PSAB_THEVB
ID PSAB_THEVB Reviewed; 741 AA.
AC P0A407; P25897;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Photosystem I P700 chlorophyll a apoprotein A2;
DE EC=1.97.1.12 {ECO:0000269|PubMed:10066799, ECO:0000269|PubMed:10066800, ECO:0000269|PubMed:11418848, ECO:0000269|PubMed:8901876};
DE AltName: Full=PsaB;
GN Name=psaB; OrderedLocusNames=tlr0732;
OS Thermosynechococcus vestitus (strain NIES-2133 / IAM M-273 / BP-1).
OC Bacteria; Cyanobacteria; Pseudanabaenales; Thermosynechococcaceae;
OC Thermosynechococcus.
OX NCBI_TaxID=197221;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NIES-2133 / IAM M-273 / BP-1;
RX PubMed=12240834; DOI=10.1093/dnares/9.4.123;
RA Nakamura Y., Kaneko T., Sato S., Ikeuchi M., Katoh H., Sasamoto S.,
RA Watanabe A., Iriguchi M., Kawashima K., Kimura T., Kishida Y., Kiyokawa C.,
RA Kohara M., Matsumoto M., Matsuno A., Nakazaki N., Shimpo S., Sugimoto M.,
RA Takeuchi C., Yamada M., Tabata S.;
RT "Complete genome structure of the thermophilic cyanobacterium
RT Thermosynechococcus elongatus BP-1.";
RL DNA Res. 9:123-130(2002).
RN [2]
RP PRESENCE OF CHLOROPHYLL A' IN PSI.
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 [3]
RP REVIEW.
RX PubMed=11687205; DOI=10.1016/s0005-2728(01)00195-5;
RA Fromme P., Jordan P., Krauss N.;
RT "Structure of photosystem I.";
RL Biochim. Biophys. Acta 1507:5-31(2001).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (4.0 ANGSTROMS), FUNCTION, CATALYTIC ACTIVITY,
RP COFACTOR, SUBUNIT, AND SUBCELLULAR LOCATION.
RX PubMed=8901876; DOI=10.1038/nsb1196-965;
RA Krauss N., Schubert W.-D., Klukas O., Fromme P., Witt H.T., Saenger W.;
RT "Photosystem I at 4-A resolution represents the first structural model of a
RT joint photosynthetic reaction centre and core antenna system.";
RL Nat. Struct. Biol. 3:965-973(1996).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (4.0 ANGSTROMS), FUNCTION, CATALYTIC ACTIVITY,
RP COFACTOR, SUBUNIT, AND SUBCELLULAR LOCATION.
RX PubMed=10066799; DOI=10.1074/jbc.274.11.7351;
RA Klukas O., Schubert W.-D., Jordan P., Krauss N., Fromme P., Witt H.T.,
RA Saenger W.;
RT "Photosystem I, an improved model of the stromal subunits PsaC, PsaD, and
RT PsaE.";
RL J. Biol. Chem. 274:7351-7360(1999).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (4.0 ANGSTROMS), FUNCTION, CATALYTIC ACTIVITY,
RP COFACTOR, SUBUNIT, AND SUBCELLULAR LOCATION.
RX PubMed=10066800; DOI=10.1074/jbc.274.11.7361;
RA Klukas O., Schubert W.-D., Jordan P., Krauss N., Fromme P., Witt H.T.,
RA Saenger W.;
RT "Localization of two phylloquinones, QK and QK', in an improved electron
RT density map of photosystem I at 4-A resolution.";
RL J. Biol. Chem. 274:7361-7367(1999).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 2-741, FUNCTION, CATALYTIC
RP ACTIVITY, COFACTOR, SUBUNIT, AND SUBCELLULAR LOCATION.
RX PubMed=11418848; DOI=10.1038/35082000;
RA Jordan P., Fromme P., Witt H.T., Klukas O., Saenger W., Krauss N.;
RT "Three-dimensional structure of cyanobacterial photosystem I at 2.5 A
RT resolution.";
RL Nature 411:909-917(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 {ECO:0000269|PubMed:10066799, ECO:0000269|PubMed:10066800,
CC ECO:0000269|PubMed:11418848, ECO:0000269|PubMed:8901876}.
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 Evidence={ECO:0000269|PubMed:10066799, ECO:0000269|PubMed:10066800,
CC ECO:0000269|PubMed:11418848, ECO:0000269|PubMed:8901876};
CC -!- COFACTOR:
CC Note=PSI electron transfer chain: 5 chlorophyll a, 1 chlorophyll a', 2
CC phylloquinones and 3 4Fe-4S clusters. PSI core antenna: 90 chlorophyll
CC a, 22 carotenoids, 3 phospholipids and 1 galactolipid. P700 is a
CC chlorophyll a/chlorophyll a' dimer, A0 is one or more chlorophyll a, A1
CC is one or both phylloquinones and FX is a shared 4Fe-4S iron-sulfur
CC center. {ECO:0000269|PubMed:10066799, ECO:0000269|PubMed:10066800,
CC ECO:0000269|PubMed:11418848, ECO:0000269|PubMed:8901876};
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
CC cyanobacterial PSI reaction center is composed of one copy each of
CC PsaA,B,C,D,E,F,I,J,K,L,M and X, and forms trimeric complexes.
CC {ECO:0000269|PubMed:10066799, ECO:0000269|PubMed:10066800,
CC ECO:0000269|PubMed:11418848, ECO:0000269|PubMed:8901876}.
CC -!- SUBCELLULAR LOCATION: Cellular thylakoid membrane {ECO:0000250}; Multi-
CC pass membrane protein {ECO:0000269|PubMed:10066799,
CC ECO:0000269|PubMed:10066800, ECO:0000269|PubMed:11418848,
CC ECO:0000269|PubMed:8901876}.
CC -!- SIMILARITY: Belongs to the PsaA/PsaB family. {ECO:0000305}.
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DR EMBL; BA000039; BAC08283.1; -; Genomic_DNA.
DR RefSeq; NP_681521.1; NC_004113.1.
DR RefSeq; WP_011056579.1; NC_004113.1.
DR PDB; 1C51; X-ray; 4.00 A; -.
DR PDB; 1JB0; X-ray; 2.50 A; B=2-741.
DR PDB; 2PPS; X-ray; 4.00 A; -.
DR PDB; 3PCQ; X-ray; 8.98 A; B=2-741.
DR PDB; 4FE1; X-ray; 4.92 A; B=2-741.
DR PDB; 5ZF0; X-ray; 4.20 A; B1/B2/B3/B4/B5/B6=2-741.
DR PDB; 6LU1; EM; 3.20 A; B=1-741.
DR PDB; 6PFY; X-ray; 2.90 A; B/H/Z=1-741.
DR PDB; 6PGK; X-ray; 2.90 A; B/H/Z=1-741.
DR PDB; 6TRA; EM; 2.85 A; B=1-741.
DR PDB; 6TRC; EM; 2.98 A; 2/B/b=1-741.
DR PDB; 6TRD; EM; 3.16 A; 2/B/b=1-741.
DR PDB; 7BW2; X-ray; 6.50 A; B=2-741.
DR PDB; 7M75; X-ray; 2.75 A; B=2-741.
DR PDB; 7M76; X-ray; 3.00 A; B=2-741.
DR PDB; 7M78; X-ray; 3.00 A; B=2-741.
DR PDBsum; 1C51; -.
DR PDBsum; 1JB0; -.
DR PDBsum; 2PPS; -.
DR PDBsum; 3PCQ; -.
DR PDBsum; 4FE1; -.
DR PDBsum; 5ZF0; -.
DR PDBsum; 6LU1; -.
DR PDBsum; 6PFY; -.
DR PDBsum; 6PGK; -.
DR PDBsum; 6TRA; -.
DR PDBsum; 6TRC; -.
DR PDBsum; 6TRD; -.
DR PDBsum; 7BW2; -.
DR PDBsum; 7M75; -.
DR PDBsum; 7M76; -.
DR PDBsum; 7M78; -.
DR AlphaFoldDB; P0A407; -.
DR SMR; P0A407; -.
DR IntAct; P0A407; 1.
DR STRING; 197221.22294453; -.
DR EnsemblBacteria; BAC08283; BAC08283; BAC08283.
DR KEGG; tel:tlr0732; -.
DR PATRIC; fig|197221.4.peg.772; -.
DR eggNOG; COG2885; Bacteria.
DR OMA; FEQWVAD; -.
DR OrthoDB; 36958at2; -.
DR BRENDA; 1.97.1.12; 7763.
DR EvolutionaryTrace; P0A407; -.
DR Proteomes; UP000000440; Chromosome.
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:0031676; C:plasma membrane-derived thylakoid membrane; IEA:UniProtKB-SubCell.
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; Chromophore; Electron transport; Iron;
KW Iron-sulfur; Magnesium; Membrane; Metal-binding; Oxidoreductase;
KW Photosynthesis; Photosystem I; Reference proteome; Thylakoid;
KW Transmembrane; Transmembrane helix; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:11418848"
FT CHAIN 2..741
FT /note="Photosystem I P700 chlorophyll a apoprotein A2"
FT /id="PRO_0000088650"
FT TOPO_DOM 2..38
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 39..70
FT /note="Helical; Name=I"
FT TOPO_DOM 71..131
FT /note="Lumenal, thylakoid"
FT /evidence="ECO:0000305"
FT TRANSMEM 132..156
FT /note="Helical; Name=II"
FT TOPO_DOM 157..172
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 173..195
FT /note="Helical; Name=III"
FT TOPO_DOM 196..269
FT /note="Lumenal, thylakoid"
FT /evidence="ECO:0000305"
FT TRANSMEM 270..287
FT /note="Helical; Name=IV"
FT TOPO_DOM 288..334
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 335..358
FT /note="Helical; Name=V"
FT TOPO_DOM 359..368
FT /note="Lumenal, thylakoid"
FT /evidence="ECO:0000305"
FT TRANSMEM 369..400
FT /note="Helical; Name=VI"
FT TOPO_DOM 401..419
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 420..449
FT /note="Helical; Name=VII"
FT TOPO_DOM 450..520
FT /note="Lumenal, thylakoid"
FT /evidence="ECO:0000305"
FT TRANSMEM 521..545
FT /note="Helical; Name=VIII"
FT TOPO_DOM 546..578
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 579..610
FT /note="Helical; Name=IX"
FT TOPO_DOM 611..650
FT /note="Lumenal, thylakoid"
FT /evidence="ECO:0000305"
FT TRANSMEM 651..672
FT /note="Helical; Name=X"
FT TOPO_DOM 673..708
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 709..737
FT /note="Helical; Name=XI"
FT TOPO_DOM 738..741
FT /note="Lumenal, thylakoid"
FT /evidence="ECO:0000305"
FT BINDING 566
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000269|PubMed:11418848"
FT BINDING 575
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000269|PubMed:11418848"
FT BINDING 661
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 /evidence="ECO:0000269|PubMed:11418848"
FT BINDING 669
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:0000269|PubMed:11418848"
FT BINDING 677
FT /ligand="chlorophyll a"
FT /ligand_id="ChEBI:CHEBI:58416"
FT /ligand_label="B3"
FT /evidence="ECO:0000269|PubMed:10066800,
FT ECO:0000269|PubMed:11418848"
FT BINDING 678
FT /ligand="phylloquinone"
FT /ligand_id="ChEBI:CHEBI:18067"
FT /ligand_label="B"
FT /evidence="ECO:0000269|PubMed:10066800,
FT ECO:0000269|PubMed:11418848"
FT STRAND 3..6
FT /evidence="ECO:0007829|PDB:6PFY"
FT HELIX 10..13
FT /evidence="ECO:0007829|PDB:1JB0"
FT HELIX 19..27
FT /evidence="ECO:0007829|PDB:1JB0"
FT HELIX 31..33
FT /evidence="ECO:0007829|PDB:1JB0"
FT STRAND 34..36
FT /evidence="ECO:0007829|PDB:6PFY"
FT HELIX 39..71
FT /evidence="ECO:0007829|PDB:1JB0"
FT HELIX 74..79
FT /evidence="ECO:0007829|PDB:1JB0"
FT TURN 81..83
FT /evidence="ECO:0007829|PDB:1JB0"
FT STRAND 87..90
FT /evidence="ECO:0007829|PDB:1JB0"
FT HELIX 98..104
FT /evidence="ECO:0007829|PDB:1JB0"
FT STRAND 113..115
FT /evidence="ECO:0007829|PDB:1JB0"
FT HELIX 120..126
FT /evidence="ECO:0007829|PDB:1JB0"
FT HELIX 132..155
FT /evidence="ECO:0007829|PDB:1JB0"
FT HELIX 159..161
FT /evidence="ECO:0007829|PDB:1JB0"
FT HELIX 165..168
FT /evidence="ECO:0007829|PDB:1JB0"
FT HELIX 171..180
FT /evidence="ECO:0007829|PDB:1JB0"
FT TURN 181..183
FT /evidence="ECO:0007829|PDB:1JB0"
FT HELIX 184..196
FT /evidence="ECO:0007829|PDB:1JB0"
FT HELIX 198..202
FT /evidence="ECO:0007829|PDB:1JB0"
FT TURN 209..211
FT /evidence="ECO:0007829|PDB:1JB0"
FT HELIX 212..214
FT /evidence="ECO:0007829|PDB:1JB0"
FT TURN 219..222
FT /evidence="ECO:0007829|PDB:6TRA"
FT HELIX 223..226
FT /evidence="ECO:0007829|PDB:1JB0"
FT HELIX 230..234
FT /evidence="ECO:0007829|PDB:1JB0"
FT STRAND 244..246
FT /evidence="ECO:0007829|PDB:6LU1"
FT TURN 263..265
FT /evidence="ECO:0007829|PDB:1JB0"
FT STRAND 266..268
FT /evidence="ECO:0007829|PDB:6PGK"
FT HELIX 270..287
FT /evidence="ECO:0007829|PDB:1JB0"
FT STRAND 293..296
FT /evidence="ECO:0007829|PDB:6TRA"
FT HELIX 301..306
FT /evidence="ECO:0007829|PDB:1JB0"
FT STRAND 310..313
FT /evidence="ECO:0007829|PDB:7M75"
FT HELIX 318..320
FT /evidence="ECO:0007829|PDB:1JB0"
FT HELIX 326..332
FT /evidence="ECO:0007829|PDB:1JB0"
FT HELIX 334..358
FT /evidence="ECO:0007829|PDB:1JB0"
FT STRAND 362..364
FT /evidence="ECO:0007829|PDB:6PGK"
FT HELIX 365..367
FT /evidence="ECO:0007829|PDB:1JB0"
FT HELIX 369..400
FT /evidence="ECO:0007829|PDB:1JB0"
FT HELIX 405..407
FT /evidence="ECO:0007829|PDB:1JB0"
FT STRAND 408..410
FT /evidence="ECO:0007829|PDB:6LU1"
FT HELIX 411..417
FT /evidence="ECO:0007829|PDB:1JB0"
FT HELIX 419..449
FT /evidence="ECO:0007829|PDB:1JB0"
FT HELIX 453..455
FT /evidence="ECO:0007829|PDB:1JB0"
FT HELIX 462..470
FT /evidence="ECO:0007829|PDB:1JB0"
FT HELIX 474..476
FT /evidence="ECO:0007829|PDB:1JB0"
FT STRAND 480..484
FT /evidence="ECO:0007829|PDB:7M75"
FT HELIX 488..491
FT /evidence="ECO:0007829|PDB:1JB0"
FT TURN 492..495
FT /evidence="ECO:0007829|PDB:1JB0"
FT HELIX 501..509
FT /evidence="ECO:0007829|PDB:1JB0"
FT STRAND 510..513
FT /evidence="ECO:0007829|PDB:1JB0"
FT HELIX 521..546
FT /evidence="ECO:0007829|PDB:1JB0"
FT TURN 547..549
FT /evidence="ECO:0007829|PDB:6TRA"
FT STRAND 552..554
FT /evidence="ECO:0007829|PDB:6PFY"
FT HELIX 557..560
FT /evidence="ECO:0007829|PDB:1JB0"
FT STRAND 565..567
FT /evidence="ECO:0007829|PDB:7M78"
FT HELIX 570..572
FT /evidence="ECO:0007829|PDB:1JB0"
FT HELIX 579..610
FT /evidence="ECO:0007829|PDB:1JB0"
FT HELIX 614..619
FT /evidence="ECO:0007829|PDB:1JB0"
FT STRAND 620..622
FT /evidence="ECO:0007829|PDB:7M76"
FT HELIX 623..629
FT /evidence="ECO:0007829|PDB:1JB0"
FT HELIX 631..634
FT /evidence="ECO:0007829|PDB:1JB0"
FT TURN 635..637
FT /evidence="ECO:0007829|PDB:1JB0"
FT HELIX 638..640
FT /evidence="ECO:0007829|PDB:1JB0"
FT STRAND 641..643
FT /evidence="ECO:0007829|PDB:1JB0"
FT HELIX 651..672
FT /evidence="ECO:0007829|PDB:1JB0"
FT HELIX 675..690
FT /evidence="ECO:0007829|PDB:1JB0"
FT HELIX 695..697
FT /evidence="ECO:0007829|PDB:1JB0"
FT STRAND 701..703
FT /evidence="ECO:0007829|PDB:1JB0"
FT HELIX 709..737
FT /evidence="ECO:0007829|PDB:1JB0"
SQ SEQUENCE 741 AA; 83044 MW; 74961EF21401FB40 CRC64;
MATKFPKFSQ DLAQDPTTRR IWYAIAMAHD FESHDGMTEE NLYQKIFASH FGHLAIIFLW
VSGSLFHVAW QGNFEQWVQD PVNTRPIAHA IWDPQFGKAA VDAFTQAGAS NPVDIAYSGV
YHWWYTIGMR TNGDLYQGAI FLLILASLAL FAGWLHLQPK FRPSLSWFKN AESRLNHHLA
GLFGVSSLAW AGHLIHVAIP ESRGQHVGWD NFLSTMPHPA GLAPFFTGNW GVYAQNPDTA
SHVFGTAQGA GTAILTFLGG FHPQTESLWL TDMAHHHLAI AVLFIVAGHM YRTQFGIGHS
IKEMMDAKDF FGTKVEGPFN MPHQGIYETY NNSLHFQLGW HLACLGVITS LVAQHMYSLP
PYAFIAQDHT TMAALYTHHQ YIAGFLMVGA FAHGAIFLVR DYDPAQNKGN VLDRVLQHKE
AIISHLSWVS LFLGFHTLGL YVHNDVVVAF GTPEKQILIE PVFAQFIQAA HGKLLYGFDT
LLSNPDSIAS TAWPNYGNVW LPGWLDAINS GTNSLFLTIG PGDFLVHHAI ALGLHTTTLI
LVKGALDARG SKLMPDKKDF GYAFPCDGPG RGGTCDISAW DAFYLAMFWM LNTIGWVTFY
WHWKHLGVWE GNVAQFNESS TYLMGWLRDY LWLNSSQLIN GYNPFGTNNL SVWAWMFLFG
HLVWATGFMF LISWRGYWQE LIETLVWAHE RTPLANLVRW KDKPVALSIV QARLVGLAHF
SVGYILTYAA FLIASTAAKF G
