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Fatty acid synthase subunit alpha (EC 2.3.1.86) [Includes: Acyl carrier; 3-oxoacyl-[acyl-carrier-protein] reductase (EC 1.1.1.100) (Beta-ketoacyl reductase); 3-oxoacyl-[acyl-carrier-protein] synthase (EC 2.3.1.41) (Beta-ketoacyl synthase)]

 FAS2_YEAST              Reviewed;        1887 AA.
P19097; D6W3D9; Q12533;
01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
15-MAY-2002, sequence version 2.
27-SEP-2017, entry version 189.
RecName: Full=Fatty acid synthase subunit alpha;
EC=2.3.1.86;
Includes:
RecName: Full=Acyl carrier;
Includes:
RecName: Full=3-oxoacyl-[acyl-carrier-protein] reductase;
EC=1.1.1.100;
AltName: Full=Beta-ketoacyl reductase;
Includes:
RecName: Full=3-oxoacyl-[acyl-carrier-protein] synthase;
EC=2.3.1.41;
AltName: Full=Beta-ketoacyl synthase;
Name=FAS2; OrderedLocusNames=YPL231W; ORFNames=P1409;
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
NCBI_TaxID=559292;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=2900835;
Mohamed A.H., Chirala S.S., Mody N.H., Huang W.Y., Wakil S.J.;
"Primary structure of the multifunctional alpha subunit protein of
yeast fatty acid synthase derived from FAS2 gene sequence.";
J. Biol. Chem. 263:12315-12325(1988).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ATCC 26786 / X2180-1A;
Schueller H.-J.;
Submitted (JAN-1994) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=9169875;
Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W.,
Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V.,
Botstein D., Bowman S., Brueckner M., Carpenter J., Cherry J.M.,
Chung E., Churcher C.M., Coster F., Davis K., Davis R.W.,
Dietrich F.S., Delius H., DiPaolo T., Dubois E., Duesterhoeft A.,
Duncan M., Floeth M., Fortin N., Friesen J.D., Fritz C., Goffeau A.,
Hall J., Hebling U., Heumann K., Hilbert H., Hillier L.W.,
Hunicke-Smith S., Hyman R.W., Johnston M., Kalman S., Kleine K.,
Komp C., Kurdi O., Lashkari D., Lew H., Lin A., Lin D., Louis E.J.,
Marathe R., Messenguy F., Mewes H.-W., Mirtipati S., Moestl D.,
Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D.,
Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S.,
Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B.,
Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A.,
Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V.,
Wambutt R., Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W.,
Zollner A., Vo D.H., Hani J.;
"The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI.";
Nature 387:103-105(1997).
[4]
GENOME REANNOTATION.
STRAIN=ATCC 204508 / S288c;
PubMed=24374639; DOI=10.1534/g3.113.008995;
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M.,
Cherry J.M.;
"The reference genome sequence of Saccharomyces cerevisiae: Then and
now.";
G3 (Bethesda) 4:389-398(2014).
[5]
MUTAGENESIS OF GLY-1250.
STRAIN=ATCC 204508 / S288c;
PubMed=8041367; DOI=10.1007/BF00280191;
Inokoshi J., Tomoda H., Hashimoto H., Watanabe A., Takeshima H.,
Omura S.;
"Cerulenin-resistant mutants of Saccharomyces cerevisiae with an
altered fatty acid synthase gene.";
Mol. Gen. Genet. 244:90-96(1994).
[6]
LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
PubMed=14562106; DOI=10.1038/nature02046;
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A.,
Dephoure N., O'Shea E.K., Weissman J.S.;
"Global analysis of protein expression in yeast.";
Nature 425:737-741(2003).
[7]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-50, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
STRAIN=YAL6B;
PubMed=15665377; DOI=10.1074/mcp.M400219-MCP200;
Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J.,
Mann M., Jensen O.N.;
"Quantitative phosphoproteomics applied to the yeast pheromone
signaling pathway.";
Mol. Cell. Proteomics 4:310-327(2005).
[8]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-958 AND SER-1440, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
STRAIN=ADR376;
PubMed=17330950; DOI=10.1021/pr060559j;
Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
Elias J.E., Gygi S.P.;
"Large-scale phosphorylation analysis of alpha-factor-arrested
Saccharomyces cerevisiae.";
J. Proteome Res. 6:1190-1197(2007).
[9]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
STRAIN=ATCC 76625 / YPH499;
PubMed=17761666; DOI=10.1074/mcp.M700098-MCP200;
Reinders J., Wagner K., Zahedi R.P., Stojanovski D., Eyrich B.,
van der Laan M., Rehling P., Sickmann A., Pfanner N., Meisinger C.;
"Profiling phosphoproteins of yeast mitochondria reveals a role of
phosphorylation in assembly of the ATP synthase.";
Mol. Cell. Proteomics 6:1896-1906(2007).
[10]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=18407956; DOI=10.1074/mcp.M700468-MCP200;
Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
"A multidimensional chromatography technology for in-depth
phosphoproteome analysis.";
Mol. Cell. Proteomics 7:1389-1396(2008).
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-523, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19779198; DOI=10.1126/science.1172867;
Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
"Global analysis of Cdk1 substrate phosphorylation sites provides
insights into evolution.";
Science 325:1682-1686(2009).
[12]
UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-37, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22106047; DOI=10.1002/pmic.201100166;
Starita L.M., Lo R.S., Eng J.K., von Haller P.D., Fields S.;
"Sites of ubiquitin attachment in Saccharomyces cerevisiae.";
Proteomics 12:236-240(2012).
[13]
X-RAY CRYSTALLOGRAPHY (4.0 ANGSTROMS) OF 671-1744 IN COMPLEX WITH
FAS1, AND SUBUNIT.
PubMed=17448991; DOI=10.1016/j.cell.2007.03.013;
Lomakin I.B., Xiong Y., Steitz T.A.;
"The crystal structure of yeast fatty acid synthase, a cellular
machine with eight active sites working together.";
Cell 129:319-332(2007).
[14]
X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS) IN COMPLEX WITH FAS1, SUBUNIT,
AND PHOSPHOPANTETHEINYLATION AT SER-180.
PubMed=17431182; DOI=10.1126/science.1138249;
Leibundgut M., Jenni S., Frick C., Ban N.;
"Structural basis for substrate delivery by acyl carrier protein in
the yeast fatty acid synthase.";
Science 316:288-290(2007).
[15]
X-RAY CRYSTALLOGRAPHY (4.0 ANGSTROMS) IN COMPLEX WITH FAS1 AND THE
INHIBITOR CERULENIN, AND ENZYME REGULATION.
PubMed=18725634; DOI=10.1073/pnas.0805827105;
Johansson P., Wiltschi B., Kumari P., Kessler B., Vonrhein C.,
Vonck J., Oesterhelt D., Grininger M.;
"Inhibition of the fungal fatty acid synthase type I multienzyme
complex.";
Proc. Natl. Acad. Sci. U.S.A. 105:12803-12808(2008).
[16]
X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 1766-1887 IN COMPLEX WITH
FAS1 AND ACETYL-COA, MUTAGENESIS OF VAL-1769; GLY-1770; VAL-1771;
ASP-1772; VAL-1773; GLU-1774; ARG-1841; VAL-1879 AND VAL-1881, AND
IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=19679086; DOI=10.1016/j.str.2009.06.014;
Johansson P., Mulinacci B., Koestler C., Vollrath R., Oesterhelt D.,
Grininger M.;
"Multimeric options for the auto-activation of the Saccharomyces
cerevisiae FAS type I megasynthase.";
Structure 17:1063-1074(2009).
-!- FUNCTION: Fatty acid synthetase catalyzes the formation of long-
chain fatty acids from acetyl-CoA, malonyl-CoA and NADPH. The
alpha subunit contains domains for: acyl carrier protein, 3-
oxoacyl-[acyl-carrier-protein] reductase, and 3-oxoacyl-[acyl-
carrier-protein] synthase. This subunit coordinates the binding of
the six beta subunits to the enzyme complex.
-!- CATALYTIC ACTIVITY: Acetyl-CoA + n malonyl-CoA + 2n NADPH = long-
chain-acyl-CoA + n CoA + n CO(2) + 2n NADP(+).
-!- CATALYTIC ACTIVITY: Acyl-[acyl-carrier-protein] + malonyl-[acyl-
carrier-protein] = 3-oxoacyl-[acyl-carrier-protein] + CO(2) +
[acyl-carrier-protein].
-!- CATALYTIC ACTIVITY: (3R)-3-hydroxyacyl-[acyl-carrier-protein] +
NADP(+) = 3-oxoacyl-[acyl-carrier-protein] + NADPH.
-!- ENZYME REGULATION: Inhibited by cerulenin by covalent binding to
active site of the ketoacyl synthase (KS) region.
{ECO:0000269|PubMed:18725634}.
-!- SUBUNIT: [Alpha(6)beta(6)] hexamers of two multifunctional
subunits (alpha and beta). {ECO:0000269|PubMed:17431182,
ECO:0000269|PubMed:17448991, ECO:0000269|PubMed:18725634,
ECO:0000269|PubMed:19679086}.
-!- INTERACTION:
P07149:FAS1; NbExp=4; IntAct=EBI-6806, EBI-6795;
-!- PTM: 4'-phosphopantetheine is transferred from CoA to a specific
serine of the Acyl carrier domain by the C-terminal PPT domain.
This modification is essential for activity because fatty acids
are bound in thioester linkage to the sulfhydryl of the prosthetic
group.
-!- MISCELLANEOUS: Present with 17000 molecules/cell in log phase SD
medium. {ECO:0000269|PubMed:14562106}.
-!- SIMILARITY: Belongs to the fungal fatty acid synthetase subunit
alpha family. {ECO:0000305}.
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EMBL; J03936; AAA34601.1; -; Genomic_DNA.
EMBL; X76890; CAA54218.1; -; Genomic_DNA.
EMBL; X94561; CAA64256.1; -; Genomic_DNA.
EMBL; Z73586; CAA97947.1; -; Genomic_DNA.
EMBL; Z73587; CAA97948.1; -; Genomic_DNA.
EMBL; BK006949; DAA11205.1; -; Genomic_DNA.
PIR; S61703; S61703.
RefSeq; NP_015093.1; NM_001184045.1.
PDB; 2ML8; NMR; -; A=138-302.
PDB; 2PFF; X-ray; 4.00 A; A/D/G=671-1744.
PDB; 2UV8; X-ray; 3.10 A; A/B/C=1-1887.
PDB; 2VKZ; X-ray; 4.00 A; A/B/C=1-1887.
PDB; 2WAS; X-ray; 1.90 A; A/B/C/D/E/F=1766-1887.
PDB; 2WAT; X-ray; 2.20 A; A/B/C/D/E/F=1766-1887.
PDB; 3HMJ; X-ray; 4.00 A; A/B/C=1-1887.
PDBsum; 2ML8; -.
PDBsum; 2PFF; -.
PDBsum; 2UV8; -.
PDBsum; 2VKZ; -.
PDBsum; 2WAS; -.
PDBsum; 2WAT; -.
PDBsum; 3HMJ; -.
ProteinModelPortal; P19097; -.
SMR; P19097; -.
BioGrid; 35931; 372.
DIP; DIP-960N; -.
IntAct; P19097; 32.
MINT; MINT-659193; -.
STRING; 4932.YPL231W; -.
iPTMnet; P19097; -.
MaxQB; P19097; -.
PRIDE; P19097; -.
TopDownProteomics; P19097; -.
EnsemblFungi; YPL231W; YPL231W; YPL231W.
GeneID; 855845; -.
KEGG; sce:YPL231W; -.
EuPathDB; FungiDB:YPL231W; -.
SGD; S000006152; FAS2.
HOGENOM; HOG000177974; -.
InParanoid; P19097; -.
KO; K00667; -.
OMA; MMDPAAI; -.
OrthoDB; EOG092C010Q; -.
BioCyc; MetaCyc:YPL231W-MONOMER; -.
BioCyc; YEAST:YPL231W-MONOMER; -.
SABIO-RK; P19097; -.
EvolutionaryTrace; P19097; -.
PRO; PR:P19097; -.
Proteomes; UP000002311; Chromosome XVI.
GO; GO:0005829; C:cytosol; IDA:SGD.
GO; GO:0005835; C:fatty acid synthase complex; IDA:SGD.
GO; GO:0102131; F:3-oxo-glutaryl-[acp] methyl ester reductase activity; IEA:UniProtKB-EC.
GO; GO:0102132; F:3-oxo-pimeloyl-[acp] methyl ester reductase activity; IEA:UniProtKB-EC.
GO; GO:0004316; F:3-oxoacyl-[acyl-carrier-protein] reductase (NADPH) activity; IDA:SGD.
GO; GO:0004315; F:3-oxoacyl-[acyl-carrier-protein] synthase activity; IMP:SGD.
GO; GO:0004314; F:[acyl-carrier-protein] S-malonyltransferase activity; IBA:GO_Central.
GO; GO:0004321; F:fatty-acyl-CoA synthase activity; IEA:UniProtKB-EC.
GO; GO:0008897; F:holo-[acyl-carrier-protein] synthase activity; IMP:SGD.
GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
GO; GO:0042759; P:long-chain fatty acid biosynthetic process; IMP:SGD.
Gene3D; 3.40.47.10; -; 2.
Gene3D; 3.90.470.20; -; 1.
HAMAP; MF_00101; AcpS; 1.
InterPro; IPR008278; 4-PPantetheinyl_Trfase_SF.
InterPro; IPR002582; ACPS.
InterPro; IPR016035; Acyl_Trfase/lysoPLipase.
InterPro; IPR026025; FAS_alpha_yeast.
InterPro; IPR018201; Ketoacyl_synth_AS.
InterPro; IPR014031; Ketoacyl_synth_C.
InterPro; IPR014030; Ketoacyl_synth_N.
InterPro; IPR016040; NAD(P)-bd_dom.
InterPro; IPR004568; Ppantetheine-prot_Trfase_dom.
InterPro; IPR016039; Thiolase-like.
Pfam; PF01648; ACPS; 1.
Pfam; PF00109; ketoacyl-synt; 1.
Pfam; PF02801; Ketoacyl-synt_C; 1.
PIRSF; PIRSF000454; FAS_yeast_alpha; 1.
ProDom; PD004282; PPantethiene-prot_Trfase; 1.
SUPFAM; SSF51735; SSF51735; 1.
SUPFAM; SSF52151; SSF52151; 1.
SUPFAM; SSF53901; SSF53901; 4.
SUPFAM; SSF56214; SSF56214; 1.
TIGRFAMs; TIGR00556; pantethn_trn; 1.
PROSITE; PS00606; B_KETOACYL_SYNTHASE; 1.
PROSITE; PS50075; CARRIER; 1.
PROSITE; PS00012; PHOSPHOPANTETHEINE; 1.
1: Evidence at protein level;
3D-structure; Complete proteome; Fatty acid biosynthesis;
Fatty acid metabolism; Isopeptide bond; Lipid biosynthesis;
Lipid metabolism; Magnesium; Metal-binding; Multifunctional enzyme;
NAD; NADP; Oxidoreductase; Phosphopantetheine; Phosphoprotein;
Reference proteome; Transferase; Ubl conjugation.
CHAIN 1 1887 Fatty acid synthase subunit alpha.
/FTId=PRO_0000180287.
DOMAIN 145 220 Carrier. {ECO:0000255|PROSITE-
ProRule:PRU00258}.
REGION 675 874 Beta-ketoacyl reductase.
REGION 1149 1363 Beta-ketoacyl synthase.
REGION 1772 1774 Acetyl-CoA binding.
REGION 1817 1833 Acetyl-CoA binding.
REGION 1841 1844 Acetyl-CoA binding.
REGION 1871 1873 Acetyl-CoA binding.
ACT_SITE 1305 1305 For beta-ketoacyl synthase activity.
METAL 1772 1772 Magnesium.
METAL 1773 1773 Magnesium; via carbonyl oxygen.
METAL 1774 1774 Magnesium.
METAL 1872 1872 Magnesium.
METAL 1873 1873 Magnesium; via carbonyl oxygen.
BINDING 1798 1798 Acetyl-CoA.
{ECO:0000269|PubMed:19679086}.
BINDING 1808 1808 Acetyl-CoA.
{ECO:0000269|PubMed:19679086}.
MOD_RES 50 50 Phosphoserine.
{ECO:0000244|PubMed:15665377}.
MOD_RES 180 180 O-(pantetheine 4'-phosphoryl)serine.
{ECO:0000255|PROSITE-ProRule:PRU00258,
ECO:0000269|PubMed:17431182}.
MOD_RES 523 523 Phosphoserine.
{ECO:0000244|PubMed:19779198}.
MOD_RES 958 958 Phosphoserine.
{ECO:0000244|PubMed:17330950}.
MOD_RES 1440 1440 Phosphoserine.
{ECO:0000244|PubMed:17330950}.
CROSSLNK 37 37 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000244|PubMed:22106047}.
MUTAGEN 1250 1250 G->S: Cerulenin-resistance.
{ECO:0000269|PubMed:8041367}.
MUTAGEN 1769 1769 V->D: Does not affect oligomerization;
when associated with S-1771 and L-1773 or
S-1771; L-1773; S-1879 and E-1881.
{ECO:0000269|PubMed:19679086}.
MUTAGEN 1770 1770 G->D: Loss of transferase activity.
{ECO:0000269|PubMed:19679086}.
MUTAGEN 1771 1771 V->S: Does not affect oligomerization but
lacks transferase activity; when
associated with D-1769 and L-1773 or D-
1769; L-1773; S-1879 and E-1881.
{ECO:0000269|PubMed:19679086}.
MUTAGEN 1772 1772 D->S: Loss of transferase activity; when
associated with S-1774.
{ECO:0000269|PubMed:19679086}.
MUTAGEN 1773 1773 V->L: Does not affect oligomerization but
lacks transferase activity; when
associated with D-1769 and S-1771 or D-
1769; S-1771; S-1879 and E-1881.
{ECO:0000269|PubMed:19679086}.
MUTAGEN 1774 1774 E->S: Loss of transferase activity; when
associated with S-1772.
{ECO:0000269|PubMed:19679086}.
MUTAGEN 1841 1841 R->A: Loss off transferase activity.
{ECO:0000269|PubMed:19679086}.
MUTAGEN 1879 1879 V->S: Does not affect oligomerization but
lacks transferase activity; when
associated with D-1769; S-1771; L-1773
and E-1881.
{ECO:0000269|PubMed:19679086}.
MUTAGEN 1881 1881 V->E: Does not affect oligomerization but
lacks transferase activity; when
associated with D-1769; S-1771; L-1773
and S-1879.
{ECO:0000269|PubMed:19679086}.
CONFLICT 310 310 G -> GTTGTGG (in Ref. 1; AAA34601).
{ECO:0000305}.
CONFLICT 594 594 T -> I (in Ref. 1; AAA34601).
{ECO:0000305}.
CONFLICT 941 1019 AKLRKELVETSEVRKAVSIETALEHKVVNGNSADAAYAQVE
IQPRANIQLDFPELKPYKQVKQIAPAELEGLLDLERVI ->
CLNCVKSWLKLLKLERQFPSKLLWSIRLSMAIALMLHMLKS
KFNQELTFNWTSQNRNHTNRLNKLLPLSLRVCWIWKELF
(in Ref. 1; AAA34601). {ECO:0000305}.
CONFLICT 1036 1041 RWEMEA -> KMGNGS (in Ref. 1; AAA34601).
{ECO:0000305}.
CONFLICT 1408 1408 A -> S (in Ref. 1; AAA34601).
{ECO:0000305}.
CONFLICT 1671 1671 N -> T (in Ref. 1; AAA34601).
{ECO:0000305}.
HELIX 3 20 {ECO:0000244|PDB:2UV8}.
TURN 21 23 {ECO:0000244|PDB:2UV8}.
HELIX 28 37 {ECO:0000244|PDB:2UV8}.
STRAND 42 51 {ECO:0000244|PDB:2UV8}.
HELIX 52 64 {ECO:0000244|PDB:2UV8}.
HELIX 66 71 {ECO:0000244|PDB:2UV8}.
STRAND 77 80 {ECO:0000244|PDB:2UV8}.
TURN 81 83 {ECO:0000244|PDB:2UV8}.
HELIX 85 88 {ECO:0000244|PDB:2UV8}.
HELIX 147 157 {ECO:0000244|PDB:2UV8}.
TURN 158 160 {ECO:0000244|PDB:2UV8}.
TURN 163 165 {ECO:0000244|PDB:2UV8}.
HELIX 172 176 {ECO:0000244|PDB:2UV8}.
HELIX 180 194 {ECO:0000244|PDB:2UV8}.
TURN 201 203 {ECO:0000244|PDB:2UV8}.
HELIX 206 216 {ECO:0000244|PDB:2UV8}.
HELIX 223 236 {ECO:0000244|PDB:2UV8}.
HELIX 243 252 {ECO:0000244|PDB:2UV8}.
TURN 258 260 {ECO:0000244|PDB:2UV8}.
HELIX 261 270 {ECO:0000244|PDB:2UV8}.
STRAND 274 276 {ECO:0000244|PDB:2ML8}.
HELIX 280 298 {ECO:0000244|PDB:2UV8}.
HELIX 329 350 {ECO:0000244|PDB:2UV8}.
HELIX 356 382 {ECO:0000244|PDB:2UV8}.
HELIX 384 389 {ECO:0000244|PDB:2UV8}.
HELIX 396 398 {ECO:0000244|PDB:2UV8}.
STRAND 400 402 {ECO:0000244|PDB:2UV8}.
HELIX 405 421 {ECO:0000244|PDB:2UV8}.
HELIX 430 440 {ECO:0000244|PDB:2UV8}.
HELIX 445 456 {ECO:0000244|PDB:2UV8}.
HELIX 460 462 {ECO:0000244|PDB:2UV8}.
HELIX 464 483 {ECO:0000244|PDB:2UV8}.
STRAND 497 503 {ECO:0000244|PDB:2UV8}.
STRAND 509 515 {ECO:0000244|PDB:2UV8}.
HELIX 522 531 {ECO:0000244|PDB:2UV8}.
TURN 605 607 {ECO:0000244|PDB:2UV8}.
HELIX 609 615 {ECO:0000244|PDB:2UV8}.
HELIX 626 629 {ECO:0000244|PDB:2UV8}.
STRAND 637 643 {ECO:0000244|PDB:2UV8}.
STRAND 649 651 {ECO:0000244|PDB:2UV8}.
HELIX 653 668 {ECO:0000244|PDB:2UV8}.
STRAND 677 682 {ECO:0000244|PDB:2UV8}.
STRAND 685 687 {ECO:0000244|PDB:2UV8}.
HELIX 688 698 {ECO:0000244|PDB:2UV8}.
STRAND 702 709 {ECO:0000244|PDB:2UV8}.
HELIX 712 725 {ECO:0000244|PDB:2UV8}.
STRAND 731 736 {ECO:0000244|PDB:2UV8}.
HELIX 742 753 {ECO:0000244|PDB:2UV8}.
TURN 756 759 {ECO:0000244|PDB:2UV8}.
STRAND 766 770 {ECO:0000244|PDB:2UV8}.
HELIX 781 783 {ECO:0000244|PDB:2UV8}.
HELIX 786 795 {ECO:0000244|PDB:2UV8}.
HELIX 797 811 {ECO:0000244|PDB:2UV8}.
TURN 812 814 {ECO:0000244|PDB:2UV8}.
STRAND 820 826 {ECO:0000244|PDB:2UV8}.
HELIX 839 845 {ECO:0000244|PDB:2UV8}.
HELIX 846 848 {ECO:0000244|PDB:2UV8}.
HELIX 849 855 {ECO:0000244|PDB:2UV8}.
TURN 859 861 {ECO:0000244|PDB:2UV8}.
STRAND 862 869 {ECO:0000244|PDB:2UV8}.
HELIX 885 889 {ECO:0000244|PDB:2UV8}.
HELIX 898 906 {ECO:0000244|PDB:2UV8}.
HELIX 907 909 {ECO:0000244|PDB:2UV8}.
HELIX 911 919 {ECO:0000244|PDB:2UV8}.
STRAND 922 927 {ECO:0000244|PDB:2UV8}.
TURN 930 932 {ECO:0000244|PDB:2UV8}.
STRAND 933 935 {ECO:0000244|PDB:2UV8}.
HELIX 936 968 {ECO:0000244|PDB:2UV8}.
TURN 971 976 {ECO:0000244|PDB:2UV8}.
HELIX 998 1004 {ECO:0000244|PDB:2UV8}.
HELIX 1007 1009 {ECO:0000244|PDB:2UV8}.
TURN 1010 1012 {ECO:0000244|PDB:2UV8}.
HELIX 1015 1017 {ECO:0000244|PDB:2UV8}.
STRAND 1019 1028 {ECO:0000244|PDB:2UV8}.
HELIX 1033 1042 {ECO:0000244|PDB:2UV8}.
HELIX 1047 1056 {ECO:0000244|PDB:2UV8}.
STRAND 1059 1067 {ECO:0000244|PDB:2UV8}.
STRAND 1070 1077 {ECO:0000244|PDB:2UV8}.
TURN 1078 1080 {ECO:0000244|PDB:2UV8}.
HELIX 1086 1088 {ECO:0000244|PDB:2UV8}.
HELIX 1089 1099 {ECO:0000244|PDB:2UV8}.
STRAND 1101 1105 {ECO:0000244|PDB:2UV8}.
HELIX 1108 1111 {ECO:0000244|PDB:2UV8}.
STRAND 1118 1126 {ECO:0000244|PDB:2UV8}.
STRAND 1134 1136 {ECO:0000244|PDB:2UV8}.
HELIX 1138 1148 {ECO:0000244|PDB:2UV8}.
HELIX 1149 1151 {ECO:0000244|PDB:2UV8}.
STRAND 1152 1156 {ECO:0000244|PDB:2UV8}.
TURN 1158 1160 {ECO:0000244|PDB:2UV8}.
STRAND 1163 1167 {ECO:0000244|PDB:2UV8}.
STRAND 1172 1179 {ECO:0000244|PDB:2UV8}.
STRAND 1185 1187 {ECO:0000244|PDB:2UV8}.
TURN 1195 1199 {ECO:0000244|PDB:2UV8}.
HELIX 1202 1207 {ECO:0000244|PDB:2UV8}.
HELIX 1210 1225 {ECO:0000244|PDB:2UV8}.
HELIX 1231 1233 {ECO:0000244|PDB:2UV8}.
HELIX 1234 1237 {ECO:0000244|PDB:2UV8}.
HELIX 1240 1242 {ECO:0000244|PDB:2UV8}.
STRAND 1243 1245 {ECO:0000244|PDB:2UV8}.
STRAND 1248 1251 {ECO:0000244|PDB:2UV8}.
HELIX 1254 1261 {ECO:0000244|PDB:2UV8}.
TURN 1262 1267 {ECO:0000244|PDB:2UV8}.
HELIX 1274 1278 {ECO:0000244|PDB:2UV8}.
HELIX 1282 1290 {ECO:0000244|PDB:2UV8}.
HELIX 1304 1306 {ECO:0000244|PDB:2UV8}.
HELIX 1307 1320 {ECO:0000244|PDB:2UV8}.
STRAND 1325 1333 {ECO:0000244|PDB:2UV8}.
HELIX 1337 1345 {ECO:0000244|PDB:2UV8}.
HELIX 1352 1357 {ECO:0000244|PDB:2UV8}.
HELIX 1362 1364 {ECO:0000244|PDB:2UV8}.
STRAND 1381 1389 {ECO:0000244|PDB:2UV8}.
HELIX 1390 1396 {ECO:0000244|PDB:2UV8}.
STRAND 1402 1410 {ECO:0000244|PDB:2UV8}.
HELIX 1424 1429 {ECO:0000244|PDB:2UV8}.
HELIX 1441 1443 {ECO:0000244|PDB:2UV8}.
HELIX 1445 1474 {ECO:0000244|PDB:2UV8}.
HELIX 1483 1508 {ECO:0000244|PDB:2UV8}.
TURN 1512 1515 {ECO:0000244|PDB:2UV8}.
STRAND 1517 1519 {ECO:0000244|PDB:2UV8}.
HELIX 1521 1527 {ECO:0000244|PDB:2UV8}.
TURN 1528 1530 {ECO:0000244|PDB:2UV8}.
HELIX 1533 1535 {ECO:0000244|PDB:2UV8}.
STRAND 1536 1540 {ECO:0000244|PDB:2UV8}.
HELIX 1547 1564 {ECO:0000244|PDB:2UV8}.
STRAND 1572 1575 {ECO:0000244|PDB:2UV8}.
HELIX 1578 1581 {ECO:0000244|PDB:2UV8}.
HELIX 1585 1587 {ECO:0000244|PDB:2UV8}.
HELIX 1588 1600 {ECO:0000244|PDB:2UV8}.
STRAND 1612 1614 {ECO:0000244|PDB:2UV8}.
HELIX 1616 1620 {ECO:0000244|PDB:2UV8}.
STRAND 1638 1645 {ECO:0000244|PDB:2UV8}.
TURN 1646 1648 {ECO:0000244|PDB:2UV8}.
STRAND 1649 1656 {ECO:0000244|PDB:2UV8}.
HELIX 1659 1662 {ECO:0000244|PDB:2UV8}.
HELIX 1667 1693 {ECO:0000244|PDB:2UV8}.
HELIX 1708 1710 {ECO:0000244|PDB:2UV8}.
HELIX 1711 1716 {ECO:0000244|PDB:2UV8}.
STRAND 1726 1728 {ECO:0000244|PDB:2UV8}.
STRAND 1730 1732 {ECO:0000244|PDB:2UV8}.
TURN 1735 1739 {ECO:0000244|PDB:2UV8}.
HELIX 1742 1745 {ECO:0000244|PDB:2UV8}.
STRAND 1769 1775 {ECO:0000244|PDB:2WAS}.
HELIX 1776 1778 {ECO:0000244|PDB:2WAS}.
HELIX 1784 1790 {ECO:0000244|PDB:2WAS}.
HELIX 1793 1800 {ECO:0000244|PDB:2WAS}.
STRAND 1802 1804 {ECO:0000244|PDB:2WAS}.
HELIX 1805 1823 {ECO:0000244|PDB:2WAS}.
STRAND 1837 1842 {ECO:0000244|PDB:2WAS}.
STRAND 1845 1851 {ECO:0000244|PDB:2WAS}.
HELIX 1853 1860 {ECO:0000244|PDB:2WAS}.
TURN 1861 1863 {ECO:0000244|PDB:2WAS}.
STRAND 1866 1873 {ECO:0000244|PDB:2WAS}.
STRAND 1875 1885 {ECO:0000244|PDB:2WAS}.
SEQUENCE 1887 AA; 206947 MW; 08B872734CF3AEEA CRC64;
MKPEVEQELA HILLTELLAY QFASPVRWIE TQDVFLKDFN TERVVEIGPS PTLAGMAQRT
LKNKYESYDA ALSLHREILC YSKDAKEIYY TPDPSELAAK EEPAKEEAPA PTPAASAPAP
AAAAPAPVAA AAPAAAAAEI ADEPVKASLL LHVLVAHKLK KSLDSIPMSK TIKDLVGGKS
TVQNEILGDL GKEFGTTPEK PEETPLEELA ETFQDTFSGA LGKQSSSLLS RLISSKMPGG
FTITVARKYL QTRWGLPSGR QDGVLLVALS NEPAARLGSE ADAKAFLDSM AQKYASIVGV
DLSSAASASG AAGAGAAAGA AMIDAGALEE ITKDHKVLAR QQLQVLARYL KMDLDNGERK
FLKEKDTVAE LQAQLDYLNA ELGEFFVNGV ATSFSRKKAR TFDSSWNWAK QSLLSLYFEI
IHGVLKNVDR EVVSEAINIM NRSNDALIKF MEYHISNTDE TKGENYQLVK TLGEQLIENC
KQVLDVDPVY KDVAKPTGPK TAIDKNGNIT YSEEPREKVR KLSQYVQEMA LGGPITKESQ
PTIEEDLTRV YKAISAQADK QDISSSTRVE FEKLYSDLMK FLESSKEIDP SQTTQLAGMD
VEDALDKDST KEVASLPNKS TISKTVSSTI PRETIPFLHL RKKTPAGDWK YDRQLSSLFL
DGLEKAAFNG VTFKDKYVLI TGAGKGSIGA EVLQGLLQGG AKVVVTTSRF SKQVTDYYQS
IYAKYGAKGS TLIVVPFNQG SKQDVEALIE FIYDTEKNGG LGWDLDAIIP FAAIPEQGIE
LEHIDSKSEF AHRIMLTNIL RMMGCVKKQK SARGIETRPA QVILPMSPNH GTFGGDGMYS
ESKLSLETLF NRWHSESWAN QLTVCGAIIG WTRGTGLMSA NNIIAEGIEK MGVRTFSQKE
MAFNLLGLLT PEVVELCQKS PVMADLNGGL QFVPELKEFT AKLRKELVET SEVRKAVSIE
TALEHKVVNG NSADAAYAQV EIQPRANIQL DFPELKPYKQ VKQIAPAELE GLLDLERVIV
VTGFAEVGPW GSARTRWEME AFGEFSLEGC VEMAWIMGFI SYHNGNLKGR PYTGWVDSKT
KEPVDDKDVK AKYETSILEH SGIRLIEPEL FNGYNPEKKE MIQEVIVEED LEPFEASKET
AEQFKHQHGD KVDIFEIPET GEYSVKLLKG ATLYIPKALR FDRLVAGQIP TGWNAKTYGI
SDDIISQVDP ITLFVLVSVV EAFIASGITD PYEMYKYVHV SEVGNCSGSG MGGVSALRGM
FKDRFKDEPV QNDILQESFI NTMSAWVNML LISSSGPIKT PVGACATSVE SVDIGVETIL
SGKARICIVG GYDDFQEEGS FEFGNMKATS NTLEEFEHGR TPAEMSRPAT TTRNGFMEAQ
GAGIQIIMQA DLALKMGVPI YGIVAMAATA TDKIGRSVPA PGKGILTTAR EHHSSVKYAS
PNLNMKYRKR QLVTREAQIK DWVENELEAL KLEAEEIPSE DQNEFLLERT REIHNEAESQ
LRAAQQQWGN DFYKRDPRIA PLRGALATYG LTIDDLGVAS FHGTSTKAND KNESATINEM
MKHLGRSEGN PVIGVFQKFL TGHPKGAAGA WMMNGALQIL NSGIIPGNRN ADNVDKILEQ
FEYVLYPSKT LKTDGVRAVS ITSFGFGQKG GQAIVVHPDY LYGAITEDRY NEYVAKVSAR
EKSAYKFFHN GMIYNKLFVS KEHAPYTDEL EEDVYLDPLA RVSKDKKSGS LTFNSKNIQS
KDSYINANTI ETAKMIENMT KEKVSNGGVG VDVELITSIN VENDTFIERN FTPQEIEYCS
AQPSVQSSFA GTWSAKEAVF KSLGVKSLGG GAALKDIEIV RVNKNAPAVE LHGNAKKAAE
EAGVTDVKVS ISHDDLQAVA VAVSTKK


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