CYCR_BLAVI
ID CYCR_BLAVI Reviewed; 356 AA.
AC P07173; B8Y5U8; E2J7X6;
DT 01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1988, sequence version 1.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=Photosynthetic reaction center cytochrome c subunit {ECO:0000255|PIRNR:PIRNR000017};
DE AltName: Full=Cytochrome c558/c559;
DE Flags: Precursor;
GN Name=pufC {ECO:0000312|EMBL:ACK86664.1, ECO:0000312|EMBL:ADN94690.1};
GN Synonyms=cytC; ORFNames=BVIRIDIS_00500 {ECO:0000312|EMBL:CUU41065.1};
OS Blastochloris viridis (Rhodopseudomonas viridis).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Blastochloridaceae; Blastochloris.
OX NCBI_TaxID=1079;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE.
RC STRAIN=ATCC 19567 / DSM 133 / F;
RX PubMed=16453786; DOI=10.1002/j.1460-2075.1987.tb02490.x;
RA Weyer K.A., Lottspeich F., Lang F., Oesterhelt D., Michel H.;
RT "Amino acid sequence of the cytochrome subunit of the photosynthetic
RT reaction centre from the purple bacterium Rhodopseudomonas viridis.";
RL EMBO J. 6:2197-2202(1987).
RN [2] {ECO:0000312|EMBL:ADN94690.1, ECO:0007744|PDB:3T6D, ECO:0007744|PDB:3T6E}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], X-RAY CRYSTALLOGRAPHY (1.92 ANGSTROMS)
RP OF WILD-TYPE AND MUTANT
RP PRO-63/MET-97/GLU-104/SER-272/THR-275/MET-297/307-THR-VAL-308/GLN-343 IN
RP COMPLEXES WITH HEME; PHOTOSYNTHETIC REACTION CENTER SUBUNITS PUFL; PUFM AND
RP PUHA, DIACYLGLYCEROL AT CYS-21, AND LACK OF PALMITOYLATION AT CYS-21.
RC STRAIN=ATCC 19567 / DSM 133 / F {ECO:0000312|EMBL:ADN94690.1};
RX PubMed=22054235; DOI=10.1042/bj20111540;
RA Roszak A.W., Moulisova V., Reksodipuro A.D., Gardiner A.T., Fujii R.,
RA Hashimoto H., Isaacs N.W., Cogdell R.J.;
RT "New insights into the structure of the reaction centre from Blastochloris
RT viridis: evolution in the laboratory.";
RL Biochem. J. 442:27-37(2012).
RN [3] {ECO:0000312|EMBL:CUU41065.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 19567 / DSM 133 / F {ECO:0000303|PubMed:26798090};
RX PubMed=26798090; DOI=10.1128/genomea.01520-15;
RA Liu L.N., Faulkner M., Liu X., Huang F., Darby A.C., Hall N.;
RT "Revised genome sequence of the purple photosynthetic bacterium
RT Blastochloris viridis.";
RL Genome Announc. 4:0-0(2016).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-46, DIACYLGLYCEROL AT CYS-21, AND
RP LACK OF PALMITOYLATION AT CYS-21.
RA Weyer K.A., Schaefer W., Lottspeich F., Michel H.;
RT "The cytochrome subunit of the photosynthetic reaction center from
RT Rhodopseudomonas viridis is a lipoprotein.";
RL Biochemistry 26:2909-2914(1987).
RN [5]
RP FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, PTM, DISRUPTION PHENOTYPE, AND
RP MUTAGENESIS OF ARG-284.
RX PubMed=10736158; DOI=10.1021/bi992443p;
RA Chen I.P., Mathis P., Koepke J., Michel H.;
RT "Uphill electron transfer in the tetraheme cytochrome subunit of the
RT Rhodopseudomonas viridis photosynthetic reaction center: evidence from
RT site-directed mutagenesis.";
RL Biochemistry 39:3592-3602(2000).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (3 ANGSTROMS) IN COMPLEX WITH HEME; PHOTOSYNTHETIC
RP REACTION CENTER SUBUNITS PUFL; PUFM AND PUHA.
RX PubMed=6392571; DOI=10.1016/s0022-2836(84)80011-x;
RA Deisenhofer J., Epp O., Miki K., Huber R., Michel H.;
RT "X-ray structure analysis of a membrane protein complex. Electron density
RT map at 3-A resolution and a model of the chromophores of the photosynthetic
RT reaction center from Rhodopseudomonas viridis.";
RL J. Mol. Biol. 180:385-398(1984).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (3 ANGSTROMS) IN COMPLEX WITH HEME; PHOTOSYNTHETIC
RP REACTION CENTER SUBUNITS PUFL; PUFM AND PUHA.
RA Deisenhofer J., Epp O., Miki K., Huber R., Michel H.;
RT "Structure of the protein subunits in the photosynthetic reaction centre of
RT Rhodopseudomonas viridis at 3-A resolution.";
RL Nature 318:618-624(1985).
RN [8] {ECO:0007744|PDB:2PRC, ECO:0007744|PDB:3PRC}
RP X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS)OF 21-356 IN COMPLEXES WITH HEME;
RP PHOTOSYNTHETIC REACTION CENTER SUBUNITS PUFL; PUFM AND PUHA, AND
RP SUBCELLULAR LOCATION.
RC STRAIN=ATCC 19567 / DSM 133 / F {ECO:0000303|PubMed:9351808};
RX PubMed=9351808; DOI=10.1016/s0969-2126(97)00285-2;
RA Lancaster C.R.D., Michel H.;
RT "The coupling of light-induced electron transfer and proton uptake as
RT derived from crystal structures of reaction centres from Rhodopseudomonas
RT viridis modified at the binding site of the secondary quinone, QB.";
RL Structure 5:1339-1359(1997).
RN [9] {ECO:0007744|PDB:5PRC, ECO:0007744|PDB:6PRC, ECO:0007744|PDB:7PRC}
RP X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 21-356 IN COMPLEXES WITH HEME;
RP PHOTOSYNTHETIC REACTION CENTER SUBUNITS PUFL; PUFM AND PUHA, AND
RP SUBCELLULAR LOCATION.
RC STRAIN=ATCC 19567 / DSM 133 / F {ECO:0000303|PubMed:10024457};
RX PubMed=10024457; DOI=10.1006/jmbi.1998.2532;
RA Lancaster C.R.D., Michel H.;
RT "Refined crystal structures of reaction centres from Rhodopseudomonas
RT viridis in complexes with the herbicide atrazine and two chiral atrazine
RT derivatives also lead to a new model of the bound carotenoid.";
RL J. Mol. Biol. 286:883-898(1999).
CC -!- FUNCTION: The reaction center of purple bacteria contains a tightly
CC bound cytochrome molecule which re-reduces the photo oxidized primary
CC electron donor. {ECO:0000269|PubMed:10736158}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Redox potential:
CC E(0) is -60 mV for heme 1. E(0) is +320 mV for heme 2. E(0) is +380
CC mV for heme 3. E(0) is +15 mV for heme 4.
CC {ECO:0000269|PubMed:10736158};
CC -!- SUBUNIT: Component of the photosynthetic reaction center composed of
CC protein subunits L (PufL), M (PufM), H (PuhA) and cytochrome C (PufC).
CC {ECO:0000269|PubMed:10024457, ECO:0000269|PubMed:22054235,
CC ECO:0000269|PubMed:6392571, ECO:0000269|PubMed:9351808,
CC ECO:0000269|Ref.7}.
CC -!- SUBCELLULAR LOCATION: Cellular chromatophore membrane
CC {ECO:0000269|PubMed:10024457, ECO:0000269|PubMed:9351808}; Lipid-anchor
CC {ECO:0000269|PubMed:22054235, ECO:0000269|Ref.4}.
CC -!- PTM: Binds 4 heme groups per subunit. {ECO:0000269|PubMed:10024457,
CC ECO:0000269|PubMed:10736158, ECO:0000269|PubMed:22054235,
CC ECO:0000269|PubMed:6392571, ECO:0000269|PubMed:9351808,
CC ECO:0000269|Ref.7}.
CC -!- PTM: After the signal sequence is removed, the N-terminal cysteine is
CC modified to form a diacylglyceride thioether, but the alpha-amino group
CC is free and is not N-palmitoylated. {ECO:0000269|PubMed:22054235,
CC ECO:0000269|Ref.4}.
CC -!- DISRUPTION PHENOTYPE: Lack of photosynthesis.
CC {ECO:0000269|PubMed:10736158}.
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DR EMBL; X05768; CAA29223.1; -; Genomic_DNA.
DR EMBL; FJ483785; ACK86664.1; -; Genomic_DNA.
DR EMBL; HQ009849; ADN94690.1; -; Genomic_DNA.
DR EMBL; LN907867; CUU41065.1; -; Genomic_DNA.
DR EMBL; M16317; AAA26093.1; -; Genomic_DNA.
DR PIR; S00139; S00139.
DR PDB; 1DXR; X-ray; 2.00 A; C=21-356.
DR PDB; 1PRC; X-ray; 2.30 A; C=21-356.
DR PDB; 1R2C; X-ray; 2.86 A; C=21-356.
DR PDB; 1VRN; X-ray; 2.20 A; C=21-352.
DR PDB; 2I5N; X-ray; 1.96 A; C=21-356.
DR PDB; 2JBL; X-ray; 2.40 A; C=1-356.
DR PDB; 2PRC; X-ray; 2.45 A; C=21-356.
DR PDB; 2WJM; X-ray; 1.95 A; C=21-356.
DR PDB; 2WJN; X-ray; 1.86 A; C=21-356.
DR PDB; 2X5U; X-ray; 3.00 A; C=21-356.
DR PDB; 2X5V; X-ray; 3.00 A; C=21-356.
DR PDB; 3D38; X-ray; 3.21 A; C=21-356.
DR PDB; 3G7F; X-ray; 2.50 A; C=21-356.
DR PDB; 3PRC; X-ray; 2.40 A; C=21-356.
DR PDB; 3T6D; X-ray; 1.95 A; C=1-356.
DR PDB; 3T6E; X-ray; 1.92 A; C=1-356.
DR PDB; 4AC5; X-ray; 8.20 A; C=21-356.
DR PDB; 4CAS; X-ray; 3.50 A; A=1-356.
DR PDB; 5M7J; X-ray; 3.50 A; A=1-356.
DR PDB; 5M7K; X-ray; 3.50 A; A=1-356.
DR PDB; 5M7L; X-ray; 3.60 A; A=1-356.
DR PDB; 5NJ4; X-ray; 2.40 A; C=21-356.
DR PDB; 5O4C; X-ray; 2.80 A; C=21-356.
DR PDB; 5O64; X-ray; 3.30 A; C=21-356.
DR PDB; 5PRC; X-ray; 2.35 A; C=21-356.
DR PDB; 6ET5; EM; 3.00 A; C=21-353.
DR PDB; 6PRC; X-ray; 2.30 A; C=21-356.
DR PDB; 6ZHW; X-ray; 2.80 A; C=21-356.
DR PDB; 6ZI4; X-ray; 2.80 A; C=21-356.
DR PDB; 6ZI5; X-ray; 2.80 A; C=21-356.
DR PDB; 6ZI6; X-ray; 2.80 A; C=21-356.
DR PDB; 6ZI9; X-ray; 2.80 A; C=21-356.
DR PDB; 6ZIA; X-ray; 2.80 A; C=21-356.
DR PDB; 6ZID; X-ray; 2.80 A; C=21-356.
DR PDB; 7PRC; X-ray; 2.65 A; C=21-356.
DR PDBsum; 1DXR; -.
DR PDBsum; 1PRC; -.
DR PDBsum; 1R2C; -.
DR PDBsum; 1VRN; -.
DR PDBsum; 2I5N; -.
DR PDBsum; 2JBL; -.
DR PDBsum; 2PRC; -.
DR PDBsum; 2WJM; -.
DR PDBsum; 2WJN; -.
DR PDBsum; 2X5U; -.
DR PDBsum; 2X5V; -.
DR PDBsum; 3D38; -.
DR PDBsum; 3G7F; -.
DR PDBsum; 3PRC; -.
DR PDBsum; 3T6D; -.
DR PDBsum; 3T6E; -.
DR PDBsum; 4AC5; -.
DR PDBsum; 4CAS; -.
DR PDBsum; 5M7J; -.
DR PDBsum; 5M7K; -.
DR PDBsum; 5M7L; -.
DR PDBsum; 5NJ4; -.
DR PDBsum; 5O4C; -.
DR PDBsum; 5O64; -.
DR PDBsum; 5PRC; -.
DR PDBsum; 6ET5; -.
DR PDBsum; 6PRC; -.
DR PDBsum; 6ZHW; -.
DR PDBsum; 6ZI4; -.
DR PDBsum; 6ZI5; -.
DR PDBsum; 6ZI6; -.
DR PDBsum; 6ZI9; -.
DR PDBsum; 6ZIA; -.
DR PDBsum; 6ZID; -.
DR PDBsum; 7PRC; -.
DR AlphaFoldDB; P07173; -.
DR SMR; P07173; -.
DR IntAct; P07173; 6.
DR STRING; 1079.BVIR_606; -.
DR DrugBank; DB07552; (2R)-2-{[4-chloro-6-(ethylamino)-1,3,5-triazin-2-yl]amino}-2-methylbutanenitrile.
DR DrugBank; DB07551; (2S)-2-{[4-chloro-6-(ethylamino)-1,3,5-triazin-2-yl]amino}-2-methylbutanenitrile.
DR DrugBank; DB07392; Atrazine.
DR DrugBank; DB04147; Dodecyldimethylamine N-oxide.
DR DrugBank; DB04464; N-Formylmethionine.
DR DrugBank; DB08215; Terbutryn.
DR DrugBank; DB08689; Ubiquinone Q1.
DR DrugBank; DB08690; Ubiquinone Q2.
DR EnsemblBacteria; CUU41065; CUU41065; BVIRIDIS_00500.
DR KEGG; bvr:BVIR_606; -.
DR PATRIC; fig|1079.6.peg.623; -.
DR OMA; CTYCHNT; -.
DR EvolutionaryTrace; P07173; -.
DR Proteomes; UP000065734; Chromosome I.
DR GO; GO:0030077; C:plasma membrane light-harvesting complex; IEA:InterPro.
DR GO; GO:0042717; C:plasma membrane-derived chromatophore membrane; IDA:UniProtKB.
DR GO; GO:0009055; F:electron transfer activity; IEA:InterPro.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0015979; P:photosynthesis; IMP:UniProtKB.
DR GO; GO:0019684; P:photosynthesis, light reaction; IEA:InterPro.
DR CDD; cd09224; CytoC_RC; 1.
DR Gene3D; 1.10.468.10; -; 2.
DR InterPro; IPR023119; Multihaem_cyt_PRC_cyt_su-like.
DR InterPro; IPR036280; Multihaem_cyt_sf.
DR InterPro; IPR003158; Photosyn_RC_cyt_c-su.
DR Pfam; PF02276; CytoC_RC; 1.
DR PIRSF; PIRSF000017; RC_cytochrome; 1.
DR SUPFAM; SSF48695; SSF48695; 1.
DR PROSITE; PS51008; MULTIHEME_CYTC; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Electron transport; Heme; Iron;
KW Lipoprotein; Membrane; Metal-binding; Photosynthesis; Reaction center;
KW Reference proteome; Signal; Transport.
FT SIGNAL 1..20
FT CHAIN 21..356
FT /note="Photosynthetic reaction center cytochrome c subunit"
FT /id="PRO_0000006551"
FT BINDING 94
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="1"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000269|PubMed:22054235,
FT ECO:0007744|PDB:3T6E"
FT BINDING 107
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="1"
FT /note="covalent"
FT /evidence="ECO:0000269|PubMed:22054235,
FT ECO:0007744|PDB:3T6E"
FT BINDING 110
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="1"
FT /note="covalent"
FT /evidence="ECO:0000269|PubMed:22054235,
FT ECO:0007744|PDB:3T6E"
FT BINDING 111
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="1"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000269|PubMed:22054235,
FT ECO:0007744|PDB:3T6E"
FT BINDING 130
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="2"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000269|PubMed:22054235,
FT ECO:0007744|PDB:3T6E"
FT BINDING 144
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="4"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000269|PubMed:22054235,
FT ECO:0007744|PDB:3T6E"
FT BINDING 152
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="2"
FT /note="covalent"
FT /evidence="ECO:0000269|PubMed:22054235,
FT ECO:0007744|PDB:3T6E"
FT BINDING 155
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="2"
FT /note="covalent"
FT /evidence="ECO:0000269|PubMed:22054235,
FT ECO:0007744|PDB:3T6E"
FT BINDING 156
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="2"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000269|PubMed:22054235,
FT ECO:0007744|PDB:3T6E"
FT BINDING 253
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="3"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000269|PubMed:22054235,
FT ECO:0007744|PDB:3T6E"
FT BINDING 264
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="3"
FT /note="covalent"
FT /evidence="ECO:0000269|PubMed:22054235,
FT ECO:0007744|PDB:3T6E"
FT BINDING 267
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="3"
FT /note="covalent"
FT /evidence="ECO:0000269|PubMed:22054235,
FT ECO:0007744|PDB:3T6E"
FT BINDING 268
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="3"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000269|PubMed:22054235,
FT ECO:0007744|PDB:3T6E"
FT BINDING 325
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="4"
FT /note="covalent"
FT /evidence="ECO:0000269|PubMed:22054235,
FT ECO:0007744|PDB:3T6E"
FT BINDING 328
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="4"
FT /note="covalent"
FT /evidence="ECO:0000269|PubMed:22054235,
FT ECO:0007744|PDB:3T6E"
FT BINDING 329
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="4"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000269|PubMed:22054235,
FT ECO:0007744|PDB:3T6E"
FT SITE 21
FT /note="Not N-palmitoylated"
FT /evidence="ECO:0000269|PubMed:22054235, ECO:0000269|Ref.4,
FT ECO:0007744|PDB:3T6E"
FT LIPID 21
FT /note="S-diacylglycerol cysteine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303,
FT ECO:0000269|PubMed:22054235, ECO:0000269|Ref.4,
FT ECO:0007744|PDB:3T6E"
FT MUTAGEN 284
FT /note="R->K: 110 mV decrease in redox potential of heme 3."
FT /evidence="ECO:0000269|PubMed:10736158"
FT CONFLICT 63
FT /note="A -> P (in Ref. 2; ACK86664)"
FT /evidence="ECO:0000305"
FT CONFLICT 97
FT /note="I -> M (in Ref. 2; ACK86664)"
FT /evidence="ECO:0000305"
FT CONFLICT 104
FT /note="Q -> E (in Ref. 2; ACK86664)"
FT /evidence="ECO:0000305"
FT CONFLICT 272
FT /note="T -> S (in Ref. 2; ACK86664)"
FT /evidence="ECO:0000305"
FT CONFLICT 275
FT /note="S -> T (in Ref. 2; ACK86664)"
FT /evidence="ECO:0000305"
FT CONFLICT 297
FT /note="L -> M (in Ref. 2; ACK86664)"
FT /evidence="ECO:0000305"
FT CONFLICT 307..308
FT /note="AS -> TV (in Ref. 2; ACK86664)"
FT /evidence="ECO:0000305"
FT CONFLICT 343
FT /note="K -> Q (in Ref. 2; ACK86664)"
FT /evidence="ECO:0000305"
FT HELIX 45..55
FT /evidence="ECO:0007829|PDB:2WJN"
FT STRAND 69..71
FT /evidence="ECO:0007829|PDB:3T6D"
FT HELIX 72..75
FT /evidence="ECO:0007829|PDB:2WJN"
FT STRAND 76..78
FT /evidence="ECO:0007829|PDB:2WJN"
FT STRAND 80..82
FT /evidence="ECO:0007829|PDB:2WJN"
FT HELIX 87..101
FT /evidence="ECO:0007829|PDB:2WJN"
FT TURN 103..105
FT /evidence="ECO:0007829|PDB:2WJN"
FT HELIX 106..109
FT /evidence="ECO:0007829|PDB:2WJN"
FT HELIX 122..140
FT /evidence="ECO:0007829|PDB:2WJN"
FT HELIX 142..145
FT /evidence="ECO:0007829|PDB:2WJN"
FT TURN 146..148
FT /evidence="ECO:0007829|PDB:2WJN"
FT HELIX 152..156
FT /evidence="ECO:0007829|PDB:2WJN"
FT STRAND 159..161
FT /evidence="ECO:0007829|PDB:2WJN"
FT STRAND 172..175
FT /evidence="ECO:0007829|PDB:2WJN"
FT TURN 182..184
FT /evidence="ECO:0007829|PDB:2WJN"
FT STRAND 185..187
FT /evidence="ECO:0007829|PDB:5O64"
FT HELIX 189..191
FT /evidence="ECO:0007829|PDB:2WJN"
FT HELIX 192..197
FT /evidence="ECO:0007829|PDB:2WJN"
FT TURN 198..202
FT /evidence="ECO:0007829|PDB:2WJN"
FT HELIX 209..213
FT /evidence="ECO:0007829|PDB:2WJN"
FT STRAND 215..217
FT /evidence="ECO:0007829|PDB:3T6E"
FT STRAND 226..229
FT /evidence="ECO:0007829|PDB:2WJN"
FT STRAND 234..236
FT /evidence="ECO:0007829|PDB:2WJN"
FT HELIX 237..239
FT /evidence="ECO:0007829|PDB:2WJN"
FT HELIX 244..260
FT /evidence="ECO:0007829|PDB:2WJN"
FT HELIX 264..266
FT /evidence="ECO:0007829|PDB:2WJN"
FT HELIX 270..272
FT /evidence="ECO:0007829|PDB:2WJN"
FT HELIX 282..300
FT /evidence="ECO:0007829|PDB:2WJN"
FT HELIX 303..307
FT /evidence="ECO:0007829|PDB:2WJN"
FT HELIX 311..313
FT /evidence="ECO:0007829|PDB:2WJN"
FT HELIX 325..329
FT /evidence="ECO:0007829|PDB:2WJN"
FT STRAND 332..334
FT /evidence="ECO:0007829|PDB:2WJN"
FT HELIX 335..338
FT /evidence="ECO:0007829|PDB:2WJN"
FT HELIX 342..344
FT /evidence="ECO:0007829|PDB:2WJN"
FT HELIX 346..348
FT /evidence="ECO:0007829|PDB:2WJN"
SQ SEQUENCE 356 AA; 39371 MW; ECE3D64F1BB0877A CRC64;
MKQLIVNSVA TVALASLVAG CFEPPPATTT QTGFRGLSMG EVLHPATVKA KKERDAQYPP
ALAAVKAEGP PVSQVYKNVK VLGNLTEAEF LRTMTAITEW VSPQEGCTYC HDENNLASEA
KYPYVVARRM LEMTRAINTN WTQHVAQTGV TCYTCHRGTP LPPYVRYLEP TLPLNNRETP
THVERVETRS GYVVRLAKYT AYSALNYDPF TMFLANDKRQ VRVVPQTALP LVGVSRGKER
RPLSDAYATF ALMMSISDSL GTNCTFCHNA QTFESWGKKS TPQRAIAWWG IRMVRDLNMN
YLAPLNASLP ASRLGRQGEA PQADCRTCHQ GVTKPLFGAS RLKDYPELGP IKAAAK
