FOL1_YEAST
ID FOL1_YEAST Reviewed; 824 AA.
AC P53848; D6W0T7; Q2VQX0;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 30-AUG-2005, sequence version 2.
DT 03-AUG-2022, entry version 193.
DE RecName: Full=Folic acid synthesis protein FOL1;
DE Includes:
DE RecName: Full=Dihydroneopterin aldolase {ECO:0000303|PubMed:15169867};
DE Short=DHNA {ECO:0000303|PubMed:15169867};
DE EC=4.1.2.25 {ECO:0000269|PubMed:15169867};
DE AltName: Full=7,8-dihydroneopterin aldolase;
DE AltName: Full=FASA;
DE AltName: Full=FASB;
DE Includes:
DE RecName: Full=6-hydroxymethyl-7,8-dihydropterin pyrophosphokinase;
DE Short=HPPK {ECO:0000303|PubMed:15169867};
DE EC=2.7.6.3 {ECO:0000269|PubMed:15169867};
DE AltName: Full=2-amino-4-hydroxy-6-hydroxymethyldihydropteridine pyrophosphokinase;
DE AltName: Full=7,8-dihydro-6-hydroxymethylpterin-pyrophosphokinase {ECO:0000303|PubMed:15169867};
DE Short=PPPK;
DE AltName: Full=FASC;
DE Includes:
DE RecName: Full=Dihydropteroate synthase {ECO:0000303|PubMed:15169867};
DE Short=DHPS {ECO:0000303|PubMed:15169867};
DE EC=2.5.1.15 {ECO:0000269|PubMed:15169867};
DE AltName: Full=Dihydropteroate pyrophosphorylase;
DE AltName: Full=FASD;
GN Name=FOL1 {ECO:0000303|PubMed:15169867}; OrderedLocusNames=YNL256W;
GN ORFNames=N0848;
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=ATCC 96604 / S288c / FY1679;
RX PubMed=9234673;
RX DOI=10.1002/(sici)1097-0061(199707)13:9<849::aid-yea106>3.0.co;2-n;
RA Sen-Gupta M., Gueldener U., Beinhauer J.D., Fiedler T.A., Hegemann J.H.;
RT "Sequence analysis of the 33 kb long region between ORC5 and SUI1 from the
RT left arm of chromosome XIV from Saccharomyces cerevisiae.";
RL Yeast 13:849-860(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169873;
RA Philippsen P., Kleine K., Poehlmann R., Duesterhoeft A., Hamberg K.,
RA Hegemann J.H., Obermaier B., Urrestarazu L.A., Aert R., Albermann K.,
RA Altmann R., Andre B., Baladron V., Ballesta J.P.G., Becam A.-M.,
RA Beinhauer J.D., Boskovic J., Buitrago M.J., Bussereau F., Coster F.,
RA Crouzet M., D'Angelo M., Dal Pero F., De Antoni A., del Rey F., Doignon F.,
RA Domdey H., Dubois E., Fiedler T.A., Fleig U., Floeth M., Fritz C.,
RA Gaillardin C., Garcia-Cantalejo J.M., Glansdorff N., Goffeau A.,
RA Gueldener U., Herbert C.J., Heumann K., Heuss-Neitzel D., Hilbert H.,
RA Hinni K., Iraqui Houssaini I., Jacquet M., Jimenez A., Jonniaux J.-L.,
RA Karpfinger-Hartl L., Lanfranchi G., Lepingle A., Levesque H., Lyck R.,
RA Maftahi M., Mallet L., Maurer C.T.C., Messenguy F., Mewes H.-W., Moestl D.,
RA Nasr F., Nicaud J.-M., Niedenthal R.K., Pandolfo D., Pierard A.,
RA Piravandi E., Planta R.J., Pohl T.M., Purnelle B., Rebischung C.,
RA Remacha M.A., Revuelta J.L., Rinke M., Saiz J.E., Sartorello F.,
RA Scherens B., Sen-Gupta M., Soler-Mira A., Urbanus J.H.M., Valle G.,
RA Van Dyck L., Verhasselt P., Vierendeels F., Vissers S., Voet M.,
RA Volckaert G., Wach A., Wambutt R., Wedler H., Zollner A., Hani J.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV and its
RT evolutionary implications.";
RL Nature 387:93-98(1997).
RN [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-85.
RC STRAIN=ATCC 208353 / W303-1A;
RX PubMed=15905473; DOI=10.1093/nar/gki583;
RA Zhang Z., Dietrich F.S.;
RT "Mapping of transcription start sites in Saccharomyces cerevisiae using 5'
RT SAGE.";
RL Nucleic Acids Res. 33:2838-2851(2005).
RN [5]
RP IDENTIFICATION OF PROBABLE INITIATION SITE.
RX PubMed=12748633; DOI=10.1038/nature01644;
RA Kellis M., Patterson N., Endrizzi M., Birren B.W., Lander E.S.;
RT "Sequencing and comparison of yeast species to identify genes and
RT regulatory elements.";
RL Nature 423:241-254(2003).
RN [6]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [7]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 76625 / YPH499;
RX PubMed=14576278; DOI=10.1073/pnas.2135385100;
RA Sickmann A., Reinders J., Wagner Y., Joppich C., Zahedi R.P., Meyer H.E.,
RA Schoenfisch B., Perschil I., Chacinska A., Guiard B., Rehling P.,
RA Pfanner N., Meisinger C.;
RT "The proteome of Saccharomyces cerevisiae mitochondria.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:13207-13212(2003).
RN [8]
RP FUNCTION, CATALYTIC ACTIVITY, AND SUBCELLULAR LOCATION.
RX PubMed=15169867; DOI=10.1091/mbc.e03-09-0680;
RA Gueldener U., Koehler G.J., Haussmann C., Bacher A., Kricke J., Becher D.,
RA Hegemann J.H.;
RT "Characterization of the Saccharomyces cerevisiae Fol1 protein: starvation
RT for C1 carrier induces pseudohyphal growth.";
RL Mol. Biol. Cell 15:3811-3828(2004).
RN [9]
RP INTERACTION WITH NAP1, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=18086883; DOI=10.1128/mcb.01035-07;
RA Calvert M.E.K., Keck K.M., Ptak C., Shabanowitz J., Hunt D.F.,
RA Pemberton L.F.;
RT "Phosphorylation by casein kinase 2 regulates Nap1 localization and
RT function.";
RL Mol. Cell. Biol. 28:1313-1325(2008).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-286, 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 [12]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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 [13]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 297-824 IN COMPLEX WITH
RP PTERIN-6-YL-METHYL-MONOPHOSPHATE, AND SUBUNIT.
RX PubMed=15826662; DOI=10.1016/j.jmb.2005.03.021;
RA Lawrence M.C., Iliades P., Fernley R.T., Berglez J., Pilling P.A.,
RA Macreadie I.G.;
RT "The three-dimensional structure of the bifunctional 6-hydroxymethyl-7,8-
RT dihydropterin pyrophosphokinase/dihydropteroate synthase of Saccharomyces
RT cerevisiae.";
RL J. Mol. Biol. 348:655-670(2005).
CC -!- FUNCTION: Catalyzes three sequential steps of tetrahydrofolate
CC biosynthesis. {ECO:0000269|PubMed:15169867}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=7,8-dihydroneopterin = 6-hydroxymethyl-7,8-dihydropterin +
CC glycolaldehyde; Xref=Rhea:RHEA:10540, ChEBI:CHEBI:17001,
CC ChEBI:CHEBI:17071, ChEBI:CHEBI:44841; EC=4.1.2.25;
CC Evidence={ECO:0000269|PubMed:15169867};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=6-hydroxymethyl-7,8-dihydropterin + ATP = (7,8-dihydropterin-
CC 6-yl)methyl diphosphate + AMP + H(+); Xref=Rhea:RHEA:11412,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:44841,
CC ChEBI:CHEBI:72950, ChEBI:CHEBI:456215; EC=2.7.6.3;
CC Evidence={ECO:0000269|PubMed:15169867};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(7,8-dihydropterin-6-yl)methyl diphosphate + 4-aminobenzoate =
CC 7,8-dihydropteroate + diphosphate; Xref=Rhea:RHEA:19949,
CC ChEBI:CHEBI:17836, ChEBI:CHEBI:17839, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:72950; EC=2.5.1.15;
CC Evidence={ECO:0000269|PubMed:15169867};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:P0AC13};
CC -!- PATHWAY: Cofactor biosynthesis; tetrahydrofolate biosynthesis; 2-amino-
CC 4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate from 7,8-
CC dihydroneopterin triphosphate: step 3/4.
CC -!- PATHWAY: Cofactor biosynthesis; tetrahydrofolate biosynthesis; 2-amino-
CC 4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate from 7,8-
CC dihydroneopterin triphosphate: step 4/4.
CC -!- PATHWAY: Cofactor biosynthesis; tetrahydrofolate biosynthesis; 7,8-
CC dihydrofolate from 2-amino-4-hydroxy-6-hydroxymethyl-7,8-
CC dihydropteridine diphosphate and 4-aminobenzoate: step 1/2.
CC -!- SUBUNIT: Homodimer. Interacts with NAP1. {ECO:0000269|PubMed:15826662,
CC ECO:0000269|PubMed:18086883}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion membrane
CC {ECO:0000269|PubMed:14576278, ECO:0000269|PubMed:15169867}.
CC -!- MISCELLANEOUS: Present with 4589 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the DHNA family.
CC {ECO:0000305}.
CC -!- SIMILARITY: In the central section; belongs to the HPPK family.
CC {ECO:0000305}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the DHPS family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA65488.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=CAA96163.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; X96722; CAA65488.1; ALT_INIT; Genomic_DNA.
DR EMBL; Z71532; CAA96163.1; ALT_INIT; Genomic_DNA.
DR EMBL; AY899248; AAX83933.1; -; mRNA.
DR EMBL; BK006947; DAA10303.1; -; Genomic_DNA.
DR PIR; S63229; S63229.
DR RefSeq; NP_014143.2; NM_001183094.1.
DR PDB; 2BMB; X-ray; 2.30 A; A=297-824.
DR PDBsum; 2BMB; -.
DR AlphaFoldDB; P53848; -.
DR SMR; P53848; -.
DR BioGRID; 35583; 11.
DR IntAct; P53848; 7.
DR MINT; P53848; -.
DR STRING; 4932.YNL256W; -.
DR DrugBank; DB00634; Sulfacetamide.
DR iPTMnet; P53848; -.
DR MaxQB; P53848; -.
DR PaxDb; P53848; -.
DR PRIDE; P53848; -.
DR EnsemblFungi; YNL256W_mRNA; YNL256W; YNL256W.
DR GeneID; 855465; -.
DR KEGG; sce:YNL256W; -.
DR SGD; S000005200; FOL1.
DR VEuPathDB; FungiDB:YNL256W; -.
DR eggNOG; KOG2544; Eukaryota.
DR HOGENOM; CLU_008023_2_0_1; -.
DR InParanoid; P53848; -.
DR OMA; LFESEPM; -.
DR BioCyc; YEAST:YNL256W-MON; -.
DR BRENDA; 2.5.1.15; 984.
DR BRENDA; 2.7.6.3; 984.
DR UniPathway; UPA00077; UER00154.
DR UniPathway; UPA00077; UER00155.
DR UniPathway; UPA00077; UER00156.
DR EvolutionaryTrace; P53848; -.
DR PRO; PR:P53848; -.
DR Proteomes; UP000002311; Chromosome XIV.
DR RNAct; P53848; protein.
DR GO; GO:0005737; C:cytoplasm; IDA:SGD.
DR GO; GO:0005740; C:mitochondrial envelope; IDA:SGD.
DR GO; GO:0031966; C:mitochondrial membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; HDA:SGD.
DR GO; GO:0003848; F:2-amino-4-hydroxy-6-hydroxymethyldihydropteridine diphosphokinase activity; IDA:SGD.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004150; F:dihydroneopterin aldolase activity; IDA:SGD.
DR GO; GO:0004156; F:dihydropteroate synthase activity; IDA:SGD.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0046656; P:folic acid biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0046654; P:tetrahydrofolate biosynthetic process; IMP:SGD.
DR CDD; cd00534; DHNA_DHNTPE; 2.
DR CDD; cd00739; DHPS; 1.
DR CDD; cd00483; HPPK; 1.
DR Gene3D; 3.20.20.20; -; 1.
DR Gene3D; 3.30.1130.10; -; 2.
DR Gene3D; 3.30.70.560; -; 1.
DR InterPro; IPR045031; DHP_synth.
DR InterPro; IPR006390; DHP_synth_dom.
DR InterPro; IPR011005; Dihydropteroate_synth-like.
DR InterPro; IPR006157; FolB_dom.
DR InterPro; IPR016261; Folic_acid_synth.
DR InterPro; IPR043133; GTP-CH-I_C/QueF.
DR InterPro; IPR000550; Hppk.
DR InterPro; IPR035907; Hppk_sf.
DR InterPro; IPR000489; Pterin-binding_dom.
DR PANTHER; PTHR20941; PTHR20941; 1.
DR Pfam; PF02152; FolB; 2.
DR Pfam; PF01288; HPPK; 1.
DR Pfam; PF00809; Pterin_bind; 1.
DR PIRSF; PIRSF000741; Folic_acid_synth; 1.
DR SMART; SM00905; FolB; 2.
DR SUPFAM; SSF51717; SSF51717; 1.
DR SUPFAM; SSF55083; SSF55083; 1.
DR TIGRFAMs; TIGR00526; folB_dom; 2.
DR TIGRFAMs; TIGR01498; folK; 1.
DR PROSITE; PS00792; DHPS_1; 1.
DR PROSITE; PS00793; DHPS_2; 1.
DR PROSITE; PS00794; HPPK; 1.
DR PROSITE; PS50972; PTERIN_BINDING; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; ATP-binding; Folate biosynthesis; Kinase; Lyase;
KW Magnesium; Membrane; Metal-binding; Mitochondrion; Multifunctional enzyme;
KW Nucleotide-binding; Phosphoprotein; Reference proteome; Transferase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22814378"
FT CHAIN 2..824
FT /note="Folic acid synthesis protein FOL1"
FT /id="PRO_0000168243"
FT DOMAIN 504..814
FT /note="Pterin-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00334"
FT REGION 22..144
FT /note="DHNA 1"
FT REGION 147..284
FT /note="DHNA 2"
FT REGION 295..466
FT /note="HPPK"
FT REGION 506..824
FT /note="DHPS"
FT BINDING 511
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P9WND1"
FT BINDING 558
FT /ligand="(7,8-dihydropterin-6-yl)methyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:72950"
FT /evidence="ECO:0000305|PubMed:15826662,
FT ECO:0007744|PDB:2BMB"
FT BINDING 596
FT /ligand="(7,8-dihydropterin-6-yl)methyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:72950"
FT /evidence="ECO:0000305|PubMed:15826662"
FT BINDING 615
FT /ligand="(7,8-dihydropterin-6-yl)methyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:72950"
FT /evidence="ECO:0000305|PubMed:15826662,
FT ECO:0007744|PDB:2BMB"
FT BINDING 715
FT /ligand="(7,8-dihydropterin-6-yl)methyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:72950"
FT /evidence="ECO:0000305|PubMed:15826662,
FT ECO:0007744|PDB:2BMB"
FT BINDING 767
FT /ligand="(7,8-dihydropterin-6-yl)methyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:72950"
FT /evidence="ECO:0000305|PubMed:15826662,
FT ECO:0007744|PDB:2BMB"
FT BINDING 802..804
FT /ligand="(7,8-dihydropterin-6-yl)methyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:72950"
FT /evidence="ECO:0000305|PubMed:15826662,
FT ECO:0007744|PDB:2BMB"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT MOD_RES 286
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT STRAND 298..306
FT /evidence="ECO:0007829|PDB:2BMB"
FT STRAND 308..310
FT /evidence="ECO:0007829|PDB:2BMB"
FT HELIX 311..324
FT /evidence="ECO:0007829|PDB:2BMB"
FT STRAND 328..333
FT /evidence="ECO:0007829|PDB:2BMB"
FT STRAND 336..339
FT /evidence="ECO:0007829|PDB:2BMB"
FT STRAND 350..361
FT /evidence="ECO:0007829|PDB:2BMB"
FT HELIX 363..377
FT /evidence="ECO:0007829|PDB:2BMB"
FT STRAND 392..399
FT /evidence="ECO:0007829|PDB:2BMB"
FT STRAND 414..416
FT /evidence="ECO:0007829|PDB:2BMB"
FT HELIX 420..422
FT /evidence="ECO:0007829|PDB:2BMB"
FT HELIX 424..430
FT /evidence="ECO:0007829|PDB:2BMB"
FT TURN 431..433
FT /evidence="ECO:0007829|PDB:2BMB"
FT TURN 441..443
FT /evidence="ECO:0007829|PDB:2BMB"
FT HELIX 447..456
FT /evidence="ECO:0007829|PDB:2BMB"
FT HELIX 460..462
FT /evidence="ECO:0007829|PDB:2BMB"
FT STRAND 464..470
FT /evidence="ECO:0007829|PDB:2BMB"
FT STRAND 479..487
FT /evidence="ECO:0007829|PDB:2BMB"
FT STRAND 498..500
FT /evidence="ECO:0007829|PDB:2BMB"
FT STRAND 505..511
FT /evidence="ECO:0007829|PDB:2BMB"
FT TURN 517..525
FT /evidence="ECO:0007829|PDB:2BMB"
FT HELIX 527..542
FT /evidence="ECO:0007829|PDB:2BMB"
FT STRAND 548..553
FT /evidence="ECO:0007829|PDB:2BMB"
FT HELIX 566..582
FT /evidence="ECO:0007829|PDB:2BMB"
FT STRAND 584..586
FT /evidence="ECO:0007829|PDB:2BMB"
FT HELIX 588..590
FT /evidence="ECO:0007829|PDB:2BMB"
FT STRAND 591..596
FT /evidence="ECO:0007829|PDB:2BMB"
FT HELIX 600..608
FT /evidence="ECO:0007829|PDB:2BMB"
FT STRAND 613..616
FT /evidence="ECO:0007829|PDB:2BMB"
FT TURN 617..620
FT /evidence="ECO:0007829|PDB:2BMB"
FT HELIX 626..631
FT /evidence="ECO:0007829|PDB:2BMB"
FT STRAND 636..641
FT /evidence="ECO:0007829|PDB:2BMB"
FT TURN 647..649
FT /evidence="ECO:0007829|PDB:2BMB"
FT HELIX 650..652
FT /evidence="ECO:0007829|PDB:2BMB"
FT TURN 660..664
FT /evidence="ECO:0007829|PDB:2BMB"
FT STRAND 665..670
FT /evidence="ECO:0007829|PDB:2BMB"
FT HELIX 675..677
FT /evidence="ECO:0007829|PDB:2BMB"
FT HELIX 681..684
FT /evidence="ECO:0007829|PDB:2BMB"
FT HELIX 686..704
FT /evidence="ECO:0007829|PDB:2BMB"
FT HELIX 709..711
FT /evidence="ECO:0007829|PDB:2BMB"
FT STRAND 712..715
FT /evidence="ECO:0007829|PDB:2BMB"
FT HELIX 724..732
FT /evidence="ECO:0007829|PDB:2BMB"
FT HELIX 734..737
FT /evidence="ECO:0007829|PDB:2BMB"
FT STRAND 740..746
FT /evidence="ECO:0007829|PDB:2BMB"
FT STRAND 749..754
FT /evidence="ECO:0007829|PDB:2BMB"
FT STRAND 760..762
FT /evidence="ECO:0007829|PDB:2BMB"
FT HELIX 768..774
FT /evidence="ECO:0007829|PDB:2BMB"
FT HELIX 779..782
FT /evidence="ECO:0007829|PDB:2BMB"
FT HELIX 783..795
FT /evidence="ECO:0007829|PDB:2BMB"
FT STRAND 799..804
FT /evidence="ECO:0007829|PDB:2BMB"
FT HELIX 806..821
FT /evidence="ECO:0007829|PDB:2BMB"
SQ SEQUENCE 824 AA; 93120 MW; D66986D8E2EB39E7 CRC64;
MSKLFSTVNS ARHSVPLGGM RDYVHIKKLE MNTVLGPDSW NQLMPQKCLL SLDMGTDFSK
SAATDDLKYS LNYAVISRDL TNFVSKKKNW GSVSNLAKSV SQFVMDKYSG VECLNLEVQA
DTTHIRSDHI SCIIQQERGN PESQEFDVVR ISELKMLTLI GVFTFERLKK QYVTLDIKLP
WPKKAELPPP VQSIIDNVVK FVEESNFKTV EALVESVSAV IAHNEYFQKF PDSPLVVKVL
KLNAITATEG VGVSCIREPR EIAMVNIPYL SSIHESSDIK FQLSSSQNTP IEGKNTWKRA
FLAFGSNIGD RFKHIQMALQ LLSREKTVKL RNISSIFESE PMYFKDQTPF MNGCVEVETL
LTPSELLKLC KKIEYEELQR VKHFDNGPRT IDLDIVMFLN SAGEDIIVNE PDLNIPHPRM
LERTFVLEPL CELISPVHLH PVTAEPIVDH LKQLYDKQHD EDTLWKLVPL PYRSGVEPRF
LKFKTATKLD EFTGETNRIT VSPTYIMAIF NATPDSFSDG GEHFADIESQ LNDIIKLCKD
ALYLHESVII DVGGCSTRPN SIQASEEEEI RRSIPLIKAI RESTELPQDK VILSIDTYRS
NVAKEAIKVG VDIINDISGG LFDSNMFAVI AENPEICYIL SHTRGDISTM NRLAHYENFA
LGDSIQQEFV HNTDIQQLDD LKDKTVLIRN VGQEIGERYI KAIDNGVKRW QILIDPGLGF
AKTWKQNLQI IRHIPILKNY SFTMNSNNSQ VYVNLRNMPV LLGPSRKKFI GHITKDVDAK
QRDFATGAVV ASCIGFGSDM VRVHDVKNCS KSIKLADAIY KGLE
