. DR jPOST; P06612; -. DR PaxDb; P06612; -. DR EnsemblBacteria; AAC74356; AAC74356; b1274. DR EnsemblBacteria; BAA14811; BAA14811; BAA14811. DR GeneID; 66674904; -. DR GeneID; 945862; -. DR KEGG; ecj:JW1266; -. DR KEGG; eco:b1274; -. DR PATRIC; fig|1411691.4.peg.1010; -. DR EchoBASE; EB1006; -. DR eggNOG; COG0550; Bacteria. DR HOGENOM; CLU_002929_4_3_6; -. DR InParanoid; P06612; -. DR OMA; PECKYTR; -. DR PhylomeDB; P06612; -. DR BioCyc; EcoCyc:EG11013-MON; -. DR BioCyc; MetaCyc:EG11013-MON; -. DR BRENDA; 5.6.2.1; 2026. DR BRENDA; 5.99.1.2; 2026. DR EvolutionaryTrace; P06612; -. DR PRO; PR:P06612; -. DR Proteomes; UP000000318; Chromosome. DR Proteomes; UP000000625; Chromosome. DR GO; GO:0005694; C:chromosome; IEA:InterPro. DR GO; GO:0005829; C:cytosol; IDA:EcoCyc. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW. DR GO; GO:0003916; F:DNA topoisomerase activity; IMP:EcoCyc. DR GO; GO:0003917; F:DNA topoisomerase type I (single strand cut, ATP-independent) activity; IMP:EcoCyc. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0006265; P:DNA topological change; IGI:EcoliWiki. DR CDD; cd00186; TOP1Ac; 1. DR CDD; cd03363; TOPRIM_TopoIA_TopoI; 1. DR Gene3D; 1.10.290.10; -; 1. DR Gene3D; 1.10.460.10; -; 1. DR Gene3D; 2.70.20.10; -; 1. DR HAMAP; MF_00952; Topoisom_1_prok; 1. DR InterPro; IPR000380; Topo_IA. DR InterPro; IPR003601; Topo_IA_2. DR InterPro; IPR023406; Topo_IA_AS. DR InterPro; IPR013497; Topo_IA_cen. DR InterPro; IPR013824; Topo_IA_cen_sub1. DR InterPro; IPR013825; Topo_IA_cen_sub2. DR InterPro; IPR013826; Topo_IA_cen_sub3. DR InterPro; IPR023405; Topo_IA_core_domain. DR InterPro; IPR003602; Topo_IA_DNA-bd_dom. DR InterPro; IPR013498; Topo_IA_Znf. DR InterPro; IPR005733; TopoI_bac-type. DR InterPro; IPR013263; TopoI_Znr_bac. DR InterPro; IPR028612; Topoisom_1_IA. DR InterPro; IPR006171; TOPRIM_domain. DR InterPro; IPR034149; TOPRIM_TopoI. DR PANTHER; PTHR42785; DNA TOPOISOMERASE, TYPE IA, CORE; 1. DR Pfam; PF08272; Topo_Zn_Ribbon; 2. DR Pfam; PF01131; Topoisom_bac; 1. DR Pfam; PF01751; Toprim; 1. DR Pfam; PF01396; zf-C4_Topoisom; 2. DR PRINTS; PR00417; PRTPISMRASEI. DR SMART; SM00437; TOP1Ac; 1. DR SMART; SM00436; TOP1Bc; 1. DR SMART; SM00493; TOPRIM; 1. DR SUPFAM; SSF56712; Prokaryotic type I DNA topoisomerase; 1. DR TIGRFAMs; TIGR01051; topA_bact; 1. DR PROSITE; PS00396; TOPOISOMERASE_I_PROK; 1. DR PROSITE; PS50880; TOPRIM; 1. PE 1: Evidence at protein level; KW 3D-structure; DNA-binding; Isomerase; Magnesium; Metal-binding; KW Reference proteome; Repeat; Topoisomerase; Zinc; Zinc-finger. FT CHAIN 1..865 FT /note="DNA topoisomerase 1" FT /id="PRO_0000145147" FT DOMAIN 3..142 FT /note="Toprim" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00952" FT ZN_FING 599..630 FT /note="C4-type 1" FT ZN_FING 662..689 FT /note="C4-type 2" FT ZN_FING 711..736 FT /note="C4-type 3" FT REGION 37..65 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 192..197 FT /note="Interaction with DNA" FT COMPBIAS 51..65 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 319 FT /note="O-(5'-phospho-DNA)-tyrosine intermediate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00952, FT ECO:0000269|PubMed:21482796, ECO:0000269|PubMed:8114910, FT ECO:0000269|PubMed:9497321" FT BINDING 9 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /ligand_note="catalytic" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00952" FT BINDING 111 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /ligand_note="catalytic" FT /evidence="ECO:0000305" FT BINDING 111 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="2" FT /evidence="ECO:0000305" FT BINDING 113 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="2" FT /evidence="ECO:0000305" FT SITE 33 FT /note="Interaction with DNA" FT SITE 168 FT /note="Interaction with DNA" FT SITE 169 FT /note="Interaction with DNA" FT SITE 172 FT /note="Interaction with DNA" FT SITE 177 FT /note="Interaction with DNA" FT SITE 184 FT /note="Interaction with DNA" FT SITE 321 FT /note="Interaction with DNA" FT SITE 507 FT /note="Interaction with DNA" FT MUTAGEN 9 FT /note="E->A: Abolishes enzyme activity." FT /evidence="ECO:0000269|PubMed:9497321" FT MUTAGEN 9 FT /note="E->Q: No effect on DNA cleavage activity." FT /evidence="ECO:0000269|PubMed:9497321" FT MUTAGEN 111 FT /note="D->A: Abolishes both magnesium binding and enzyme FT activity; when associated with A-113 and A-115." FT /evidence="ECO:0000269|PubMed:10681504" FT MUTAGEN 113 FT /note="D->A: Abolishes both magnesium binding and enzyme FT activity; when associated with A-111 and A-115." FT /evidence="ECO:0000269|PubMed:10681504" FT MUTAGEN 115 FT /note="E->A: Abolishes both magnesium binding and enzyme FT activity; when associated with A-111 and A-113." FT /evidence="ECO:0000269|PubMed:10681504" FT MUTAGEN 168 FT /note="R->A: Abolishes enzyme activity." FT /evidence="ECO:0000269|PubMed:21482796" FT MUTAGEN 172 FT /note="D->A: Abolishes enzyme activity." FT /evidence="ECO:0000269|PubMed:21482796" FT MUTAGEN 319 FT /note="Y->A: Abolishes enzyme activity." FT /evidence="ECO:0000269|PubMed:9497321" FT MUTAGEN 321 FT /note="R->A: Abolishes enzyme activity." FT /evidence="ECO:0000269|PubMed:9497321" FT MUTAGEN 321 FT /note="R->K: No effect." FT /evidence="ECO:0000269|PubMed:9497321" FT MUTAGEN 365 FT /note="H->A: No effect." FT /evidence="ECO:0000269|PubMed:14604525, FT ECO:0000269|PubMed:9497321" FT MUTAGEN 365 FT /note="H->R: Increases DNA binding affinity." FT /evidence="ECO:0000269|PubMed:14604525, FT ECO:0000269|PubMed:9497321" FT MUTAGEN 496 FT /note="T->A: No effect." FT /evidence="ECO:0000269|PubMed:9497321" FT CONFLICT 787 FT /note="P -> R (in Ref. 6; AAA23641)" FT /evidence="ECO:0000305" FT STRAND 4..9 FT /evidence="ECO:0007829|PDB:1MW9" FT HELIX 11..18 FT /evidence="ECO:0007829|PDB:1MW9" FT STRAND 25..29 FT /evidence="ECO:0007829|PDB:1MW9" FT STRAND 35..37 FT /evidence="ECO:0007829|PDB:1MW9" FT HELIX 64..71 FT /evidence="ECO:0007829|PDB:1MW9" FT STRAND 72..74 FT /evidence="ECO:0007829|PDB:1ECL" FT TURN 75..79 FT /evidence="ECO:0007829|PDB:1MW9" FT TURN 87..89 FT /evidence="ECO:0007829|PDB:1ECL" FT HELIX 90..101 FT /evidence="ECO:0007829|PDB:1MW9" FT STRAND 104..108 FT /evidence="ECO:0007829|PDB:1MW9" FT HELIX 114..127 FT /evidence="ECO:0007829|PDB:1MW9" FT HELIX 131..133 FT /evidence="ECO:0007829|PDB:1MW9" FT STRAND 134..136 FT /evidence="ECO:0007829|PDB:1MW9" FT HELIX 144..152 FT /evidence="ECO:0007829|PDB:1MW9" FT HELIX 159..186 FT /evidence="ECO:0007829|PDB:1MW9" FT HELIX 197..213 FT /evidence="ECO:0007829|PDB:1MW9" FT STRAND 218..227 FT /evidence="ECO:0007829|PDB:1MW9" FT STRAND 229..231 FT /evidence="ECO:0007829|PDB:3PWT" FT STRAND 233..241 FT /evidence="ECO:0007829|PDB:1MW9" FT HELIX 251..263 FT /evidence="ECO:0007829|PDB:1MW9" FT STRAND 266..278 FT /evidence="ECO:0007829|PDB:1MW9" FT HELIX 286..297 FT /evidence="ECO:0007829|PDB:1MW9" FT HELIX 301..313 FT /evidence="ECO:0007829|PDB:1MW9" FT STRAND 316..318 FT /evidence="ECO:0007829|PDB:1ECL" FT HELIX 329..342 FT /evidence="ECO:0007829|PDB:1MW9" FT HELIX 345..347 FT /evidence="ECO:0007829|PDB:1MW9" FT STRAND 356..358 FT /evidence="ECO:0007829|PDB:1CYY" FT STRAND 362..364 FT /evidence="ECO:0007829|PDB:1CYY" FT HELIX 377..379 FT /evidence="ECO:0007829|PDB:1MW9" FT HELIX 385..401 FT /evidence="ECO:0007829|PDB:1MW9" FT STRAND 406..417 FT /evidence="ECO:0007829|PDB:1MW9" FT STRAND 420..431 FT /evidence="ECO:0007829|PDB:1MW9" FT HELIX 433..437 FT /evidence="ECO:0007829|PDB:1MW9" FT STRAND 458..470 FT /evidence="ECO:0007829|PDB:1MW9" FT HELIX 479..488 FT /evidence="ECO:0007829|PDB:1MW9" FT TURN 494..496 FT /evidence="ECO:0007829|PDB:1MW9" FT HELIX 497..506 FT /evidence="ECO:0007829|PDB:1MW9" FT STRAND 509..513 FT /evidence="ECO:0007829|PDB:1MW9" FT STRAND 516..519 FT /evidence="ECO:0007829|PDB:1MW9" FT HELIX 521..533 FT /evidence="ECO:0007829|PDB:1MW9" FT HELIX 535..538 FT /evidence="ECO:0007829|PDB:1MW9" FT HELIX 540..554 FT /evidence="ECO:0007829|PDB:1MW9" FT HELIX 560..579 FT /evidence="ECO:0007829|PDB:1MW9" FT HELIX 582..584 FT /evidence="ECO:0007829|PDB:1MW9" FT STRAND 593..598 FT /evidence="ECO:0007829|PDB:4RUL" FT STRAND 600..603 FT /evidence="ECO:0007829|PDB:4RUL" FT STRAND 605..610 FT /evidence="ECO:0007829|PDB:4RUL" FT STRAND 615..620 FT /evidence="ECO:0007829|PDB:4RUL" FT HELIX 626..628 FT /evidence="ECO:0007829|PDB:4RUL" FT STRAND 633..635 FT /evidence="ECO:0007829|PDB:4RUL" FT HELIX 648..650 FT /evidence="ECO:0007829|PDB:4RUL" FT HELIX 651..657 FT /evidence="ECO:0007829|PDB:4RUL" FT TURN 663..665 FT /evidence="ECO:0007829|PDB:4RUL" FT STRAND 668..675 FT /evidence="ECO:0007829|PDB:4RUL" FT STRAND 678..683 FT /evidence="ECO:0007829|PDB:4RUL" FT TURN 684..688 FT /evidence="ECO:0007829|PDB:4RUL" FT STRAND 692..694 FT /evidence="ECO:0007829|PDB:4RUL" FT TURN 702..705 FT /evidence="ECO:0007829|PDB:4RUL" FT STRAND 712..714 FT /evidence="ECO:0007829|PDB:4RUL" FT STRAND 717..722 FT /evidence="ECO:0007829|PDB:4RUL" FT STRAND 724..733 FT /evidence="ECO:0007829|PDB:4RUL" FT STRAND 740..742 FT /evidence="ECO:0007829|PDB:4RUL" FT HELIX 744..746 FT /evidence="ECO:0007829|PDB:4RUL" FT STRAND 756..762 FT /evidence="ECO:0007829|PDB:4RUL" FT STRAND 764..767 FT /evidence="ECO:0007829|PDB:4RUL" FT STRAND 769..775 FT /evidence="ECO:0007829|PDB:4RUL" FT STRAND 778..785 FT /evidence="ECO:0007829|PDB:4RUL" FT TURN 786..788 FT /evidence="ECO:0007829|PDB:4RUL" FT HELIX 797..802 FT /evidence="ECO:0007829|PDB:1YUA" FT TURN 803..806 FT /evidence="ECO:0007829|PDB:1YUA" FT HELIX 809..811 FT /evidence="ECO:0007829|PDB:4RUL" FT HELIX 812..815 FT /evidence="ECO:0007829|PDB:4RUL" FT STRAND 826..829 FT /evidence="ECO:0007829|PDB:4RUL" FT TURN 833..835 FT /evidence="ECO:0007829|PDB:4RUL" FT STRAND 840..843 FT /evidence="ECO:0007829|PDB:4RUL" FT STRAND 851..855 FT /evidence="ECO:0007829|PDB:4RUL" SQ SEQUENCE 865 AA; 97350 MW; 8C13F767FE5B178C CRC64; MGKALVIVES PAKAKTINKY LGSDYVVKSS VGHIRDLPTS GSAAKKSADS TSTKTAKKPK KDERGALVNR MGVDPWHNWE AHYEVLPGKE KVVSELKQLA EKADHIYLAT DLDREGEAIA WHLREVIGGD DARYSRVVFN EITKNAIRQA FNKPGELNID RVNAQQARRF MDRVVGYMVS PLLWKKIARG LSAGRVQSVA VRLVVERERE IKAFVPEEFW EVDASTTTPS GEALALQVTH QNDKPFRPVN KEQTQAAVSL LEKARYSVLE REDKPTTSKP GAPFITSTLQ QAASTRLGFG VKKTMMMAQR LYEAGYITYM RTDSTNLSQD AVNMVRGYIS DNFGKKYLPE SPNQYASKEN SQEAHEAIRP SDVNVMAESL KDMEADAQKL YQLIWRQFVA CQMTPAKYDS TTLTVGAGDF RLKARGRILR FDGWTKVMPA LRKGDEDRIL PAVNKGDALT LVELTPAQHF TKPPARFSEA SLVKELEKRG IGRPSTYASI ISTIQDRGYV RVENRRFYAE KMGEIVTDRL EENFRELMNY DFTAQMENSL DQVANHEAEW KAVLDHFFSD FTQQLDKAEK DPEEGGMRPN QMVLTSIDCP TCGRKMGIRT ASTGVFLGCS GYALPPKERC KTTINLVPEN EVLNVLEGED AETNALRAKR RCPKCGTAMD SYLIDPKRKL HVCGNNPTCD GYEIEEGEFR IKGYDGPIVE CEKCGSEMHL KMGRFGKYMA CTNEECKNTR KILRNGEVAP PKEDPVPLPE LPCEKSDAYF VLRDGAAGVF LAANTFPKSR ETRAPLVEEL YRFRDRLPEK LRYLADAPQQ DPEGNKTMVR FSRKTKQQYV SSEKDGKATG WSAFYVDGKW VEGKK //