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Entry: TOP1_ECOLI
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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   26-NOV-2014, entry version 158.
DE   RecName: Full=DNA topoisomerase 1 {ECO:0000255|HAMAP-Rule:MF_00952};
DE            EC=5.99.1.2 {ECO:0000255|HAMAP-Rule:MF_00952};
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; Enterobacteriales;
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
RT   coli 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.,
RA   Makino K., Miki T., Mizobuchi K., Mori H., Mori T., Motomura K.,
RA   Nakade S., Nakamura Y., Nashimoto H., Nishio Y., Oshima T., Saito N.,
RA   Sampei G., Seki Y., Sivasundaram S., Tagami H., Takeda J.,
RA   Takemoto K., Takeuchi Y., Wada C., Yamamoto Y., Horiuchi T.;
RT   "A 570-kb DNA sequence of the Escherichia coli K-12 genome
RT   corresponding to 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.,
RA   Mau B., 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
RT   MG1655 and W3110.";
RL   Mol. Syst. Biol. 2:E1-E5(2006).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 698-865.
RX   PubMed=3032952;
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.,
RA   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,
RP   ENZYME 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
RT   for binding of Mg(II) and subsequent conformational change.";
RL   J. Biol. Chem. 275:5318-5322(2000).
RN   [10]
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
RT   DNA topoisomerase I.";
RL   Nature 367:138-146(1994).
RN   [11]
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
RT   domain of Escherichia coli topoisomerase I.";
RL   Biochemistry 34:7622-7628(1995).
RN   [12]
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   [13]
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   [14]
RP   X-RAY CRYSTALLOGRAPHY (1.67 ANGSTROMS) OF 1-592 OF MUTANT ARG-365 IN
RP   COMPLEX WITH SINGLE-STANDED 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
RT   single-stranded DNA.";
RL   Structure 11:1349-1358(2003).
RN   [15]
RP   X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 1-596 OF MUTANT ASN-111 IN
RP   COMPLEX WITH DNA, FUNCTION, CATALYTIC ACTIVITY, ACTIVE SITE, COFACTOR,
RP   MUTAGENESIS OF ARG-168 AND ASP-172, DNA-BINDING SITES, AND ENZYME
RP   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
RT   rejoining 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,
CC       which is introduced during the DNA replication and transcription,
CC       by transiently cleaving and rejoining one strand of the DNA
CC       duplex. Introduces a single-strand break via transesterification
CC       at a target site in duplex DNA. The scissile phosphodiester is
CC       attacked by the catalytic tyrosine of the enzyme, resulting in the
CC       formation of a DNA-(5'-phosphotyrosyl)-enzyme intermediate and the
CC       expulsion of a 3'-OH DNA strand. The free DNA strand then
CC       undergoes passage around the unbroken strand, thus removing DNA
CC       supercoils. Finally, in the religation step, the DNA 3'-OH attacks
CC       the covalent intermediate to expel the active-site tyrosine and
CC       restore the DNA phosphodiester backbone. {ECO:0000255|HAMAP-
CC       Rule:MF_00952, ECO:0000269|PubMed:10681504,
CC       ECO:0000269|PubMed:21482796, ECO:0000269|PubMed:9497321}.
CC   -!- CATALYTIC ACTIVITY: ATP-independent breakage of single-stranded
CC       DNA, followed by passage and rejoining. {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,
CC         ECO:0000269|PubMed:21482796};
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000269|PubMed:10681504,
CC         ECO:0000269|PubMed:21482796};
CC       Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC         Evidence={ECO:0000269|PubMed:10681504,
CC         ECO:0000269|PubMed:21482796};
CC       Note=Binds two Mg(2+) ions per subunit. The magnesium ions form
CC       salt bridges with both the protein and the DNA. Can also accept
CC       other 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   -!- SIMILARITY: Belongs to the type IA topoisomerase family.
CC       {ECO:0000255|HAMAP-Rule:MF_00952}.
CC   -!- SIMILARITY: Contains 1 Toprim domain. {ECO:0000255|HAMAP-
CC       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; YP_489542.1; NC_007779.1.
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   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   ProteinModelPortal; P06612; -.
DR   SMR; P06612; 2-619, 745-865.
DR   DIP; DIP-11011N; -.
DR   IntAct; P06612; 68.
DR   MINT; MINT-1218330; -.
DR   STRING; 511145.b1274; -.
DR   PaxDb; P06612; -.
DR   PRIDE; P06612; -.
DR   EnsemblBacteria; AAC74356; AAC74356; b1274.
DR   EnsemblBacteria; BAA14811; BAA14811; BAA14811.
DR   GeneID; 12930585; -.
DR   GeneID; 945862; -.
DR   KEGG; ecj:Y75_p1248; -.
DR   KEGG; eco:b1274; -.
DR   PATRIC; 32117806; VBIEscCol129921_1323.
DR   EchoBASE; EB1006; -.
DR   EcoGene; EG11013; topA.
DR   eggNOG; COG0551; -.
DR   HOGENOM; HOG000004018; -.
DR   InParanoid; P06612; -.
DR   KO; K03168; -.
DR   OMA; VVECDKC; -.
DR   OrthoDB; EOG6S7XQ9; -.
DR   PhylomeDB; P06612; -.
DR   BioCyc; EcoCyc:EG11013-MONOMER; -.
DR   BioCyc; ECOL316407:JW1266-MONOMER; -.
DR   BioCyc; MetaCyc:EG11013-MONOMER; -.
DR   EvolutionaryTrace; P06612; -.
DR   PRO; PR:P06612; -.
DR   Genevestigator; P06612; -.
DR   GO; GO:0005694; C:chromosome; IEA:InterPro.
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 activity; IMP:EcoCyc.
DR   GO; GO:0003918; F:DNA topoisomerase type II (ATP-hydrolyzing) activity; IEA:InterPro.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0022616; P:DNA strand elongation; IMP:EcoCyc.
DR   GO; GO:0006265; P:DNA topological change; IGI:EcoliWiki.
DR   Gene3D; 1.10.460.10; -; 3.
DR   Gene3D; 2.70.20.10; -; 2.
DR   Gene3D; 3.40.50.140; -; 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; 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   PANTHER; PTHR11390; PTHR11390; 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; Complete proteome; DNA-binding; Isomerase; Magnesium;
KW   Metal-binding; Reference proteome; Repeat; Topoisomerase; Zinc;
KW   Zinc-finger.
FT   CHAIN         1    865       DNA topoisomerase 1.
FT                                /FTId=PRO_0000145147.
FT   DOMAIN        3    142       Toprim. {ECO:0000255|HAMAP-
FT                                Rule:MF_00952}.
FT   ZN_FING     599    630       C4-type 1.
FT   ZN_FING     662    689       C4-type 2.
FT   ZN_FING     711    736       C4-type 3.
FT   REGION      192    197       Interaction with DNA.
FT   ACT_SITE    319    319       O-(5'-phospho-DNA)-tyrosine intermediate.
FT                                {ECO:0000255|HAMAP-Rule:MF_00952,
FT                                ECO:0000269|PubMed:21482796,
FT                                ECO:0000269|PubMed:8114910,
FT                                ECO:0000269|PubMed:9497321}.
FT   METAL         9      9       Magnesium 1; catalytic.
FT                                {ECO:0000255|HAMAP-Rule:MF_00952}.
FT   METAL       111    111       Magnesium 1; catalytic. {ECO:0000305}.
FT   METAL       111    111       Magnesium 2. {ECO:0000305}.
FT   METAL       113    113       Magnesium 2. {ECO:0000305}.
FT   SITE         33     33       Interaction with DNA.
FT   SITE        168    168       Interaction with DNA.
FT   SITE        169    169       Interaction with DNA.
FT   SITE        172    172       Interaction with DNA.
FT   SITE        177    177       Interaction with DNA.
FT   SITE        184    184       Interaction with DNA.
FT   SITE        321    321       Interaction with DNA.
FT   SITE        507    507       Interaction with DNA.
FT   MUTAGEN       9      9       E->A: Abolishes enzyme activity.
FT                                {ECO:0000269|PubMed:9497321}.
FT   MUTAGEN       9      9       E->Q: No effect on DNA cleavage activity.
FT                                {ECO:0000269|PubMed:9497321}.
FT   MUTAGEN     111    111       D->A: Abolishes both magnesium binding
FT                                and enzyme activity; when associated with
FT                                A-113 and A-115.
FT                                {ECO:0000269|PubMed:10681504}.
FT   MUTAGEN     113    113       D->A: Abolishes both magnesium binding
FT                                and enzyme activity; when associated with
FT                                A-111 and A-115.
FT                                {ECO:0000269|PubMed:10681504}.
FT   MUTAGEN     115    115       E->A: Abolishes both magnesium binding
FT                                and enzyme activity; when associated with
FT                                A-111 and A-113.
FT                                {ECO:0000269|PubMed:10681504}.
FT   MUTAGEN     168    168       R->A: Abolishes enzyme activity.
FT                                {ECO:0000269|PubMed:21482796}.
FT   MUTAGEN     172    172       D->A: Abolishes enzyme activity.
FT                                {ECO:0000269|PubMed:21482796}.
FT   MUTAGEN     319    319       Y->A: Abolishes enzyme activity.
FT                                {ECO:0000269|PubMed:9497321}.
FT   MUTAGEN     321    321       R->A: Abolishes enzyme activity.
FT                                {ECO:0000269|PubMed:9497321}.
FT   MUTAGEN     321    321       R->K: No effect.
FT                                {ECO:0000269|PubMed:9497321}.
FT   MUTAGEN     365    365       H->A: No effect.
FT                                {ECO:0000269|PubMed:14604525,
FT                                ECO:0000269|PubMed:9497321}.
FT   MUTAGEN     365    365       H->R: Increases DNA binding affinity.
FT                                {ECO:0000269|PubMed:14604525,
FT                                ECO:0000269|PubMed:9497321}.
FT   MUTAGEN     496    496       T->A: No effect.
FT                                {ECO:0000269|PubMed:9497321}.
FT   CONFLICT    787    787       P -> R (in Ref. 6; AAA23641).
FT                                {ECO:0000305}.
FT   STRAND        4      9       {ECO:0000244|PDB:1MW9}.
FT   HELIX        11     18       {ECO:0000244|PDB:1MW9}.
FT   STRAND       25     29       {ECO:0000244|PDB:1MW9}.
FT   STRAND       35     37       {ECO:0000244|PDB:1MW9}.
FT   HELIX        64     71       {ECO:0000244|PDB:1MW9}.
FT   STRAND       72     74       {ECO:0000244|PDB:1ECL}.
FT   TURN         75     79       {ECO:0000244|PDB:1MW9}.
FT   TURN         87     89       {ECO:0000244|PDB:1ECL}.
FT   HELIX        90    101       {ECO:0000244|PDB:1MW9}.
FT   STRAND      104    108       {ECO:0000244|PDB:1MW9}.
FT   HELIX       114    127       {ECO:0000244|PDB:1MW9}.
FT   HELIX       131    133       {ECO:0000244|PDB:1MW9}.
FT   STRAND      134    136       {ECO:0000244|PDB:1MW9}.
FT   HELIX       144    152       {ECO:0000244|PDB:1MW9}.
FT   HELIX       159    186       {ECO:0000244|PDB:1MW9}.
FT   HELIX       197    213       {ECO:0000244|PDB:1MW9}.
FT   STRAND      218    227       {ECO:0000244|PDB:1MW9}.
FT   STRAND      229    231       {ECO:0000244|PDB:3PWT}.
FT   STRAND      233    241       {ECO:0000244|PDB:1MW9}.
FT   HELIX       251    263       {ECO:0000244|PDB:1MW9}.
FT   STRAND      266    278       {ECO:0000244|PDB:1MW9}.
FT   HELIX       286    297       {ECO:0000244|PDB:1MW9}.
FT   HELIX       301    313       {ECO:0000244|PDB:1MW9}.
FT   STRAND      316    318       {ECO:0000244|PDB:1ECL}.
FT   HELIX       329    342       {ECO:0000244|PDB:1MW9}.
FT   HELIX       345    347       {ECO:0000244|PDB:1MW9}.
FT   STRAND      356    358       {ECO:0000244|PDB:1CYY}.
FT   STRAND      362    364       {ECO:0000244|PDB:1CYY}.
FT   HELIX       377    379       {ECO:0000244|PDB:1MW9}.
FT   HELIX       385    401       {ECO:0000244|PDB:1MW9}.
FT   STRAND      406    417       {ECO:0000244|PDB:1MW9}.
FT   STRAND      420    431       {ECO:0000244|PDB:1MW9}.
FT   HELIX       433    437       {ECO:0000244|PDB:1MW9}.
FT   STRAND      458    470       {ECO:0000244|PDB:1MW9}.
FT   HELIX       479    488       {ECO:0000244|PDB:1MW9}.
FT   TURN        494    496       {ECO:0000244|PDB:1MW9}.
FT   HELIX       497    506       {ECO:0000244|PDB:1MW9}.
FT   STRAND      509    513       {ECO:0000244|PDB:1MW9}.
FT   STRAND      516    519       {ECO:0000244|PDB:1MW9}.
FT   HELIX       521    533       {ECO:0000244|PDB:1MW9}.
FT   HELIX       535    538       {ECO:0000244|PDB:1MW9}.
FT   HELIX       540    554       {ECO:0000244|PDB:1MW9}.
FT   HELIX       560    579       {ECO:0000244|PDB:1MW9}.
FT   HELIX       582    584       {ECO:0000244|PDB:1MW9}.
FT   STRAND      755    762       {ECO:0000244|PDB:1YUA}.
FT   STRAND      764    767       {ECO:0000244|PDB:1YUA}.
FT   STRAND      769    773       {ECO:0000244|PDB:1YUA}.
FT   STRAND      776    778       {ECO:0000244|PDB:1YUA}.
FT   STRAND      780    783       {ECO:0000244|PDB:1YUA}.
FT   TURN        784    787       {ECO:0000244|PDB:1YUA}.
FT   HELIX       797    802       {ECO:0000244|PDB:1YUA}.
FT   TURN        803    806       {ECO:0000244|PDB:1YUA}.
FT   HELIX       812    816       {ECO:0000244|PDB:1YUA}.
FT   STRAND      827    832       {ECO:0000244|PDB:1YUA}.
FT   TURN        833    836       {ECO:0000244|PDB:1YUA}.
FT   STRAND      837    842       {ECO:0000244|PDB:1YUA}.
FT   STRAND      853    855       {ECO:0000244|PDB:1YUA}.
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
//
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