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   27-MAR-2024, entry version 154.
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; Pseudomonadota; 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   PDB; 7Q7P; X-ray; 2.40 A; CCC=1-356.
DR   PDB; 7Q7Q; X-ray; 2.25 A; CCC=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   PDBsum; 7Q7P; -.
DR   PDBsum; 7Q7Q; -.
DR   AlphaFoldDB; P07173; -.
DR   EMDB; EMD-3951; -.
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   KEGG; bvr:BVIR_606; -.
DR   PATRIC; fig|1079.6.peg.623; -.
DR   OrthoDB; 9813732at2; -.
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; Photosynthetic Reaction Center, subunit C, domain 2; 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   NCBIfam; NF040706; photo_cyt_PufC; 1.
DR   Pfam; PF02276; CytoC_RC; 1.
DR   PIRSF; PIRSF000017; RC_cytochrome; 1.
DR   SUPFAM; SSF48695; Multiheme cytochromes; 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
//