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Calmodulin-sensitive adenylate cyclase (EC 4.6.1.1) (ATP pyrophosphate-lyase) (Adenylyl cyclase) (Anthrax edema toxin adenylate cyclase component) (Edema factor) (EF)

 CYAA_BACAN              Reviewed;         800 AA.
P40136; Q937W4; Q937W5;
01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
01-FEB-1995, sequence version 1.
05-JUL-2017, entry version 161.
RecName: Full=Calmodulin-sensitive adenylate cyclase;
EC=4.6.1.1;
AltName: Full=ATP pyrophosphate-lyase;
AltName: Full=Adenylyl cyclase;
AltName: Full=Anthrax edema toxin adenylate cyclase component;
AltName: Full=Edema factor;
Short=EF;
Flags: Precursor;
Name=cya; OrderedLocusNames=pXO1-122, BXA0141, GBAA_pXO1_0142;
Bacillus anthracis.
Plasmid pXO1.
Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
Bacillus cereus group.
NCBI_TaxID=1392;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=2906312; DOI=10.1016/0378-1119(88)90045-5;
Escuyer V., Duflot E., Sezer O., Danchin A., Mock M.;
"Structural homology between virulence-associated bacterial adenylate
cyclases.";
Gene 71:293-298(1988).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 34-48.
PubMed=3149607; DOI=10.1016/0378-1119(88)90501-X;
Robertson D.L., Tippetts M.T., Leppla S.H.;
"Nucleotide sequence of the Bacillus anthracis edema factor gene
(cya): a calmodulin-dependent adenylate cyclase.";
Gene 73:363-371(1988).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Escuyer V., Duflot E., Mock M., Danchin A.;
"Nucleotide sequences expressing adenylate cyclase from B.anthracis,
proteins having the activity of this adenylate cyclase and biological
uses.";
Patent number EP0366550, 02-MAY-1990.
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=2834337; DOI=10.1128/jb.170.5.2263-2266.1988;
Tippetts M.T., Robertson D.L.;
"Molecular cloning and expression of the Bacillus anthracis edema
factor toxin gene: a calmodulin-dependent adenylate cyclase.";
J. Bacteriol. 170:2263-2266(1988).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Sterne;
PubMed=10515943;
Okinaka R.T., Cloud K., Hampton O., Hoffmaster A.R., Hill K.K.,
Keim P., Koehler T.M., Lamke G., Kumano S., Mahillon J., Manter D.,
Martinez Y., Ricke D., Svensson R., Jackson P.J.;
"Sequence and organization of pXO1, the large Bacillus anthracis
plasmid harboring the anthrax toxin genes.";
J. Bacteriol. 181:6509-6515(1999).
[6]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=Ames / isolate Florida / A2012;
PubMed=12004073; DOI=10.1126/science.1071837;
Read T.D., Salzberg S.L., Pop M., Shumway M.F., Umayam L., Jiang L.,
Holtzapple E., Busch J.D., Smith K.L., Schupp J.M., Solomon D.,
Keim P., Fraser C.M.;
"Comparative genome sequencing for discovery of novel polymorphisms in
Bacillus anthracis.";
Science 296:2028-2033(2002).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Ames ancestor;
PubMed=18952800; DOI=10.1128/JB.01347-08;
Ravel J., Jiang L., Stanley S.T., Wilson M.R., Decker R.S., Read T.D.,
Worsham P., Keim P.S., Salzberg S.L., Fraser-Liggett C.M., Rasko D.A.;
"The complete genome sequence of Bacillus anthracis Ames 'Ancestor'.";
J. Bacteriol. 191:445-446(2009).
[8]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-783.
STRAIN=Carbosap, and Ferrara;
PubMed=12067380; DOI=10.1046/j.1365-2672.2002.01660.x;
Adone R., Pasquali P., La Rosa G., Marianelli C., Muscillo M.,
Fasanella A., Francia M., Ciuchini F.;
"Sequence analysis of the genes encoding for the major virulence
factors of Bacillus anthracis vaccine strain 'Carbosap'.";
J. Appl. Microbiol. 93:117-121(2002).
[9]
CHARACTERIZATION.
STRAIN=Sterne;
PubMed=9398214; DOI=10.1021/bi971661k;
Wang X.-M., Wattiez R., Mock M., Falmagne P., Ruysschaert J.-M.,
Cabiaux V.;
"Structure and interaction of PA63 and EF (edema toxin) of Bacillus
anthracis with lipid membrane.";
Biochemistry 36:14906-14913(1997).
[10]
CHARACTERIZATION.
STRAIN=Sterne;
PubMed=11207582; DOI=10.1046/j.1462-5822.2000.00057.x;
Guidi-Rontani C., Weber-Levy M., Mock M., Cabiaux V.;
"Translocation of Bacillus anthracis lethal and oedema factors across
endosome membranes.";
Cell. Microbiol. 2:259-264(2000).
[11]
CHARACTERIZATION OF CALMODULIN-BINDING DOMAIN.
PubMed=2114169; DOI=10.1021/bi00472a024;
Labruyere E., Mock M., Ladant D., Michelson S., Gilles A.-M.,
Laoide B., Barzu O.;
"Characterization of ATP and calmodulin-binding properties of a
truncated form of Bacillus anthracis adenylate cyclase.";
Biochemistry 29:4922-4928(1990).
[12]
EFFECT ON SPORE GERMINATION.
STRAIN=Sterne;
PubMed=11737637; DOI=10.1046/j.1365-2958.2001.02695.x;
Guidi-Rontani C., Levy M., Ohayon H., Mock M.;
"Fate of germinated Bacillus anthracis spores in primary murine
macrophages.";
Mol. Microbiol. 42:931-938(2001).
[13]
INHIBITION BY QUINAZOLINE COMPOUNDS.
PubMed=12676933; DOI=10.1074/jbc.M301232200;
Soelaiman S., Wei B.Q., Bergson P., Lee Y.-S., Shen Y., Mrksich M.,
Shoichet B.K., Tang W.-J.;
"Structure-based inhibitor discovery against adenylyl cyclase toxins
from pathogenic bacteria that cause anthrax and whooping cough.";
J. Biol. Chem. 278:25990-25997(2003).
[14]
MUTAGENESIS OF LYS-346; LYS-353 AND GLU-436.
STRAIN=SRI-1;
PubMed=2108958;
Xia Z., Storm D.R.;
"A-type ATP binding consensus sequences are critical for the catalytic
activity of the calmodulin-sensitive adenylyl cyclase from Bacillus
anthracis.";
J. Biol. Chem. 265:6517-6520(1990).
[15]
MUTAGENESIS OF LYS-346.
STRAIN=Sterne;
PubMed=1900429; DOI=10.1021/bi00224a008;
Labruyere E., Mock M., Surewicz W.K., Mantsch H.H., Rose T.,
Munier H., Sarfati R.S., Barzu O.;
"Structural and ligand-binding properties of a truncated form of
Bacillus anthracis adenylate cyclase and of a catalytically inactive
variant in which glutamine substitutes for lysine-346.";
Biochemistry 30:2619-2624(1991).
[16]
MUTAGENESIS OF VAL-169; TYR-170; TYR-171; GLU-172; ILE-173; GLY-174
AND LYS-175.
PubMed=11553601; DOI=10.1128/IAI.69.10.6532-6536.2001;
Kumar P., Ahuja N., Bhatnagar R.;
"Purification of anthrax edema factor from Escherichia coli and
identification of residues required for binding to anthrax protective
antigen.";
Infect. Immun. 69:6532-6536(2001).
[17]
MUTAGENESIS OF ARG-329; GLU-443; ASP-491 AND ASP-493.
PubMed=10926933; DOI=10.1074/jbc.M004778200;
Drum C.L., Yan S.-Z., Sarac R., Mabuchi Y., Beckingham K., Bohm A.,
Grabarek Z., Tang W.-J.;
"An extended conformation of calmodulin induces interactions between
the structural domains of adenylyl cyclase from Bacillus anthracis to
promote catalysis.";
J. Biol. Chem. 275:36334-36340(2000).
[18]
X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS), AND MUTAGENESIS.
PubMed=11807546; DOI=10.1038/415396a;
Drum C.L., Yan S.-Z., Bard J., Shen Y.-Q., Lu D., Soelaiman S.,
Grabarek Z., Bohm A., Tang W.-J.;
"Structural basis for the activation of anthrax adenylyl cyclase
exotoxin by calmodulin.";
Nature 415:396-402(2002).
[19]
REVIEW.
PubMed=8418825;
Danchin A.;
"Phylogeny of adenylyl cyclases.";
Adv. Second Messenger Phosphoprotein Res. 27:109-162(1993).
[20]
REVIEW.
PubMed=11544370; DOI=10.1146/annurev.micro.55.1.647;
Mock M., Fouet A.;
"Anthrax.";
Annu. Rev. Microbiol. 55:647-671(2001).
-!- FUNCTION: One of the three proteins composing the anthrax toxin,
the agent which infects many mammalian species and that may cause
death. EF is a calmodulin-dependent adenylyl cyclase that, when
associated with PA, causes edema. EF is not toxic by itself and it
is required for the survival of germinated spores within
macrophages at the early stages of infection. Provokes dramatic
elevation of intracellular cAMP levels in the host.
-!- CATALYTIC ACTIVITY: ATP = 3',5'-cyclic AMP + diphosphate.
-!- COFACTOR:
Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
-!- ENZYME REGULATION: It has an absolute requirement for host
calmodulin for its activation. Inhibited by ethyl 5-
aminopyrazolo[1,5-a]quinazoline-3-carboxylate.
-!- SUBUNIT: Anthrax toxins are composed of three distinct proteins, a
protective antigen (PA), a lethal factor (LF) and an edema factor
(EF). None of these is toxic by itself. PA+LF forms the lethal
toxin (LeTx); PA+EF forms the edema toxin (EdTx). EF probably
forms oligomers as part of the translocation machinery, formed by
a heterocomplex of PA63 monomers and EF subunits, and it is
functional as a monomer in the host cell.
-!- INTERACTION:
P62155:calm2 (xeno); NbExp=2; IntAct=EBI-457011, EBI-397568;
P62158:CALM3 (xeno); NbExp=8; IntAct=EBI-457011, EBI-397435;
-!- SUBCELLULAR LOCATION: Secreted.
-!- DOMAIN: The N-terminal region contains the residues responsible
for binding to PA63. The C-terminal region contains the
calmodulin-dependent activation domain and the catalytic site.
This region is composed of three globular domains: CA, CB and a
helical domain connected to CA by a linker. The active site lies
at the interface of CA and CB. The metal ion is coordinated by
residues from CA; calmodulin probably binds in a multistep fashion
first to residues in CA and then to residues present in the linker
and the helical domain.
-!- DOMAIN: The PA-binding region is found in both B.anthracis EF and
LF.
-!- MISCELLANEOUS: EF binds to the heptamer formed by cleaved PA on
the host cell membrane. This step is followed by internalization
of the hetero-oligomeric complex by receptor-mediated endocytosis.
EF requires passage through an acidic vesicle for activity. At
acidic pH, the pore is inserted into the membrane, allowing
translocation of EF, which probably contributes actively to its
own insertion into the membrane. EF remains associated to the
vesicle membrane after translocation to the cytosol, with the
catalytic domains being exposed on the cytoplasmic face.
-!- SIMILARITY: Belongs to the adenylyl cyclase class-2 family.
{ECO:0000305}.
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EMBL; M23179; AAA22374.1; -; Genomic_DNA.
EMBL; M24074; AAA79215.1; -; Genomic_DNA.
EMBL; A07289; CAA00652.1; ALT_SEQ; Unassigned_DNA.
EMBL; AF065404; AAD32426.1; -; Genomic_DNA.
EMBL; AE011190; AAM26089.1; -; Genomic_DNA.
EMBL; AE017336; AAT28883.2; -; Genomic_DNA.
EMBL; AJ413930; CAC93924.1; -; Genomic_DNA.
EMBL; AJ413931; CAC93925.1; -; Genomic_DNA.
PIR; B59106; B59106.
PIR; JS0029; JS0029.
RefSeq; NP_052818.1; NC_001496.1.
RefSeq; WP_000197748.1; NZ_MVKJ01000025.1.
PDB; 1K8T; X-ray; 2.60 A; A=291-800.
PDB; 1K90; X-ray; 2.75 A; A/B/C=291-800.
PDB; 1K93; X-ray; 2.95 A; A/B/C=291-800.
PDB; 1LVC; X-ray; 3.60 A; A/B/C=291-800.
PDB; 1PK0; X-ray; 3.30 A; A/B/C=292-798.
PDB; 1S26; X-ray; 3.00 A; A/B/C=291-800.
PDB; 1SK6; X-ray; 3.20 A; A/B/C=291-800.
PDB; 1XFU; X-ray; 3.35 A; A/B/C/D/E/F=64-800.
PDB; 1XFV; X-ray; 3.35 A; A/B/C/D/E/F=33-800.
PDB; 1XFW; X-ray; 3.40 A; A/B/C/D/E/F=33-800.
PDB; 1XFX; X-ray; 3.20 A; A/B/C/D/E/F=33-800.
PDB; 1XFY; X-ray; 3.30 A; A/B/C/D/E/F=33-800.
PDB; 1XFZ; X-ray; 3.25 A; A/B/C/D/E/F=33-800.
PDB; 1Y0V; X-ray; 3.60 A; A/B/C/D/E/F=33-800.
PDBsum; 1K8T; -.
PDBsum; 1K90; -.
PDBsum; 1K93; -.
PDBsum; 1LVC; -.
PDBsum; 1PK0; -.
PDBsum; 1S26; -.
PDBsum; 1SK6; -.
PDBsum; 1XFU; -.
PDBsum; 1XFV; -.
PDBsum; 1XFW; -.
PDBsum; 1XFX; -.
PDBsum; 1XFY; -.
PDBsum; 1XFZ; -.
PDBsum; 1Y0V; -.
DisProt; DP00395; -.
ProteinModelPortal; P40136; -.
SMR; P40136; -.
DIP; DIP-31055N; -.
IntAct; P40136; 3.
BindingDB; P40136; -.
ChEMBL; CHEMBL5396; -.
PRIDE; P40136; -.
EnsemblBacteria; AAM26089; AAM26089; BX_A0142.
EnsemblBacteria; AAT28883; AAT28883; GBAA_pXO1_0142.
GeneID; 3361726; -.
KEGG; bar:GBAA_pXO1_0142; -.
HOGENOM; HOG000034573; -.
KO; K11029; -.
Reactome; R-HSA-5210891; Uptake and function of anthrax toxins.
EvolutionaryTrace; P40136; -.
PRO; PR:P40136; -.
Proteomes; UP000000594; Plasmid pXO1.
GO; GO:1902494; C:catalytic complex; IMP:CAFA.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0010008; C:endosome membrane; TAS:Reactome.
GO; GO:0005576; C:extracellular region; TAS:Reactome.
GO; GO:0005886; C:plasma membrane; TAS:Reactome.
GO; GO:0004016; F:adenylate cyclase activity; IMP:CAFA.
GO; GO:0005524; F:ATP binding; IMP:CAFA.
GO; GO:0008294; F:calcium- and calmodulin-responsive adenylate cyclase activity; IDA:CACAO.
GO; GO:0005516; F:calmodulin binding; IPI:CAFA.
GO; GO:0046872; F:metal ion binding; IMP:CAFA.
GO; GO:0008237; F:metallopeptidase activity; IEA:InterPro.
GO; GO:0052007; P:biosynthesis by symbiont of substance in host; TAS:Reactome.
GO; GO:0006171; P:cAMP biosynthetic process; IMP:CAFA.
GO; GO:0009405; P:pathogenesis; IEA:UniProtKB-KW.
Gene3D; 3.40.390.10; -; 1.
Gene3D; 3.90.1760.10; -; 1.
InterPro; IPR035099; Anthrax_toxin_C-terminal.
InterPro; IPR005165; Anthrax_toxin_edema_cen.
InterPro; IPR003541; Anthrax_toxin_lethal/edema.
InterPro; IPR014781; Anthrax_toxin_lethal/edema_N/C.
InterPro; IPR024079; MetalloPept_cat_dom.
Pfam; PF03497; Anthrax_toxA; 1.
Pfam; PF07737; ATLF; 1.
PRINTS; PR01392; ANTHRAXTOXNA.
SUPFAM; SSF81298; SSF81298; 1.
1: Evidence at protein level;
3D-structure; ATP-binding; Calcium; Calmodulin-binding;
cAMP biosynthesis; Complete proteome; Direct protein sequencing;
Lyase; Magnesium; Metal-binding; Nucleotide-binding; Plasmid;
Reference proteome; Secreted; Signal; Toxin; Virulence.
SIGNAL 1 33 {ECO:0000269|PubMed:3149607}.
CHAIN 34 800 Calmodulin-sensitive adenylate cyclase.
/FTId=PRO_0000001317.
REGION 34 290 Interaction with protective antigen.
REGION 294 349 Catalytic CA1.
REGION 350 489 Catalytic CB.
REGION 490 622 Catalytic CA2.
REGION 623 800 Interaction with calmodulin.
ACT_SITE 351 351 Proton acceptor.
METAL 491 491 Magnesium.
METAL 493 493 Magnesium.
MUTAGEN 169 169 V->A: No effect.
{ECO:0000269|PubMed:11553601}.
MUTAGEN 170 170 Y->A: Loss of cytotoxicity due to
inability to bind PA.
{ECO:0000269|PubMed:11553601}.
MUTAGEN 171 171 Y->A: Loss of cytotoxicity due to
inability to bind PA.
{ECO:0000269|PubMed:11553601}.
MUTAGEN 172 172 E->A: No effect.
{ECO:0000269|PubMed:11553601}.
MUTAGEN 173 173 I->A: Loss of cytotoxicity due to
inability to bind PA.
{ECO:0000269|PubMed:11553601}.
MUTAGEN 174 174 G->A: No effect.
{ECO:0000269|PubMed:11553601}.
MUTAGEN 175 175 K->A: Loss of cytotoxicity due to
inability to bind PA.
{ECO:0000269|PubMed:11553601}.
MUTAGEN 329 329 R->M: Great decrease in activity.
{ECO:0000269|PubMed:10926933}.
MUTAGEN 346 346 K->M,R: Loss of activity.
{ECO:0000269|PubMed:1900429,
ECO:0000269|PubMed:2108958}.
MUTAGEN 346 346 K->Q: Loss of activity due to inability
to bind the substrate.
{ECO:0000269|PubMed:1900429,
ECO:0000269|PubMed:2108958}.
MUTAGEN 353 353 K->M,R,A: Loss of activity.
{ECO:0000269|PubMed:2108958}.
MUTAGEN 436 436 E->Q: Decreases activity.
{ECO:0000269|PubMed:2108958}.
MUTAGEN 443 443 E->Q: Decreases activity.
{ECO:0000269|PubMed:10926933}.
MUTAGEN 491 491 D->N: Great decrease in activity.
{ECO:0000269|PubMed:10926933}.
MUTAGEN 493 493 D->N: Great decrease in activity.
{ECO:0000269|PubMed:10926933}.
MUTAGEN 523 523 L->A: Little effect on activation by
calmodulin.
{ECO:0000269|PubMed:11807546}.
MUTAGEN 525 525 K->A: Great decrease in calmodulin
binding. {ECO:0000269|PubMed:11807546}.
MUTAGEN 526 526 Q->A: Little effect on activation by
calmodulin.
{ECO:0000269|PubMed:11807546}.
MUTAGEN 529 529 V->A: Little effect on activation by
calmodulin.
{ECO:0000269|PubMed:11807546}.
MUTAGEN 577 577 H->N,D: Loss of function.
{ECO:0000269|PubMed:11807546}.
MUTAGEN 583 583 N->A: Decreases activity.
{ECO:0000269|PubMed:11807546}.
MUTAGEN 583 583 N->Q,H: Loss of function.
{ECO:0000269|PubMed:11807546}.
MUTAGEN 588 588 E->A: Loss of function.
{ECO:0000269|PubMed:11807546}.
MUTAGEN 590 590 D->A: Decreases activity.
{ECO:0000269|PubMed:11807546}.
MUTAGEN 639 639 N->A: Decreases catalysis rate.
{ECO:0000269|PubMed:11807546}.
MUTAGEN 647 647 D->A: Decreases activity due to reduced
activation by calmodulin.
{ECO:0000269|PubMed:11807546}.
CONFLICT 350 350 V -> E (in Ref. 2; AAA79215).
{ECO:0000305}.
CONFLICT 510 510 Q -> T (in Ref. 2; AA sequence).
{ECO:0000305}.
CONFLICT 512 513 EW -> RM (in Ref. 2; AA sequence).
{ECO:0000305}.
CONFLICT 760 760 V -> L (in Ref. 3; CAA00652).
{ECO:0000305}.
STRAND 67 69 {ECO:0000244|PDB:1XFX}.
HELIX 76 86 {ECO:0000244|PDB:1XFX}.
HELIX 91 99 {ECO:0000244|PDB:1XFX}.
STRAND 103 109 {ECO:0000244|PDB:1XFX}.
TURN 111 114 {ECO:0000244|PDB:1XFY}.
STRAND 119 122 {ECO:0000244|PDB:1XFX}.
STRAND 130 132 {ECO:0000244|PDB:1XFX}.
HELIX 137 139 {ECO:0000244|PDB:1XFX}.
STRAND 141 144 {ECO:0000244|PDB:1XFX}.
STRAND 147 149 {ECO:0000244|PDB:1XFX}.
STRAND 151 155 {ECO:0000244|PDB:1XFX}.
TURN 163 168 {ECO:0000244|PDB:1XFX}.
HELIX 169 176 {ECO:0000244|PDB:1XFX}.
TURN 177 182 {ECO:0000244|PDB:1XFX}.
STRAND 183 188 {ECO:0000244|PDB:1XFX}.
HELIX 192 197 {ECO:0000244|PDB:1XFX}.
TURN 198 202 {ECO:0000244|PDB:1XFX}.
STRAND 203 206 {ECO:0000244|PDB:1XFX}.
TURN 211 213 {ECO:0000244|PDB:1XFX}.
STRAND 215 217 {ECO:0000244|PDB:1XFX}.
STRAND 226 229 {ECO:0000244|PDB:1XFX}.
TURN 230 235 {ECO:0000244|PDB:1XFX}.
HELIX 236 249 {ECO:0000244|PDB:1XFX}.
STRAND 250 252 {ECO:0000244|PDB:1XFX}.
HELIX 255 259 {ECO:0000244|PDB:1XFX}.
STRAND 260 262 {ECO:0000244|PDB:1XFX}.
HELIX 263 273 {ECO:0000244|PDB:1XFX}.
HELIX 275 290 {ECO:0000244|PDB:1XFX}.
STRAND 296 298 {ECO:0000244|PDB:1SK6}.
HELIX 299 305 {ECO:0000244|PDB:1K8T}.
HELIX 309 322 {ECO:0000244|PDB:1K8T}.
STRAND 324 328 {ECO:0000244|PDB:1K8T}.
TURN 333 335 {ECO:0000244|PDB:1K8T}.
HELIX 336 340 {ECO:0000244|PDB:1K8T}.
STRAND 356 360 {ECO:0000244|PDB:1K8T}.
STRAND 365 367 {ECO:0000244|PDB:1K8T}.
HELIX 368 370 {ECO:0000244|PDB:1K8T}.
TURN 372 375 {ECO:0000244|PDB:1K90}.
HELIX 377 393 {ECO:0000244|PDB:1K8T}.
TURN 394 396 {ECO:0000244|PDB:1K8T}.
STRAND 397 402 {ECO:0000244|PDB:1K8T}.
HELIX 407 415 {ECO:0000244|PDB:1K8T}.
STRAND 424 427 {ECO:0000244|PDB:1K8T}.
STRAND 430 436 {ECO:0000244|PDB:1K8T}.
STRAND 440 450 {ECO:0000244|PDB:1K8T}.
STRAND 452 457 {ECO:0000244|PDB:1K8T}.
TURN 464 466 {ECO:0000244|PDB:1XFZ}.
STRAND 471 473 {ECO:0000244|PDB:1K90}.
STRAND 475 489 {ECO:0000244|PDB:1K8T}.
STRAND 494 500 {ECO:0000244|PDB:1K8T}.
HELIX 501 507 {ECO:0000244|PDB:1K8T}.
HELIX 510 516 {ECO:0000244|PDB:1K8T}.
STRAND 517 521 {ECO:0000244|PDB:1K8T}.
HELIX 527 535 {ECO:0000244|PDB:1K8T}.
TURN 536 538 {ECO:0000244|PDB:1XFX}.
STRAND 541 543 {ECO:0000244|PDB:1K93}.
STRAND 544 546 {ECO:0000244|PDB:1K90}.
STRAND 547 549 {ECO:0000244|PDB:1K93}.
HELIX 551 565 {ECO:0000244|PDB:1K8T}.
TURN 566 568 {ECO:0000244|PDB:1K8T}.
HELIX 580 582 {ECO:0000244|PDB:1K90}.
STRAND 593 596 {ECO:0000244|PDB:1K8T}.
STRAND 598 600 {ECO:0000244|PDB:1XFU}.
STRAND 602 607 {ECO:0000244|PDB:1K8T}.
HELIX 608 618 {ECO:0000244|PDB:1K8T}.
HELIX 620 622 {ECO:0000244|PDB:1K8T}.
TURN 630 633 {ECO:0000244|PDB:1K90}.
STRAND 634 636 {ECO:0000244|PDB:1XFV}.
TURN 637 639 {ECO:0000244|PDB:1K90}.
TURN 648 650 {ECO:0000244|PDB:1K8T}.
TURN 652 655 {ECO:0000244|PDB:1K90}.
HELIX 660 674 {ECO:0000244|PDB:1K8T}.
STRAND 679 681 {ECO:0000244|PDB:1K90}.
STRAND 683 685 {ECO:0000244|PDB:1PK0}.
HELIX 687 706 {ECO:0000244|PDB:1K8T}.
HELIX 707 710 {ECO:0000244|PDB:1K8T}.
HELIX 714 737 {ECO:0000244|PDB:1K8T}.
HELIX 743 767 {ECO:0000244|PDB:1K8T}.
HELIX 771 777 {ECO:0000244|PDB:1K8T}.
STRAND 778 780 {ECO:0000244|PDB:1SK6}.
HELIX 786 798 {ECO:0000244|PDB:1K8T}.
SEQUENCE 800 AA; 92478 MW; F4F7EB485DF4C5A6 CRC64;
MTRNKFIPNK FSIISFSVLL FAISSSQAIE VNAMNEHYTE SDIKRNHKTE KNKTEKEKFK
DSINNLVKTE FTNETLDKIQ QTQDLLKKIP KDVLEIYSEL GGEIYFTDID LVEHKELQDL
SEEEKNSMNS RGEKVPFASR FVFEKKRETP KLIINIKDYA INSEQSKEVY YEIGKGISLD
IISKDKSLDP EFLNLIKSLS DDSDSSDLLF SQKFKEKLEL NNKSIDINFI KENLTEFQHA
FSLAFSYYFA PDHRTVLELY APDMFEYMNK LEKGGFEKIS ESLKKEGVEK DRIDVLKGEK
ALKASGLVPE HADAFKKIAR ELNTYILFRP VNKLATNLIK SGVATKGLNV HGKSSDWGPV
AGYIPFDQDL SKKHGQQLAV EKGNLENKKS ITEHEGEIGK IPLKLDHLRI EELKENGIIL
KGKKEIDNGK KYYLLESNNQ VYEFRISDEN NEVQYKTKEG KITVLGEKFN WRNIEVMAKN
VEGVLKPLTA DYDLFALAPS LTEIKKQIPQ KEWDKVVNTP NSLEKQKGVT NLLIKYGIER
KPDSTKGTLS NWQKQMLDRL NEAVKYTGYT GGDVVNHGTE QDNEEFPEKD NEIFIINPEG
EFILTKNWEM TGRFIEKNIT GKDYLYYFNR SYNKIAPGNK AYIEWTDPIT KAKINTIPTS
AEFIKNLSSI RRSSNVGVYK DSGDKDEFAK KESVKKIAGY LSDYYNSANH IFSQEKKRKI
SIFRGIQAYN EIENVLKSKQ IAPEYKNYFQ YLKERITNQV QLLLTHQKSN IEFKLLYKQL
NFTENETDNF EVFQKIIDEK


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