ID   HEM11_ARATH             Reviewed;         543 AA.
AC   P42804; Q0WWL6; Q9LQB9;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   03-APR-2002, sequence version 2.
DT   24-JAN-2024, entry version 183.
DE   RecName: Full=Glutamyl-tRNA reductase 1, chloroplastic;
DE            Short=GluTR;
DE            EC=1.2.1.70;
DE   Flags: Precursor;
GN   Name=HEMA1; Synonyms=HEMA; OrderedLocusNames=At1g58290;
GN   ORFNames=F19C14.9;
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 [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY,
RP   SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND INDUCTION.
RC   STRAIN=cv. Columbia; TISSUE=Leaf;
RX   PubMed=7908550; DOI=10.1105/tpc.6.2.265;
RA   Ilag L.L., Kumar A.M., Soell D.;
RT   "Light regulation of chlorophyll biosynthesis at the level of 5-
RT   aminolevulinate formation in Arabidopsis.";
RL   Plant Cell 6:265-275(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=11130712; DOI=10.1038/35048500;
RA   Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA   Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA   Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA   Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA   Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA   Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA   Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA   Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA   Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA   Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA   Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA   Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA   Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA   Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA   Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT   "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL   Nature 408:816-820(2000).
RN   [3]
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   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RA   Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA   Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA   Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA   Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA   Shinozaki K.;
RT   "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL   Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   INDUCTION BY LIGHT, AND TISSUE SPECIFICITY.
RX   PubMed=11309145; DOI=10.1046/j.1365-313x.2001.00986.x;
RA   McCormac A.C., Fischer A., Kumar A.M., Soll D., Terry M.J.;
RT   "Regulation of HEMA1 expression by phytochrome and a plastid signal during
RT   de-etiolation in Arabidopsis thaliana.";
RL   Plant J. 25:549-561(2001).
RN   [7]
RP   FUNCTION, TISSUE SPECIFICITY, AND INDUCTION BY LIGHT.
RX   PubMed=12139011; DOI=10.1023/a:1016081114758;
RA   Ujwal M.L., McCormac A.C., Goulding A., Kumar A.M., Soell D., Terry M.J.;
RT   "Divergent regulation of the HEMA gene family encoding glutamyl-tRNA
RT   reductase in Arabidopsis thaliana: expression of HEMA2 is regulated by
RT   sugars, but is independent of light and plastid signalling.";
RL   Plant Mol. Biol. 50:83-91(2002).
RN   [8]
RP   INTERACTION WITH FLU, ACTIVITY REGULATION, AND DOMAIN.
RC   STRAIN=cv. Landsberg erecta;
RX   PubMed=15584960; DOI=10.1111/j.1365-313x.2004.02262.x;
RA   Goslings D., Meskauskiene R., Kim C., Lee K.P., Nater M., Apel K.;
RT   "Concurrent interactions of heme and FLU with Glu tRNA reductase (HEMA1),
RT   the target of metabolic feedback inhibition of tetrapyrrole biosynthesis,
RT   in dark- and light-grown Arabidopsis plants.";
RL   Plant J. 40:957-967(2004).
RN   [9]
RP   INDUCTION BY LIGHT.
RX   PubMed=19380736; DOI=10.1073/pnas.0811684106;
RA   Stephenson P.G., Fankhauser C., Terry M.J.;
RT   "PIF3 is a repressor of chloroplast development.";
RL   Proc. Natl. Acad. Sci. U.S.A. 106:7654-7659(2009).
RN   [10]
RP   SUBCELLULAR LOCATION, AND INTERACTION WITH GLUTRBP.
RX   PubMed=22180625; DOI=10.1105/tpc.111.086421;
RA   Czarnecki O., Hedtke B., Melzer M., Rothbart M., Richter A., Schroter Y.,
RA   Pfannschmidt T., Grimm B.;
RT   "An Arabidopsis GluTR binding protein mediates spatial separation of 5-
RT   aminolevulinic acid synthesis in chloroplasts.";
RL   Plant Cell 23:4476-4491(2011).
RN   [11]
RP   SUBCELLULAR LOCATION, IDENTIFICATION IN THE FLU-CONTAINING CHLOROPLAST
RP   MEMBRANE COMPLEX, AND ACTIVITY REGULATION.
RX   PubMed=22212719; DOI=10.1016/j.febslet.2011.12.029;
RA   Kauss D., Bischof S., Steiner S., Apel K., Meskauskiene R.;
RT   "FLU, a negative feedback regulator of tetrapyrrole biosynthesis, is
RT   physically linked to the final steps of the Mg(++)-branch of this
RT   pathway.";
RL   FEBS Lett. 586:211-216(2012).
RN   [12]
RP   INTERACTION WITH CLPF.
RX   PubMed=26419670; DOI=10.1105/tpc.15.00574;
RA   Nishimura K., Apitz J., Friso G., Kim J., Ponnala L., Grimm B.,
RA   van Wijk K.J.;
RT   "Discovery of a unique Clp Component, ClpF, in chloroplasts: A proposed
RT   binary ClpF-ClpS1 adaptor complex functions in substrate recognition and
RT   delivery.";
RL   Plant Cell 27:2677-2691(2015).
RN   [13]
RP   X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS) OF 73-543, AND SUBUNIT.
RX   PubMed=24753615; DOI=10.1073/pnas.1400166111;
RA   Zhao A., Fang Y., Chen X., Zhao S., Dong W., Lin Y., Gong W., Liu L.;
RT   "Crystal structure of Arabidopsis glutamyl-tRNA reductase in complex with
RT   its stimulator protein.";
RL   Proc. Natl. Acad. Sci. U.S.A. 111:6630-6635(2014).
CC   -!- FUNCTION: Catalyzes the NADPH-dependent reduction of glutamyl-tRNA(Glu)
CC       to glutamate 1-semialdehyde (GSA). Probably involved in the
CC       tetrapyrrole synthesis required for the chlorophyll biosynthesis.
CC       {ECO:0000269|PubMed:12139011, ECO:0000269|PubMed:7908550}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(S)-4-amino-5-oxopentanoate + NADP(+) + tRNA(Glu) = H(+) + L-
CC         glutamyl-tRNA(Glu) + NADPH; Xref=Rhea:RHEA:12344, Rhea:RHEA-
CC         COMP:9663, Rhea:RHEA-COMP:9680, ChEBI:CHEBI:15378, ChEBI:CHEBI:57501,
CC         ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:78442,
CC         ChEBI:CHEBI:78520; EC=1.2.1.70;
CC         Evidence={ECO:0000269|PubMed:7908550};
CC   -!- ACTIVITY REGULATION: Negatively regulated by FLU and heme.
CC       {ECO:0000269|PubMed:15584960, ECO:0000269|PubMed:22212719}.
CC   -!- PATHWAY: Porphyrin-containing compound metabolism; chlorophyll
CC       biosynthesis.
CC   -!- PATHWAY: Porphyrin-containing compound metabolism; protoporphyrin-IX
CC       biosynthesis; 5-aminolevulinate from L-glutamyl-tRNA(Glu): step 1/2.
CC   -!- SUBUNIT: Part of the FLU-containing chloroplast membrane complex
CC       composed of FLU, CRD1, PORB, PORC, CHLP and HEMA1. Interacts (via C-
CC       terminus) with FLU, only in the absence of light. Interacts with
CC       GLUTRBP and forms a heterotetramer of two GLUTRBP and two HEMA1
CC       subunits. Interacts with CLPF (PubMed:26419670).
CC       {ECO:0000269|PubMed:15584960, ECO:0000269|PubMed:22180625,
CC       ECO:0000269|PubMed:22212719, ECO:0000269|PubMed:24753615,
CC       ECO:0000269|PubMed:26419670}.
CC   -!- INTERACTION:
CC       P42804; Q940U6: FLU; NbExp=3; IntAct=EBI-2319900, EBI-2319882;
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast membrane
CC       {ECO:0000269|PubMed:22180625, ECO:0000269|PubMed:22212719,
CC       ECO:0000269|PubMed:7908550}.
CC   -!- TISSUE SPECIFICITY: Strongly expressed in photosynthetic tissues.
CC       Detected in all tissues tested. {ECO:0000269|PubMed:11309145,
CC       ECO:0000269|PubMed:12139011, ECO:0000269|PubMed:7908550}.
CC   -!- INDUCTION: Circadian-regulation. Up-regulated by light.
CC       {ECO:0000269|PubMed:11309145, ECO:0000269|PubMed:12139011,
CC       ECO:0000269|PubMed:19380736, ECO:0000269|PubMed:7908550}.
CC   -!- DOMAIN: The N-terminus (65-92) is required for heme inhibition, but not
CC       for activity. {ECO:0000269|PubMed:15584960}.
CC   -!- MISCELLANEOUS: During catalysis, the active site Cys acts as a
CC       nucleophile attacking the alpha-carbonyl group of tRNA-bound glutamate
CC       with the formation of a thioester intermediate between enzyme and
CC       glutamate, and the concomitant release of tRNA(Glu). The thioester
CC       intermediate is finally reduced by direct hydride transfer from NADPH,
CC       to form the product GSA (By similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the glutamyl-tRNA reductase family.
CC       {ECO:0000305}.
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DR   EMBL; U03774; AAA19118.1; -; Genomic_DNA.
DR   EMBL; AC008051; AAF82258.1; -; Genomic_DNA.
DR   EMBL; CP002684; AEE33532.1; -; Genomic_DNA.
DR   EMBL; AY072223; AAL60044.1; -; mRNA.
DR   EMBL; AY096600; AAM20250.1; -; mRNA.
DR   EMBL; AK226332; BAE98482.1; -; mRNA.
DR   PIR; E96616; E96616.
DR   RefSeq; NP_176125.1; NM_104609.4.
DR   PDB; 4N7R; X-ray; 2.80 A; A/B=73-543.
DR   PDB; 4YVQ; X-ray; 2.40 A; A=440-543.
DR   PDB; 5CHE; X-ray; 3.20 A; A/B=73-543.
DR   PDB; 5YJL; X-ray; 2.70 A; A/B=73-543.
DR   PDBsum; 4N7R; -.
DR   PDBsum; 4YVQ; -.
DR   PDBsum; 5CHE; -.
DR   PDBsum; 5YJL; -.
DR   AlphaFoldDB; P42804; -.
DR   SMR; P42804; -.
DR   BioGRID; 27423; 5.
DR   IntAct; P42804; 4.
DR   MINT; P42804; -.
DR   STRING; 3702.P42804; -.
DR   PaxDb; 3702-AT1G58290-1; -.
DR   ProteomicsDB; 247356; -.
DR   EnsemblPlants; AT1G58290.1; AT1G58290.1; AT1G58290.
DR   GeneID; 842198; -.
DR   Gramene; AT1G58290.1; AT1G58290.1; AT1G58290.
DR   KEGG; ath:AT1G58290; -.
DR   Araport; AT1G58290; -.
DR   TAIR; AT1G58290; HEMA1.
DR   eggNOG; ENOG502QQ1H; Eukaryota.
DR   HOGENOM; CLU_035113_2_1_1; -.
DR   InParanoid; P42804; -.
DR   OMA; FAFKCAA; -.
DR   OrthoDB; 463at2759; -.
DR   PhylomeDB; P42804; -.
DR   BioCyc; ARA:AT1G58290-MONOMER; -.
DR   BioCyc; MetaCyc:AT1G58290-MONOMER; -.
DR   BRENDA; 1.2.1.70; 399.
DR   UniPathway; UPA00251; UER00316.
DR   UniPathway; UPA00668; -.
DR   PRO; PR:P42804; -.
DR   Proteomes; UP000006548; Chromosome 1.
DR   ExpressionAtlas; P42804; baseline and differential.
DR   GO; GO:0009507; C:chloroplast; TAS:TAIR.
DR   GO; GO:0031969; C:chloroplast membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0032991; C:protein-containing complex; IPI:TAIR.
DR   GO; GO:0008883; F:glutamyl-tRNA reductase activity; TAS:TAIR.
DR   GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR   GO; GO:0015995; P:chlorophyll biosynthetic process; IMP:TAIR.
DR   GO; GO:0006783; P:heme biosynthetic process; IMP:TAIR.
DR   GO; GO:0006782; P:protoporphyrinogen IX biosynthetic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd05213; NAD_bind_Glutamyl_tRNA_reduct; 1.
DR   Gene3D; 3.30.460.30; Glutamyl-tRNA reductase, N-terminal domain; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   HAMAP; MF_00087; Glu_tRNA_reductase; 1.
DR   InterPro; IPR000343; 4pyrrol_synth_GluRdtase.
DR   InterPro; IPR015896; 4pyrrol_synth_GluRdtase_dimer.
DR   InterPro; IPR015895; 4pyrrol_synth_GluRdtase_N.
DR   InterPro; IPR018214; GluRdtase_CS.
DR   InterPro; IPR036453; GluRdtase_dimer_dom_sf.
DR   InterPro; IPR036343; GluRdtase_N_sf.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR006151; Shikm_DH/Glu-tRNA_Rdtase.
DR   NCBIfam; TIGR01035; hemA; 1.
DR   PANTHER; PTHR43120; GLUTAMYL-TRNA REDUCTASE 1, CHLOROPLASTIC; 1.
DR   PANTHER; PTHR43120:SF1; GLUTAMYL-TRNA REDUCTASE 1, CHLOROPLASTIC; 1.
DR   Pfam; PF00745; GlutR_dimer; 1.
DR   Pfam; PF05201; GlutR_N; 1.
DR   Pfam; PF01488; Shikimate_DH; 1.
DR   SUPFAM; SSF69742; Glutamyl tRNA-reductase catalytic, N-terminal domain; 1.
DR   SUPFAM; SSF69075; Glutamyl tRNA-reductase dimerization domain; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR   PROSITE; PS00747; GLUTR; 1.
DR   Genevisible; P42804; AT.
PE   1: Evidence at protein level;
KW   3D-structure; Chlorophyll biosynthesis; Chloroplast; Membrane; NADP;
KW   Oxidoreductase; Plastid; Porphyrin biosynthesis; Reference proteome;
KW   Transit peptide.
FT   TRANSIT         1..61
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000305"
FT   CHAIN           62..543
FT                   /note="Glutamyl-tRNA reductase 1, chloroplastic"
FT                   /id="PRO_0000013307"
FT   REGION          20..44
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        20..38
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        144
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   BINDING         143..146
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         203
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         208..210
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         214
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         285..290
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250"
FT   SITE            193
FT                   /note="Important for activity"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        62
FT                   /note="E -> V (in Ref. 1; AAA19118)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        169
FT                   /note="K -> N (in Ref. 1; AAA19118)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        291
FT                   /note="K -> L (in Ref. 1; AAA19118)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        443
FT                   /note="V -> G (in Ref. 5; BAE98482)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        542
FT                   /note="Q -> H (in Ref. 1; AAA19118)"
FT                   /evidence="ECO:0000305"
FT   STRAND          96..103
FT                   /evidence="ECO:0007829|PDB:5YJL"
FT   TURN            104..106
FT                   /evidence="ECO:0007829|PDB:5YJL"
FT   HELIX           109..112
FT                   /evidence="ECO:0007829|PDB:5YJL"
FT   HELIX           113..115
FT                   /evidence="ECO:0007829|PDB:5CHE"
FT   HELIX           119..121
FT                   /evidence="ECO:0007829|PDB:5YJL"
FT   HELIX           122..131
FT                   /evidence="ECO:0007829|PDB:5YJL"
FT   STRAND          135..142
FT                   /evidence="ECO:0007829|PDB:5YJL"
FT   STRAND          144..155
FT                   /evidence="ECO:0007829|PDB:5YJL"
FT   HELIX           156..171
FT                   /evidence="ECO:0007829|PDB:5YJL"
FT   HELIX           175..181
FT                   /evidence="ECO:0007829|PDB:5YJL"
FT   STRAND          183..186
FT                   /evidence="ECO:0007829|PDB:5YJL"
FT   HELIX           188..199
FT                   /evidence="ECO:0007829|PDB:5YJL"
FT   STRAND          201..207
FT                   /evidence="ECO:0007829|PDB:5YJL"
FT   HELIX           212..222
FT                   /evidence="ECO:0007829|PDB:5YJL"
FT   STRAND          226..228
FT                   /evidence="ECO:0007829|PDB:5CHE"
FT   HELIX           230..250
FT                   /evidence="ECO:0007829|PDB:5YJL"
FT   HELIX           251..253
FT                   /evidence="ECO:0007829|PDB:5CHE"
FT   HELIX           255..270
FT                   /evidence="ECO:0007829|PDB:5YJL"
FT   STRAND          273..276
FT                   /evidence="ECO:0007829|PDB:4N7R"
FT   STRAND          281..284
FT                   /evidence="ECO:0007829|PDB:5YJL"
FT   HELIX           288..299
FT                   /evidence="ECO:0007829|PDB:5YJL"
FT   STRAND          304..310
FT                   /evidence="ECO:0007829|PDB:5YJL"
FT   HELIX           312..321
FT                   /evidence="ECO:0007829|PDB:5YJL"
FT   STRAND          325..331
FT                   /evidence="ECO:0007829|PDB:5YJL"
FT   HELIX           332..334
FT                   /evidence="ECO:0007829|PDB:5YJL"
FT   HELIX           335..340
FT                   /evidence="ECO:0007829|PDB:5YJL"
FT   STRAND          343..347
FT                   /evidence="ECO:0007829|PDB:5YJL"
FT   HELIX           358..362
FT                   /evidence="ECO:0007829|PDB:5YJL"
FT   HELIX           369..371
FT                   /evidence="ECO:0007829|PDB:5YJL"
FT   STRAND          375..379
FT                   /evidence="ECO:0007829|PDB:5YJL"
FT   HELIX           388..392
FT                   /evidence="ECO:0007829|PDB:5YJL"
FT   STRAND          396..399
FT                   /evidence="ECO:0007829|PDB:5YJL"
FT   HELIX           401..406
FT                   /evidence="ECO:0007829|PDB:5YJL"
FT   HELIX           412..415
FT                   /evidence="ECO:0007829|PDB:5YJL"
FT   HELIX           417..438
FT                   /evidence="ECO:0007829|PDB:5YJL"
FT   HELIX           440..442
FT                   /evidence="ECO:0007829|PDB:4YVQ"
FT   HELIX           443..466
FT                   /evidence="ECO:0007829|PDB:4YVQ"
FT   TURN            467..470
FT                   /evidence="ECO:0007829|PDB:4YVQ"
FT   HELIX           474..497
FT                   /evidence="ECO:0007829|PDB:4YVQ"
FT   HELIX           509..523
FT                   /evidence="ECO:0007829|PDB:4YVQ"
SQ   SEQUENCE   543 AA;  59515 MW;  04A095FEC96CC014 CRC64;
     MAVSSAFVGC PKLETLLNHH NLSPSSSSSS SVSQTPLGLN GVRVLPKNNR TRRGLIQKAR
     CELSASSDSA SNAASISALE QLKNSAADRY TKERSSIVVI GLSIHTAPVE MREKLAIPEA
     EWPRAIAELC GLNHIEEAAV LSTCNRMEIY VLALSQHRGV KEVTEWMSKT SGIPVSEICQ
     HRFLLYNKDA TQHIFEVSAG LDSLVLGEGQ ILAQVKQVVK VGQGVNGFGR NISGLFKHAI
     TVGKRVRTET NIASGAVSVS SAAVELALMK LPQSSNVSAR MCVIGAGKMG KLVIKHLMAK
     GCTKVVVVNR SEERVSAIRE EMPGIEIIYR PLDEMLACAS EADVVFTSTA SETPLFLKEH
     VENLPQASPE VGGLRHFVDI SVPRNVGSCV GEVETARVYN VDDLKEVVAA NKEDRMRKAM
     EAQTIITEES TQFEAWRDSL ETVPTIKKLR AYAERIRVAE LEKCMSKMGD DINKKTTRAV
     DDLSRGIVNR FLHGPMQHLR CDGSDSRTLS ETLENMHALN RMYGLEKDIL EEKLKAMAEQ
     QQK
//