ID   P2C57_ARATH             Reviewed;         388 AA.
AC   P49599; Q3E9V3; Q3E9V4; Q9M0J6; Q9STP6;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   24-JAN-2001, sequence version 2.
DT   02-SEP-2026, entry version 184.
DE   RecName: Full=Protein phosphatase 2C 57 {ECO:0000303|PubMed:19021904};
DE            Short=AtPP2C57 {ECO:0000303|PubMed:19021904};
DE            EC=3.1.3.16 {ECO:0000269|PubMed:20126264};
DE   AltName: Full=Protein phosphatase 2C PPH1 {ECO:0000303|PubMed:15130549};
DE            Short=PP2C PPH1 {ECO:0000303|PubMed:15130549};
DE   AltName: Full=Thylakoid-associated phosphatase of 38 kDa {ECO:0000303|PubMed:20126264};
GN   Name=PPH1 {ECO:0000303|PubMed:15130549};
GN   Synonyms=PP2C57 {ECO:0000303|PubMed:19021904}, TAP38
GN   {ECO:0000303|PubMed:20126264};
GN   OrderedLocusNames=At4g27800 {ECO:0000312|Araport:AT4G27800};
GN   ORFNames=T27E11.40 {ECO:0000312|EMBL:CAB43968.1};
OS   Arabidopsis thaliana (Mouse-ear cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX   NCBI_TaxID=3702;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=10617198; DOI=10.1038/47134;
RA   Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA   Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA   Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA   de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA   Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA   Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA   Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA   Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA   Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA   Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA   Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA   Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA   Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA   Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA   Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA   Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA   Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA   Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA   Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA   Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA   Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA   Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA   Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA   Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA   Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA   Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA   Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA   de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA   Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA   Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA   Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA   Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA   Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA   Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA   Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA   Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA   Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA   O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA   Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA   Martienssen R., McCombie W.R.;
RT   "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL   Nature 402:769-777(1999).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Columbia;
RX   PubMed=27862469; DOI=10.1111/tpj.13415;
RA   Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA   Town C.D.;
RT   "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT   genome.";
RL   Plant J. 89:789-804(2017).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Columbia;
RG   The Arabidopsis Information Resource (TAIR);
RT   "Community-consensus reference genome of Arabidopsis thaliana Col-0.";
RL   Submitted (FEB-2026) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=cv. Columbia;
RX   PubMed=14593172; DOI=10.1126/science.1088305;
RA   Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA   Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA   Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA   Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA   Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA   Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA   Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA   Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA   Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA   Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA   Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA   Ecker J.R.;
RT   "Empirical analysis of transcriptional activity in the Arabidopsis
RT   genome.";
RL   Science 302:842-846(2003).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 1-365 (ISOFORM 1).
RC   STRAIN=cv. Columbia;
RX   PubMed=7569999; DOI=10.1126/science.270.5235.467;
RA   Schena M., Shalon D., Davis R.W., Brown P.O.;
RT   "Quantitative monitoring of gene expression patterns with a complementary
RT   DNA microarray.";
RL   Science 270:467-470(1995).
RN   [6]
RP   GENE FAMILY, AND NOMENCLATURE.
RX   PubMed=15130549; DOI=10.1016/j.tplants.2004.03.007;
RA   Schweighofer A., Hirt H., Meskiene I.;
RT   "Plant PP2C phosphatases: emerging functions in stress signaling.";
RL   Trends Plant Sci. 9:236-243(2004).
RN   [7]
RP   GENE FAMILY, AND NOMENCLATURE.
RX   PubMed=19021904; DOI=10.1186/1471-2164-9-550;
RA   Xue T., Wang D., Zhang S., Ehlting J., Ni F., Jacab S., Zheng C., Zhong Y.;
RT   "Genome-wide and expression analysis of protein phosphatase 2C in rice and
RT   Arabidopsis.";
RL   BMC Genomics 9:550-550(2008).
RN   [8]
RP   FUNCTION, AND CATALYTIC ACTIVITY.
RX   PubMed=20126264; DOI=10.1371/journal.pbio.1000288;
RA   Pribil M., Pesaresi P., Hertle A., Barbato R., Leister D.;
RT   "Role of plastid protein phosphatase TAP38 in LHCII dephosphorylation and
RT   thylakoid electron flow.";
RL   PLoS Biol. 8:e1000288-e1000288(2010).
RN   [9]
RP   FUNCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=20176943; DOI=10.1073/pnas.0913810107;
RA   Shapiguzov A., Ingelsson B., Samol I., Andres C., Kessler F., Rochaix J.D.,
RA   Vener A.V., Goldschmidt-Clermont M.;
RT   "The PPH1 phosphatase is specifically involved in LHCII dephosphorylation
RT   and state transitions in Arabidopsis.";
RL   Proc. Natl. Acad. Sci. U.S.A. 107:4782-4787(2010).
RN   [10]
RP   X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) OF 59-351 IN COMPLEX WITH MANGANESE
RP   IONS.
RX   PubMed=25888588; DOI=10.1105/tpc.15.00102;
RA   Wei X., Guo J., Li M., Liu Z.;
RT   "Structural mechanism underlying the specific recognition between the
RT   Arabidopsis state-transition phosphatase TAP38/PPH1 and phosphorylated
RT   light-harvesting complex protein Lhcb1.";
RL   Plant Cell 27:1113-1127(2015).
CC   -!- FUNCTION: [Isoform 2]: Protein phosphatase specifically required for
CC       efficient dephosphorylation of the light-harvesting complex II outer
CC       antennae (LCHII) and transition from state 2 to state 1
CC       (PubMed:20126264, PubMed:20176943). State transition plays a central
CC       role in response to environmental changes and allows to adjust to
CC       changing light conditions via the redistribution of light excitation
CC       energy between photosystem II (PSII) and photosystem I (PSI) in a short
CC       time by relocating LHCII proteins (Probable). Mainly responsible for
CC       the dephosphorylation of Lhcb1 and Lhcb2 but not of the photosystem II
CC       core proteins (PubMed:20176943). {ECO:0000269|PubMed:20126264,
CC       ECO:0000269|PubMed:20176943, ECO:0000305}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=O-phospho-L-seryl-[protein] + H2O = L-seryl-[protein] +
CC         phosphate; Xref=Rhea:RHEA:20629, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC         COMP:11604, ChEBI:CHEBI:15377, ChEBI:CHEBI:29999, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:83421; EC=3.1.3.16;
CC         Evidence={ECO:0000269|PubMed:20126264};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:20630;
CC         Evidence={ECO:0000269|PubMed:20126264};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=O-phospho-L-threonyl-[protein] + H2O = L-threonyl-[protein] +
CC         phosphate; Xref=Rhea:RHEA:47004, Rhea:RHEA-COMP:11060, Rhea:RHEA-
CC         COMP:11605, ChEBI:CHEBI:15377, ChEBI:CHEBI:30013, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:61977; EC=3.1.3.16;
CC         Evidence={ECO:0000269|PubMed:20126264};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47005;
CC         Evidence={ECO:0000269|PubMed:20126264};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000269|PubMed:25888588};
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000269|PubMed:25888588};
CC       Note=Binds 2 magnesium or manganese ions per subunit.
CC       {ECO:0000269|PubMed:25888588};
CC   -!- SUBCELLULAR LOCATION: [Isoform 1]: Membrane {ECO:0000255}; Single-pass
CC       membrane protein {ECO:0000305}.
CC   -!- SUBCELLULAR LOCATION: [Isoform 2]: Plastid, chloroplast stroma
CC       {ECO:0000269|PubMed:20176943}. Note=Associates with the stroma lamellae
CC       of the thylakoid membranes. {ECO:0000269|PubMed:20176943}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=P49599-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=P49599-2; Sequence=VSP_034837, VSP_034838;
CC       Name=3;
CC         IsoId=P49599-3; Sequence=VSP_034835, VSP_034836;
CC   -!- SIMILARITY: Belongs to the PP2C family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAA92889.1; Type=Frameshift; Evidence={ECO:0000305};
CC       Sequence=CAB43968.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AL078579; CAB43968.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AL161571; CAB81429.1; -; Genomic_DNA.
DR   EMBL; CP002687; AEE85393.1; -; Genomic_DNA.
DR   EMBL; CP002687; AEE85394.1; -; Genomic_DNA.
DR   EMBL; CP002687; AEE85395.1; -; Genomic_DNA.
DR   EMBL; OZ408686; CAO7048983.1; -; Genomic_DNA.
DR   EMBL; AY080875; AAL87346.1; -; mRNA.
DR   EMBL; AY114060; AAM45108.1; -; mRNA.
DR   EMBL; U34803; AAA92889.1; ALT_FRAME; mRNA.
DR   PIR; C85323; C85323.
DR   PIR; T09019; T09019.
DR   RefSeq; NP_194509.1; NM_118918.5. [P49599-1]
DR   RefSeq; NP_849459.1; NM_179128.2. [P49599-2]
DR   RefSeq; NP_849460.1; NM_179129.1. [P49599-3]
DR   PDB; 4YZG; X-ray; 1.60 A; A/B=59-351.
DR   PDB; 4YZH; X-ray; 2.00 A; A=59-351.
DR   AlphaFoldDB; P49599; -.
DR   SMR; P49599; -.
DR   FunCoup; P49599; 932.
DR   STRING; 3702.P49599; -.
DR   PaxDb; 3702-P49599; -.
DR   ProteomicsDB; 248723; -. [P49599-1]
DR   GeneID; 828893; -.
DR   KEGG; ath:AT4G27800; -.
DR   Araport; AT4G27800; -.
DR   TAIR; AT4G27800; TAP38.
DR   eggNOG; KOG0698; Eukaryota.
DR   HOGENOM; CLU_013173_1_0_1; -.
DR   InParanoid; P49599; -.
DR   OMA; WCHASAA; -.
DR   PhylomeDB; P49599; -.
DR   EvolutionaryTrace; P49599; -.
DR   PRO; PR:P49599; -.
DR   Proteomes; UP000006548; Chromosome 4.
DR   GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR   GO; GO:0009570; C:chloroplast stroma; IDA:TAIR.
DR   GO; GO:0005737; C:cytoplasm; HDA:TAIR.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005730; C:nucleolus; HDA:TAIR.
DR   GO; GO:0005634; C:nucleus; HDA:TAIR.
DR   GO; GO:0009579; C:thylakoid; IDA:TAIR.
DR   GO; GO:0000287; F:magnesium ion binding; IDA:UniProtKB.
DR   GO; GO:0030145; F:manganese ion binding; IDA:UniProtKB.
DR   GO; GO:0016791; F:phosphatase activity; IDA:TAIR.
DR   GO; GO:0004722; F:protein serine/threonine phosphatase activity; EXP:UniProtKB.
DR   GO; GO:0016311; P:dephosphorylation; IMP:TAIR.
DR   GO; GO:0009767; P:photosynthetic electron transport chain; IMP:TAIR.
DR   GO; GO:0080005; P:photosystem stoichiometry adjustment; IMP:TAIR.
DR   CDD; cd00143; PP2Cc; 1.
DR   FunFam; 3.60.40.10:FF:000049; Protein phosphatase 2C 57; 1.
DR   Gene3D; 3.60.40.10; PPM-type phosphatase domain; 1.
DR   InterPro; IPR015655; PP2C.
DR   InterPro; IPR000222; PP2C_BS.
DR   InterPro; IPR036457; PPM-type-like_dom_sf.
DR   InterPro; IPR001932; PPM-type_phosphatase-like_dom.
DR   PANTHER; PTHR13832:SF589; [PYRUVATE DEHYDROGENASE [ACETYL-TRANSFERRING]]-PHOSPHATASE 2, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR13832; PROTEIN PHOSPHATASE 2C; 1.
DR   Pfam; PF00481; PP2C; 1.
DR   SMART; SM00332; PP2Cc; 1.
DR   SUPFAM; SSF81606; PP2C-like; 1.
DR   PROSITE; PS01032; PPM_1; 1.
DR   PROSITE; PS51746; PPM_2; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Chloroplast; Hydrolase; Magnesium;
KW   Manganese; Membrane; Metal-binding; Plastid; Protein phosphatase;
KW   Reference proteome; Transmembrane; Transmembrane helix.
FT   CHAIN           1..388
FT                   /note="Protein phosphatase 2C 57"
FT                   /id="PRO_0000057768"
FT   TRANSMEM        363..383
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          59..348
FT                   /note="PPM-type phosphatase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01082"
FT   BINDING         93
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000269|PubMed:25888588,
FT                   ECO:0007744|PDB:4YZG"
FT   BINDING         93
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000269|PubMed:25888588,
FT                   ECO:0007744|PDB:4YZG"
FT   BINDING         94
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000269|PubMed:25888588,
FT                   ECO:0007744|PDB:4YZG"
FT   BINDING         296
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000269|PubMed:25888588,
FT                   ECO:0007744|PDB:4YZG"
FT   BINDING         339
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000269|PubMed:25888588,
FT                   ECO:0007744|PDB:4YZG"
FT   VAR_SEQ         323..326
FT                   /note="LACE -> ATCL (in isoform 3)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_034835"
FT   VAR_SEQ         327..388
FT                   /note="Missing (in isoform 3)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_034836"
FT   VAR_SEQ         334..335
FT                   /note="DR -> VK (in isoform 2)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_034837"
FT   VAR_SEQ         336..388
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_034838"
FT   CONFLICT        1..4
FT                   /note="MALL -> SNSS (in Ref. 5; AAA92889)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        69..70
FT                   /note="RD -> QY (in Ref. 5; AAA92889)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        271
FT                   /note="D -> N (in Ref. 5; AAA92889)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        353
FT                   /note="W -> C (in Ref. 5; AAA92889)"
FT                   /evidence="ECO:0000305"
FT   STRAND          59..65
FT                   /evidence="ECO:0007829|PDB:4YZG"
FT   STRAND          69..71
FT                   /evidence="ECO:0007829|PDB:4YZG"
FT   STRAND          74..81
FT                   /evidence="ECO:0007829|PDB:4YZG"
FT   TURN            82..85
FT                   /evidence="ECO:0007829|PDB:4YZG"
FT   STRAND          86..98
FT                   /evidence="ECO:0007829|PDB:4YZG"
FT   HELIX           99..115
FT                   /evidence="ECO:0007829|PDB:4YZG"
FT   HELIX           119..123
FT                   /evidence="ECO:0007829|PDB:4YZG"
FT   HELIX           127..151
FT                   /evidence="ECO:0007829|PDB:4YZG"
FT   STRAND          160..169
FT                   /evidence="ECO:0007829|PDB:4YZG"
FT   STRAND          172..180
FT                   /evidence="ECO:0007829|PDB:4YZG"
FT   STRAND          182..187
FT                   /evidence="ECO:0007829|PDB:4YZG"
FT   STRAND          190..193
FT                   /evidence="ECO:0007829|PDB:4YZG"
FT   STRAND          202..204
FT                   /evidence="ECO:0007829|PDB:4YZG"
FT   HELIX           205..216
FT                   /evidence="ECO:0007829|PDB:4YZG"
FT   TURN            227..229
FT                   /evidence="ECO:0007829|PDB:4YZG"
FT   HELIX           239..241
FT                   /evidence="ECO:0007829|PDB:4YZG"
FT   TURN            242..244
FT                   /evidence="ECO:0007829|PDB:4YZG"
FT   HELIX           245..254
FT                   /evidence="ECO:0007829|PDB:4YZG"
FT   HELIX           260..264
FT                   /evidence="ECO:0007829|PDB:4YZG"
FT   STRAND          272..274
FT                   /evidence="ECO:0007829|PDB:4YZG"
FT   STRAND          278..283
FT                   /evidence="ECO:0007829|PDB:4YZG"
FT   STRAND          288..294
FT                   /evidence="ECO:0007829|PDB:4YZG"
FT   HELIX           296..299
FT                   /evidence="ECO:0007829|PDB:4YZG"
FT   HELIX           304..318
FT                   /evidence="ECO:0007829|PDB:4YZG"
FT   HELIX           321..334
FT                   /evidence="ECO:0007829|PDB:4YZG"
FT   STRAND          341..347
FT                   /evidence="ECO:0007829|PDB:4YZG"
SQ   SEQUENCE   388 AA;  42719 MW;  496ECCC786AEB802 CRC64;
     MALLRPHLHR FHSNTLRHSA YPSADAGGGL VVYPTYGRHR CSAIAIDAPS SLTGVTPIRW
     GYTSVQGFRD EMEDDIVIRS DAVDSFSYAA VFDGHAGSSS VKFLREELYK ECVGALQAGS
     LLNGGDFAAI KEALIKAFES VDRNLLKWLE ANGDEEDESG STATVMIIRN DVSFIAHIGD
     SCAVLSRSGQ IEELTDYHRP YGSSRAAIQE VKRVKEAGGW IVNGRICGDI AVSRAFGDIR
     FKTKKNDMLK KGVDEGRWSE KFVSRIEFKG DMVVATPDIF QVPLTSDVEF IILASDGLWD
     YMKSSDVVSY VRDQLRKHGN VQLACESLAQ VALDRRSQDN ISIIIADLGR TEWKNLPAQR
     QNVVVELVQA ATTIGLVTVG IWMSSHLS
//