SIR2A_PLAF7
ID SIR2A_PLAF7 Reviewed; 273 AA.
AC Q8IE47;
DT 16-MAY-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=NAD-dependent protein deacylase Sir2A {ECO:0000255|HAMAP-Rule:MF_03160};
DE EC=2.3.1.- {ECO:0000255|HAMAP-Rule:MF_03160, ECO:0000269|PubMed:21992006};
DE AltName: Full=PfSir2 {ECO:0000303|PubMed:15820676};
DE AltName: Full=PfSir2A {ECO:0000303|PubMed:19402747};
DE AltName: Full=Regulatory protein SIR2 homolog A;
GN Name=Sir2A {ECO:0000303|PubMed:19402747}; Synonyms=Sir2;
GN ORFNames=PF13_0152, PF3D7_1328800;
OS Plasmodium falciparum (isolate 3D7).
OC Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Haemosporida;
OC Plasmodiidae; Plasmodium; Plasmodium (Laverania).
OX NCBI_TaxID=36329;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=3D7;
RX PubMed=12368864; DOI=10.1038/nature01097;
RA Gardner M.J., Hall N., Fung E., White O., Berriman M., Hyman R.W.,
RA Carlton J.M., Pain A., Nelson K.E., Bowman S., Paulsen I.T., James K.D.,
RA Eisen J.A., Rutherford K.M., Salzberg S.L., Craig A., Kyes S., Chan M.-S.,
RA Nene V., Shallom S.J., Suh B., Peterson J., Angiuoli S., Pertea M.,
RA Allen J., Selengut J., Haft D., Mather M.W., Vaidya A.B., Martin D.M.A.,
RA Fairlamb A.H., Fraunholz M.J., Roos D.S., Ralph S.A., McFadden G.I.,
RA Cummings L.M., Subramanian G.M., Mungall C., Venter J.C., Carucci D.J.,
RA Hoffman S.L., Newbold C., Davis R.W., Fraser C.M., Barrell B.G.;
RT "Genome sequence of the human malaria parasite Plasmodium falciparum.";
RL Nature 419:498-511(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=3D7;
RX PubMed=12368867; DOI=10.1038/nature01095;
RA Hall N., Pain A., Berriman M., Churcher C.M., Harris B., Harris D.,
RA Mungall K.L., Bowman S., Atkin R., Baker S., Barron A., Brooks K.,
RA Buckee C.O., Burrows C., Cherevach I., Chillingworth C., Chillingworth T.,
RA Christodoulou Z., Clark L., Clark R., Corton C., Cronin A., Davies R.M.,
RA Davis P., Dear P., Dearden F., Doggett J., Feltwell T., Goble A.,
RA Goodhead I., Gwilliam R., Hamlin N., Hance Z., Harper D., Hauser H.,
RA Hornsby T., Holroyd S., Horrocks P., Humphray S., Jagels K., James K.D.,
RA Johnson D., Kerhornou A., Knights A., Konfortov B., Kyes S., Larke N.,
RA Lawson D., Lennard N., Line A., Maddison M., Mclean J., Mooney P.,
RA Moule S., Murphy L., Oliver K., Ormond D., Price C., Quail M.A.,
RA Rabbinowitsch E., Rajandream M.A., Rutter S., Rutherford K.M., Sanders M.,
RA Simmonds M., Seeger K., Sharp S., Smith R., Squares R., Squares S.,
RA Stevens K., Taylor K., Tivey A., Unwin L., Whitehead S., Woodward J.R.,
RA Sulston J.E., Craig A., Newbold C., Barrell B.G.;
RT "Sequence of Plasmodium falciparum chromosomes 1, 3-9 and 13.";
RL Nature 419:527-531(2002).
RN [3]
RP FUNCTION IN VAR GENE REPRESSION, AND SUBCELLULAR LOCATION.
RX PubMed=15820676; DOI=10.1016/j.cell.2005.01.037;
RA Freitas-Junior L.H., Hernandez-Rivas R., Ralph S.A., Montiel-Condado D.,
RA Ruvalcaba-Salazar O.K., Rojas-Meza A.P., Mancio-Silva L.,
RA Leal-Silvestre R.J., Gontijo A.M., Shorte S., Scherf A.;
RT "Telomeric heterochromatin propagation and histone acetylation control
RT mutually exclusive expression of antigenic variation genes in malaria
RT parasites.";
RL Cell 121:25-36(2005).
RN [4]
RP FUNCTION, ACTIVITY REGULATION, AND SUBCELLULAR LOCATION.
RX PubMed=17827348; DOI=10.1128/ec.00114-07;
RA Merrick C.J., Duraisingh M.T.;
RT "Plasmodium falciparum Sir2: an unusual sirtuin with dual histone
RT deacetylase and ADP-ribosyltransferase activity.";
RL Eukaryot. Cell 6:2081-2091(2007).
RN [5]
RP FUNCTION, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=18729382; DOI=10.1021/bi800767t;
RA French J.B., Cen Y., Sauve A.A.;
RT "Plasmodium falciparum Sir2 is an NAD+-dependent deacetylase and an
RT acetyllysine-dependent and acetyllysine-independent NAD+ glycohydrolase.";
RL Biochemistry 47:10227-10239(2008).
RN [6]
RP FUNCTION, ACTIVITY REGULATION, AND DEVELOPMENTAL STAGE.
RX PubMed=18397290; DOI=10.1111/j.1574-6968.2008.01135.x;
RA Prusty D., Mehra P., Srivastava S., Shivange A.V., Gupta A., Roy N.,
RA Dhar S.K.;
RT "Nicotinamide inhibits Plasmodium falciparum Sir2 activity in vitro and
RT parasite growth.";
RL FEMS Microbiol. Lett. 282:266-272(2008).
RN [7]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=18525026; DOI=10.1242/jcs.026427;
RA Mancio-Silva L., Rojas-Meza A.P., Vargas M., Scherf A., Hernandez-Rivas R.;
RT "Differential association of Orc1 and Sir2 proteins to telomeric domains in
RT Plasmodium falciparum.";
RL J. Cell Sci. 121:2046-2053(2008).
RN [8]
RP FUNCTION, ACTIVITY REGULATION, SUBUNIT, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=18221799; DOI=10.1016/j.molbiopara.2007.12.003;
RA Chakrabarty S.P., Saikumari Y.K., Bopanna M.P., Balaram H.;
RT "Biochemical characterization of Plasmodium falciparum Sir2, a NAD+-
RT dependent deacetylase.";
RL Mol. Biochem. Parasitol. 158:139-151(2008).
RN [9]
RP FUNCTION IN VAR GENE REPRESSION.
RX PubMed=19402747; DOI=10.1371/journal.pbio.1000084;
RA Tonkin C.J., Carret C.K., Duraisingh M.T., Voss T.S., Ralph S.A.,
RA Hommel M., Duffy M.F., Silva L.M., Scherf A., Ivens A., Speed T.P.,
RA Beeson J.G., Cowman A.F.;
RT "Sir2 paralogues cooperate to regulate virulence genes and antigenic
RT variation in Plasmodium falciparum.";
RL PLoS Biol. 7:E84-E84(2009).
RN [10]
RP FUNCTION, COFACTOR, AND SUBUNIT.
RX PubMed=20601220; DOI=10.1016/j.bbapap.2010.06.010;
RA Chakrabarty S.P., Balaram H.;
RT "Reversible binding of zinc in Plasmodium falciparum Sir2: structure and
RT activity of the apoenzyme.";
RL Biochim. Biophys. Acta 1804:1743-1750(2010).
RN [11]
RP FUNCTION, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=22379140; DOI=10.1093/nar/gks202;
RA Deshmukh A.S., Srivastava S., Herrmann S., Gupta A., Mitra P.,
RA Gilberger T.W., Dhar S.K.;
RT "The role of N-terminus of Plasmodium falciparum ORC1 in telomeric
RT localization and var gene silencing.";
RL Nucleic Acids Res. 40:5313-5331(2012).
RN [12]
RP X-RAY CRYSTALLOGRAPHY (2.65 ANGSTROMS) OF 10-273 IN COMPLEX WITH AMP AND
RP ZINC.
RG Structural genomics consortium (SGC);
RA Wernimont A.K., Hutchinson A., Lin Y.H., MacKenzie F., Senisterra G.,
RA Allali-Hassanali A., Vedadi M., Ravichandran M., Cossar D., Kozieradzki I.,
RA Zhao Y., Schapira M., Arrowsmith C.H., Bountra C., Weigelt J.,
RA Edwards A.M., Hui R., Qiu W., Brand V.;
RT "Crystal structure of Plasmodium falciparum SIR2A (PF13_0152) in complex
RT with AMP.";
RL Submitted (SEP-2009) to the PDB data bank.
RN [13]
RP X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) IN COMPLEX WITH NAD; ZINC AND
RP SUBSTRATE ANALOG, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL
RP PROPERTIES, AND SUBUNIT.
RX PubMed=21992006; DOI=10.1021/cb200230x;
RA Zhu A.Y., Zhou Y., Khan S., Deitsch K.W., Hao Q., Lin H.;
RT "Plasmodium falciparum Sir2A preferentially hydrolyzes medium and long
RT chain fatty acyl lysine.";
RL ACS Chem. Biol. 7:155-159(2012).
CC -!- FUNCTION: NAD-dependent protein deacylase (PubMed:21992006). Catalyzes
CC the NAD-dependent hydrolysis of medium and long chain fatty acyl groups
CC from lysine residues (PubMed:21992006). Has weak NAD-dependent protein
CC deacetylase activity; however this activity may not be physiologically
CC relevant in vivo (PubMed:17827348, PubMed:18729382, PubMed:18397290,
CC PubMed:18221799, PubMed:20601220, PubMed:21992006). Regulates the
CC expression of the surface antigen-coding var genes central to the
CC malaria pathogenesis (PubMed:15820676, PubMed:22379140). Cooperates
CC with Sir2B to mediate silencing and mutual exclusive expression of only
CC 1 of the 60 subtelomeric var genes at a time, coding for functionally
CC different but epitopically variant versions of the erythrocyte membrane
CC protein 1 (PfEMP1) molecule, to evade the detection by host immune
CC surveillance (PubMed:19402747). Involved in recruiting ORC1 to the
CC telomers and subtelomeric repeat regions (TAREs) and promoters of var
CC genes (PubMed:22379140). Can ADP-ribosylate both histones and itself
CC (PubMed:17827348). May also have a role in telomeric end protection
CC (PubMed:18525026). {ECO:0000269|PubMed:15820676,
CC ECO:0000269|PubMed:17827348, ECO:0000269|PubMed:18221799,
CC ECO:0000269|PubMed:18397290, ECO:0000269|PubMed:18525026,
CC ECO:0000269|PubMed:18729382, ECO:0000269|PubMed:19402747,
CC ECO:0000269|PubMed:20601220, ECO:0000269|PubMed:21992006,
CC ECO:0000269|PubMed:22379140}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N(6)-acyl-L-lysyl-[protein] + NAD(+) = 2''-O-acyl-ADP-D-
CC ribose + L-lysyl-[protein] + nicotinamide; Xref=Rhea:RHEA:54172,
CC Rhea:RHEA-COMP:9752, Rhea:RHEA-COMP:13709, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:17154, ChEBI:CHEBI:29969, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:137967, ChEBI:CHEBI:138087;
CC Evidence={ECO:0000269|PubMed:21992006};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54173;
CC Evidence={ECO:0000269|PubMed:21992006};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000269|PubMed:20601220};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000269|PubMed:21992006,
CC ECO:0000269|Ref.12};
CC -!- ACTIVITY REGULATION: Inhibited by nicotinamide. Inhibited by surfactin,
CC which is a competitive inhibitor of NAD and an uncompetitive inhibitor
CC of acetylated peptide. {ECO:0000269|PubMed:17827348,
CC ECO:0000269|PubMed:18221799, ECO:0000269|PubMed:18397290}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=12.2 uM for NAD(+) {ECO:0000269|PubMed:18221799};
CC KM=39 uM for a synthetic histone H3K9 acetyllysine peptide
CC {ECO:0000269|PubMed:21992006};
CC KM=8 uM for a synthetic H3K9 butyryllysine peptide
CC {ECO:0000269|PubMed:21992006};
CC KM=1.2 uM for a synthetic H3K9 octanoyllysine peptide
CC {ECO:0000269|PubMed:21992006};
CC KM=1 uM for a synthetic H3K9 myristoyllysine peptide
CC {ECO:0000269|PubMed:21992006};
CC KM=372 uM for a synthetic histone H3K9K14 acetyllysine peptide
CC {ECO:0000269|PubMed:18729382};
CC KM=176 uM for a synthetic H4K5K8K12K16 acetyllysine peptide
CC {ECO:0000269|PubMed:18729382};
CC KM=85 uM for a synthetic p300 peptide acetylated at 'Lys-1020' and
CC 'Lys-1024' {ECO:0000269|PubMed:18729382};
CC -!- SUBUNIT: Homotrimer. Dissociates into monomers on binding NAD.
CC {ECO:0000269|PubMed:18221799, ECO:0000269|PubMed:20601220,
CC ECO:0000269|PubMed:21992006, ECO:0000269|Ref.12}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:17827348}. Nucleus,
CC nucleolus {ECO:0000269|PubMed:15820676, ECO:0000269|PubMed:18525026}.
CC Chromosome, telomere {ECO:0000269|PubMed:15820676,
CC ECO:0000269|PubMed:22379140}. Note=At the late ring stage/early
CC trophozoites, co-localizes with ORC1 to telomeres and subtelomeric
CC regions (TAREs) in the nuclear periphery (PubMed:18525026,
CC PubMed:22379140). Spreads out from the telomere over a distance of at
CC least 20-40 kb and is an important component of the heterochromatin
CC complex around Rep20, a region that lies adjacent to the regulatory 5'-
CC UTR element of telomeric var genes (PubMed:15820676). May relocate to
CC the cytoplasm during the multiple rounds of DNA synthesis and nuclear
CC mitosis in trophozoite stage (PubMed:18525026).
CC {ECO:0000269|PubMed:15820676, ECO:0000269|PubMed:18525026,
CC ECO:0000269|PubMed:22379140}.
CC -!- DEVELOPMENTAL STAGE: Expressed during the asexual blood stage,
CC specifically during the trophozoite and schizont stages (at protein
CC level) (PubMed:18397290, PubMed:22379140). Not detected at the ring
CC stage (PubMed:18397290). {ECO:0000269|PubMed:18397290,
CC ECO:0000269|PubMed:22379140}.
CC -!- DISRUPTION PHENOTYPE: Loss of binding to telomers and subtelomeric
CC repeat regions (TAREs) and promoters of var genes.
CC {ECO:0000269|PubMed:22379140}.
CC -!- MISCELLANEOUS: The reported ADP-ribosyltransferase activity of sirtuins
CC is likely to be some inefficient side reaction of the deacetylase
CC activity and may not be physiologically relevant.
CC {ECO:0000250|UniProtKB:P06700}.
CC -!- SIMILARITY: Belongs to the sirtuin family. Class III subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_03160}.
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DR EMBL; AL844509; CAD52419.1; -; Genomic_DNA.
DR RefSeq; XP_001350011.1; XM_001349975.1.
DR PDB; 3JWP; X-ray; 2.65 A; A=10-273.
DR PDB; 3U31; X-ray; 2.20 A; A=1-273.
DR PDB; 3U3D; X-ray; 2.40 A; A=1-273.
DR PDBsum; 3JWP; -.
DR PDBsum; 3U31; -.
DR PDBsum; 3U3D; -.
DR AlphaFoldDB; Q8IE47; -.
DR SMR; Q8IE47; -.
DR STRING; 5833.PF13_0152; -.
DR PRIDE; Q8IE47; -.
DR EnsemblProtists; CAD52419; CAD52419; PF3D7_1328800.
DR GeneID; 814122; -.
DR KEGG; pfa:PF3D7_1328800; -.
DR VEuPathDB; PlasmoDB:PF3D7_1328800; -.
DR HOGENOM; CLU_023643_3_0_1; -.
DR InParanoid; Q8IE47; -.
DR OMA; SMQVYPA; -.
DR PhylomeDB; Q8IE47; -.
DR BRENDA; 2.3.1.286; 4889.
DR BRENDA; 2.3.1.B41; 4889.
DR Reactome; R-PFA-2151201; Transcriptional activation of mitochondrial biogenesis.
DR EvolutionaryTrace; Q8IE47; -.
DR Proteomes; UP000001450; Chromosome 13.
DR GO; GO:0005677; C:chromatin silencing complex; ISS:GeneDB.
DR GO; GO:0000781; C:chromosome, telomeric region; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; IDA:GeneDB.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-UniRule.
DR GO; GO:0005730; C:nucleolus; IDA:GeneDB.
DR GO; GO:0005634; C:nucleus; IDA:GeneDB.
DR GO; GO:0003677; F:DNA binding; ISS:GeneDB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0070403; F:NAD+ binding; IBA:GO_Central.
DR GO; GO:0017136; F:NAD-dependent histone deacetylase activity; IBA:GO_Central.
DR GO; GO:0036054; F:protein-malonyllysine demalonylase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0036055; F:protein-succinyllysine desuccinylase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0006476; P:protein deacetylation; IEA:UniProtKB-UniRule.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IDA:GeneDB.
DR GO; GO:0016233; P:telomere capping; IDA:GeneDB.
DR Gene3D; 3.30.1600.10; -; 1.
DR HAMAP; MF_01121; Sirtuin_ClassIII; 1.
DR InterPro; IPR029035; DHS-like_NAD/FAD-binding_dom.
DR InterPro; IPR003000; Sirtuin.
DR InterPro; IPR026591; Sirtuin_cat_small_dom_sf.
DR InterPro; IPR027546; Sirtuin_class_III.
DR InterPro; IPR026590; Ssirtuin_cat_dom.
DR Pfam; PF02146; SIR2; 1.
DR SUPFAM; SSF52467; SSF52467; 1.
DR PROSITE; PS50305; SIRTUIN; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Chromosome; Metal-binding; NAD; Nucleus; Reference proteome;
KW Telomere; Transferase; Zinc.
FT CHAIN 1..273
FT /note="NAD-dependent protein deacylase Sir2A"
FT /id="PRO_0000417341"
FT DOMAIN 19..273
FT /note="Deacetylase sirtuin-type"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03160"
FT ACT_SITE 132
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03160"
FT BINDING 36..56
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03160,
FT ECO:0000269|PubMed:21992006"
FT BINDING 114..117
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03160"
FT BINDING 132
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 140
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03160,
FT ECO:0000269|PubMed:21992006, ECO:0000269|Ref.12"
FT BINDING 143
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03160,
FT ECO:0000269|PubMed:21992006, ECO:0000269|Ref.12"
FT BINDING 168
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03160,
FT ECO:0000269|PubMed:21992006, ECO:0000269|Ref.12"
FT BINDING 170
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03160,
FT ECO:0000269|PubMed:21992006, ECO:0000269|Ref.12"
FT BINDING 207..209
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03160"
FT BINDING 233..235
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03160,
FT ECO:0000269|PubMed:21992006"
FT BINDING 252
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03160,
FT ECO:0000269|PubMed:21992006"
FT STRAND 14..16
FT /evidence="ECO:0007829|PDB:3U31"
FT HELIX 18..26
FT /evidence="ECO:0007829|PDB:3U31"
FT STRAND 29..35
FT /evidence="ECO:0007829|PDB:3U31"
FT HELIX 37..39
FT /evidence="ECO:0007829|PDB:3U31"
FT HELIX 41..43
FT /evidence="ECO:0007829|PDB:3U31"
FT STRAND 47..50
FT /evidence="ECO:0007829|PDB:3U3D"
FT HELIX 55..58
FT /evidence="ECO:0007829|PDB:3U31"
FT HELIX 61..64
FT /evidence="ECO:0007829|PDB:3U31"
FT HELIX 67..72
FT /evidence="ECO:0007829|PDB:3U31"
FT HELIX 75..87
FT /evidence="ECO:0007829|PDB:3U31"
FT HELIX 94..104
FT /evidence="ECO:0007829|PDB:3U31"
FT STRAND 108..114
FT /evidence="ECO:0007829|PDB:3U31"
FT HELIX 119..122
FT /evidence="ECO:0007829|PDB:3U31"
FT STRAND 128..130
FT /evidence="ECO:0007829|PDB:3U31"
FT STRAND 133..140
FT /evidence="ECO:0007829|PDB:3U31"
FT TURN 141..143
FT /evidence="ECO:0007829|PDB:3U31"
FT STRAND 146..148
FT /evidence="ECO:0007829|PDB:3U31"
FT HELIX 152..154
FT /evidence="ECO:0007829|PDB:3U31"
FT TURN 160..162
FT /evidence="ECO:0007829|PDB:3U31"
FT STRAND 163..165
FT /evidence="ECO:0007829|PDB:3U31"
FT STRAND 173..178
FT /evidence="ECO:0007829|PDB:3U31"
FT HELIX 187..199
FT /evidence="ECO:0007829|PDB:3U31"
FT STRAND 201..207
FT /evidence="ECO:0007829|PDB:3U31"
FT HELIX 213..224
FT /evidence="ECO:0007829|PDB:3U31"
FT STRAND 229..235
FT /evidence="ECO:0007829|PDB:3U31"
FT TURN 238..243
FT /evidence="ECO:0007829|PDB:3U31"
FT STRAND 245..250
FT /evidence="ECO:0007829|PDB:3U31"
FT HELIX 252..254
FT /evidence="ECO:0007829|PDB:3U31"
FT HELIX 255..266
FT /evidence="ECO:0007829|PDB:3U31"
FT TURN 267..269
FT /evidence="ECO:0007829|PDB:3U31"
SQ SEQUENCE 273 AA; 30344 MW; 3DAD7D1BCC09B849 CRC64;
MGNLMISFLK KDTQSITLEE LAKIIKKCKH VVALTGSGTS AESNIPSFRG SSNSIWSKYD
PRIYGTIWGF WKYPEKIWEV IRDISSDYEI EINNGHVALS TLESLGYLKS VVTQNVDGLH
EASGNTKVIS LHGNVFEAVC CTCNKIVKLN KIMLQKTSHF MHQLPPECPC GGIFKPNIIL
FGEVVSSDLL KEAEEEIAKC DLLLVIGTSS TVSTATNLCH FACKKKKKIV EINISKTYIT
NKMSDYHVCA KFSELTKVAN ILKGSSEKNK KIM
