TOP1_ECOLI
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 03-AUG-2022, entry version 206.
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}.
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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 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 PRIDE; 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; PTHR42785; 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; SSF56712; 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
