PSBA_THEVL
ID PSBA_THEVL Reviewed; 360 AA.
AC P51765;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=Photosystem II protein D1 {ECO:0000255|HAMAP-Rule:MF_01379};
DE Short=PSII D1 protein {ECO:0000255|HAMAP-Rule:MF_01379};
DE EC=1.10.3.9 {ECO:0000255|HAMAP-Rule:MF_01379};
DE AltName: Full=Photosystem II Q(B) protein {ECO:0000255|HAMAP-Rule:MF_01379};
DE Flags: Precursor;
GN Name=psbA {ECO:0000255|HAMAP-Rule:MF_01379}; Synonyms=psbA-1;
OS Thermostichus vulcanus (Synechococcus vulcanus).
OC Bacteria; Cyanobacteria; Thermostichales; Thermostichaceae; Thermostichus.
OX NCBI_TaxID=32053;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Copeland;
RA Dibrov Y., Rahat A., Ohad N., Hirschberg J.;
RT "Structure of the D1 subunit of photosystem II in the thermophyllic
RT cyanobacterium Synechococcus vulcanus.";
RL Submitted (MAY-1994) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP X-RAY CRYSTALLOGRAPHY (3.7 ANGSTROMS) IN PHOTOSYSTEM II, COFACTOR, SUBUNIT,
RP AND SUBCELLULAR LOCATION.
RX PubMed=12518057; DOI=10.1073/pnas.0135651100;
RA Kamiya N., Shen J.-R.;
RT "Crystal structure of oxygen-evolving photosystem II from
RT Thermosynechococcus vulcanus at 3.7-A resolution.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:98-103(2003).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (3.7 ANGSTROMS) OF 1-344 IN COMPLEX WITH CHLOROPHYLL
RP A AND PHEOPHYTIN A IN PHOTOSYSTEM II, FUNCTION, COFACTOR, SUBUNIT,
RP SUBCELLULAR LOCATION, AND POSSIBLE CL(-) LIGAND.
RX PubMed=19433803; DOI=10.1073/pnas.0812797106;
RA Kawakami K., Umena Y., Kamiya N., Shen J.R.;
RT "Location of chloride and its possible functions in oxygen-evolving
RT photosystem II revealed by X-ray crystallography.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:8567-8572(2009).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 1-344 IN COMPLEX WITH CA-4MN-5O
RP CLUSTER; CHLOROPHYLL A AND PHEOPHYTIN A IN PHOTOSYSTEM II, COFACTOR,
RP SUBUNIT, SUBCELLULAR LOCATION, AND TOPOLOGY.
RX PubMed=21499260; DOI=10.1038/nature09913;
RA Umena Y., Kawakami K., Shen J.R., Kamiya N.;
RT "Crystal structure of oxygen-evolving photosystem II at a resolution of 1.9
RT A.";
RL Nature 473:55-60(2011).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 11-344 IN PHOTOSYSTEM II,
RP FUNCTION, COFACTOR, SUBUNIT, AND SUBCELLULAR LOCATION.
RX PubMed=23426624; DOI=10.1073/pnas.1219922110;
RA Koua F.H., Umena Y., Kawakami K., Shen J.R.;
RT "Structure of Sr-substituted photosystem II at 2.1 A resolution and its
RT implications in the mechanism of water oxidation.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:3889-3894(2013).
CC -!- FUNCTION: Photosystem II (PSII) is a light-driven water:plastoquinone
CC oxidoreductase that uses light energy to abstract electrons from H(2)O,
CC generating O(2) and a proton gradient subsequently used for ATP
CC formation. It consists of a core antenna complex that captures photons,
CC and an electron transfer chain that converts photonic excitation into a
CC charge separation. The D1/D2 (PsbA/PsbA) reaction center heterodimer
CC binds P680, the primary electron donor of PSII as well as several
CC subsequent electron acceptors. {ECO:0000255|HAMAP-Rule:MF_01379,
CC ECO:0000269|PubMed:19433803, ECO:0000269|PubMed:23426624}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 a plastoquinone + 2 H2O + 4 hnu = 2 a plastoquinol + O2;
CC Xref=Rhea:RHEA:36359, Rhea:RHEA-COMP:9561, Rhea:RHEA-COMP:9562,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:17757,
CC ChEBI:CHEBI:30212, ChEBI:CHEBI:62192; EC=1.10.3.9;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01379};
CC -!- COFACTOR:
CC Note=The D1/D2 heterodimer binds P680, chlorophylls that are the
CC primary electron donor of PSII, and subsequent electron acceptors. It
CC shares a non-heme iron and each subunit binds pheophytin, quinone,
CC additional chlorophylls, carotenoids and lipids. D1 provides most of
CC the ligands for the Mn4-Ca-O5 cluster of the oxygen-evolving complex
CC (OEC). There is also a Cl(-1) ion associated with D1 and D2, which is
CC required for oxygen evolution. The PSII complex binds additional
CC chlorophylls, carotenoids and specific lipids. {ECO:0000255|HAMAP-
CC Rule:MF_01379, ECO:0000269|PubMed:12518057,
CC ECO:0000269|PubMed:19433803, ECO:0000269|PubMed:21499260,
CC ECO:0000269|PubMed:23426624};
CC -!- SUBUNIT: Cyanobacterial PSII is composed of 1 copy each of membrane
CC proteins PsbA, PsbB, PsbC, PsbD, PsbE, PsbF, PsbH, PsbI, PsbJ, PsbK,
CC PsbL, PsbM, PsbT, PsbX, PsbY, PsbZ, Ycf12, at least 3 peripheral
CC proteins PsbO, PsbU, PsbV and a large number of cofactors. It forms
CC dimeric complexes. {ECO:0000255|HAMAP-Rule:MF_01379,
CC ECO:0000269|PubMed:12518057, ECO:0000269|PubMed:19433803,
CC ECO:0000269|PubMed:21499260, ECO:0000269|PubMed:23426624}.
CC -!- SUBCELLULAR LOCATION: Cellular thylakoid membrane {ECO:0000255|HAMAP-
CC Rule:MF_01379, ECO:0000269|PubMed:12518057,
CC ECO:0000269|PubMed:19433803, ECO:0000269|PubMed:21499260,
CC ECO:0000269|PubMed:23426624}; Multi-pass membrane protein
CC {ECO:0000255|HAMAP-Rule:MF_01379, ECO:0000269|PubMed:12518057,
CC ECO:0000269|PubMed:19433803, ECO:0000269|PubMed:21499260,
CC ECO:0000269|PubMed:23426624}.
CC -!- PTM: C-terminally processed by CtpA; processing is essential to allow
CC assembly of the oxygen-evolving complex and thus photosynthetic growth.
CC {ECO:0000255|HAMAP-Rule:MF_01379}.
CC -!- PTM: Tyr-161 forms a radical intermediate that is referred to as redox-
CC active TyrZ, YZ or Y-Z. {ECO:0000255|HAMAP-Rule:MF_01379,
CC ECO:0000269|PubMed:21499260, ECO:0000303|PubMed:12518057,
CC ECO:0000303|PubMed:23426624}.
CC -!- MISCELLANEOUS: 2 of the reaction center chlorophylls (ChlD1 and ChlD2)
CC are entirely coordinated by water. {ECO:0000255|HAMAP-Rule:MF_01379,
CC ECO:0000269|PubMed:21499260}.
CC -!- MISCELLANEOUS: Cyanobacteria usually contain more than 2 copies of the
CC psbA gene. {ECO:0000255|HAMAP-Rule:MF_01379, ECO:0000305}.
CC -!- MISCELLANEOUS: Herbicides such as atrazine, BNT, diuron or ioxynil bind
CC in the Q(B) binding site and block subsequent electron transfer.
CC {ECO:0000255|HAMAP-Rule:MF_01379}.
CC -!- SIMILARITY: Belongs to the reaction center PufL/M/PsbA/D family.
CC {ECO:0000255|HAMAP-Rule:MF_01379}.
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DR EMBL; X79222; CAA55806.1; -; Genomic_DNA.
DR PIR; S45009; S45009.
DR PDB; 1IZL; X-ray; 3.70 A; A/J=1-360.
DR PDB; 3A0B; X-ray; 3.70 A; A/a=1-344.
DR PDB; 3A0H; X-ray; 4.00 A; A/a=1-344.
DR PDB; 3WU2; X-ray; 1.90 A; A/a=1-344.
DR PDB; 4IL6; X-ray; 2.10 A; A/a=11-344.
DR PDB; 4UB6; X-ray; 1.95 A; A/a=1-344.
DR PDB; 4UB8; X-ray; 1.95 A; A/a=1-344.
DR PDB; 5B5E; X-ray; 1.87 A; A/a=1-344.
DR PDB; 5B66; X-ray; 1.85 A; A/a=1-344.
DR PDB; 5GTH; X-ray; 2.50 A; A/a=1-344.
DR PDB; 5GTI; X-ray; 2.50 A; A/a=1-344.
DR PDB; 5V2C; X-ray; 1.90 A; A/a=1-344.
DR PDB; 5WS5; X-ray; 2.35 A; A/a=1-344.
DR PDB; 5WS6; X-ray; 2.35 A; A/a=1-344.
DR PDB; 6JLJ; X-ray; 2.15 A; A/a=1-344.
DR PDB; 6JLK; X-ray; 2.15 A; A/a=1-344.
DR PDB; 6JLL; X-ray; 2.15 A; A/a=1-344.
DR PDB; 6JLM; X-ray; 2.35 A; A/a=1-344.
DR PDB; 6JLN; X-ray; 2.40 A; A/a=1-344.
DR PDB; 6JLO; X-ray; 2.40 A; A/a=1-344.
DR PDB; 6JLP; X-ray; 2.50 A; A/a=1-344.
DR PDB; 7CJI; X-ray; 2.35 A; A/a=1-344.
DR PDB; 7CJJ; X-ray; 2.40 A; A/a=1-344.
DR PDB; 7COU; X-ray; 2.25 A; A/a=1-344.
DR PDB; 7CZL; EM; 3.78 A; A/a=10-333.
DR PDB; 7D1T; EM; 1.95 A; A/a=11-344.
DR PDB; 7D1U; EM; 2.08 A; A/a=11-344.
DR PDB; 7DXA; EM; 3.14 A; a=1-360.
DR PDB; 7DXH; EM; 3.14 A; a=1-360.
DR PDB; 7EDA; EM; 2.78 A; A=11-344.
DR PDBsum; 1IZL; -.
DR PDBsum; 3A0B; -.
DR PDBsum; 3A0H; -.
DR PDBsum; 3WU2; -.
DR PDBsum; 4IL6; -.
DR PDBsum; 4UB6; -.
DR PDBsum; 4UB8; -.
DR PDBsum; 5B5E; -.
DR PDBsum; 5B66; -.
DR PDBsum; 5GTH; -.
DR PDBsum; 5GTI; -.
DR PDBsum; 5V2C; -.
DR PDBsum; 5WS5; -.
DR PDBsum; 5WS6; -.
DR PDBsum; 6JLJ; -.
DR PDBsum; 6JLK; -.
DR PDBsum; 6JLL; -.
DR PDBsum; 6JLM; -.
DR PDBsum; 6JLN; -.
DR PDBsum; 6JLO; -.
DR PDBsum; 6JLP; -.
DR PDBsum; 7CJI; -.
DR PDBsum; 7CJJ; -.
DR PDBsum; 7COU; -.
DR PDBsum; 7CZL; -.
DR PDBsum; 7D1T; -.
DR PDBsum; 7D1U; -.
DR PDBsum; 7DXA; -.
DR PDBsum; 7DXH; -.
DR PDBsum; 7EDA; -.
DR AlphaFoldDB; P51765; -.
DR SMR; P51765; -.
DR DIP; DIP-48859N; -.
DR IntAct; P51765; 1.
DR EvolutionaryTrace; P51765; -.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0009523; C:photosystem II; IEA:UniProtKB-KW.
DR GO; GO:0031676; C:plasma membrane-derived thylakoid membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016168; F:chlorophyll binding; IEA:UniProtKB-UniRule.
DR GO; GO:0045156; F:electron transporter, transferring electrons within the cyclic electron transport pathway of photosynthesis activity; IEA:InterPro.
DR GO; GO:0005506; F:iron ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016682; F:oxidoreductase activity, acting on diphenols and related substances as donors, oxygen as acceptor; IEA:UniProtKB-UniRule.
DR GO; GO:0010242; F:oxygen evolving activity; IEA:UniProtKB-EC.
DR GO; GO:0009772; P:photosynthetic electron transport in photosystem II; IEA:InterPro.
DR GO; GO:0009635; P:response to herbicide; IEA:UniProtKB-KW.
DR CDD; cd09289; Photosystem-II_D1; 1.
DR Gene3D; 1.20.85.10; -; 1.
DR HAMAP; MF_01379; PSII_PsbA_D1; 1.
DR InterPro; IPR036854; Photo_II_D1/D2_sf.
DR InterPro; IPR000484; Photo_RC_L/M.
DR InterPro; IPR005867; PSII_D1.
DR PANTHER; PTHR33149; PTHR33149; 1.
DR Pfam; PF00124; Photo_RC; 1.
DR SUPFAM; SSF81483; SSF81483; 1.
DR TIGRFAMs; TIGR01151; psbA; 1.
DR PROSITE; PS00244; REACTION_CENTER; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Calcium; Chlorophyll; Chromophore; Electron transport;
KW Herbicide resistance; Iron; Magnesium; Manganese; Membrane; Metal-binding;
KW Oxidoreductase; Photosynthesis; Photosystem II; Thylakoid; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..344
FT /note="Photosystem II protein D1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01379"
FT /id="PRO_0000090491"
FT PROPEP 345..360
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01379"
FT /id="PRO_0000316426"
FT TOPO_DOM 1..28
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:21499260"
FT TRANSMEM 29..46
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01379,
FT ECO:0000269|PubMed:21499260"
FT TOPO_DOM 47..117
FT /note="Lumenal"
FT /evidence="ECO:0000269|PubMed:21499260"
FT TRANSMEM 118..133
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01379,
FT ECO:0000269|PubMed:21499260"
FT TOPO_DOM 134..141
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:21499260"
FT TRANSMEM 142..156
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01379,
FT ECO:0000269|PubMed:21499260"
FT TOPO_DOM 157..196
FT /note="Lumenal"
FT /evidence="ECO:0000269|PubMed:21499260"
FT TRANSMEM 197..218
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01379,
FT ECO:0000269|PubMed:21499260"
FT TOPO_DOM 219..273
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:21499260"
FT TRANSMEM 274..288
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01379,
FT ECO:0000269|PubMed:21499260"
FT TOPO_DOM 289..360
FT /note="Lumenal"
FT /evidence="ECO:0000269|PubMed:21499260"
FT BINDING 118
FT /ligand="chlorophyll a"
FT /ligand_id="ChEBI:CHEBI:58416"
FT /ligand_label="ChlzD1"
FT /ligand_part="Mg"
FT /ligand_part_id="ChEBI:CHEBI:25107"
FT /note="axial binding residue"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01379,
FT ECO:0000269|PubMed:21499260"
FT BINDING 126
FT /ligand="pheophytin a"
FT /ligand_id="ChEBI:CHEBI:136840"
FT /ligand_label="D1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01379,
FT ECO:0000269|PubMed:19433803, ECO:0000269|PubMed:21499260,
FT ECO:0000269|PubMed:23426624"
FT BINDING 130
FT /ligand="pheophytin a"
FT /ligand_id="ChEBI:CHEBI:136840"
FT /ligand_label="D1"
FT /evidence="ECO:0000269|PubMed:21499260,
FT ECO:0000269|PubMed:23426624, ECO:0000303|PubMed:19433803"
FT BINDING 147
FT /ligand="pheophytin a"
FT /ligand_id="ChEBI:CHEBI:136840"
FT /ligand_label="D1"
FT /evidence="ECO:0000269|PubMed:19433803,
FT ECO:0000269|PubMed:21499260, ECO:0000269|PubMed:23426624"
FT BINDING 170
FT /ligand="[CaMn4O5] cluster"
FT /ligand_id="ChEBI:CHEBI:189552"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01379,
FT ECO:0000269|PubMed:21499260, ECO:0000269|PubMed:23426624,
FT ECO:0000303|PubMed:12518057, ECO:0000303|PubMed:19433803"
FT BINDING 189
FT /ligand="[CaMn4O5] cluster"
FT /ligand_id="ChEBI:CHEBI:189552"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01379,
FT ECO:0000269|PubMed:21499260, ECO:0000269|PubMed:23426624,
FT ECO:0000303|PubMed:19433803"
FT BINDING 198
FT /ligand="chlorophyll a"
FT /ligand_id="ChEBI:CHEBI:58416"
FT /ligand_label="PD1"
FT /ligand_part="Mg"
FT /ligand_part_id="ChEBI:CHEBI:25107"
FT /note="axial binding residue"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01379,
FT ECO:0000269|PubMed:21499260, ECO:0000269|PubMed:23426624"
FT BINDING 214
FT /ligand="pheophytin a"
FT /ligand_id="ChEBI:CHEBI:136840"
FT /ligand_label="D1"
FT /evidence="ECO:0000269|PubMed:19433803,
FT ECO:0000269|PubMed:21499260"
FT BINDING 215
FT /ligand="a quinone"
FT /ligand_id="ChEBI:CHEBI:132124"
FT /ligand_label="B"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01379,
FT ECO:0000269|PubMed:21499260, ECO:0000269|PubMed:23426624,
FT ECO:0000303|PubMed:19433803"
FT BINDING 215
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="ligand shared with heterodimeric partner"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01379,
FT ECO:0000269|PubMed:21499260, ECO:0000269|PubMed:23426624,
FT ECO:0000303|PubMed:19433803"
FT BINDING 264..265
FT /ligand="a quinone"
FT /ligand_id="ChEBI:CHEBI:132124"
FT /ligand_label="B"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01379,
FT ECO:0000269|PubMed:21499260, ECO:0000269|PubMed:23426624,
FT ECO:0000303|PubMed:19433803"
FT BINDING 272
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="ligand shared with heterodimeric partner"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01379,
FT ECO:0000269|PubMed:21499260, ECO:0000269|PubMed:23426624,
FT ECO:0000303|PubMed:19433803"
FT BINDING 332
FT /ligand="[CaMn4O5] cluster"
FT /ligand_id="ChEBI:CHEBI:189552"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01379,
FT ECO:0000269|PubMed:21499260, ECO:0000269|PubMed:23426624,
FT ECO:0000303|PubMed:19433803"
FT BINDING 333
FT /ligand="[CaMn4O5] cluster"
FT /ligand_id="ChEBI:CHEBI:189552"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01379,
FT ECO:0000269|PubMed:21499260, ECO:0000269|PubMed:23426624,
FT ECO:0000303|PubMed:19433803"
FT BINDING 342
FT /ligand="[CaMn4O5] cluster"
FT /ligand_id="ChEBI:CHEBI:189552"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01379,
FT ECO:0000269|PubMed:21499260, ECO:0000269|PubMed:23426624,
FT ECO:0000303|PubMed:19433803"
FT BINDING 344
FT /ligand="[CaMn4O5] cluster"
FT /ligand_id="ChEBI:CHEBI:189552"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01379,
FT ECO:0000269|PubMed:21499260, ECO:0000269|PubMed:23426624,
FT ECO:0000303|PubMed:12518057, ECO:0000303|PubMed:19433803"
FT SITE 161
FT /note="Tyrosine radical intermediate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01379,
FT ECO:0000269|PubMed:21499260, ECO:0000303|PubMed:12518057,
FT ECO:0000303|PubMed:23426624"
FT SITE 190
FT /note="Stabilizes free radical intermediate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01379"
FT SITE 344..345
FT /note="Cleavage; by CtpA"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01379"
FT HELIX 13..21
FT /evidence="ECO:0007829|PDB:5B66"
FT STRAND 26..28
FT /evidence="ECO:0007829|PDB:5B66"
FT HELIX 31..54
FT /evidence="ECO:0007829|PDB:5B66"
FT STRAND 62..64
FT /evidence="ECO:0007829|PDB:5B66"
FT HELIX 71..73
FT /evidence="ECO:0007829|PDB:5B66"
FT TURN 77..79
FT /evidence="ECO:0007829|PDB:5B66"
FT TURN 87..91
FT /evidence="ECO:0007829|PDB:5B66"
FT HELIX 96..98
FT /evidence="ECO:0007829|PDB:5B66"
FT STRAND 99..101
FT /evidence="ECO:0007829|PDB:5B66"
FT HELIX 102..107
FT /evidence="ECO:0007829|PDB:5B66"
FT HELIX 110..136
FT /evidence="ECO:0007829|PDB:5B66"
FT HELIX 143..158
FT /evidence="ECO:0007829|PDB:5B66"
FT HELIX 160..165
FT /evidence="ECO:0007829|PDB:5B66"
FT HELIX 168..170
FT /evidence="ECO:0007829|PDB:5B66"
FT HELIX 176..190
FT /evidence="ECO:0007829|PDB:5B66"
FT HELIX 192..194
FT /evidence="ECO:0007829|PDB:5B66"
FT HELIX 196..221
FT /evidence="ECO:0007829|PDB:5B66"
FT STRAND 225..227
FT /evidence="ECO:0007829|PDB:7DXH"
FT HELIX 233..236
FT /evidence="ECO:0007829|PDB:5B66"
FT HELIX 248..258
FT /evidence="ECO:0007829|PDB:5B66"
FT HELIX 261..263
FT /evidence="ECO:0007829|PDB:5B66"
FT HELIX 268..293
FT /evidence="ECO:0007829|PDB:5B66"
FT TURN 294..296
FT /evidence="ECO:0007829|PDB:5B66"
FT STRAND 297..299
FT /evidence="ECO:0007829|PDB:5B66"
FT STRAND 306..308
FT /evidence="ECO:0007829|PDB:7DXH"
FT STRAND 309..311
FT /evidence="ECO:0007829|PDB:5B66"
FT HELIX 317..331
FT /evidence="ECO:0007829|PDB:5B66"
FT TURN 332..336
FT /evidence="ECO:0007829|PDB:5B66"
FT STRAND 339..341
FT /evidence="ECO:0007829|PDB:7D1T"
SQ SEQUENCE 360 AA; 39766 MW; D4B7FD7418E3E335 CRC64;
MTTTLQRRES ANLWERFCNW VTSTDNRLYV GWFGVIMIPT LLAATICFVI AFIAAPPVDI
DGIREPVSGS LLYGNNIITG AVVPSSNAIG LHFYPIWEAA SLDEWLYNGG PYQLIIFHFL
LGASCYMGRQ WELSYRLGMR PWICVAYSAP LASAFAVFLI YPIGQGSFSD GMPLGISGTF
NFMIVFQAEH NILMHPFHQL GVAGVFGGAL FCAMHGSLVT SSLIRETTET ESANYGYKFG
QEEETYNIVA AHGYFGRLIF QYASFNNSRS LHFFLAAWRV VGVWFAALGI STMAFNLNGF
NFNHSVIDAK GNVINTWADI INRANLGMEV MHERNAHNFP LDLASAESAP VAMIAPSING
