ID PSAB_CHLRE Reviewed; 735 AA. AC P09144; B7U1I8; Q36714; Q8HR52; Q9GH44; DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot. DT 28-MAR-2003, sequence version 4. DT 24-JAN-2024, entry version 172. DE RecName: Full=Photosystem I P700 chlorophyll a apoprotein A2; DE EC=1.97.1.12; DE AltName: Full=PSI-B; DE AltName: Full=PsaB; GN Name=psaB; Synonyms=ps1a2; OS Chlamydomonas reinhardtii (Chlamydomonas smithii). OG Plastid; Chloroplast. OC Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Chlorophyceae; OC CS clade; Chlamydomonadales; Chlamydomonadaceae; Chlamydomonas. OX NCBI_TaxID=3055; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=CC-406; RX PubMed=16453785; DOI=10.1002/j.1460-2075.1987.tb02489.x; RA Kueck U., Choquet Y., Schneider M., Dron M., Bennoun P.; RT "Structural and transcription analysis of two homologous genes for the P700 RT chlorophyll a-apoproteins in Chlamydomonas reinhardtii: evidence for in RT vivo trans-splicing."; RL EMBO J. 6:2185-2195(1987). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RA Forsyth A.M., Redding K., Purton S.; RT "Revised sequence of the Chlamydomonas reinhardtii chloroplast gene psaB."; RL Submitted (NOV-2002) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CC-503; RX PubMed=19473533; DOI=10.1186/1471-2148-9-120; RA Smith D.R., Lee R.W.; RT "Nucleotide diversity of the Chlamydomonas reinhardtii plastid genome: RT addressing the mutational-hazard hypothesis."; RL BMC Evol. Biol. 9:120-120(2009). RN [4] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 80-578. RC STRAIN=137c / CC-125; RX PubMed=11083939; DOI=10.1006/mpev.2000.0831; RA Nozaki H., Misawa K., Kajita T., Kato M., Nohara S., Watanabe M.M.; RT "Origin and evolution of the colonial Volvocales (Chlorophyceae) as RT inferred from multiple, chloroplast gene sequences."; RL Mol. Phylogenet. Evol. 17:256-268(2000). RN [5] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 493-735. RX PubMed=6302265; DOI=10.1016/0022-2836(82)90547-2; RA Dron M., Rahire M., Rochaix J.-D.; RT "Sequence of the chloroplast DNA region of Chlamydomonas reinhardii RT containing the gene of the large subunit of ribulose bisphosphate RT carboxylase and parts of its flanking genes."; RL J. Mol. Biol. 162:775-793(1982). RN [6] RP PARTIAL NUCLEOTIDE SEQUENCE [GENOMIC DNA] (MUTANT AC-U-G-2.3). RC STRAIN=CC-2341; RX PubMed=1959594; DOI=10.1016/0014-5793(91)80851-s; RA Bingham S.E., Xu R.H., Webber A.N.; RT "Transformation of chloroplasts with the psaB gene encoding a polypeptide RT of the photosystem I reaction center."; RL FEBS Lett. 292:137-140(1991). RN [7] RP IDENTIFICATION, AND COMPLETE PLASTID GENOME. RX PubMed=12417694; DOI=10.1105/tpc.006155; RA Maul J.E., Lilly J.W., Cui L., dePamphilis C.W., Miller W., Harris E.H., RA Stern D.B.; RT "The Chlamydomonas reinhardtii plastid chromosome: islands of genes in a RT sea of repeats."; RL Plant Cell 14:2659-2679(2002). RN [8] RP MUTAGENESIS OF PRO-559 AND CYS-560. RC STRAIN=137c / CC-125, and CC-2341; RX PubMed=8509430; DOI=10.1016/s0021-9258(18)31484-4; RA Webber A.N., Gibbs P.B., Ward J.B., Bingham S.E.; RT "Site-directed mutagenesis of the photosystem I reaction center in RT chloroplasts. The proline-cysteine motif."; RL J. Biol. Chem. 268:12990-12995(1993). RN [9] RP MUTAGENESIS OF ASP-561; PRO-563 AND ARG-565. RC STRAIN=137c / CC-125; RX PubMed=7756260; DOI=10.1021/bi00019a010; RA Rodday S.M., Webber A.N., Bingham S.E., Biggins J.; RT "Evidence that the FX domain in photosystem I interacts with the subunit RT PsaC: site-directed changes in PsaB destabilize the subunit interaction in RT Chlamydomonas reinhardtii."; RL Biochemistry 34:6328-6334(1995). RN [10] RP MUTAGENESIS OF HIS-655. RC STRAIN=FuD7; RX PubMed=8841129; DOI=10.1021/bi961198w; RA Webber A.N., Su H., Bingham S.E., Kaess H., Krabben L., Kuhn M., Jordan R., RA Schlodder E., Lubitz W.; RT "Site-directed mutations affecting the spectroscopic characteristics and RT midpoint potential of the primary donor in photosystem I."; RL Biochemistry 35:12857-12863(1996). RN [11] RP MUTAGENESIS OF CONSERVED HISTIDINES. RC STRAIN=137c / CC-125; RX PubMed=9427740; DOI=10.1093/emboj/17.1.50; RA Redding K., MacMillan F., Leibl W., Brettel K., Hanley J., Rutherford A.W., RA Breton J., Rochaix J.-D.; RT "A systematic survey of conserved histidines in the core subunits of RT photosystem I by site-directed mutagenesis reveals the likely axial ligands RT of P700."; RL EMBO J. 17:50-60(1998). RN [12] RP MUTAGENESIS OF HIS-655. RC STRAIN=CC-2696; RX PubMed=11041867; DOI=10.1021/bi001200q; RA Krabben L., Schlodder E., Jordan R., Carbonera D., Giacometti G., Lee H., RA Webber A.N., Lubitz W.; RT "Influence of the axial ligands on the spectral properties of P700 of RT photosystem I: a study of site-directed mutants."; RL Biochemistry 39:13012-13025(2000). RN [13] RP MUTAGENESIS OF A1 PHYLLOQUINONE LIGANDS. RC STRAIN=137c / CC-125; RX PubMed=11274371; DOI=10.1073/pnas.081078898; RA Guergova-Kuras M., Boudreaux B., Joliot A., Joliot P., Redding K.; RT "Evidence for two active branches for electron transfer in photosystem I."; RL Proc. Natl. Acad. Sci. U.S.A. 98:4437-4442(2001). RN [14] RP PRESENCE OF CHLOROPHYLL A' IN PSI. RC STRAIN=IAM C-9; RX PubMed=12755700; DOI=10.1046/j.1432-1033.2003.03616.x; RA Nakamura A., Akai M., Yoshida E., Taki T., Watanabe T.; RT "Reversed-phase HPLC determination of chlorophyll a' and phylloquinone in RT photosystem I of oxygenic photosynthetic organisms."; RL Eur. J. Biochem. 270:2446-2458(2003). RN [15] RP MUTAGENESIS OF A1 PHYLLOQUINONE LIGANDS. RC STRAIN=137c / CC-125; RX PubMed=11489879; DOI=10.1074/jbc.m102327200; RA Boudreaux B., MacMillan F., Teutloff C., Agalarov R., Gu F., Grimaldi S., RA Bittl R., Brettel K., Redding K.; RT "Mutations in both sides of the photosystem I reaction center identify the RT phylloquinone observed by electron paramagnetic resonance spectroscopy."; RL J. Biol. Chem. 276:37299-37306(2001). CC -!- FUNCTION: PsaA and PsaB bind P700, the primary electron donor of CC photosystem I (PSI), as well as the electron acceptors A0, A1 and FX. CC PSI is a plastocyanin/cytochrome c6-ferredoxin oxidoreductase, CC converting photonic excitation into a charge separation, which CC transfers an electron from the donor P700 chlorophyll pair to the CC spectroscopically characterized acceptors A0, A1, FX, FA and FB in CC turn. Oxidized P700 is reduced on the lumenal side of the thylakoid CC membrane by plastocyanin or cytochrome c6. CC -!- FUNCTION: Both potential cofactor branches in PSI seem to be active; CC however, electron transfer seems to proceed preferentially down the CC path including the phylloquinone bound by PsaA. CC -!- CATALYTIC ACTIVITY: CC Reaction=hnu + oxidized [2Fe-2S]-[ferredoxin] + reduced [plastocyanin] CC = oxidized [plastocyanin] + reduced [2Fe-2S]-[ferredoxin]; CC Xref=Rhea:RHEA:30407, Rhea:RHEA-COMP:10000, Rhea:RHEA-COMP:10001, CC Rhea:RHEA-COMP:10039, Rhea:RHEA-COMP:10040, ChEBI:CHEBI:29036, CC ChEBI:CHEBI:30212, ChEBI:CHEBI:33737, ChEBI:CHEBI:33738, CC ChEBI:CHEBI:49552; EC=1.97.1.12; CC -!- COFACTOR: CC Note=P700 is a chlorophyll a/chlorophyll a' dimer, A0 is one or more CC chlorophyll a, A1 is one or both phylloquinones and FX is a shared 4Fe- CC 4S iron-sulfur center. {ECO:0000250}; CC -!- SUBUNIT: The PsaA/B heterodimer binds the P700 chlorophyll special pair CC and subsequent electron acceptors. PSI consists of a core antenna CC complex that captures photons, and an electron transfer chain that CC converts photonic excitation into a charge separation. The eukaryotic CC PSI reaction center is composed of at least 11 subunits. CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane; Multi- CC pass membrane protein. CC -!- SIMILARITY: Belongs to the PsaA/PsaB family. {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; X05848; CAA29287.1; -; Genomic_DNA. DR EMBL; U57326; AAN78307.1; -; Genomic_DNA. DR EMBL; FJ423446; ACJ50135.1; -; Genomic_DNA. DR EMBL; AB044470; BAB18396.1; -; Genomic_DNA. DR EMBL; J01399; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; S67792; AAB20423.2; -; Genomic_DNA. DR EMBL; BK000554; DAA00949.2; -; Genomic_DNA. DR PIR; B28341; B28341. DR PIR; S18319; S18319. DR RefSeq; NP_958404.1; NC_005353.1. DR PDB; 6IJJ; EM; 2.89 A; B=1-735. DR PDB; 6IJO; EM; 3.30 A; B=1-735. DR PDB; 6JO5; EM; 2.90 A; B=4-735. DR PDB; 6JO6; EM; 2.90 A; B=4-735. DR PDB; 7BGI; EM; 2.54 A; B=2-734. DR PDB; 7BLX; EM; 3.15 A; B=2-734. DR PDB; 7D0J; EM; 3.42 A; B=2-735. DR PDB; 7DZ7; EM; 2.84 A; B=1-735. DR PDB; 7DZ8; EM; 3.16 A; B=1-735. DR PDB; 7O01; EM; 17.10 A; B/b=2-734. DR PDB; 7R3K; EM; 2.52 A; B=1-735. DR PDB; 7WYI; EM; 3.90 A; B=1-735. DR PDB; 7WZN; EM; 4.90 A; B=1-735. DR PDB; 7ZQ9; EM; 2.74 A; B=1-735. DR PDB; 7ZQC; EM; 2.31 A; B=1-735. DR PDB; 7ZQD; EM; 2.97 A; B/B2=1-735. DR PDB; 8H2U; X-ray; 3.40 A; B=1-735. DR PDBsum; 6IJJ; -. DR PDBsum; 6IJO; -. DR PDBsum; 6JO5; -. DR PDBsum; 6JO6; -. DR PDBsum; 7BGI; -. DR PDBsum; 7BLX; -. DR PDBsum; 7D0J; -. DR PDBsum; 7DZ7; -. DR PDBsum; 7DZ8; -. DR PDBsum; 7O01; -. DR PDBsum; 7R3K; -. DR PDBsum; 7WYI; -. DR PDBsum; 7WZN; -. DR PDBsum; 7ZQ9; -. DR PDBsum; 7ZQC; -. DR PDBsum; 7ZQD; -. DR PDBsum; 8H2U; -. DR AlphaFoldDB; P09144; -. DR EMDB; EMD-12180; -. DR EMDB; EMD-12227; -. DR EMDB; EMD-12672; -. DR EMDB; EMD-14248; -. DR EMDB; EMD-14867; -. DR EMDB; EMD-14870; -. DR EMDB; EMD-14871; -. DR EMDB; EMD-30536; -. DR EMDB; EMD-30925; -. DR EMDB; EMD-30926; -. DR EMDB; EMD-32892; -. DR EMDB; EMD-32907; -. DR EMDB; EMD-9678; -. DR EMDB; EMD-9680; -. DR EMDB; EMD-9853; -. DR EMDB; EMD-9854; -. DR SMR; P09144; -. DR IntAct; P09144; 5. DR STRING; 3055.P09144; -. DR PaxDb; 3055-DAA00949; -. DR GeneID; 2717038; -. DR KEGG; cre:ChreCp048; -. DR eggNOG; ENOG502QRYE; Eukaryota. DR HOGENOM; CLU_016126_1_0_1; -. DR InParanoid; P09144; -. DR BioCyc; CHLAMY:CHRECP048-MONOMER; -. DR BioCyc; MetaCyc:CHRECP048-MONOMER; -. DR BRENDA; 1.97.1.12; 1318. DR Proteomes; UP000006906; Chloroplast. DR GO; GO:0009535; C:chloroplast thylakoid membrane; IEA:UniProtKB-SubCell. DR GO; GO:0009522; C:photosystem I; IEA:UniProtKB-KW. DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW. DR GO; GO:0016168; F:chlorophyll binding; IEA:UniProtKB-KW. DR GO; GO:0009055; F:electron transfer activity; IEA:UniProtKB-UniRule. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule. DR GO; GO:0015979; P:photosynthesis; IEA:UniProtKB-UniRule. DR Gene3D; 1.20.1130.10; Photosystem I PsaA/PsaB; 1. DR HAMAP; MF_00482; PSI_PsaB; 1. DR InterPro; IPR001280; PSI_PsaA/B. DR InterPro; IPR020586; PSI_PsaA/B_CS. DR InterPro; IPR036408; PSI_PsaA/B_sf. DR InterPro; IPR006244; PSI_PsaB. DR NCBIfam; TIGR01336; psaB; 1. DR PANTHER; PTHR30128; OUTER MEMBRANE PROTEIN, OMPA-RELATED; 1. DR PANTHER; PTHR30128:SF75; PHOTOSYSTEM I P700 CHLOROPHYLL A APOPROTEIN A2; 1. DR Pfam; PF00223; PsaA_PsaB; 1. DR PIRSF; PIRSF002905; PSI_A; 1. DR PRINTS; PR00257; PHOTSYSPSAAB. DR SUPFAM; SSF81558; Photosystem I subunits PsaA/PsaB; 1. DR PROSITE; PS00419; PHOTOSYSTEM_I_PSAAB; 1. PE 1: Evidence at protein level; KW 3D-structure; 4Fe-4S; Chlorophyll; Chloroplast; Chromophore; KW Electron transport; Iron; Iron-sulfur; Magnesium; Membrane; Metal-binding; KW Oxidoreductase; Photosynthesis; Photosystem I; Plastid; Reference proteome; KW Thylakoid; Transmembrane; Transmembrane helix; Transport. FT CHAIN 1..735 FT /note="Photosystem I P700 chlorophyll a apoprotein A2" FT /id="PRO_0000088609" FT TRANSMEM 47..70 FT /note="Helical; Name=I" FT /evidence="ECO:0000255" FT TRANSMEM 136..159 FT /note="Helical; Name=II" FT /evidence="ECO:0000255" FT TRANSMEM 176..200 FT /note="Helical; Name=III" FT /evidence="ECO:0000255" FT TRANSMEM 274..292 FT /note="Helical; Name=IV" FT /evidence="ECO:0000255" FT TRANSMEM 331..354 FT /note="Helical; Name=V" FT /evidence="ECO:0000255" FT TRANSMEM 370..396 FT /note="Helical; Name=VI" FT /evidence="ECO:0000255" FT TRANSMEM 418..440 FT /note="Helical; Name=VII" FT /evidence="ECO:0000255" FT TRANSMEM 518..536 FT /note="Helical; Name=VIII" FT /evidence="ECO:0000255" FT TRANSMEM 576..597 FT /note="Helical; Name=IX" FT /evidence="ECO:0000255" FT TRANSMEM 644..666 FT /note="Helical; Name=X" FT /evidence="ECO:0000255" FT TRANSMEM 708..728 FT /note="Helical; Name=XI" FT /evidence="ECO:0000255" FT BINDING 560 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /ligand_note="ligand shared between dimeric partners" FT BINDING 569 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /ligand_note="ligand shared between dimeric partners" FT /evidence="ECO:0000250" FT BINDING 655 FT /ligand="chlorophyll a" FT /ligand_id="ChEBI:CHEBI:58416" FT /ligand_label="B1" FT /ligand_part="Mg" FT /ligand_part_id="ChEBI:CHEBI:25107" FT /note="axial binding residue" FT BINDING 663 FT /ligand="chlorophyll a" FT /ligand_id="ChEBI:CHEBI:58416" FT /ligand_label="B3" FT /ligand_part="Mg" FT /ligand_part_id="ChEBI:CHEBI:25107" FT /note="axial binding residue" FT /evidence="ECO:0000250" FT BINDING 671 FT /ligand="chlorophyll a" FT /ligand_id="ChEBI:CHEBI:58416" FT /ligand_label="B3" FT /evidence="ECO:0000250" FT BINDING 672 FT /ligand="phylloquinone" FT /ligand_id="ChEBI:CHEBI:18067" FT /ligand_label="B" FT MUTAGEN 559 FT /note="P->A,L: Assembles functional PSI. Reaction center is FT somewhat unstable and interaction with PsaC is impaired. FT The L mutant is less stable than the A mutant." FT /evidence="ECO:0000269|PubMed:8509430" FT MUTAGEN 560 FT /note="C->H: Loss of PSI assembly and function." FT /evidence="ECO:0000269|PubMed:8509430" FT MUTAGEN 561 FT /note="D->N: Loss of PSI assembly and function." FT /evidence="ECO:0000269|PubMed:7756260" FT MUTAGEN 563 FT /note="P->L: Assembles functional PSI. Reaction center is FT somewhat unstable and interaction with PsaC is impaired." FT /evidence="ECO:0000269|PubMed:7756260" FT MUTAGEN 565 FT /note="R->E: Loss of PSI assembly and function." FT /evidence="ECO:0000269|PubMed:7756260" FT MUTAGEN 655 FT /note="H->C,G,N,S: Contains somewhat decreased amounts of FT PSI, depending on the strain; significantly changes the FT spin density of the P700+ cation radical." FT /evidence="ECO:0000269|PubMed:11041867, FT ECO:0000269|PubMed:8841129" FT MUTAGEN 655 FT /note="H->D: Very little PSI detected." FT /evidence="ECO:0000269|PubMed:11041867, FT ECO:0000269|PubMed:8841129" FT MUTAGEN 655 FT /note="H->F,L: Loss of P700 function." FT /evidence="ECO:0000269|PubMed:11041867, FT ECO:0000269|PubMed:8841129" FT MUTAGEN 655 FT /note="H->Q: Impairment of P700 function. More severe; when FT associated with 'Q-676' in PsaA." FT /evidence="ECO:0000269|PubMed:11041867, FT ECO:0000269|PubMed:8841129" FT MUTAGEN 655 FT /note="H->R: No PSI detected." FT /evidence="ECO:0000269|PubMed:11041867, FT ECO:0000269|PubMed:8841129" FT MUTAGEN 672 FT /note="W->F: Still able to photoaccumulate an electron on FT A1." FT CONFLICT 15 FT /note="Q -> R (in Ref. 1; CAA29287)" FT /evidence="ECO:0000305" FT CONFLICT 18 FT /note="T -> A (in Ref. 1; CAA29287)" FT /evidence="ECO:0000305" FT CONFLICT 21 FT /note="R -> I (in Ref. 1; CAA29287)" FT /evidence="ECO:0000305" FT CONFLICT 37..38 FT /note="GM -> VW (in Ref. 1; CAA29287)" FT /evidence="ECO:0000305" FT CONFLICT 48..49 FT /note="FA -> IS (in Ref. 1; CAA29287)" FT /evidence="ECO:0000305" FT CONFLICT 89 FT /note="A -> C (in Ref. 1; CAA29287)" FT /evidence="ECO:0000305" FT CONFLICT 203 FT /note="S -> LQ (in Ref. 1; CAA29287)" FT /evidence="ECO:0000305" FT CONFLICT 298 FT /note="I -> N (in Ref. 1; CAA29287)" FT /evidence="ECO:0000305" FT CONFLICT 335 FT /note="L -> I (in Ref. 1; CAA29287)" FT /evidence="ECO:0000305" FT CONFLICT 515 FT /note="P -> L (in Ref. 1; CAA29287 and 5; J01399)" FT /evidence="ECO:0000305" FT STRAND 4..6 FT /evidence="ECO:0007829|PDB:7R3K" FT HELIX 11..14 FT /evidence="ECO:0007829|PDB:7R3K" FT STRAND 17..19 FT /evidence="ECO:0007829|PDB:7D0J" FT HELIX 20..27 FT /evidence="ECO:0007829|PDB:7R3K" FT STRAND 28..30 FT /evidence="ECO:0007829|PDB:7DZ7" FT HELIX 32..34 FT /evidence="ECO:0007829|PDB:7R3K" FT HELIX 40..72 FT /evidence="ECO:0007829|PDB:7R3K" FT HELIX 75..78 FT /evidence="ECO:0007829|PDB:7R3K" FT TURN 82..84 FT /evidence="ECO:0007829|PDB:7R3K" FT STRAND 88..91 FT /evidence="ECO:0007829|PDB:7R3K" FT HELIX 99..105 FT /evidence="ECO:0007829|PDB:7R3K" FT STRAND 111..116 FT /evidence="ECO:0007829|PDB:7R3K" FT HELIX 121..127 FT /evidence="ECO:0007829|PDB:7R3K" FT HELIX 133..156 FT /evidence="ECO:0007829|PDB:7R3K" FT HELIX 160..162 FT /evidence="ECO:0007829|PDB:7DZ7" FT HELIX 166..170 FT /evidence="ECO:0007829|PDB:7R3K" FT HELIX 172..181 FT /evidence="ECO:0007829|PDB:7R3K" FT TURN 182..184 FT /evidence="ECO:0007829|PDB:7R3K" FT HELIX 185..197 FT /evidence="ECO:0007829|PDB:7R3K" FT HELIX 199..203 FT /evidence="ECO:0007829|PDB:7R3K" FT TURN 210..212 FT /evidence="ECO:0007829|PDB:7R3K" FT TURN 213..215 FT /evidence="ECO:0007829|PDB:6IJO" FT TURN 220..223 FT /evidence="ECO:0007829|PDB:7R3K" FT HELIX 224..228 FT /evidence="ECO:0007829|PDB:7R3K" FT HELIX 231..235 FT /evidence="ECO:0007829|PDB:7R3K" FT TURN 264..266 FT /evidence="ECO:0007829|PDB:7R3K" FT HELIX 271..288 FT /evidence="ECO:0007829|PDB:7R3K" FT STRAND 294..297 FT /evidence="ECO:0007829|PDB:7R3K" FT HELIX 302..308 FT /evidence="ECO:0007829|PDB:7R3K" FT HELIX 312..314 FT /evidence="ECO:0007829|PDB:7DZ7" FT TURN 315..322 FT /evidence="ECO:0007829|PDB:7R3K" FT HELIX 323..328 FT /evidence="ECO:0007829|PDB:7R3K" FT HELIX 331..355 FT /evidence="ECO:0007829|PDB:7R3K" FT STRAND 363..365 FT /evidence="ECO:0007829|PDB:7DZ7" FT HELIX 366..397 FT /evidence="ECO:0007829|PDB:7R3K" FT HELIX 401..404 FT /evidence="ECO:0007829|PDB:7R3K" FT STRAND 405..407 FT /evidence="ECO:0007829|PDB:6IJO" FT HELIX 408..414 FT /evidence="ECO:0007829|PDB:7R3K" FT HELIX 416..446 FT /evidence="ECO:0007829|PDB:7R3K" FT HELIX 450..452 FT /evidence="ECO:0007829|PDB:7R3K" FT HELIX 459..468 FT /evidence="ECO:0007829|PDB:7R3K" FT HELIX 478..480 FT /evidence="ECO:0007829|PDB:7R3K" FT STRAND 482..484 FT /evidence="ECO:0007829|PDB:8H2U" FT HELIX 485..489 FT /evidence="ECO:0007829|PDB:7R3K" FT TURN 490..494 FT /evidence="ECO:0007829|PDB:7R3K" FT HELIX 495..502 FT /evidence="ECO:0007829|PDB:7R3K" FT STRAND 505..508 FT /evidence="ECO:0007829|PDB:6JO5" FT HELIX 515..540 FT /evidence="ECO:0007829|PDB:7R3K" FT HELIX 551..553 FT /evidence="ECO:0007829|PDB:7R3K" FT STRAND 559..561 FT /evidence="ECO:0007829|PDB:7R3K" FT HELIX 573..604 FT /evidence="ECO:0007829|PDB:7R3K" FT HELIX 608..613 FT /evidence="ECO:0007829|PDB:7R3K" FT STRAND 614..616 FT /evidence="ECO:0007829|PDB:7BLX" FT HELIX 617..623 FT /evidence="ECO:0007829|PDB:7R3K" FT TURN 624..626 FT /evidence="ECO:0007829|PDB:7R3K" FT HELIX 627..629 FT /evidence="ECO:0007829|PDB:7R3K" FT HELIX 630..633 FT /evidence="ECO:0007829|PDB:7R3K" FT STRAND 635..637 FT /evidence="ECO:0007829|PDB:7R3K" FT HELIX 645..666 FT /evidence="ECO:0007829|PDB:7R3K" FT HELIX 669..685 FT /evidence="ECO:0007829|PDB:7R3K" FT HELIX 689..691 FT /evidence="ECO:0007829|PDB:7R3K" FT STRAND 695..697 FT /evidence="ECO:0007829|PDB:7R3K" FT HELIX 703..733 FT /evidence="ECO:0007829|PDB:7R3K" SQ SEQUENCE 735 AA; 82109 MW; 82F9914CE07A7908 CRC64; MATKLFPKFS QGLAQDPTTR RIWYGLAMAH DFESHDGMTE ENLYQKIFAS HFGQLSIIFL WTSGNLFHVA WQGNFEQWVT DPVHIRPIAH AIWDPHFGQP AVEAFTRGGA SGPVNISTSG VYQWWYTIGM RTNQDLYVGS VFLALVSAIF LFAGWLHLQP NFQPSLSWFK DAESRLNHHL SGLFGVSSLA WTGHLVHVAI PESRGQHVGW DNFLSVLPHP QGLTPFFTGN WAAYAQSPDT ASHVFGTAQG SGQAILTFLG GFHPQTQSLW LTDMAHHHLA IAVIFIVAGH MYRTNFGIGH RMQAILEAHT PPSGSLGAGH KGLFDTVNNS LHFQLGLALA SVGTITSLVA QHMYSLPPYA FQAIDFTTQA ALYTHHQYIA GFIMCGAFAH GAIFFIRDYD PEQNKGNVLA RMLDHKEALI SHLSWVSLFL GFHTLGLYVH NDVMQAFGTP EKQILIEPVF AQWIQAAHGK ALYGFDFLLS SKTSAAFANG QSLWLPGWLD AINNNQNSLF LTIGPGDFLV HHAIALGLHT TTLILVKGAL DARGSKLMPD KKDFGYSFPC DGPGRGGTCD ISAYDAFYLA VFWMLNTIGW VTFYWHWKHL TLWQGNVAQF DESSTYLMGW LRDYLWLNSS QLINGYNPFG MNSLSVWAWT FLFGHLIYAT GFMFLISWRG YWQELIETLV WAHEKTPLAN LVYWKDKPVA LSIVQARLVG LAHFSVGYIF TYAAFLIAST SGRFG //