PSBO_THEVB
ID PSBO_THEVB Reviewed; 272 AA.
AC P0A431; P55221; Q54074;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=Photosystem II manganese-stabilizing polypeptide;
DE Short=MSP;
DE Flags: Precursor;
GN Name=psbO; OrderedLocusNames=tll0444;
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] {ECO:0007744|PDB:1S5L}
RP X-RAY CRYSTALLOGRAPHY (3.50 ANGSTROMS) OF 27-272 IN PHOTOSYSTEM II,
RP COFACTOR, SUBUNIT, AND SUBCELLULAR LOCATION.
RX PubMed=14764885; DOI=10.1126/science.1093087;
RA Ferreira K.N., Iverson T.M., Maghlaoui K., Barber J., Iwata S.;
RT "Architecture of the photosynthetic oxygen-evolving center.";
RL Science 303:1831-1838(2004).
RN [3] {ECO:0007744|PDB:2AXT}
RP X-RAY CRYSTALLOGRAPHY (3.00 ANGSTROMS) OF 26-272 IN PHOTOSYSTEM II,
RP COFACTOR, SUBUNIT, AND SUBCELLULAR LOCATION.
RC STRAIN=NIES-2133 / IAM M-273 / BP-1;
RX PubMed=16355230; DOI=10.1038/nature04224;
RA Loll B., Kern J., Saenger W., Zouni A., Biesiadka J.;
RT "Towards complete cofactor arrangement in the 3.0 A resolution structure of
RT photosystem II.";
RL Nature 438:1040-1044(2005).
RN [4] {ECO:0007744|PDB:4V62}
RP X-RAY CRYSTALLOGRAPHY (2.90 ANGSTROMS) OF 26-272 IN PHOTOSYSTEM II,
RP COFACTOR, SUBUNIT, SUBCELLULAR LOCATION, AND MASS SPECTROMETRY.
RC STRAIN=NIES-2133 / IAM M-273 / BP-1;
RX PubMed=19219048; DOI=10.1038/nsmb.1559;
RA Guskov A., Kern J., Gabdulkhakov A., Broser M., Zouni A., Saenger W.;
RT "Cyanobacterial photosystem II at 2.9-A resolution and the role of
RT quinones, lipids, channels and chloride.";
RL Nat. Struct. Mol. Biol. 16:334-342(2009).
RN [5] {ECO:0007744|PDB:3KZI}
RP X-RAY CRYSTALLOGRAPHY (3.60 ANGSTROMS) OF 27-272 IN PHOTOSYSTEM II,
RP FUNCTION, COFACTOR, SUBUNIT, SUBCELLULAR LOCATION, AND MASS SPECTROMETRY.
RC STRAIN=NIES-2133 / IAM M-273 / BP-1;
RX PubMed=20558739; DOI=10.1074/jbc.m110.127589;
RA Broser M., Gabdulkhakov A., Kern J., Guskov A., Muh F., Saenger W.,
RA Zouni A.;
RT "Crystal structure of monomeric photosystem II from Thermosynechococcus
RT elongatus at 3.6 A resolution.";
RL J. Biol. Chem. 285:26255-26262(2010).
RN [6] {ECO:0007744|PDB:4V82}
RP X-RAY CRYSTALLOGRAPHY (3.20 ANGSTROMS) OF 26-272 IN PHOTOSYSTEM II,
RP FUNCTION, COFACTOR, SUBUNIT, AND SUBCELLULAR LOCATION.
RX PubMed=21367867; DOI=10.1074/jbc.m110.215970;
RA Broser M., Glockner C., Gabdulkhakov A., Guskov A., Buchta J., Kern J.,
RA Muh F., Dau H., Saenger W., Zouni A.;
RT "Structural basis of cyanobacterial photosystem II inhibition by the
RT herbicide terbutryn.";
RL J. Biol. Chem. 286:15964-15972(2011).
RN [7] {ECO:0007744|PDB:4FBY}
RP X-RAY CRYSTALLOGRAPHY (6.56 ANGSTROMS) OF 27-272 IN PHOTOSYSTEM II,
RP COFACTOR, SUBUNIT, AND SUBCELLULAR LOCATION.
RC STRAIN=NIES-2133 / IAM M-273 / BP-1;
RX PubMed=22665786; DOI=10.1073/pnas.1204598109;
RA Kern J., Alonso-Mori R., Hellmich J., Tran R., Hattne J., Laksmono H.,
RA Glockner C., Echols N., Sierra R.G., Sellberg J., Lassalle-Kaiser B.,
RA Gildea R.J., Glatzel P., Grosse-Kunstleve R.W., Latimer M.J., McQueen T.A.,
RA DiFiore D., Fry A.R., Messerschmidt M., Miahnahri A., Schafer D.W.,
RA Seibert M.M., Sokaras D., Weng T.C., Zwart P.H., White W.E., Adams P.D.,
RA Bogan M.J., Boutet S., Williams G.J., Messinger J., Sauter N.K., Zouni A.,
RA Bergmann U., Yano J., Yachandra V.K.;
RT "Room temperature femtosecond X-ray diffraction of photosystem II
RT microcrystals.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:9721-9726(2012).
RN [8] {ECO:0007744|PDB:4IXQ, ECO:0007744|PDB:4IXR}
RP X-RAY CRYSTALLOGRAPHY (5.70 ANGSTROMS) IN PHOTOSYSTEM II, COFACTOR,
RP SUBUNIT, AND SUBCELLULAR LOCATION.
RC STRAIN=NIES-2133 / IAM M-273 / BP-1;
RX PubMed=23413188; DOI=10.1126/science.1234273;
RA Kern J., Alonso-Mori R., Tran R., Hattne J., Gildea R.J., Echols N.,
RA Glockner C., Hellmich J., Laksmono H., Sierra R.G., Lassalle-Kaiser B.,
RA Koroidov S., Lampe A., Han G., Gul S., Difiore D., Milathianaki D.,
RA Fry A.R., Miahnahri A., Schafer D.W., Messerschmidt M., Seibert M.M.,
RA Koglin J.E., Sokaras D., Weng T.C., Sellberg J., Latimer M.J.,
RA Grosse-Kunstleve R.W., Zwart P.H., White W.E., Glatzel P., Adams P.D.,
RA Bogan M.J., Williams G.J., Boutet S., Messinger J., Zouni A., Sauter N.K.,
RA Yachandra V.K., Bergmann U., Yano J.;
RT "Simultaneous femtosecond X-ray spectroscopy and diffraction of photosystem
RT II at room temperature.";
RL Science 340:491-495(2013).
RN [9] {ECO:0007744|PDB:4PBU, ECO:0007744|PDB:4RVY}
RP X-RAY CRYSTALLOGRAPHY (5.00 ANGSTROMS) OF 30-272 IN PHOTOSYSTEM II,
RP COFACTOR, SUBUNIT, AND SUBCELLULAR LOCATION.
RC STRAIN=NIES-2133 / IAM M-273 / BP-1;
RX PubMed=25043005; DOI=10.1038/nature13453;
RA Kupitz C., Basu S., Grotjohann I., Fromme R., Zatsepin N.A., Rendek K.N.,
RA Hunter M.S., Shoeman R.L., White T.A., Wang D., James D., Yang J.H.,
RA Cobb D.E., Reeder B., Sierra R.G., Liu H., Barty A., Aquila A.L.,
RA Deponte D., Kirian R.A., Bari S., Bergkamp J.J., Beyerlein K.R.,
RA Bogan M.J., Caleman C., Chao T.C., Conrad C.E., Davis K.M.,
RA Fleckenstein H., Galli L., Hau-Riege S.P., Kassemeyer S., Laksmono H.,
RA Liang M., Lomb L., Marchesini S., Martin A.V., Messerschmidt M.,
RA Milathianaki D., Nass K., Ros A., Roy-Chowdhury S., Schmidt K., Seibert M.,
RA Steinbrener J., Stellato F., Yan L., Yoon C., Moore T.A., Moore A.L.,
RA Pushkar Y., Williams G.J., Boutet S., Doak R.B., Weierstall U., Frank M.,
RA Chapman H.N., Spence J.C., Fromme P.;
RT "Serial time-resolved crystallography of photosystem II using a femtosecond
RT X-ray laser.";
RL Nature 513:261-265(2014).
RN [10] {ECO:0007744|PDB:4TNH, ECO:0007744|PDB:4TNI, ECO:0007744|PDB:4TNJ, ECO:0007744|PDB:4TNK}
RP X-RAY CRYSTALLOGRAPHY (4.50 ANGSTROMS) IN PHOTOSYSTEM II, FUNCTION,
RP COFACTOR, SUBUNIT, AND SUBCELLULAR LOCATION.
RC STRAIN=NIES-2133 / IAM M-273 / BP-1;
RX PubMed=25006873; DOI=10.1038/ncomms5371;
RA Kern J., Tran R., Alonso-Mori R., Koroidov S., Echols N., Hattne J.,
RA Ibrahim M., Gul S., Laksmono H., Sierra R.G., Gildea R.J., Han G.,
RA Hellmich J., Lassalle-Kaiser B., Chatterjee R., Brewster A.S., Stan C.A.,
RA Gloeckner C., Lampe A., DiFiore D., Milathianaki D., Fry A.R.,
RA Seibert M.M., Koglin J.E., Gallo E., Uhlig J., Sokaras D., Weng T.C.,
RA Zwart P.H., Skinner D.E., Bogan M.J., Messerschmidt M., Glatzel P.,
RA Williams G.J., Boutet S., Adams P.D., Zouni A., Messinger J., Sauter N.K.,
RA Bergmann U., Yano J., Yachandra V.K.;
RT "Taking snapshots of photosynthetic water oxidation using femtosecond X-ray
RT diffraction and spectroscopy.";
RL Nat. Commun. 5:4371-4371(2014).
CC -!- FUNCTION: Part of the oxygen-evolving complex associated with
CC photosystem II (PSII). PSII is a light-driven water plastoquinone
CC oxidoreductase, using light energy to abstract electrons from H(2)O,
CC generating a proton gradient subsequently used for ATP formation.
CC {ECO:0000269|PubMed:20558739, ECO:0000269|PubMed:21367867,
CC ECO:0000269|PubMed:25006873}.
CC -!- COFACTOR:
CC Note=PSII binds multiple chlorophylls, carotenoids and specific lipids.
CC {ECO:0000269|PubMed:14764885, ECO:0000269|PubMed:16355230,
CC ECO:0000269|PubMed:19219048, ECO:0000269|PubMed:20558739,
CC ECO:0000269|PubMed:21367867, ECO:0000269|PubMed:22665786,
CC ECO:0000269|PubMed:23413188, ECO:0000269|PubMed:25006873,
CC ECO:0000269|PubMed:25043005};
CC -!- SUBUNIT: The cyanobacterial oxygen-evolving complex is composed of
CC PsbO, PsbP, PsbQ, PsbV and PsbU. PsbP and PsbQ are not seen in the
CC crystal structures; however there is biochemical evidence that they are
CC part of the OEC (By similarity). Cyanobacterial PSII is composed of 1
CC copy each of membrane proteins PsbA, PsbB, PsbC, PsbD, PsbE, PsbF,
CC PsbH, PsbI, PsbJ, PsbK, PsbL, PsbM, PsbT, PsbX, PsbY, PsbZ, Ycf12, 3
CC peripheral proteins PsbO, PsbU, PsbV and a large number of cofactors.
CC It forms dimeric complexes. {ECO:0000250, ECO:0000269|PubMed:14764885,
CC ECO:0000269|PubMed:16355230, ECO:0000269|PubMed:19219048,
CC ECO:0000269|PubMed:20558739, ECO:0000269|PubMed:21367867,
CC ECO:0000269|PubMed:22665786, ECO:0000269|PubMed:23413188,
CC ECO:0000269|PubMed:25006873, ECO:0000269|PubMed:25043005}.
CC -!- SUBCELLULAR LOCATION: Cellular thylakoid membrane
CC {ECO:0000269|PubMed:14764885, ECO:0000269|PubMed:16355230,
CC ECO:0000269|PubMed:19219048, ECO:0000269|PubMed:20558739,
CC ECO:0000269|PubMed:21367867, ECO:0000269|PubMed:22665786,
CC ECO:0000269|PubMed:23413188, ECO:0000269|PubMed:25006873,
CC ECO:0000269|PubMed:25043005}; Peripheral membrane protein
CC {ECO:0000269|PubMed:14764885, ECO:0000269|PubMed:16355230,
CC ECO:0000269|PubMed:19219048, ECO:0000269|PubMed:20558739,
CC ECO:0000269|PubMed:21367867, ECO:0000269|PubMed:22665786,
CC ECO:0000269|PubMed:23413188, ECO:0000269|PubMed:25006873,
CC ECO:0000269|PubMed:25043005}; Lumenal side
CC {ECO:0000269|PubMed:14764885, ECO:0000269|PubMed:16355230,
CC ECO:0000269|PubMed:19219048, ECO:0000269|PubMed:20558739,
CC ECO:0000269|PubMed:21367867, ECO:0000269|PubMed:22665786,
CC ECO:0000269|PubMed:23413188, ECO:0000269|PubMed:25006873,
CC ECO:0000269|PubMed:25043005}. Note=Associated with PSII on the lumenal
CC side of the thylakoid membrane.
CC -!- MASS SPECTROMETRY: Mass=26830; Mass_error=30; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:19219048};
CC -!- MASS SPECTROMETRY: Mass=26820; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:20558739};
CC -!- SIMILARITY: Belongs to the PsbO family. {ECO:0000305}.
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DR EMBL; BA000039; BAC07996.1; -; Genomic_DNA.
DR RefSeq; NP_681234.1; NC_004113.1.
DR RefSeq; WP_011056297.1; NC_004113.1.
DR PDB; 1S5L; X-ray; 3.50 A; O/o=27-272.
DR PDB; 2AXT; X-ray; 3.00 A; O/o=26-272.
DR PDB; 3KZI; X-ray; 3.60 A; O=27-272.
DR PDB; 4FBY; X-ray; 6.56 A; O/f=27-272.
DR PDB; 4IXQ; X-ray; 5.70 A; O/o=1-272.
DR PDB; 4IXR; X-ray; 5.90 A; O/o=1-272.
DR PDB; 4PBU; X-ray; 5.00 A; O/o=30-272.
DR PDB; 4PJ0; X-ray; 2.44 A; O/o=1-272.
DR PDB; 4RVY; X-ray; 5.50 A; O/o=30-272.
DR PDB; 4TNH; X-ray; 4.90 A; O/o=1-272.
DR PDB; 4TNI; X-ray; 4.60 A; O/o=1-272.
DR PDB; 4TNJ; X-ray; 4.50 A; O/o=1-272.
DR PDB; 4TNK; X-ray; 5.20 A; O/o=1-272.
DR PDB; 4V62; X-ray; 2.90 A; AO/BO=26-272.
DR PDB; 4V82; X-ray; 3.20 A; AO/BO=26-272.
DR PDB; 5E79; X-ray; 3.50 A; O/o=30-272.
DR PDB; 5E7C; X-ray; 4.50 A; O/o=30-272.
DR PDB; 5H2F; X-ray; 2.20 A; O/o=30-272.
DR PDB; 5KAF; X-ray; 3.00 A; O/o=1-272.
DR PDB; 5KAI; X-ray; 2.80 A; O/o=1-272.
DR PDB; 5MX2; X-ray; 2.20 A; O/o=1-272.
DR PDB; 5TIS; X-ray; 2.25 A; O/o=1-272.
DR PDB; 5ZZN; X-ray; 2.10 A; O/o=30-272.
DR PDB; 6DHE; X-ray; 2.05 A; O/o=29-272.
DR PDB; 6DHF; X-ray; 2.08 A; O/o=29-272.
DR PDB; 6DHG; X-ray; 2.50 A; O/o=29-272.
DR PDB; 6DHH; X-ray; 2.20 A; O/o=29-272.
DR PDB; 6DHO; X-ray; 2.07 A; O/o=29-272.
DR PDB; 6DHP; X-ray; 2.04 A; O/o=29-272.
DR PDB; 6W1O; X-ray; 2.08 A; O/o=1-272.
DR PDB; 6W1P; X-ray; 2.26 A; O/o=1-272.
DR PDB; 6W1Q; X-ray; 2.27 A; O/o=1-272.
DR PDB; 6W1R; X-ray; 2.23 A; O/o=1-272.
DR PDB; 6W1T; X-ray; 2.01 A; O/o=1-272.
DR PDB; 6W1U; X-ray; 2.09 A; O/o=1-272.
DR PDB; 6W1V; X-ray; 2.09 A; O/o=1-272.
DR PDB; 7RF1; X-ray; 1.89 A; O/o=1-272.
DR PDB; 7RF2; X-ray; 2.08 A; O/o=1-272.
DR PDB; 7RF3; X-ray; 2.26 A; O/o=1-272.
DR PDB; 7RF4; X-ray; 2.27 A; O/o=1-272.
DR PDB; 7RF5; X-ray; 2.23 A; O/o=1-272.
DR PDB; 7RF6; X-ray; 2.01 A; O/o=1-272.
DR PDB; 7RF7; X-ray; 2.09 A; O/o=1-272.
DR PDB; 7RF8; X-ray; 2.09 A; O/o=1-272.
DR PDBsum; 1S5L; -.
DR PDBsum; 2AXT; -.
DR PDBsum; 3KZI; -.
DR PDBsum; 4FBY; -.
DR PDBsum; 4IXQ; -.
DR PDBsum; 4IXR; -.
DR PDBsum; 4PBU; -.
DR PDBsum; 4PJ0; -.
DR PDBsum; 4RVY; -.
DR PDBsum; 4TNH; -.
DR PDBsum; 4TNI; -.
DR PDBsum; 4TNJ; -.
DR PDBsum; 4TNK; -.
DR PDBsum; 4V62; -.
DR PDBsum; 4V82; -.
DR PDBsum; 5E79; -.
DR PDBsum; 5E7C; -.
DR PDBsum; 5H2F; -.
DR PDBsum; 5KAF; -.
DR PDBsum; 5KAI; -.
DR PDBsum; 5MX2; -.
DR PDBsum; 5TIS; -.
DR PDBsum; 5ZZN; -.
DR PDBsum; 6DHE; -.
DR PDBsum; 6DHF; -.
DR PDBsum; 6DHG; -.
DR PDBsum; 6DHH; -.
DR PDBsum; 6DHO; -.
DR PDBsum; 6DHP; -.
DR PDBsum; 6W1O; -.
DR PDBsum; 6W1P; -.
DR PDBsum; 6W1Q; -.
DR PDBsum; 6W1R; -.
DR PDBsum; 6W1T; -.
DR PDBsum; 6W1U; -.
DR PDBsum; 6W1V; -.
DR PDBsum; 7RF1; -.
DR PDBsum; 7RF2; -.
DR PDBsum; 7RF3; -.
DR PDBsum; 7RF4; -.
DR PDBsum; 7RF5; -.
DR PDBsum; 7RF6; -.
DR PDBsum; 7RF7; -.
DR PDBsum; 7RF8; -.
DR AlphaFoldDB; P0A431; -.
DR SMR; P0A431; -.
DR DIP; DIP-48499N; -.
DR IntAct; P0A431; 1.
DR STRING; 197221.22294165; -.
DR EnsemblBacteria; BAC07996; BAC07996; BAC07996.
DR KEGG; tel:tll0444; -.
DR PATRIC; fig|197221.4.peg.468; -.
DR eggNOG; ENOG502Z7ZP; Bacteria.
DR OMA; GKANDCP; -.
DR OrthoDB; 1569080at2; -.
DR EvolutionaryTrace; P0A431; -.
DR Proteomes; UP000000440; Chromosome.
DR GO; GO:0009654; C:photosystem II oxygen evolving complex; IEA:InterPro.
DR GO; GO:0031676; C:plasma membrane-derived thylakoid membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0010242; F:oxygen evolving activity; IEA:InterPro.
DR GO; GO:0010207; P:photosystem II assembly; IEA:InterPro.
DR GO; GO:0042549; P:photosystem II stabilization; IEA:InterPro.
DR InterPro; IPR011250; OMP/PagP_b-brl.
DR InterPro; IPR002628; PSII_MSP.
DR PANTHER; PTHR34058; PTHR34058; 1.
DR Pfam; PF01716; MSP; 1.
DR SUPFAM; SSF56925; SSF56925; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Membrane; Photosynthesis; Photosystem II; Reference proteome;
KW Signal; Thylakoid.
FT SIGNAL 1..26
FT /evidence="ECO:0000269|PubMed:19219048,
FT ECO:0000269|PubMed:20558739"
FT CHAIN 27..272
FT /note="Photosystem II manganese-stabilizing polypeptide"
FT /id="PRO_0000029567"
FT HELIX 33..36
FT /evidence="ECO:0007829|PDB:5ZZN"
FT TURN 37..40
FT /evidence="ECO:0007829|PDB:5MX2"
FT HELIX 41..43
FT /evidence="ECO:0007829|PDB:5ZZN"
FT STRAND 55..57
FT /evidence="ECO:0007829|PDB:5ZZN"
FT STRAND 60..62
FT /evidence="ECO:0007829|PDB:5TIS"
FT STRAND 64..79
FT /evidence="ECO:0007829|PDB:5ZZN"
FT STRAND 84..86
FT /evidence="ECO:0007829|PDB:4PJ0"
FT STRAND 91..93
FT /evidence="ECO:0007829|PDB:5ZZN"
FT STRAND 95..98
FT /evidence="ECO:0007829|PDB:1S5L"
FT STRAND 104..113
FT /evidence="ECO:0007829|PDB:5ZZN"
FT STRAND 119..127
FT /evidence="ECO:0007829|PDB:5ZZN"
FT STRAND 129..135
FT /evidence="ECO:0007829|PDB:5ZZN"
FT TURN 136..138
FT /evidence="ECO:0007829|PDB:1S5L"
FT STRAND 141..147
FT /evidence="ECO:0007829|PDB:5ZZN"
FT STRAND 152..154
FT /evidence="ECO:0007829|PDB:5ZZN"
FT STRAND 160..163
FT /evidence="ECO:0007829|PDB:5ZZN"
FT STRAND 167..175
FT /evidence="ECO:0007829|PDB:5ZZN"
FT STRAND 190..196
FT /evidence="ECO:0007829|PDB:5ZZN"
FT HELIX 206..208
FT /evidence="ECO:0007829|PDB:5ZZN"
FT HELIX 209..212
FT /evidence="ECO:0007829|PDB:5ZZN"
FT STRAND 218..231
FT /evidence="ECO:0007829|PDB:5ZZN"
FT TURN 232..235
FT /evidence="ECO:0007829|PDB:5ZZN"
FT STRAND 236..246
FT /evidence="ECO:0007829|PDB:5ZZN"
FT TURN 250..253
FT /evidence="ECO:0007829|PDB:5ZZN"
FT STRAND 258..271
FT /evidence="ECO:0007829|PDB:5ZZN"
SQ SEQUENCE 272 AA; 29608 MW; 1F053A3453990141 CRC64;
MKYRILMATL LAVCLGIFSL SAPAFAAKQT LTYDDIVGTG LANKCPTLDD TARGAYPIDS
SQTYRIARLC LQPTTFLVKE EPKNKRQEAE FVPTKLVTRE TTSLDQIQGE LKVNSDGSLT
FVEEDGIDFQ PVTVQMAGGE RIPLLFTVKN LVASTQPNVT SITTSTDFKG EFNVPSYRTA
NFLDPKGRGL ASGYDSAIAL PQAKEEELAR ANVKRFSLTK GQISLNVAKV DGRTGEIAGT
FESEQLSDDD MGAHEPHEVK IQGVFYASIE PA
