ID   RCEM_CERSP              Reviewed;         308 AA.
AC   P0C0Y9; P02953; Q9RFB8;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   27-MAR-2024, entry version 102.
DE   RecName: Full=Reaction center protein M chain;
DE   AltName: Full=Photosynthetic reaction center M subunit;
GN   Name=pufM;
OS   Cereibacter sphaeroides (Rhodobacter sphaeroides).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Paracoccaceae; Cereibacter.
OX   NCBI_TaxID=1063;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=16593385; DOI=10.1073/pnas.80.21.6505;
RA   Williams J.C., Steiner L.A., Ogden R.C., Simon M.I., Feher G.;
RT   "Primary structure of the M subunit of the reaction center from
RT   Rhodopseudomonas sphaeroides.";
RL   Proc. Natl. Acad. Sci. U.S.A. 80:6505-6509(1983).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=Y;
RX   PubMed=2126457; DOI=10.1016/0300-9084(90)90116-x;
RA   Arnoux B., Ducruix A., Astier C., Picaud M., Roth M., Reiss-Husson F.;
RT   "Towards the understanding of the function of Rb sphaeroides Y wild type
RT   reaction center: gene cloning, protein and detergent structures in the
RT   three-dimensional crystals.";
RL   Biochimie 72:525-530(1990).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-11.
RX   PubMed=6095283; DOI=10.1073/pnas.81.23.7303;
RA   Williams J.C., Steiner L.A., Feher G., Simon M.I.;
RT   "Primary structure of the L subunit of the reaction center from
RT   Rhodopseudomonas sphaeroides.";
RL   Proc. Natl. Acad. Sci. U.S.A. 81:7303-7307(1984).
RN   [4]
RP   X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS).
RX   PubMed=2036404; DOI=10.1021/bi00236a005;
RA   Chang C.-H., El-Kabbani O., Tiede D., Norris J., Schiffer M.;
RT   "Structure of the membrane-bound protein photosynthetic reaction center
RT   from Rhodobacter sphaeroides.";
RL   Biochemistry 30:5352-5360(1991).
RN   [5]
RP   X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS).
RC   STRAIN=R-26;
RX   PubMed=3054889; DOI=10.1073/pnas.85.22.8487;
RA   Allen J.P., Feher G., Yeates T.O., Komiya H., Rees D.C.;
RT   "Structure of the reaction center from Rhodobacter sphaeroides R-26:
RT   protein-cofactor (quinones and Fe2+) interactions.";
RL   Proc. Natl. Acad. Sci. U.S.A. 85:8487-8491(1988).
RN   [6]
RP   X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS).
RC   STRAIN=R-26;
RX   PubMed=2819866; DOI=10.1073/pnas.84.17.6162;
RA   Allen J.P., Feher G., Yeates T.O., Komiya H., Rees D.C.;
RT   "Structure of the reaction center from Rhodobacter sphaeroides R-26: the
RT   protein subunits.";
RL   Proc. Natl. Acad. Sci. U.S.A. 84:6162-6166(1987).
RN   [7]
RP   X-RAY CRYSTALLOGRAPHY (2.55 ANGSTROMS).
RX   PubMed=9537989; DOI=10.1021/bi971717a;
RA   McAuley-Hecht K.E., Fyfe P.K., Ridge J.P., Prince S.M., Hunter C.N.,
RA   Isaacs N.W., Cogdell R.J., Jones M.R.;
RT   "Structural studies of wild-type and mutant reaction centers from an
RT   antenna-deficient strain of Rhodobacter sphaeroides: monitoring the optical
RT   properties of the complex from bacterial cell to crystal.";
RL   Biochemistry 37:4740-4750(1998).
CC   -!- FUNCTION: The reaction center is a membrane-bound complex that mediates
CC       the initial photochemical event in the electron transfer process of
CC       photosynthesis.
CC   -!- SUBUNIT: Reaction center is composed of four bacteriochlorophylls, two
CC       bacteriopheophytins, two ubiquinones, one iron, and three highly
CC       hydrophobic polypeptide chains (designated L, M, and H).
CC   -!- SUBCELLULAR LOCATION: Cellular chromatophore membrane; Multi-pass
CC       membrane protein.
CC   -!- SIMILARITY: Belongs to the reaction center PufL/M/PsbA/D family.
CC       {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; K00827; AAA26179.1; -; Genomic_DNA.
DR   EMBL; X63405; CAA45001.1; -; Genomic_DNA.
DR   EMBL; X63404; CAA45000.1; -; Genomic_DNA.
DR   EMBL; M10206; AAA26178.1; -; Genomic_DNA.
DR   PIR; A03456; WNRFMS.
DR   PIR; S24213; S24213.
DR   RefSeq; WP_002720420.1; NZ_WTFI01000042.1.
DR   PDB; 1AIG; X-ray; 2.60 A; M/O=2-308.
DR   PDB; 1AIJ; X-ray; 2.20 A; M/S=2-308.
DR   PDB; 1DS8; X-ray; 2.50 A; M/S=2-307.
DR   PDB; 1DV3; X-ray; 2.50 A; M/S=2-307.
DR   PDB; 1DV6; X-ray; 2.50 A; M/S=2-307.
DR   PDB; 1E14; X-ray; 2.70 A; M=2-308.
DR   PDB; 1E6D; X-ray; 2.30 A; M=2-308.
DR   PDB; 1F6N; X-ray; 2.80 A; M=2-308.
DR   PDB; 1FNP; X-ray; 2.60 A; M=2-308.
DR   PDB; 1FNQ; X-ray; 2.60 A; M=2-308.
DR   PDB; 1JGW; X-ray; 2.80 A; M=2-308.
DR   PDB; 1JGX; X-ray; 3.01 A; M=2-308.
DR   PDB; 1JGY; X-ray; 2.70 A; M=2-308.
DR   PDB; 1JGZ; X-ray; 2.70 A; M=2-308.
DR   PDB; 1JH0; X-ray; 3.50 A; M=2-308.
DR   PDB; 1K6L; X-ray; 3.10 A; M=2-308.
DR   PDB; 1K6N; X-ray; 3.10 A; M=2-308.
DR   PDB; 1KBY; X-ray; 2.50 A; M=2-308.
DR   PDB; 1L9B; X-ray; 2.40 A; M=2-308.
DR   PDB; 1L9J; X-ray; 3.25 A; M/S=2-308.
DR   PDB; 1M3X; X-ray; 2.55 A; M=2-308.
DR   PDB; 1MPS; X-ray; 2.55 A; M=2-308.
DR   PDB; 1OGV; X-ray; 2.35 A; M=2-308.
DR   PDB; 1PCR; X-ray; 2.65 A; M=2-308.
DR   PDB; 1PSS; X-ray; 3.00 A; M=7-302.
DR   PDB; 1PST; X-ray; 3.00 A; M=7-302.
DR   PDB; 1QOV; X-ray; 2.10 A; M=2-308.
DR   PDB; 1RG5; X-ray; 2.50 A; M=2-308.
DR   PDB; 1RGN; X-ray; 2.80 A; M=2-308.
DR   PDB; 1RQK; X-ray; 2.70 A; M=2-308.
DR   PDB; 1RVJ; X-ray; 2.75 A; M=2-307.
DR   PDB; 1RY5; X-ray; 2.10 A; M=2-308.
DR   PDB; 1RZH; X-ray; 1.80 A; M=2-308.
DR   PDB; 1RZZ; X-ray; 2.40 A; M/S=2-308.
DR   PDB; 1S00; X-ray; 2.60 A; M/S=2-308.
DR   PDB; 1UMX; X-ray; 2.80 A; M=2-308.
DR   PDB; 1YF6; X-ray; 2.25 A; M=2-308.
DR   PDB; 1YST; X-ray; 3.00 A; M=2-306.
DR   PDB; 1Z9J; X-ray; 4.50 A; B=2-308.
DR   PDB; 1Z9K; X-ray; 4.60 A; B=2-308.
DR   PDB; 2BNP; X-ray; 2.70 A; B=2-308.
DR   PDB; 2BNS; X-ray; 2.50 A; B=2-308.
DR   PDB; 2BOZ; X-ray; 2.40 A; M=2-308.
DR   PDB; 2GMR; X-ray; 2.50 A; M=2-308.
DR   PDB; 2GNU; X-ray; 2.20 A; M=3-302.
DR   PDB; 2HG3; X-ray; 2.70 A; M=2-308.
DR   PDB; 2HG9; X-ray; 2.45 A; M=2-308.
DR   PDB; 2HH1; X-ray; 2.55 A; M=2-308.
DR   PDB; 2HHK; X-ray; 2.50 A; M=2-308.
DR   PDB; 2HIT; X-ray; 2.75 A; M=2-308.
DR   PDB; 2HJ6; X-ray; 3.00 A; M=2-308.
DR   PDB; 2J8C; X-ray; 1.87 A; M=2-308.
DR   PDB; 2J8D; X-ray; 2.07 A; M=2-308.
DR   PDB; 2JIY; X-ray; 2.20 A; M=1-308.
DR   PDB; 2JJ0; X-ray; 2.80 A; M=2-308.
DR   PDB; 2RCR; X-ray; 3.10 A; M=2-308.
DR   PDB; 2UWS; X-ray; 2.90 A; M=2-308.
DR   PDB; 2UWT; X-ray; 2.50 A; M=2-308.
DR   PDB; 2UWU; X-ray; 2.04 A; M=2-308.
DR   PDB; 2UWV; X-ray; 2.13 A; M=2-308.
DR   PDB; 2UWW; X-ray; 2.05 A; M=2-308.
DR   PDB; 2UX3; X-ray; 2.50 A; M=2-308.
DR   PDB; 2UX4; X-ray; 2.51 A; M=2-308.
DR   PDB; 2UX5; X-ray; 2.21 A; M=2-308.
DR   PDB; 2UXJ; X-ray; 2.25 A; M=2-308.
DR   PDB; 2UXK; X-ray; 2.31 A; M=2-308.
DR   PDB; 2UXL; X-ray; 2.88 A; M=2-308.
DR   PDB; 2UXM; X-ray; 2.70 A; M=2-308.
DR   PDB; 3DSY; X-ray; 3.00 A; M=2-308.
DR   PDB; 3DTA; X-ray; 3.20 A; M=2-308.
DR   PDB; 3DTR; X-ray; 3.10 A; M=2-308.
DR   PDB; 3DTS; X-ray; 3.10 A; M=2-308.
DR   PDB; 3DU2; X-ray; 3.10 A; M=2-308.
DR   PDB; 3DU3; X-ray; 2.80 A; M=2-308.
DR   PDB; 3DUQ; X-ray; 2.70 A; M=2-308.
DR   PDB; 3I4D; X-ray; 2.01 A; M=2-308.
DR   PDB; 3V3Y; X-ray; 2.80 A; M=2-303.
DR   PDB; 3V3Z; X-ray; 2.90 A; M=2-303.
DR   PDB; 3ZUM; X-ray; 2.50 A; M=2-308.
DR   PDB; 3ZUW; X-ray; 2.31 A; M=2-308.
DR   PDB; 4H99; X-ray; 2.97 A; M=2-303.
DR   PDB; 4H9L; X-ray; 2.77 A; M=2-303.
DR   PDB; 4HBH; X-ray; 2.93 A; M=2-303.
DR   PDB; 4HBJ; X-ray; 2.74 A; M=2-303.
DR   PDB; 4IN7; X-ray; 2.85 A; M=2-303.
DR   PDB; 4LWY; X-ray; 2.90 A; M=1-303.
DR   PDB; 4N7K; X-ray; 2.85 A; M=2-304.
DR   PDB; 4RCR; X-ray; 2.80 A; M=2-308.
DR   PDB; 4TQQ; X-ray; 2.50 A; M=2-303.
DR   PDB; 4V9G; X-ray; 7.78 A; AM/BM=1-308.
DR   PDB; 5LSE; X-ray; 2.50 A; M=2-308.
DR   PDB; 5V33; X-ray; 3.49 A; M=2-303.
DR   PDB; 6Z02; X-ray; 2.10 A; M=2-303.
DR   PDB; 6Z1J; X-ray; 2.10 A; M=2-303.
DR   PDB; 6Z27; X-ray; 2.10 A; M=2-303.
DR   PDB; 7MH3; X-ray; 2.30 A; M=1-308.
DR   PDB; 7MH4; X-ray; 2.48 A; M=1-308.
DR   PDB; 7MH5; X-ray; 2.85 A; M=1-308.
DR   PDB; 7MH8; X-ray; 2.75 A; M=1-308.
DR   PDB; 7MH9; X-ray; 3.10 A; M=1-308.
DR   PDB; 7MHA; X-ray; 2.79 A; M=1-308.
DR   PDB; 7OD5; X-ray; 2.10 A; M=2-304.
DR   PDB; 7P0Q; X-ray; 1.73 A; M=2-304.
DR   PDB; 7P17; X-ray; 2.22 A; M=2-304.
DR   PDB; 7Q7F; X-ray; 2.75 A; M=2-303.
DR   PDB; 7Q7G; X-ray; 2.69 A; M=2-303.
DR   PDB; 7Q7H; X-ray; 2.49 A; M=2-303.
DR   PDB; 7Q7J; X-ray; 2.69 A; M=2-303.
DR   PDB; 7Q7M; X-ray; 2.55 A; M=2-303.
DR   PDB; 7Q7N; X-ray; 2.87 A; M=2-303.
DR   PDB; 7Q7O; X-ray; 2.65 A; M=2-303.
DR   PDB; 7Z8D; X-ray; 2.14 A; M=2-303.
DR   PDB; 8C3F; X-ray; 2.60 A; M=2-304.
DR   PDB; 8C5X; X-ray; 2.60 A; M=2-304.
DR   PDB; 8C6K; X-ray; 2.86 A; M=2-304.
DR   PDB; 8C7C; X-ray; 2.60 A; M=2-304.
DR   PDB; 8C87; X-ray; 2.45 A; M=2-304.
DR   PDB; 8C88; X-ray; 2.75 A; M=2-304.
DR   PDBsum; 1AIG; -.
DR   PDBsum; 1AIJ; -.
DR   PDBsum; 1DS8; -.
DR   PDBsum; 1DV3; -.
DR   PDBsum; 1DV6; -.
DR   PDBsum; 1E14; -.
DR   PDBsum; 1E6D; -.
DR   PDBsum; 1F6N; -.
DR   PDBsum; 1FNP; -.
DR   PDBsum; 1FNQ; -.
DR   PDBsum; 1JGW; -.
DR   PDBsum; 1JGX; -.
DR   PDBsum; 1JGY; -.
DR   PDBsum; 1JGZ; -.
DR   PDBsum; 1JH0; -.
DR   PDBsum; 1K6L; -.
DR   PDBsum; 1K6N; -.
DR   PDBsum; 1KBY; -.
DR   PDBsum; 1L9B; -.
DR   PDBsum; 1L9J; -.
DR   PDBsum; 1M3X; -.
DR   PDBsum; 1MPS; -.
DR   PDBsum; 1OGV; -.
DR   PDBsum; 1PCR; -.
DR   PDBsum; 1PSS; -.
DR   PDBsum; 1PST; -.
DR   PDBsum; 1QOV; -.
DR   PDBsum; 1RG5; -.
DR   PDBsum; 1RGN; -.
DR   PDBsum; 1RQK; -.
DR   PDBsum; 1RVJ; -.
DR   PDBsum; 1RY5; -.
DR   PDBsum; 1RZH; -.
DR   PDBsum; 1RZZ; -.
DR   PDBsum; 1S00; -.
DR   PDBsum; 1UMX; -.
DR   PDBsum; 1YF6; -.
DR   PDBsum; 1YST; -.
DR   PDBsum; 1Z9J; -.
DR   PDBsum; 1Z9K; -.
DR   PDBsum; 2BNP; -.
DR   PDBsum; 2BNS; -.
DR   PDBsum; 2BOZ; -.
DR   PDBsum; 2GMR; -.
DR   PDBsum; 2GNU; -.
DR   PDBsum; 2HG3; -.
DR   PDBsum; 2HG9; -.
DR   PDBsum; 2HH1; -.
DR   PDBsum; 2HHK; -.
DR   PDBsum; 2HIT; -.
DR   PDBsum; 2HJ6; -.
DR   PDBsum; 2J8C; -.
DR   PDBsum; 2J8D; -.
DR   PDBsum; 2JIY; -.
DR   PDBsum; 2JJ0; -.
DR   PDBsum; 2RCR; -.
DR   PDBsum; 2UWS; -.
DR   PDBsum; 2UWT; -.
DR   PDBsum; 2UWU; -.
DR   PDBsum; 2UWV; -.
DR   PDBsum; 2UWW; -.
DR   PDBsum; 2UX3; -.
DR   PDBsum; 2UX4; -.
DR   PDBsum; 2UX5; -.
DR   PDBsum; 2UXJ; -.
DR   PDBsum; 2UXK; -.
DR   PDBsum; 2UXL; -.
DR   PDBsum; 2UXM; -.
DR   PDBsum; 3DSY; -.
DR   PDBsum; 3DTA; -.
DR   PDBsum; 3DTR; -.
DR   PDBsum; 3DTS; -.
DR   PDBsum; 3DU2; -.
DR   PDBsum; 3DU3; -.
DR   PDBsum; 3DUQ; -.
DR   PDBsum; 3I4D; -.
DR   PDBsum; 3V3Y; -.
DR   PDBsum; 3V3Z; -.
DR   PDBsum; 3ZUM; -.
DR   PDBsum; 3ZUW; -.
DR   PDBsum; 4H99; -.
DR   PDBsum; 4H9L; -.
DR   PDBsum; 4HBH; -.
DR   PDBsum; 4HBJ; -.
DR   PDBsum; 4IN7; -.
DR   PDBsum; 4LWY; -.
DR   PDBsum; 4N7K; -.
DR   PDBsum; 4RCR; -.
DR   PDBsum; 4TQQ; -.
DR   PDBsum; 4V9G; -.
DR   PDBsum; 5LSE; -.
DR   PDBsum; 5V33; -.
DR   PDBsum; 6Z02; -.
DR   PDBsum; 6Z1J; -.
DR   PDBsum; 6Z27; -.
DR   PDBsum; 7MH3; -.
DR   PDBsum; 7MH4; -.
DR   PDBsum; 7MH5; -.
DR   PDBsum; 7MH8; -.
DR   PDBsum; 7MH9; -.
DR   PDBsum; 7MHA; -.
DR   PDBsum; 7OD5; -.
DR   PDBsum; 7P0Q; -.
DR   PDBsum; 7P17; -.
DR   PDBsum; 7Q7F; -.
DR   PDBsum; 7Q7G; -.
DR   PDBsum; 7Q7H; -.
DR   PDBsum; 7Q7J; -.
DR   PDBsum; 7Q7M; -.
DR   PDBsum; 7Q7N; -.
DR   PDBsum; 7Q7O; -.
DR   PDBsum; 7Z8D; -.
DR   PDBsum; 8C3F; -.
DR   PDBsum; 8C5X; -.
DR   PDBsum; 8C6K; -.
DR   PDBsum; 8C7C; -.
DR   PDBsum; 8C87; -.
DR   PDBsum; 8C88; -.
DR   AlphaFoldDB; P0C0Y9; -.
DR   SMR; P0C0Y9; -.
DR   DIP; DIP-60490N; -.
DR   IntAct; P0C0Y9; 1.
DR   DrugBank; DB04147; Dodecyldimethylamine N-oxide.
DR   DrugBank; DB08215; Terbutryn.
DR   DrugBank; DB08690; Ubiquinone Q2.
DR   TCDB; 3.E.2.1.1; the photosynthetic reaction center (prc) family.
DR   GeneID; 67446989; -.
DR   OMA; IFPHLDW; -.
DR   EvolutionaryTrace; P0C0Y9; -.
DR   GO; GO:0030077; C:plasma membrane light-harvesting complex; IEA:InterPro.
DR   GO; GO:0042717; C:plasma membrane-derived chromatophore membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0042314; F:bacteriochlorophyll binding; IEA:UniProtKB-KW.
DR   GO; GO:0045156; F:electron transporter, transferring electrons within the cyclic electron transport pathway of photosynthesis activity; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0009772; P:photosynthetic electron transport in photosystem II; IEA:InterPro.
DR   CDD; cd09291; Photo-RC_M; 1.
DR   Gene3D; 1.20.85.10; Photosystem II protein D1-like; 2.
DR   InterPro; IPR036854; Photo_II_D1/D2_sf.
DR   InterPro; IPR000484; Photo_RC_L/M.
DR   InterPro; IPR005781; Photo_RC_M.
DR   NCBIfam; TIGR01115; pufM; 1.
DR   Pfam; PF00124; Photo_RC; 1.
DR   PRINTS; PR00256; REACTNCENTRE.
DR   SUPFAM; SSF81483; Bacterial photosystem II reaction centre, L and M subunits; 1.
DR   PROSITE; PS00244; REACTION_CENTER; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Bacteriochlorophyll; Chlorophyll; Chromophore;
KW   Electron transport; Iron; Magnesium; Membrane; Metal-binding;
KW   Photosynthesis; Reaction center; Transmembrane; Transmembrane helix;
KW   Transport.
FT   INIT_MET        1
FT                   /note="Removed"
FT   CHAIN           2..308
FT                   /note="Reaction center protein M chain"
FT                   /id="PRO_0000090417"
FT   TRANSMEM        54..80
FT                   /note="Helical"
FT   TRANSMEM        111..140
FT                   /note="Helical"
FT   TRANSMEM        143..168
FT                   /note="Helical"
FT   TRANSMEM        198..226
FT                   /note="Helical"
FT   TRANSMEM        260..286
FT                   /note="Helical"
FT   BINDING         183
FT                   /ligand="(7R,8Z)-bacteriochlorophyll b"
FT                   /ligand_id="ChEBI:CHEBI:30034"
FT                   /ligand_part="Mg"
FT                   /ligand_part_id="ChEBI:CHEBI:25107"
FT                   /note="axial binding residue"
FT   BINDING         203
FT                   /ligand="(7R,8Z)-bacteriochlorophyll b"
FT                   /ligand_id="ChEBI:CHEBI:30034"
FT                   /ligand_part="Mg"
FT                   /ligand_part_id="ChEBI:CHEBI:25107"
FT                   /note="axial binding residue"
FT   BINDING         220
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT   BINDING         235
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT   BINDING         253
FT                   /ligand="a ubiquinone"
FT                   /ligand_id="ChEBI:CHEBI:16389"
FT   BINDING         267
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT   CONFLICT        141
FT                   /note="L -> M (in Ref. 2; CAA45001)"
FT                   /evidence="ECO:0000305"
FT   STRAND          6..8
FT                   /evidence="ECO:0007829|PDB:7P0Q"
FT   STRAND          10..14
FT                   /evidence="ECO:0007829|PDB:7P0Q"
FT   STRAND          24..26
FT                   /evidence="ECO:0007829|PDB:1PSS"
FT   HELIX           27..29
FT                   /evidence="ECO:0007829|PDB:7P0Q"
FT   HELIX           38..41
FT                   /evidence="ECO:0007829|PDB:7P0Q"
FT   STRAND          46..48
FT                   /evidence="ECO:0007829|PDB:3V3Y"
FT   HELIX           54..78
FT                   /evidence="ECO:0007829|PDB:7P0Q"
FT   TURN            79..81
FT                   /evidence="ECO:0007829|PDB:7P0Q"
FT   HELIX           83..88
FT                   /evidence="ECO:0007829|PDB:7P0Q"
FT   TURN            89..92
FT                   /evidence="ECO:0007829|PDB:7P0Q"
FT   HELIX           100..102
FT                   /evidence="ECO:0007829|PDB:7P0Q"
FT   STRAND          104..106
FT                   /evidence="ECO:0007829|PDB:2RCR"
FT   HELIX           110..112
FT                   /evidence="ECO:0007829|PDB:7P0Q"
FT   HELIX           114..140
FT                   /evidence="ECO:0007829|PDB:7P0Q"
FT   HELIX           146..162
FT                   /evidence="ECO:0007829|PDB:7P0Q"
FT   HELIX           164..169
FT                   /evidence="ECO:0007829|PDB:7P0Q"
FT   HELIX           172..174
FT                   /evidence="ECO:0007829|PDB:7P0Q"
FT   HELIX           180..193
FT                   /evidence="ECO:0007829|PDB:7P0Q"
FT   HELIX           197..199
FT                   /evidence="ECO:0007829|PDB:7P0Q"
FT   HELIX           201..226
FT                   /evidence="ECO:0007829|PDB:7P0Q"
FT   HELIX           228..230
FT                   /evidence="ECO:0007829|PDB:7P0Q"
FT   TURN            231..233
FT                   /evidence="ECO:0007829|PDB:7P0Q"
FT   HELIX           235..240
FT                   /evidence="ECO:0007829|PDB:7P0Q"
FT   HELIX           244..257
FT                   /evidence="ECO:0007829|PDB:7P0Q"
FT   HELIX           265..286
FT                   /evidence="ECO:0007829|PDB:7P0Q"
FT   TURN            289..291
FT                   /evidence="ECO:0007829|PDB:7P0Q"
FT   STRAND          292..294
FT                   /evidence="ECO:0007829|PDB:1YST"
FT   HELIX           295..300
FT                   /evidence="ECO:0007829|PDB:7P0Q"
FT   STRAND          302..306
FT                   /evidence="ECO:0007829|PDB:2J8D"
SQ   SEQUENCE   308 AA;  34509 MW;  30B3737DF8658250 CRC64;
     MAEYQNIFSQ VQVRGPADLG MTEDVNLANR SGVGPFSTLL GWFGNAQLGP IYLGSLGVLS
     LFSGLMWFFT IGIWFWYQAG WNPAVFLRDL FFFSLEPPAP EYGLSFAAPL KEGGLWLIAS
     FFMFVAVWSW WGRTYLRAQA LGMGKHTAWA FLSAIWLWMV LGFIRPILMG SWSEAVPYGI
     FSHLDWTNNF SLVHGNLFYN PFHGLSIAFL YGSALLFAMH GATILAVSRF GGERELEQIA
     DRGTAAERAA LFWRWTMGFN ATMEGIHRWA IWMAVLVTLT GGIGILLSGT VVDNWYVWGQ
     NHGMAPLN
//