ID   EX1_ECOLI               Reviewed;         475 AA.
AC   P04995;
DT   13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1994, sequence version 2.
DT   24-JAN-2024, entry version 196.
DE   RecName: Full=Exodeoxyribonuclease I;
DE            Short=ExoI {ECO:0000303|PubMed:11101894};
DE            Short=Exonuclease I {ECO:0000303|PubMed:11101894};
DE            EC=3.1.11.1 {ECO:0000269|PubMed:18591666, ECO:0000269|PubMed:20018747, ECO:0000269|PubMed:23609540};
DE   AltName: Full=DNA deoxyribophosphodiesterase;
DE            Short=dRPase;
GN   Name=sbcB; Synonyms=cpeA, xonA; OrderedLocusNames=b2011, JW1993;
OS   Escherichia coli (strain K12).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83333;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 1-12.
RC   STRAIN=K12;
RX   PubMed=3539937; DOI=10.1016/s0021-9258(19)75948-1;
RA   Phillips G.J., Kushner S.R.;
RT   "Determination of the nucleotide sequence for the exonuclease I structural
RT   gene (sbcB) of Escherichia coli K12.";
RL   J. Biol. Chem. 262:455-459(1987).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / BHB2600;
RA   Richterich P., Lakey N., Gryan G., Jaehn L., Mintz L., Robison K.,
RA   Church G.M.;
RT   "Automated multiplex sequencing of the E.coli genome.";
RL   Submitted (OCT-1993) 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=9097040; DOI=10.1093/dnares/3.6.379;
RA   Itoh T., Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K.,
RA   Kasai H., Kimura S., Kitakawa M., Kitagawa M., Makino K., Miki T.,
RA   Mizobuchi K., Mori H., Mori T., Motomura K., Nakade S., Nakamura Y.,
RA   Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G., Seki Y.,
RA   Sivasundaram S., Tagami H., Takeda J., Takemoto K., Wada C., Yamamoto Y.,
RA   Horiuchi T.;
RT   "A 460-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT   the 40.1-50.0 min region on the linkage map.";
RL   DNA Res. 3:379-392(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   FUNCTION AS A DRPASE.
RX   PubMed=1329027; DOI=10.1093/nar/20.18.4699;
RA   Sandigursky M., Franklin W.A.;
RT   "DNA deoxyribophosphodiesterase of Escherichia coli is associated with
RT   exonuclease I.";
RL   Nucleic Acids Res. 20:4699-4703(1992).
RN   [7]
RP   X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) IN COMPLEX WITH MAGNESIUM, AND
RP   DOMAIN.
RC   STRAIN=K12 / DH5-alpha {ECO:0000303|PubMed:11101894};
RX   PubMed=11101894; DOI=10.1038/81978;
RA   Breyer W.A., Matthews B.W.;
RT   "Structure of Escherichia coli exonuclease I suggests how processivity is
RT   achieved.";
RL   Nat. Struct. Biol. 7:1125-1128(2000).
RN   [8]
RP   X-RAY CRYSTALLOGRAPHY (1.50 ANGSTROMS) IN COMPLEX WITH DTMP PRODUCT AND
RP   MAGNESIUM, COFACTOR, AND DOMAIN.
RC   STRAIN=K12 {ECO:0000303|PubMed:18219121};
RX   PubMed=18219121; DOI=10.1107/s090744490706012x;
RA   Busam R.D.;
RT   "Structure of Escherichia coli exonuclease I in complex with thymidine 5'-
RT   monophosphate.";
RL   Acta Crystallogr. D 64:206-210(2008).
RN   [9]
RP   X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) OF APO FORM AND IN COMPLEX WITH SSB
RP   TAIL PEPTIDE AND MAGNESIUM, CATALYTIC ACTIVITY, COFACTOR, INTERACTION WITH
RP   SSB, DOMAIN, SITES, AND MUTAGENESIS OF ARG-148; GLU-150; TYR-207; LYS-227;
RP   GLN-311; ARG-316; GLU-318; ASP-319; ARG-327; LEU-331; ARG-338; GLN-448 AND
RP   GLN-452.
RX   PubMed=18591666; DOI=10.1073/pnas.0800741105;
RA   Lu D., Keck J.L.;
RT   "Structural basis of Escherichia coli single-stranded DNA-binding protein
RT   stimulation of exonuclease I.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:9169-9174(2008).
RN   [10]
RP   X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS) IN COMPLEXES WITH INHIBITORS AND
RP   MAGNESIUM, CATALYTIC ACTIVITY, COFACTOR, INTERACTION WITH SSB, AND SITE.
RX   PubMed=20018747; DOI=10.1073/pnas.0909191107;
RA   Lu D., Bernstein D.A., Satyshur K.A., Keck J.L.;
RT   "Small-molecule tools for dissecting the roles of SSB/protein interactions
RT   in genome maintenance.";
RL   Proc. Natl. Acad. Sci. U.S.A. 107:633-638(2010).
RN   [11]
RP   X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) IN COMPLEXES WITH SINGLE-STRANDED
RP   DNA SUBSTRATES AND ZINC.
RA   Qiu R., Lou T., Wei J., Liu M., Gu S., Tang R., Ji C., Gong W.;
RT   "The structures of Escherichia coli exonuclease I in complex with the
RT   single strand DNA.";
RL   Submitted (SEP-2012) to the PDB data bank.
RN   [12]
RP   X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) IN COMPLEXES WITH SINGLE-STRANDED
RP   DNA SUBSTRATES AND MAGNESIUM, FUNCTION, CATALYTIC ACTIVITY, COFACTOR,
RP   ACTIVITY REGULATION, SUBUNIT, DOMAIN, AND MUTAGENESIS OF HIS-181.
RC   STRAIN=K12 {ECO:0000303|PubMed:23609540};
RX   PubMed=23609540; DOI=10.1093/nar/gkt278;
RA   Korada S.K., Johns T.D., Smith C.E., Jones N.D., McCabe K.A., Bell C.E.;
RT   "Crystal structures of Escherichia coli exonuclease I in complex with
RT   single-stranded DNA provide insights into the mechanism of processive
RT   digestion.";
RL   Nucleic Acids Res. 41:5887-5897(2013).
CC   -!- FUNCTION: Degrades single-stranded DNA (ssDNA) in a highly processive
CC       manner (PubMed:23609540). Also functions as a DNA
CC       deoxyribophosphodiesterase that releases deoxyribose-phosphate moieties
CC       following the cleavage of DNA at an apurinic/apyrimidinic (AP) site by
CC       either an AP endonuclease or AP lyase (PubMed:1329027).
CC       {ECO:0000269|PubMed:1329027, ECO:0000269|PubMed:23609540}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Exonucleolytic cleavage in the 3'- to 5'-direction to yield
CC         nucleoside 5'-phosphates.; EC=3.1.11.1;
CC         Evidence={ECO:0000269|PubMed:18591666, ECO:0000269|PubMed:20018747,
CC         ECO:0000269|PubMed:23609540};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000269|PubMed:18219121, ECO:0000269|PubMed:18591666,
CC         ECO:0000269|PubMed:20018747, ECO:0000269|PubMed:23609540};
CC       Note=Binds 2 Mg(2+) ions per monomer. {ECO:0000269|PubMed:18591666};
CC   -!- ACTIVITY REGULATION: Inhibited by 10 mM EDTA.
CC       {ECO:0000269|PubMed:23609540}.
CC   -!- SUBUNIT: Monomer (PubMed:23609540). Interacts with ssb (via C-
CC       terminus); this interaction stimulates the exonuclease activity by
CC       recruiting the enzyme to its substrate (PubMed:18591666,
CC       PubMed:20018747). {ECO:0000269|PubMed:18591666,
CC       ECO:0000269|PubMed:20018747, ECO:0000269|PubMed:23609540}.
CC   -!- DOMAIN: The N-terminal exonuclease domain and the exonuclease C-
CC       terminal domain form a central positively charged groove which binds
CC       the DNA. {ECO:0000269|PubMed:18591666, ECO:0000269|PubMed:23609540,
CC       ECO:0000305|PubMed:11101894, ECO:0000305|PubMed:18219121}.
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DR   EMBL; J02641; AAA19938.1; -; Unassigned_DNA.
DR   EMBL; U00009; AAA16417.1; -; Genomic_DNA.
DR   EMBL; U00096; AAC75072.1; -; Genomic_DNA.
DR   EMBL; AP009048; BAA15839.1; -; Genomic_DNA.
DR   PIR; B64966; NCECX1.
DR   RefSeq; NP_416515.1; NC_000913.3.
DR   RefSeq; WP_000980589.1; NZ_LN832404.1.
DR   PDB; 1FXX; X-ray; 2.40 A; A=1-475.
DR   PDB; 2QXF; X-ray; 1.50 A; A=1-475.
DR   PDB; 3C94; X-ray; 2.70 A; A=1-475.
DR   PDB; 3C95; X-ray; 1.70 A; A=1-475.
DR   PDB; 3HL8; X-ray; 1.55 A; A=1-475.
DR   PDB; 3HP9; X-ray; 1.60 A; A=1-475.
DR   PDB; 4HCB; X-ray; 2.00 A; A/B=1-475.
DR   PDB; 4HCC; X-ray; 2.96 A; A/B=1-475.
DR   PDB; 4JRP; X-ray; 1.95 A; A/B=1-475.
DR   PDB; 4JRQ; X-ray; 3.00 A; A/B=1-475.
DR   PDB; 4JS4; X-ray; 3.10 A; A/B=1-475.
DR   PDB; 4JS5; X-ray; 3.50 A; A/B=1-475.
DR   PDBsum; 1FXX; -.
DR   PDBsum; 2QXF; -.
DR   PDBsum; 3C94; -.
DR   PDBsum; 3C95; -.
DR   PDBsum; 3HL8; -.
DR   PDBsum; 3HP9; -.
DR   PDBsum; 4HCB; -.
DR   PDBsum; 4HCC; -.
DR   PDBsum; 4JRP; -.
DR   PDBsum; 4JRQ; -.
DR   PDBsum; 4JS4; -.
DR   PDBsum; 4JS5; -.
DR   AlphaFoldDB; P04995; -.
DR   SMR; P04995; -.
DR   BioGRID; 4260414; 102.
DR   DIP; DIP-10827N; -.
DR   IntAct; P04995; 7.
DR   STRING; 511145.b2011; -.
DR   jPOST; P04995; -.
DR   PaxDb; 511145-b2011; -.
DR   EnsemblBacteria; AAC75072; AAC75072; b2011.
DR   GeneID; 946529; -.
DR   KEGG; ecj:JW1993; -.
DR   KEGG; eco:b2011; -.
DR   EchoBASE; EB0919; -.
DR   eggNOG; COG2925; Bacteria.
DR   HOGENOM; CLU_043508_1_1_6; -.
DR   InParanoid; P04995; -.
DR   OMA; RDRPAQF; -.
DR   OrthoDB; 9763470at2; -.
DR   PhylomeDB; P04995; -.
DR   BioCyc; EcoCyc:EG10926-MONOMER; -.
DR   BioCyc; MetaCyc:EG10926-MONOMER; -.
DR   BRENDA; 3.1.11.1; 2026.
DR   EvolutionaryTrace; P04995; -.
DR   PRO; PR:P04995; -.
DR   Proteomes; UP000000318; Chromosome.
DR   Proteomes; UP000000625; Chromosome.
DR   GO; GO:0000175; F:3'-5'-RNA exonuclease activity; IBA:GO_Central.
DR   GO; GO:0051575; F:5'-deoxyribose-5-phosphate lyase activity; IDA:UniProtKB.
DR   GO; GO:0000287; F:magnesium ion binding; IDA:UniProtKB.
DR   GO; GO:0008310; F:single-stranded DNA 3'-5' DNA exonuclease activity; IDA:UniProtKB.
DR   GO; GO:0003697; F:single-stranded DNA binding; IDA:UniProtKB.
DR   GO; GO:0006308; P:DNA catabolic process; IDA:UniProtKB.
DR   GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR   CDD; cd06138; ExoI_N; 1.
DR   Gene3D; 1.10.287.1240; -; 1.
DR   Gene3D; 3.30.1520.20; Exonuclease ExoI, domain 2; 1.
DR   Gene3D; 1.20.1280.70; Exonuclease ExoI, domain 3; 1.
DR   Gene3D; 3.30.420.10; Ribonuclease H-like superfamily/Ribonuclease H; 1.
DR   InterPro; IPR023607; Exodeoxyribonuclease_I.
DR   InterPro; IPR034748; EXOI_C.
DR   InterPro; IPR034747; EXOI_SH3.
DR   InterPro; IPR038649; EXOI_SH3_sf.
DR   InterPro; IPR013620; Exonuc_1_C.
DR   InterPro; IPR013520; Exonuclease_RNaseT/DNA_pol3.
DR   InterPro; IPR022894; Oligoribonuclease.
DR   InterPro; IPR012337; RNaseH-like_sf.
DR   InterPro; IPR036397; RNaseH_sf.
DR   PANTHER; PTHR11046:SF11; EXODEOXYRIBONUCLEASE I; 1.
DR   PANTHER; PTHR11046; OLIGORIBONUCLEASE, MITOCHONDRIAL; 1.
DR   Pfam; PF08411; Exonuc_X-T_C; 1.
DR   Pfam; PF00929; RNase_T; 1.
DR   PIRSF; PIRSF000977; Exodeoxyribonuclease_I; 1.
DR   SMART; SM00479; EXOIII; 1.
DR   SUPFAM; SSF53098; Ribonuclease H-like; 1.
DR   PROSITE; PS51785; EXOI_C; 1.
DR   PROSITE; PS51784; EXOI_SH3; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Direct protein sequencing; DNA damage; DNA repair;
KW   DNA-binding; Exonuclease; Hydrolase; Magnesium; Metal-binding; Nuclease;
KW   Reference proteome; Zinc.
FT   CHAIN           1..475
FT                   /note="Exodeoxyribonuclease I"
FT                   /id="PRO_0000087110"
FT   DOMAIN          13..192
FT                   /note="Exonuclease"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          202..355
FT                   /note="ExoI SH3-like"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01120"
FT   DOMAIN          358..475
FT                   /note="ExoI C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01121"
FT   BINDING         15
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000269|PubMed:11101894,
FT                   ECO:0000269|PubMed:18219121, ECO:0000269|PubMed:18591666,
FT                   ECO:0000269|PubMed:20018747, ECO:0000269|PubMed:23609540"
FT   BINDING         17
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000269|PubMed:18219121"
FT   BINDING         17
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000269|PubMed:18219121"
FT   BINDING         165
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000269|PubMed:18219121"
FT   BINDING         186
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000269|PubMed:18219121"
FT   SITE            18
FT                   /note="Interaction with single-stranded DNA"
FT                   /evidence="ECO:0000269|PubMed:23609540"
FT   SITE            66
FT                   /note="Interaction with single-stranded DNA"
FT                   /evidence="ECO:0000269|PubMed:23609540"
FT   SITE            113
FT                   /note="Interaction with single-stranded DNA"
FT                   /evidence="ECO:0000269|PubMed:23609540"
FT   SITE            124
FT                   /note="Interaction with single-stranded DNA"
FT                   /evidence="ECO:0000269|PubMed:23609540"
FT   SITE            128
FT                   /note="Interaction with single-stranded DNA"
FT                   /evidence="ECO:0000269|PubMed:23609540"
FT   SITE            142
FT                   /note="Interaction with single-stranded DNA"
FT                   /evidence="ECO:0000269|PubMed:23609540"
FT   SITE            148
FT                   /note="Important for interaction with ssb"
FT                   /evidence="ECO:0000269|PubMed:18591666"
FT   SITE            164
FT                   /note="Interaction with single-stranded DNA"
FT                   /evidence="ECO:0000269|PubMed:23609540,
FT                   ECO:0007744|PDB:4HCC"
FT   SITE            181
FT                   /note="Important for activity"
FT                   /evidence="ECO:0000269|PubMed:23609540"
FT   SITE            207
FT                   /note="Important for interaction with ssb"
FT                   /evidence="ECO:0000269|PubMed:18591666"
FT   SITE            214
FT                   /note="Interaction with single-stranded DNA"
FT                   /evidence="ECO:0000269|PubMed:23609540"
FT   SITE            257
FT                   /note="Interaction with single-stranded DNA"
FT                   /evidence="ECO:0000269|PubMed:23609540,
FT                   ECO:0007744|PDB:4HCC"
FT   SITE            284
FT                   /note="Interaction with single-stranded DNA"
FT                   /evidence="ECO:0000269|PubMed:23609540"
FT   SITE            304
FT                   /note="Interaction with single-stranded DNA"
FT                   /evidence="ECO:0000269|PubMed:23609540,
FT                   ECO:0007744|PDB:4HCC"
FT   SITE            311
FT                   /note="Important for interaction with ssb"
FT                   /evidence="ECO:0000269|PubMed:18591666"
FT   SITE            338
FT                   /note="Important for interaction with ssb"
FT                   /evidence="ECO:0000305|PubMed:20018747"
FT   SITE            368
FT                   /note="Interaction with single-stranded DNA"
FT                   /evidence="ECO:0000269|PubMed:23609540"
FT   SITE            371
FT                   /note="Interaction with single-stranded DNA"
FT                   /evidence="ECO:0000269|PubMed:23609540"
FT   MUTAGEN         148
FT                   /note="R->A: Strongly reduced ssb-binding. Reduced
FT                   ssb-dependent nuclease activity."
FT                   /evidence="ECO:0000269|PubMed:18591666"
FT   MUTAGEN         150
FT                   /note="E->A: About 2-fold increased ssb-binding. Weakly
FT                   increased ssb-independent and ssb-dependent nuclease
FT                   activity."
FT                   /evidence="ECO:0000269|PubMed:18591666"
FT   MUTAGEN         181
FT                   /note="H->A: Residual nuclease activity."
FT                   /evidence="ECO:0000269|PubMed:23609540"
FT   MUTAGEN         207
FT                   /note="Y->A: Strongly reduced ssb-binding. Reduced
FT                   ssb-dependent nuclease activity."
FT                   /evidence="ECO:0000269|PubMed:18591666"
FT   MUTAGEN         227
FT                   /note="K->A: 7-fold reduced ssb-binding. Reduced
FT                   ssb-dependent nuclease activity."
FT                   /evidence="ECO:0000269|PubMed:18591666"
FT   MUTAGEN         311
FT                   /note="Q->A: 2-fold reduced ssb-binding. Weakly reduced
FT                   ssb-dependent nuclease activity."
FT                   /evidence="ECO:0000269|PubMed:18591666"
FT   MUTAGEN         316
FT                   /note="R->A: Strongly reduced ssb-binding. Strongly reduced
FT                   ssb-dependent nuclease activity."
FT                   /evidence="ECO:0000269|PubMed:18591666"
FT   MUTAGEN         318
FT                   /note="E->A: About 2-fold increased ssb-binding. No effect
FT                   on ssb-dependent nuclease activity."
FT                   /evidence="ECO:0000269|PubMed:18591666"
FT   MUTAGEN         319
FT                   /note="D->A: 2-fold reduced ssb-binding. No effect on
FT                   ssb-dependent nuclease activity."
FT                   /evidence="ECO:0000269|PubMed:18591666"
FT   MUTAGEN         327
FT                   /note="R->A: No effect on ssb-binding and on ssb-dependent
FT                   nuclease activity."
FT                   /evidence="ECO:0000269|PubMed:18591666"
FT   MUTAGEN         331
FT                   /note="L->A: No effect on ssb-binding and on ssb-dependent
FT                   nuclease activity."
FT                   /evidence="ECO:0000269|PubMed:18591666"
FT   MUTAGEN         338
FT                   /note="R->A: 3-fold reduced ssb-binding. Reduced
FT                   ssb-dependent nuclease activity."
FT                   /evidence="ECO:0000269|PubMed:18591666"
FT   MUTAGEN         448
FT                   /note="Q->A: No effect on ssb-binding and on ssb-dependent
FT                   nuclease activity."
FT                   /evidence="ECO:0000269|PubMed:18591666"
FT   MUTAGEN         452
FT                   /note="Q->A: No effect on ssb-binding and on ssb-dependent
FT                   nuclease activity."
FT                   /evidence="ECO:0000269|PubMed:18591666"
FT   CONFLICT        210..218
FT                   /note="Missing (in Ref. 1; AAA19938)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        225
FT                   /note="Q -> H (in Ref. 1; AAA19938)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        343
FT                   /note="V -> E (in Ref. 1; AAA19938)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        475
FT                   /note="V -> A (in Ref. 1; AAA19938)"
FT                   /evidence="ECO:0000305"
FT   STRAND          10..21
FT                   /evidence="ECO:0007829|PDB:2QXF"
FT   TURN            23..25
FT                   /evidence="ECO:0007829|PDB:2QXF"
FT   STRAND          28..36
FT                   /evidence="ECO:0007829|PDB:2QXF"
FT   STRAND          47..51
FT                   /evidence="ECO:0007829|PDB:2QXF"
FT   HELIX           61..67
FT                   /evidence="ECO:0007829|PDB:2QXF"
FT   HELIX           71..77
FT                   /evidence="ECO:0007829|PDB:2QXF"
FT   HELIX           81..92
FT                   /evidence="ECO:0007829|PDB:2QXF"
FT   STRAND          97..103
FT                   /evidence="ECO:0007829|PDB:2QXF"
FT   TURN            104..107
FT                   /evidence="ECO:0007829|PDB:2QXF"
FT   HELIX           108..118
FT                   /evidence="ECO:0007829|PDB:2QXF"
FT   HELIX           125..127
FT                   /evidence="ECO:0007829|PDB:2QXF"
FT   HELIX           129..131
FT                   /evidence="ECO:0007829|PDB:2QXF"
FT   STRAND          133..136
FT                   /evidence="ECO:0007829|PDB:2QXF"
FT   HELIX           137..147
FT                   /evidence="ECO:0007829|PDB:2QXF"
FT   STRAND          160..162
FT                   /evidence="ECO:0007829|PDB:2QXF"
FT   HELIX           166..172
FT                   /evidence="ECO:0007829|PDB:2QXF"
FT   HELIX           185..200
FT                   /evidence="ECO:0007829|PDB:2QXF"
FT   HELIX           202..210
FT                   /evidence="ECO:0007829|PDB:2QXF"
FT   HELIX           214..219
FT                   /evidence="ECO:0007829|PDB:2QXF"
FT   TURN            223..226
FT                   /evidence="ECO:0007829|PDB:2QXF"
FT   STRAND          229..232
FT                   /evidence="ECO:0007829|PDB:2QXF"
FT   HELIX           234..236
FT                   /evidence="ECO:0007829|PDB:2QXF"
FT   HELIX           238..240
FT                   /evidence="ECO:0007829|PDB:2QXF"
FT   STRAND          243..251
FT                   /evidence="ECO:0007829|PDB:2QXF"
FT   STRAND          258..263
FT                   /evidence="ECO:0007829|PDB:2QXF"
FT   HELIX           269..273
FT                   /evidence="ECO:0007829|PDB:2QXF"
FT   HELIX           276..285
FT                   /evidence="ECO:0007829|PDB:3HL8"
FT   HELIX           287..289
FT                   /evidence="ECO:0007829|PDB:4HCB"
FT   STRAND          298..302
FT                   /evidence="ECO:0007829|PDB:2QXF"
FT   HELIX           303..305
FT                   /evidence="ECO:0007829|PDB:4JRQ"
FT   STRAND          308..311
FT                   /evidence="ECO:0007829|PDB:2QXF"
FT   HELIX           312..314
FT                   /evidence="ECO:0007829|PDB:2QXF"
FT   HELIX           317..323
FT                   /evidence="ECO:0007829|PDB:2QXF"
FT   HELIX           327..339
FT                   /evidence="ECO:0007829|PDB:2QXF"
FT   HELIX           343..346
FT                   /evidence="ECO:0007829|PDB:2QXF"
FT   HELIX           363..365
FT                   /evidence="ECO:0007829|PDB:2QXF"
FT   HELIX           367..369
FT                   /evidence="ECO:0007829|PDB:2QXF"
FT   HELIX           374..385
FT                   /evidence="ECO:0007829|PDB:2QXF"
FT   TURN            388..390
FT                   /evidence="ECO:0007829|PDB:2QXF"
FT   TURN            391..393
FT                   /evidence="ECO:0007829|PDB:4HCB"
FT   HELIX           402..414
FT                   /evidence="ECO:0007829|PDB:2QXF"
FT   HELIX           416..418
FT                   /evidence="ECO:0007829|PDB:2QXF"
FT   HELIX           421..434
FT                   /evidence="ECO:0007829|PDB:2QXF"
FT   HELIX           437..453
FT                   /evidence="ECO:0007829|PDB:2QXF"
FT   TURN            454..456
FT                   /evidence="ECO:0007829|PDB:2QXF"
FT   HELIX           458..473
FT                   /evidence="ECO:0007829|PDB:2QXF"
SQ   SEQUENCE   475 AA;  54501 MW;  A6A02AC17922C313 CRC64;
     MMNDGKQQST FLFHDYETFG THPALDRPAQ FAAIRTDSEF NVIGEPEVFY CKPADDYLPQ
     PGAVLITGIT PQEARAKGEN EAAFAARIHS LFTVPKTCIL GYNNVRFDDE VTRNIFYRNF
     YDPYAWSWQH DNSRWDLLDV MRACYALRPE GINWPENDDG LPSFRLEHLT KANGIEHSNA
     HDAMADVYAT IAMAKLVKTR QPRLFDYLFT HRNKHKLMAL IDVPQMKPLV HVSGMFGAWR
     GNTSWVAPLA WHPENRNAVI MVDLAGDISP LLELDSDTLR ERLYTAKTDL GDNAAVPVKL
     VHINKCPVLA QANTLRPEDA DRLGINRQHC LDNLKILREN PQVREKVVAI FAEAEPFTPS
     DNVDAQLYNG FFSDADRAAM KIVLETEPRN LPALDITFVD KRIEKLLFNY RARNFPGTLD
     YAEQQRWLEH RRQVFTPEFL QGYADELQML VQQYADDKEK VALLKALWQY AEEIV
//