ID PSBA2_SYNY3 Reviewed; 360 AA. AC P16033; DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot. DT 01-APR-1990, sequence version 1. DT 27-NOV-2024, entry version 182. DE RecName: Full=Photosystem II protein D1 2 {ECO:0000255|HAMAP-Rule:MF_01379}; DE Short=PSII D1 protein 2 {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 2 {ECO:0000255|HAMAP-Rule:MF_01379}; DE Flags: Precursor; GN Name=psbA2 {ECO:0000255|HAMAP-Rule:MF_01379, ECO:0000305}; Synonyms=psbA-2; GN OrderedLocusNames=slr1311; GN and GN Name=psbA3 {ECO:0000255|HAMAP-Rule:MF_01379, ECO:0000305}; Synonyms=psbA-3; GN OrderedLocusNames=sll1867; OS Synechocystis sp. (strain ATCC 27184 / PCC 6803 / Kazusa). OC Bacteria; Cyanobacteriota; Cyanophyceae; Synechococcales; Merismopediaceae; OC Synechocystis. OX NCBI_TaxID=1111708; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=2499875; DOI=10.1093/nar/17.10.3991; RA Ravnikar P.D., Debus R., Sevrinck J., Saetaert P., McIntosh L.; RT "Nucleotide sequence of a second psbA gene from the unicellular RT cyanobacterium Synechocystis 6803."; RL Nucleic Acids Res. 17:3991-3991(1989). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=2123543; DOI=10.1093/nar/18.22.6715; RA Metz J., Nixon P., Diner B.; RT "Nucleotide sequence of the psbA3 gene from the cyanobacterium RT Synechocystis PCC 6803."; RL Nucleic Acids Res. 18:6715-6715(1990). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 27184 / PCC 6803 / Kazusa; RX PubMed=8905231; DOI=10.1093/dnares/3.3.109; RA Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y., RA Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T., Hosouchi T., RA Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S., Shimpo S., RA Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.; RT "Sequence analysis of the genome of the unicellular cyanobacterium RT Synechocystis sp. strain PCC6803. II. Sequence determination of the entire RT genome and assignment of potential protein-coding regions."; RL DNA Res. 3:109-136(1996). RN [4] RP MUTAGENESIS OF PHE-255; SER-264 AND LEU-271. RX PubMed=1498597; DOI=10.1105/tpc.4.3.273; RA Ohad N., Hirschberg J.; RT "Mutations in the D1 subunit of photosystem II distinguish between quinone RT and herbicide binding sites."; RL Plant Cell 4:273-282(1992). RN [5] RP MUTAGENESIS OF 221-SER-SER-222; 227-THR-THR-228; TYR-237; LYS-238 AND RP ARG-257. RX PubMed=8068689; DOI=10.1021/bi00200a035; RA Kless H., Oren-Shamir M., Malkin S., McIntosh L., Edelman M.; RT "The D-E region of the D1 protein is involved in multiple quinone and RT herbicide interactions in photosystem II."; RL Biochemistry 33:10501-10507(1994). RN [6] RP PROBABLE CLEAVAGE. RC STRAIN=ATCC 27184 / PCC 6803 / N-1; RX PubMed=8034700; DOI=10.1016/s0021-9258(17)32175-0; RA Shestakov S.V., Anbudurai P.R., Stanbekova G.E., Gadzhiev A., Lind L.K., RA Pakrasi H.B.; RT "Molecular cloning and characterization of the ctpA gene encoding a RT carboxyl-terminal processing protease. Analysis of a spontaneous RT photosystem II-deficient mutant strain of the cyanobacterium Synechocystis RT sp. PCC 6803."; RL J. Biol. Chem. 269:19354-19359(1994). RN [7] RP SUBCELLULAR LOCATION, AND LACK OF PHOSPHORYLATION. RC STRAIN=ATCC 27184 / PCC 6803 / Kazusa; RX PubMed=9512353; DOI=10.1016/s0014-5793(98)00088-x; RA Pursiheimo S., Rintamaeki E., Baena-Gonzalez E., Aro E.-M.; RT "Thylakoid protein phosphorylation in evolutionally divergent species with RT oxygenic photosynthesis."; RL FEBS Lett. 423:178-182(1998). RN [8] RP IDENTIFICATION BY MASS SPECTROMETRY, SUBUNIT, AND SUBCELLULAR LOCATION. RC STRAIN=ATCC 27184 / PCC 6803 / Kazusa; RX PubMed=12069591; DOI=10.1021/bi026012+; RA Kashino Y., Lauber W.M., Carroll J.A., Wang Q., Whitmarsh J., Satoh K., RA Pakrasi H.B.; RT "Proteomic analysis of a highly active photosystem II preparation from the RT cyanobacterium Synechocystis sp. PCC 6803 reveals the presence of novel RT polypeptides."; RL Biochemistry 41:8004-8012(2002). RN [9] {ECO:0007744|PDB:7N8O, ECO:0007744|PDB:7RCV} RP STRUCTURE BY ELECTRON MICROSCOPY (1.93 ANGSTROMS) OF 11-344, FUNCTION, RP COFACTOR, SUBUNIT, SUBCELLULAR LOCATION, AND TOPOLOGY. RC STRAIN=ATCC 27184 / PCC 6803 / Kazusa; RX PubMed=34937700; DOI=10.1073/pnas.2116765118; RA Gisriel C.J., Wang J., Liu J., Flesher D.A., Reiss K.M., Huang H.L., RA Yang K.R., Armstrong W.H., Gunner M.R., Batista V.S., Debus R.J., RA Brudvig G.W.; RT "High-resolution cryo-electron microscopy structure of photosystem II from RT the mesophilic cyanobacterium, Synechocystis sp. PCC 6803."; RL Proc. Natl. Acad. Sci. U.S.A. 119:0-0(2022). 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/PsbD) 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:34937700}. CC -!- CATALYTIC ACTIVITY: CC Reaction=2 a plastoquinone + 4 hnu + 2 H2O = 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:34937700, ECO:0000312|PDB:7N8O}; CC -!- SUBUNIT: PSII is composed of 1 copy each of membrane proteins PsbA, CC PsbB, PsbC, PsbD, PsbE, PsbF, PsbH, PsbI, PsbJ, PsbK, PsbL, PsbM, PsbT, CC PsbX, PsbY, PsbZ, Psb30/Ycf12, peripheral proteins PsbO, CyanoQ (PsbQ), CC PsbU, PsbV and a large number of cofactors. It forms dimeric complexes. CC {ECO:0000255|HAMAP-Rule:MF_01379, ECO:0000269|PubMed:12069591, CC ECO:0000269|PubMed:34937700}. CC -!- SUBCELLULAR LOCATION: Cellular thylakoid membrane {ECO:0000255|HAMAP- CC Rule:MF_01379, ECO:0000269|PubMed:12069591, CC ECO:0000269|PubMed:34937700, ECO:0000305|PubMed:9512353}; Multi-pass CC membrane protein {ECO:0000255|HAMAP-Rule:MF_01379, CC ECO:0000269|PubMed:34937700, ECO:0000305|PubMed:9512353}. CC -!- PTM: C-terminally processed by CtpA; processing is essential to allow CC assembly of the oxygen-evolving complex and photosynthetic growth. CC {ECO:0000255|HAMAP-Rule:MF_01379, ECO:0000269|PubMed:34937700, CC ECO:0000305|PubMed:8034700}. 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 -!- MISCELLANEOUS: Cyanobacteria usually contain more than 2 copies of the CC psbA gene. {ECO:0000255|HAMAP-Rule:MF_01379}. CC -!- MISCELLANEOUS: 2 of the reaction center chlorophylls (ChlD1 and ChlD2) CC are entirely coordinated by water. {ECO:0000255|HAMAP-Rule:MF_01379}. 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}. 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; X56000; CAA39472.1; -; Genomic_DNA. DR EMBL; X13547; CAA31899.1; -; Genomic_DNA. DR EMBL; BA000022; BAA18230.1; -; Genomic_DNA. DR EMBL; BA000022; BAA16586.1; -; Genomic_DNA. DR PIR; S13112; F2YB16. DR PDB; 6WJ6; EM; 2.58 A; A=1-360. DR PDB; 7N8O; EM; 1.93 A; A/a=11-344. DR PDB; 7RCV; EM; 2.01 A; A/a=11-344. DR PDB; 8AM5; EM; 3.10 A; A=1-344. DR PDB; 8ASL; EM; 3.15 A; A=1-344. DR PDB; 8TOW; EM; 2.14 A; A/a=1-360. DR PDBsum; 6WJ6; -. DR PDBsum; 7N8O; -. DR PDBsum; 7RCV; -. DR PDBsum; 8AM5; -. DR PDBsum; 8ASL; -. DR PDBsum; 8TOW; -. DR AlphaFoldDB; P16033; -. DR EMDB; EMD-15522; -. DR EMDB; EMD-15618; -. DR EMDB; EMD-21690; -. DR EMDB; EMD-24239; -. DR EMDB; EMD-24407; -. DR EMDB; EMD-41460; -. DR SMR; P16033; -. DR IntAct; P16033; 5. DR STRING; 1148.gene:10497441; -. DR TCDB; 3.E.2.2.2; the photosynthetic reaction center (prc) family. DR PaxDb; 1148-1651658; -. DR EnsemblBacteria; BAA16586; BAA16586; BAA16586. DR EnsemblBacteria; BAA18230; BAA18230; BAA18230. DR KEGG; syn:sll1867; -. DR KEGG; syn:slr1311; -. DR eggNOG; ENOG502Z87P; Bacteria. DR InParanoid; P16033; -. DR PhylomeDB; P16033; -. DR BRENDA; 1.10.3.9; 6192. DR Proteomes; UP000001425; Chromosome. DR GO; GO:0031676; C:plasma membrane-derived thylakoid membrane; IEA:UniProtKB-SubCell. DR GO; GO:0030096; C:plasma membrane-derived thylakoid photosystem II; IDA:UniProtKB. 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 FunFam; 1.20.85.10:FF:000002; Photosystem II protein D1; 1. DR Gene3D; 1.20.85.10; Photosystem II protein D1-like; 2. 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 NCBIfam; TIGR01151; psbA; 1. DR PANTHER; PTHR33149; PHOTOSYSTEM II PROTEIN D1; 1. DR PANTHER; PTHR33149:SF12; PHOTOSYSTEM II PROTEIN D1; 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; Calcium; Chlorophyll; Chromophore; Electron transport; KW Herbicide resistance; Iron; Magnesium; Manganese; Membrane; Metal-binding; KW Oxidoreductase; Photosynthesis; Photosystem II; Reference proteome; KW Thylakoid; Transmembrane; Transmembrane helix; Transport. FT CHAIN 1..344 FT /note="Photosystem II protein D1 2" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01379" FT /id="PRO_0000090493" FT PROPEP 345..360 FT /evidence="ECO:0000255|HAMAP-Rule:MF_01379, FT ECO:0000305|PubMed:8034700" FT /id="PRO_0000316429" FT TOPO_DOM 1..31 FT /note="Cytoplasmic" FT /evidence="ECO:0000269|PubMed:34937700, FT ECO:0000312|PDB:7N8O" FT TRANSMEM 32..53 FT /note="Helical" FT /evidence="ECO:0000269|PubMed:34937700, FT ECO:0000312|PDB:7N8O" FT TOPO_DOM 54..110 FT /note="Lumenal, thylakoid" FT /evidence="ECO:0000269|PubMed:34937700, FT ECO:0000312|PDB:7N8O" FT TRANSMEM 111..134 FT /note="Helical" FT /evidence="ECO:0000269|PubMed:34937700, FT ECO:0000312|PDB:7N8O" FT TOPO_DOM 135..142 FT /note="Cytoplasmic" FT /evidence="ECO:0000269|PubMed:34937700, FT ECO:0000312|PDB:7N8O" FT TRANSMEM 143..161 FT /note="Helical" FT /evidence="ECO:0000269|PubMed:34937700, FT ECO:0000312|PDB:7N8O" FT TOPO_DOM 162..191 FT /note="Lumenal, thylakoid" FT /evidence="ECO:0000269|PubMed:34937700, FT ECO:0000312|PDB:7N8O" FT TRANSMEM 192..218 FT /note="Helical" FT /evidence="ECO:0000269|PubMed:34937700, FT ECO:0000312|PDB:7N8O" FT TOPO_DOM 219..270 FT /note="Cytoplasmic" FT /evidence="ECO:0000269|PubMed:34937700, FT ECO:0000312|PDB:7N8O" FT TRANSMEM 271..295 FT /note="Helical" FT /evidence="ECO:0000269|PubMed:34937700, FT ECO:0000312|PDB:7N8O" FT TOPO_DOM 296..360 FT /note="Lumenal, thylakoid" FT /evidence="ECO:0000269|PubMed:34937700, FT ECO:0000312|PDB:7N8O" 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:34937700, ECO:0000312|PDB:7N8O" 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:34937700, ECO:0000312|PDB:7N8O" FT BINDING 147 FT /ligand="pheophytin a" FT /ligand_id="ChEBI:CHEBI:136840" FT /ligand_label="D1" FT /evidence="ECO:0000269|PubMed:34937700, FT ECO:0000312|PDB:7N8O" 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:34937700, ECO:0000312|PDB:7N8O" 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:34937700, ECO:0000312|PDB:7N8O" 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:34937700, ECO:0000312|PDB:7N8O" 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:34937700, ECO:0000312|PDB:7N8O" 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:34937700, ECO:0000312|PDB:7N8O" FT BINDING 264 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:34937700, ECO:0000312|PDB:7N8O" FT BINDING 265 FT /ligand="a quinone" FT /ligand_id="ChEBI:CHEBI:132124" FT /ligand_label="B" FT /evidence="ECO:0000269|PubMed:34937700, FT ECO:0000312|PDB:7N8O" 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:34937700, ECO:0000312|PDB:7N8O" 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:34937700, ECO:0000312|PDB:7N8O" FT BINDING 333 FT /ligand="[CaMn4O5] cluster" FT /ligand_id="ChEBI:CHEBI:189552" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01379" FT BINDING 337 FT /ligand="[CaMn4O5] cluster" FT /ligand_id="ChEBI:CHEBI:189552" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01379, FT ECO:0000269|PubMed:34937700, ECO:0000312|PDB:7N8O" 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:34937700, ECO:0000312|PDB:7N8O" FT BINDING 344 FT /ligand="[CaMn4O5] cluster" FT /ligand_id="ChEBI:CHEBI:189552" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01379, FT ECO:0000305|PubMed:34937700, ECO:0000312|PDB:7N8O" FT SITE 161 FT /note="Tyrosine radical intermediate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01379" 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 ECO:0000269|PubMed:34937700, ECO:0000305|PubMed:8034700, FT ECO:0000312|PDB:7N8O" FT MUTAGEN 221..222 FT /note="SS->LA: Strong herbicide resistance." FT /evidence="ECO:0000269|PubMed:8068689" FT MUTAGEN 227..228 FT /note="TT->AA: Herbicide resistance." FT /evidence="ECO:0000269|PubMed:8068689" FT MUTAGEN 237 FT /note="Y->F: Weak herbicide resistance." FT /evidence="ECO:0000269|PubMed:8068689" FT MUTAGEN 238 FT /note="K->V: Weak herbicide resistance." FT /evidence="ECO:0000269|PubMed:8068689" FT MUTAGEN 255 FT /note="F->W: Herbicide resistance." FT /evidence="ECO:0000269|PubMed:1498597" FT MUTAGEN 257 FT /note="R->V: Herbicide resistance." FT /evidence="ECO:0000269|PubMed:8068689" FT MUTAGEN 264 FT /note="S->A: Strong herbicide resistance." FT /evidence="ECO:0000269|PubMed:1498597" FT MUTAGEN 271 FT /note="L->V,M,A,S: Herbicide resistance." FT /evidence="ECO:0000269|PubMed:1498597" FT HELIX 13..21 FT /evidence="ECO:0007829|PDB:7N8O" FT STRAND 26..28 FT /evidence="ECO:0007829|PDB:7N8O" FT HELIX 31..54 FT /evidence="ECO:0007829|PDB:7N8O" FT STRAND 62..64 FT /evidence="ECO:0007829|PDB:7N8O" FT HELIX 71..73 FT /evidence="ECO:0007829|PDB:7N8O" FT TURN 77..79 FT /evidence="ECO:0007829|PDB:7N8O" FT TURN 87..91 FT /evidence="ECO:0007829|PDB:7N8O" FT HELIX 96..98 FT /evidence="ECO:0007829|PDB:7N8O" FT STRAND 99..101 FT /evidence="ECO:0007829|PDB:7N8O" FT HELIX 102..107 FT /evidence="ECO:0007829|PDB:7N8O" FT HELIX 110..136 FT /evidence="ECO:0007829|PDB:7N8O" FT HELIX 143..158 FT /evidence="ECO:0007829|PDB:7N8O" FT HELIX 160..165 FT /evidence="ECO:0007829|PDB:7N8O" FT HELIX 168..170 FT /evidence="ECO:0007829|PDB:7N8O" FT HELIX 176..190 FT /evidence="ECO:0007829|PDB:7N8O" FT HELIX 192..194 FT /evidence="ECO:0007829|PDB:7N8O" FT HELIX 196..221 FT /evidence="ECO:0007829|PDB:7N8O" FT STRAND 229..231 FT /evidence="ECO:0007829|PDB:7N8O" FT HELIX 233..236 FT /evidence="ECO:0007829|PDB:7N8O" FT HELIX 248..258 FT /evidence="ECO:0007829|PDB:7N8O" FT HELIX 261..263 FT /evidence="ECO:0007829|PDB:7N8O" FT HELIX 268..293 FT /evidence="ECO:0007829|PDB:7N8O" FT TURN 294..296 FT /evidence="ECO:0007829|PDB:7N8O" FT STRAND 297..299 FT /evidence="ECO:0007829|PDB:7N8O" FT STRAND 309..311 FT /evidence="ECO:0007829|PDB:7N8O" FT HELIX 317..331 FT /evidence="ECO:0007829|PDB:7N8O" FT TURN 332..336 FT /evidence="ECO:0007829|PDB:7N8O" FT STRAND 339..341 FT /evidence="ECO:0007829|PDB:7N8O" SQ SEQUENCE 360 AA; 39721 MW; 2FE4088498A416C2 CRC64; MTTTLQQRES ASLWEQFCQW VTSTNNRIYV GWFGTLMIPT LLTATTCFII AFIAAPPVDI DGIREPVAGS LLYGNNIISG AVVPSSNAIG LHFYPIWEAA SLDEWLYNGG PYQLVVFHFL IGIFCYMGRQ WELSYRLGMR PWICVAYSAP VSAATAVFLI YPIGQGSFSD GMPLGISGTF NFMIVFQAEH NILMHPFHML GVAGVFGGSL FSAMHGSLVT SSLVRETTEV ESQNYGYKFG QEEETYNIVA AHGYFGRLIF QYASFNNSRS LHFFLGAWPV IGIWFTAMGV STMAFNLNGF NFNQSILDSQ GRVIGTWADV LNRANIGFEV MHERNAHNFP LDLASGEQAP VALTAPAVNG //