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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   29-OCT-2014, entry version 157.
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: Magnesium. Binds two Mg(2+) ions per subunit. The
CC       magnesium ions form salt bridges with both the protein and the
CC       DNA. Can also accept other divalent metal cations, such as Mn(2+)
CC       and Ca(2+). {ECO:0000269|PubMed:10681504,
CC       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
FT   HELIX        11     18
FT   STRAND       25     29
FT   STRAND       35     37
FT   HELIX        64     71
FT   STRAND       72     74
FT   TURN         75     79
FT   TURN         87     89
FT   HELIX        90    101
FT   STRAND      104    108
FT   HELIX       114    127
FT   HELIX       131    133
FT   STRAND      134    136
FT   HELIX       144    152
FT   HELIX       159    186
FT   HELIX       197    213
FT   STRAND      218    227
FT   STRAND      229    231
FT   STRAND      233    241
FT   HELIX       251    263
FT   STRAND      266    278
FT   HELIX       286    297
FT   HELIX       301    313
FT   STRAND      316    318
FT   HELIX       329    342
FT   HELIX       345    347
FT   STRAND      356    358
FT   STRAND      362    364
FT   HELIX       377    379
FT   HELIX       385    401
FT   STRAND      406    417
FT   STRAND      420    431
FT   HELIX       433    437
FT   STRAND      458    470
FT   HELIX       479    488
FT   TURN        494    496
FT   HELIX       497    506
FT   STRAND      509    513
FT   STRAND      516    519
FT   HELIX       521    533
FT   HELIX       535    538
FT   HELIX       540    554
FT   HELIX       560    579
FT   HELIX       582    584
FT   STRAND      755    762
FT   STRAND      764    767
FT   STRAND      769    773
FT   STRAND      776    778
FT   STRAND      780    783
FT   TURN        784    787
FT   HELIX       797    802
FT   TURN        803    806
FT   HELIX       812    816
FT   STRAND      827    832
FT   TURN        833    836
FT   STRAND      837    842
FT   STRAND      853    855
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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