ID   GAL1_YEAST              Reviewed;         528 AA.
AC   P04385; D6VQ22;
DT   20-MAR-1987, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 4.
DT   02-SEP-2026, entry version 212.
DE   RecName: Full=Galactokinase {ECO:0000303|PubMed:200486};
DE            EC=2.7.1.6 {ECO:0000269|PubMed:12106903, ECO:0000269|PubMed:13495476, ECO:0000269|PubMed:14144};
DE   AltName: Full=Galactose kinase {ECO:0000303|PubMed:200486};
GN   Name=GAL1 {ECO:0000303|PubMed:6092912}; OrderedLocusNames=YBR020W;
GN   ORFNames=YBR0302;
OS   Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=559292;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=Carlsbergensis;
RX   PubMed=6715281; DOI=10.1128/jb.158.1.269-278.1984;
RA   Citron B.A., Donelson J.E.;
RT   "Sequence of the Saccharomyces GAL region and its transcription in vivo.";
RL   J. Bacteriol. 158:269-278(1984).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=8091864; DOI=10.1002/yea.320100010;
RA   Smits P.H.M., de Haan M., Maat C., Grivell L.A.;
RT   "The complete sequence of a 33 kb fragment on the right arm of chromosome
RT   II from Saccharomyces cerevisiae reveals 16 open reading frames, including
RT   ten new open reading frames, five previously identified genes and a
RT   homologue of the SCO1 gene.";
RL   Yeast 10:S75-S80(1994).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=7813418; DOI=10.1002/j.1460-2075.1994.tb06923.x;
RA   Feldmann H., Aigle M., Aljinovic G., Andre B., Baclet M.C., Barthe C.,
RA   Baur A., Becam A.-M., Biteau N., Boles E., Brandt T., Brendel M.,
RA   Brueckner M., Bussereau F., Christiansen C., Contreras R., Crouzet M.,
RA   Cziepluch C., Demolis N., Delaveau T., Doignon F., Domdey H.,
RA   Duesterhus S., Dubois E., Dujon B., El Bakkoury M., Entian K.-D.,
RA   Feuermann M., Fiers W., Fobo G.M., Fritz C., Gassenhuber J., Glansdorff N.,
RA   Goffeau A., Grivell L.A., de Haan M., Hein C., Herbert C.J.,
RA   Hollenberg C.P., Holmstroem K., Jacq C., Jacquet M., Jauniaux J.-C.,
RA   Jonniaux J.-L., Kallesoee T., Kiesau P., Kirchrath L., Koetter P.,
RA   Korol S., Liebl S., Logghe M., Lohan A.J.E., Louis E.J., Li Z.Y.,
RA   Maat M.J., Mallet L., Mannhaupt G., Messenguy F., Miosga T., Molemans F.,
RA   Mueller S., Nasr F., Obermaier B., Perea J., Pierard A., Piravandi E.,
RA   Pohl F.M., Pohl T.M., Potier S., Proft M., Purnelle B., Ramezani Rad M.,
RA   Rieger M., Rose M., Schaaff-Gerstenschlaeger I., Scherens B.,
RA   Schwarzlose C., Skala J., Slonimski P.P., Smits P.H.M., Souciet J.-L.,
RA   Steensma H.Y., Stucka R., Urrestarazu L.A., van der Aart Q.J.M.,
RA   Van Dyck L., Vassarotti A., Vetter I., Vierendeels F., Vissers S.,
RA   Wagner G., de Wergifosse P., Wolfe K.H., Zagulski M., Zimmermann F.K.,
RA   Mewes H.-W., Kleine K.;
RT   "Complete DNA sequence of yeast chromosome II.";
RL   EMBO J. 13:5795-5809(1994).
RN   [4]
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=24374639; DOI=10.1534/g3.113.008995;
RA   Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA   Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA   Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT   "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL   G3 (Bethesda) 4:389-398(2014).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-29.
RX   PubMed=6092912; DOI=10.1128/mcb.4.8.1440-1448.1984;
RA   Johnston M., Davis R.W.;
RT   "Sequences that regulate the divergent GAL1-GAL10 promoter in Saccharomyces
RT   cerevisiae.";
RL   Mol. Cell. Biol. 4:1440-1448(1984).
RN   [6]
RP   PROTEIN SEQUENCE OF 2-12.
RX   PubMed=200486; DOI=10.1016/0014-5793(77)80638-8;
RA   Schlesinger D.H., Schell M.A., Wilson D.B.;
RT   "The NH2-terminal sequences of galactokinase from Escherichia coli and
RT   Saccharomyces cerevisiae.";
RL   FEBS Lett. 83:45-47(1977).
RN   [7]
RP   FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY.
RX   PubMed=13495476; DOI=10.1126/science.127.3288.28;
RA   de Robichon-Szulmajster H.;
RT   "Induction of enzymes of the galactose pathway in mutants of Saccharomyces
RT   cerevisiae.";
RL   Science 127:28-29(1958).
RN   [8]
RP   FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND PATHWAY.
RX   PubMed=14144; DOI=10.1016/s0021-9258(17)40635-1;
RA   Schell M.A., Wilson D.B.;
RT   "Purification and properties of galactokinase from Saccharomyces
RT   cerevisiae.";
RL   J. Biol. Chem. 252:1162-1166(1977).
RN   [9]
RP   INDUCTION.
RX   PubMed=3886158; DOI=10.1016/0092-8674(85)90336-8;
RA   Giniger E., Varnum S.M., Ptashne M.;
RT   "Specific DNA binding of GAL4, a positive regulatory protein of yeast.";
RL   Cell 40:767-774(1985).
RN   [10]
RP   FUNCTION.
RX   PubMed=2656659; DOI=10.1128/jb.171.6.3539-3544.1989;
RA   Ramos J., Szkutnicka K., Cirillo V.P.;
RT   "Characteristics of galactose transport in Saccharomyces cerevisiae cells
RT   and reconstituted lipid vesicles.";
RL   J. Bacteriol. 171:3539-3544(1989).
RN   [11]
RP   FUNCTION.
RX   PubMed=1317007; DOI=10.1128/mcb.12.6.2701-2707.1992;
RA   Bhat P.J., Hopper J.E.;
RT   "Overproduction of the GAL1 or GAL3 protein causes galactose-independent
RT   activation of the GAL4 protein: evidence for a new model of induction for
RT   the yeast GAL/MEL regulon.";
RL   Mol. Cell. Biol. 12:2701-2707(1992).
RN   [12]
RP   FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND PATHWAY.
RX   PubMed=12106903; DOI=10.1016/s0300-9084(02)01399-8;
RA   Timson D.J., Reece R.J.;
RT   "Kinetic analysis of yeast galactokinase: implications for transcriptional
RT   activation of the GAL genes.";
RL   Biochimie 84:265-272(2002).
RN   [13]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-381, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19779198; DOI=10.1126/science.1172867;
RA   Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT   "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT   into evolution.";
RL   Science 325:1682-1686(2009).
RN   [14]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA   Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA   Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA   Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT   "N-terminal acetylome analyses and functional insights of the N-terminal
RT   acetyltransferase NatB.";
RL   Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN   [15] {ECO:0007744|PDB:2AJ4}
RP   X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) OF 2-528 IN COMPLEX WITH ATP AND
RP   ALPHA-D-GALACTOSE.
RX   PubMed=16115868; DOI=10.1074/jbc.m508446200;
RA   Thoden J.B., Sellick C.A., Timson D.J., Reece R.J., Holden H.M.;
RT   "Molecular structure of Saccharomyces cerevisiae Gal1p, a bifunctional
RT   galactokinase and transcriptional inducer.";
RL   J. Biol. Chem. 280:36905-36911(2005).
CC   -!- FUNCTION: Galactokinase is a key enzyme in the galactose metabolism
CC       where it catalyzes the conversion of alpha-D-galactose to galactose 1-
CC       phosphate (PubMed:12106903, PubMed:13495476, PubMed:14144). Can also
CC       induce the transcription of the yeast GAL genes in response to the
CC       organism being challenged with galactose as the sole source of carbon
CC       (PubMed:1317007, PubMed:2656659). Its striking amino acid sequence
CC       similarity to GAL3 might explain its GAL3-like induction activity
CC       (PubMed:1317007, PubMed:2656659). {ECO:0000269|PubMed:12106903,
CC       ECO:0000269|PubMed:1317007, ECO:0000269|PubMed:13495476,
CC       ECO:0000269|PubMed:14144, ECO:0000269|PubMed:2656659}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=alpha-D-galactose + ATP = alpha-D-galactose 1-phosphate + ADP
CC         + H(+); Xref=Rhea:RHEA:13553, ChEBI:CHEBI:15378, ChEBI:CHEBI:28061,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:58336, ChEBI:CHEBI:456216; EC=2.7.1.6;
CC         Evidence={ECO:0000269|PubMed:12106903, ECO:0000269|PubMed:13495476,
CC         ECO:0000269|PubMed:14144};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13554;
CC         Evidence={ECO:0000269|PubMed:12106903, ECO:0000269|PubMed:13495476,
CC         ECO:0000269|PubMed:14144};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=1200 uM for alpha-D-galactose {ECO:0000269|PubMed:12106903,
CC         ECO:0000269|PubMed:14144};
CC         KM=32 uM for ATP {ECO:0000269|PubMed:12106903};
CC         Note=kcat is 11.7 sec(-1) for alpha-D-galactose and 8.7 sec(-1) for
CC         ATP utilization. {ECO:0000269|PubMed:12106903};
CC       pH dependence:
CC         Optimum pH is 8.0-9.0. {ECO:0000269|PubMed:14144};
CC   -!- PATHWAY: Carbohydrate metabolism; galactose metabolism.
CC       {ECO:0000269|PubMed:12106903, ECO:0000269|PubMed:13495476,
CC       ECO:0000269|PubMed:14144}.
CC   -!- INTERACTION:
CC       P04385; P04387: GAL80; NbExp=2; IntAct=EBI-7272, EBI-2061197;
CC   -!- INDUCTION: Expression is regulated by the GAL4 transcription factor.
CC       {ECO:0000269|PubMed:3886158}.
CC   -!- SIMILARITY: Belongs to the GHMP kinase family. GalK subfamily.
CC       {ECO:0000305}.
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DR   EMBL; AH001375; AAA34631.1; -; Genomic_DNA.
DR   EMBL; X76078; CAA53677.1; -; Genomic_DNA.
DR   EMBL; Z35889; CAA84962.1; -; Genomic_DNA.
DR   EMBL; K02115; AAA34621.1; -; Genomic_DNA.
DR   EMBL; BK006936; DAA07142.1; -; Genomic_DNA.
DR   PIR; S45876; KIBYGG.
DR   RefSeq; NP_009576.1; NM_001178368.1.
DR   PDB; 2AJ4; X-ray; 2.40 A; A/B=2-528.
DR   AlphaFoldDB; P04385; -.
DR   SMR; P04385; -.
DR   BioGRID; 32723; 92.
DR   ComplexPortal; CPX-1043; GAL1-GAL80 transcription regulation complex.
DR   DIP; DIP-2333N; -.
DR   FunCoup; P04385; 1166.
DR   IntAct; P04385; 99.
DR   STRING; 4932.YBR020W; -.
DR   iPTMnet; P04385; -.
DR   PaxDb; 4932-YBR020W; -.
DR   PeptideAtlas; P04385; -.
DR   EnsemblFungi; YBR020W_mRNA; YBR020W; YBR020W.
DR   GeneID; 852308; -.
DR   KEGG; sce:YBR020W; -.
DR   AGR; SGD:S000000224; -.
DR   SGD; S000000224; GAL1.
DR   VEuPathDB; FungiDB:YBR020W; -.
DR   eggNOG; KOG0631; Eukaryota.
DR   HOGENOM; CLU_017814_6_2_1; -.
DR   InParanoid; P04385; -.
DR   OMA; GFHDTYF; -.
DR   OrthoDB; 187738at2759; -.
DR   BioCyc; YEAST:YBR020W-MONOMER; -.
DR   UniPathway; UPA00214; -.
DR   BioGRID-ORCS; 852308; 1 hit in 10 CRISPR screens.
DR   EvolutionaryTrace; P04385; -.
DR   PRO; PR:P04385; -.
DR   Proteomes; UP000002311; Chromosome II.
DR   RNAct; P04385; protein.
DR   GO; GO:0005737; C:cytoplasm; IGI:SGD.
DR   GO; GO:0005667; C:transcription regulator complex; IPI:ComplexPortal.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0004335; F:galactokinase activity; IDA:SGD.
DR   GO; GO:0046835; P:carbohydrate phosphorylation; IDA:SGD.
DR   GO; GO:0033499; P:galactose catabolic process via UDP-galactose, Leloir pathway; IDA:SGD.
DR   GO; GO:0006012; P:galactose metabolic process; NAS:ComplexPortal.
DR   GO; GO:0000411; P:positive regulation of transcription by galactose; IGI:SGD.
DR   GO; GO:0000435; P:positive regulation of transcription from RNA polymerase II promoter by galactose; NAS:ComplexPortal.
DR   FunFam; 1.20.1440.340:FF:000003; GAL1p Galactokinase; 1.
DR   FunFam; 3.30.230.10:FF:000056; GAL1p Galactokinase; 1.
DR   Gene3D; 1.20.1440.340; -; 1.
DR   Gene3D; 3.30.230.10; -; 1.
DR   InterPro; IPR000705; Galactokinase.
DR   InterPro; IPR019741; Galactokinase_CS.
DR   InterPro; IPR019539; GalKase_N.
DR   InterPro; IPR013750; GHMP_kinase_C_dom.
DR   InterPro; IPR036554; GHMP_kinase_C_sf.
DR   InterPro; IPR006204; GHMP_kinase_N_dom.
DR   InterPro; IPR006203; GHMP_knse_ATP-bd_CS.
DR   InterPro; IPR006206; Mevalonate/galactokinase.
DR   InterPro; IPR020568; Ribosomal_Su5_D2-typ_SF.
DR   InterPro; IPR014721; Ribsml_uS5_D2-typ_fold_subgr.
DR   NCBIfam; TIGR00131; gal_kin; 1.
DR   PANTHER; PTHR10457:SF7; GALACTOKINASE-RELATED; 1.
DR   PANTHER; PTHR10457; MEVALONATE KINASE/GALACTOKINASE; 1.
DR   Pfam; PF10509; GalKase_gal_bdg; 1.
DR   Pfam; PF08544; GHMP_kinases_C; 1.
DR   Pfam; PF00288; GHMP_kinases_N; 1.
DR   PIRSF; PIRSF000530; Galactokinase; 1.
DR   PRINTS; PR00473; GALCTOKINASE.
DR   PRINTS; PR00959; MEVGALKINASE.
DR   SUPFAM; SSF55060; GHMP Kinase, C-terminal domain; 1.
DR   SUPFAM; SSF54211; Ribosomal protein S5 domain 2-like; 1.
DR   PROSITE; PS00106; GALACTOKINASE; 1.
DR   PROSITE; PS00627; GHMP_KINASES_ATP; 1.
DR   PDBsum; 2AJ4; -.
PE   1: Evidence at protein level;
KW   3D-structure; ATP-binding; Carbohydrate metabolism;
KW   Direct protein sequencing; Galactose metabolism; Kinase;
KW   Nucleotide-binding; Phosphoprotein; Reference proteome; Transferase.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:200486"
FT   CHAIN           2..528
FT                   /note="Galactokinase"
FT                   /id="PRO_0000184657"
FT   ACT_SITE        217
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:Q9HHB6"
FT   BINDING         53
FT                   /ligand="alpha-D-galactose"
FT                   /ligand_id="ChEBI:CHEBI:28061"
FT                   /evidence="ECO:0000269|PubMed:16115868,
FT                   ECO:0007744|PDB:2AJ4"
FT   BINDING         59
FT                   /ligand="alpha-D-galactose"
FT                   /ligand_id="ChEBI:CHEBI:28061"
FT                   /evidence="ECO:0000269|PubMed:16115868,
FT                   ECO:0007744|PDB:2AJ4"
FT   BINDING         60
FT                   /ligand="alpha-D-galactose"
FT                   /ligand_id="ChEBI:CHEBI:28061"
FT                   /evidence="ECO:0000269|PubMed:16115868,
FT                   ECO:0007744|PDB:2AJ4"
FT   BINDING         62
FT                   /ligand="alpha-D-galactose"
FT                   /ligand_id="ChEBI:CHEBI:28061"
FT                   /evidence="ECO:0000269|PubMed:16115868,
FT                   ECO:0007744|PDB:2AJ4"
FT   BINDING         165
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000269|PubMed:16115868,
FT                   ECO:0007744|PDB:2AJ4"
FT   BINDING         167
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000269|PubMed:16115868,
FT                   ECO:0007744|PDB:2AJ4"
FT   BINDING         169
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000269|PubMed:16115868,
FT                   ECO:0007744|PDB:2AJ4"
FT   BINDING         170
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000269|PubMed:16115868,
FT                   ECO:0007744|PDB:2AJ4"
FT   BINDING         213
FT                   /ligand="alpha-D-galactose"
FT                   /ligand_id="ChEBI:CHEBI:28061"
FT                   /evidence="ECO:0000269|PubMed:16115868,
FT                   ECO:0007744|PDB:2AJ4"
FT   BINDING         217
FT                   /ligand="alpha-D-galactose"
FT                   /ligand_id="ChEBI:CHEBI:28061"
FT                   /evidence="ECO:0000269|PubMed:16115868,
FT                   ECO:0007744|PDB:2AJ4"
FT   BINDING         264
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000269|PubMed:16115868,
FT                   ECO:0007744|PDB:2AJ4"
FT   BINDING         265
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000269|PubMed:16115868,
FT                   ECO:0007744|PDB:2AJ4"
FT   BINDING         266
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000269|PubMed:16115868,
FT                   ECO:0007744|PDB:2AJ4"
FT   BINDING         274
FT                   /ligand="alpha-D-galactose"
FT                   /ligand_id="ChEBI:CHEBI:28061"
FT                   /evidence="ECO:0000269|PubMed:16115868,
FT                   ECO:0007744|PDB:2AJ4"
FT   SITE            53
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000250|UniProtKB:Q9HHB6"
FT   MOD_RES         381
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19779198"
FT   CONFLICT        6
FT                   /note="S -> R (in Ref. 6; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        162
FT                   /note="V -> I (in Ref. 1; AAA34631)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        206..239
FT                   /note="EHYVGVNNGGMDQAASVCGEEDHALYVEFKPQLK -> DIMLVLTMAVWIRL
FT                   PLFAVRKIMLYTLSSNAVE (in Ref. 1; AAA34631)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        297
FT                   /note="L -> P (in Ref. 1; AAA34631)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        428
FT                   /note="A -> V (in Ref. 1; AAA34631)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        483
FT                   /note="N -> NN (in Ref. 1; AAA34631)"
FT                   /evidence="ECO:0000305"
FT   HELIX           23..40
FT                   /evidence="ECO:0007829|PDB:2AJ4"
FT   STRAND          45..57
FT                   /evidence="ECO:0007829|PDB:2AJ4"
FT   HELIX           62..64
FT                   /evidence="ECO:0007829|PDB:2AJ4"
FT   STRAND          68..84
FT                   /evidence="ECO:0007829|PDB:2AJ4"
FT   STRAND          90..97
FT                   /evidence="ECO:0007829|PDB:2AJ4"
FT   STRAND          103..106
FT                   /evidence="ECO:0007829|PDB:2AJ4"
FT   HELIX           112..115
FT                   /evidence="ECO:0007829|PDB:2AJ4"
FT   HELIX           123..141
FT                   /evidence="ECO:0007829|PDB:2AJ4"
FT   HELIX           143..146
FT                   /evidence="ECO:0007829|PDB:2AJ4"
FT   STRAND          147..149
FT                   /evidence="ECO:0007829|PDB:2AJ4"
FT   HELIX           150..152
FT                   /evidence="ECO:0007829|PDB:2AJ4"
FT   STRAND          153..160
FT                   /evidence="ECO:0007829|PDB:2AJ4"
FT   STRAND          166..168
FT                   /evidence="ECO:0007829|PDB:2AJ4"
FT   HELIX           170..187
FT                   /evidence="ECO:0007829|PDB:2AJ4"
FT   HELIX           195..202
FT                   /evidence="ECO:0007829|PDB:2AJ4"
FT   HELIX           205..209
FT                   /evidence="ECO:0007829|PDB:2AJ4"
FT   HELIX           216..223
FT                   /evidence="ECO:0007829|PDB:2AJ4"
FT   STRAND          229..233
FT                   /evidence="ECO:0007829|PDB:2AJ4"
FT   STRAND          235..237
FT                   /evidence="ECO:0007829|PDB:2AJ4"
FT   STRAND          239..243
FT                   /evidence="ECO:0007829|PDB:2AJ4"
FT   HELIX           244..247
FT                   /evidence="ECO:0007829|PDB:2AJ4"
FT   STRAND          252..259
FT                   /evidence="ECO:0007829|PDB:2AJ4"
FT   TURN            266..273
FT                   /evidence="ECO:0007829|PDB:2AJ4"
FT   HELIX           274..291
FT                   /evidence="ECO:0007829|PDB:2AJ4"
FT   HELIX           310..322
FT                   /evidence="ECO:0007829|PDB:2AJ4"
FT   HELIX           332..350
FT                   /evidence="ECO:0007829|PDB:2AJ4"
FT   HELIX           351..353
FT                   /evidence="ECO:0007829|PDB:2AJ4"
FT   HELIX           359..366
FT                   /evidence="ECO:0007829|PDB:2AJ4"
FT   HELIX           370..378
FT                   /evidence="ECO:0007829|PDB:2AJ4"
FT   STRAND          379..381
FT                   /evidence="ECO:0007829|PDB:2AJ4"
FT   HELIX           390..412
FT                   /evidence="ECO:0007829|PDB:2AJ4"
FT   HELIX           419..435
FT                   /evidence="ECO:0007829|PDB:2AJ4"
FT   HELIX           436..440
FT                   /evidence="ECO:0007829|PDB:2AJ4"
FT   HELIX           446..457
FT                   /evidence="ECO:0007829|PDB:2AJ4"
FT   STRAND          461..465
FT                   /evidence="ECO:0007829|PDB:2AJ4"
FT   STRAND          470..481
FT                   /evidence="ECO:0007829|PDB:2AJ4"
FT   HELIX           486..493
FT                   /evidence="ECO:0007829|PDB:2AJ4"
FT   HELIX           494..498
FT                   /evidence="ECO:0007829|PDB:2AJ4"
FT   HELIX           507..513
FT                   /evidence="ECO:0007829|PDB:2AJ4"
FT   STRAND          514..517
FT                   /evidence="ECO:0007829|PDB:2AJ4"
FT   STRAND          523..527
FT                   /evidence="ECO:0007829|PDB:2AJ4"
SQ   SEQUENCE   528 AA;  57944 MW;  1DA31A1915C19107 CRC64;
     MTKSHSEEVI VPEFNSSAKE LPRPLAEKCP SIIKKFISAY DAKPDFVARS PGRVNLIGEH
     IDYCDFSVLP LAIDFDMLCA VKVLNEKNPS ITLINADPKF AQRKFDLPLD GSYVTIDPSV
     SDWSNYFKCG LHVAHSFLKK LAPERFASAP LAGLQVFCEG DVPTGSGLSS SAAFICAVAL
     AVVKANMGPG YHMSKQNLMR ITVVAEHYVG VNNGGMDQAA SVCGEEDHAL YVEFKPQLKA
     TPFKFPQLKN HEISFVIANT LVVSNKFETA PTNYNLRVVE VTTAANVLAA TYGVVLLSGK
     EGSSTNKGNL RDFMNVYYAR YHNISTPWNG DIESGIERLT KMLVLVEESL ANKKQGFSVD
     DVAQSLNCSR EEFTRDYLTT SPVRFQVLKL YQRAKHVYSE SLRVLKAVKL MTTASFTADE
     DFFKQFGALM NESQASCDKL YECSCPEIDK ICSIALSNGS YGSRLTGAGW GGCTVHLVPG
     GPNGNIEKVK EALANEFYKV KYPKITDAEL ENAIIVSKPA LGSCLYEL
//