PSAB_CHLRE
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 03-AUG-2022, entry version 165.
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}.
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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 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 AlphaFoldDB; P09144; -.
DR SMR; P09144; -.
DR IntAct; P09144; 5.
DR STRING; 3055.DAA00949; -.
DR PaxDb; P09144; -.
DR PRIDE; P09144; -.
DR GeneID; 2717038; -.
DR KEGG; cre:ChreCp048; -.
DR eggNOG; ENOG502QRYE; Eukaryota.
DR HOGENOM; CLU_016126_1_0_1; -.
DR InParanoid; P09144; -.
DR OrthoDB; 209831at2759; -.
DR BioCyc; MetaCyc:CHRECP048-MON; -.
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:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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; -; 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 Pfam; PF00223; PsaA_PsaB; 1.
DR PIRSF; PIRSF002905; PSI_A; 1.
DR PRINTS; PR00257; PHOTSYSPSAAB.
DR SUPFAM; SSF81558; SSF81558; 1.
DR TIGRFAMs; TIGR01336; 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:7BGI"
FT HELIX 11..14
FT /evidence="ECO:0007829|PDB:7BGI"
FT STRAND 17..19
FT /evidence="ECO:0007829|PDB:7D0J"
FT HELIX 20..27
FT /evidence="ECO:0007829|PDB:7BGI"
FT STRAND 28..30
FT /evidence="ECO:0007829|PDB:7DZ7"
FT HELIX 32..34
FT /evidence="ECO:0007829|PDB:7BGI"
FT HELIX 40..72
FT /evidence="ECO:0007829|PDB:7BGI"
FT HELIX 75..78
FT /evidence="ECO:0007829|PDB:7BGI"
FT TURN 82..84
FT /evidence="ECO:0007829|PDB:7BGI"
FT STRAND 88..91
FT /evidence="ECO:0007829|PDB:7BGI"
FT HELIX 99..105
FT /evidence="ECO:0007829|PDB:7BGI"
FT STRAND 114..116
FT /evidence="ECO:0007829|PDB:7BGI"
FT HELIX 121..128
FT /evidence="ECO:0007829|PDB:7BGI"
FT HELIX 133..156
FT /evidence="ECO:0007829|PDB:7BGI"
FT HELIX 160..162
FT /evidence="ECO:0007829|PDB:7DZ7"
FT HELIX 166..169
FT /evidence="ECO:0007829|PDB:7BGI"
FT HELIX 172..181
FT /evidence="ECO:0007829|PDB:7BGI"
FT TURN 182..184
FT /evidence="ECO:0007829|PDB:7BGI"
FT HELIX 185..197
FT /evidence="ECO:0007829|PDB:7BGI"
FT HELIX 199..203
FT /evidence="ECO:0007829|PDB:7BGI"
FT TURN 210..214
FT /evidence="ECO:0007829|PDB:7BGI"
FT TURN 220..223
FT /evidence="ECO:0007829|PDB:7BGI"
FT HELIX 224..228
FT /evidence="ECO:0007829|PDB:7BGI"
FT HELIX 231..235
FT /evidence="ECO:0007829|PDB:7BGI"
FT TURN 264..266
FT /evidence="ECO:0007829|PDB:7BGI"
FT HELIX 271..288
FT /evidence="ECO:0007829|PDB:7BGI"
FT STRAND 294..297
FT /evidence="ECO:0007829|PDB:7BGI"
FT HELIX 302..307
FT /evidence="ECO:0007829|PDB:7BGI"
FT HELIX 312..314
FT /evidence="ECO:0007829|PDB:7DZ7"
FT TURN 315..318
FT /evidence="ECO:0007829|PDB:7BGI"
FT TURN 320..322
FT /evidence="ECO:0007829|PDB:7BGI"
FT HELIX 323..328
FT /evidence="ECO:0007829|PDB:7BGI"
FT HELIX 331..355
FT /evidence="ECO:0007829|PDB:7BGI"
FT STRAND 363..365
FT /evidence="ECO:0007829|PDB:7DZ7"
FT HELIX 366..397
FT /evidence="ECO:0007829|PDB:7BGI"
FT TURN 401..403
FT /evidence="ECO:0007829|PDB:7BGI"
FT STRAND 404..407
FT /evidence="ECO:0007829|PDB:7BGI"
FT HELIX 408..414
FT /evidence="ECO:0007829|PDB:7BGI"
FT HELIX 416..446
FT /evidence="ECO:0007829|PDB:7BGI"
FT HELIX 450..452
FT /evidence="ECO:0007829|PDB:7BGI"
FT HELIX 459..467
FT /evidence="ECO:0007829|PDB:7BGI"
FT HELIX 478..480
FT /evidence="ECO:0007829|PDB:7BGI"
FT HELIX 485..488
FT /evidence="ECO:0007829|PDB:7BGI"
FT TURN 491..494
FT /evidence="ECO:0007829|PDB:7BGI"
FT HELIX 495..502
FT /evidence="ECO:0007829|PDB:7BGI"
FT STRAND 505..508
FT /evidence="ECO:0007829|PDB:6JO5"
FT HELIX 515..540
FT /evidence="ECO:0007829|PDB:7BGI"
FT HELIX 551..554
FT /evidence="ECO:0007829|PDB:7BGI"
FT STRAND 559..561
FT /evidence="ECO:0007829|PDB:7BGI"
FT HELIX 573..604
FT /evidence="ECO:0007829|PDB:7BGI"
FT HELIX 607..613
FT /evidence="ECO:0007829|PDB:7BGI"
FT STRAND 614..616
FT /evidence="ECO:0007829|PDB:7BLX"
FT HELIX 617..623
FT /evidence="ECO:0007829|PDB:7BGI"
FT TURN 624..629
FT /evidence="ECO:0007829|PDB:7BGI"
FT HELIX 630..633
FT /evidence="ECO:0007829|PDB:7BGI"
FT STRAND 635..637
FT /evidence="ECO:0007829|PDB:7BGI"
FT HELIX 645..666
FT /evidence="ECO:0007829|PDB:7BGI"
FT HELIX 669..684
FT /evidence="ECO:0007829|PDB:7BGI"
FT TURN 687..691
FT /evidence="ECO:0007829|PDB:7BGI"
FT STRAND 695..697
FT /evidence="ECO:0007829|PDB:7BGI"
FT HELIX 703..733
FT /evidence="ECO:0007829|PDB:7BGI"
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
