PSBI_THEVB
ID PSBI_THEVB Reviewed; 38 AA.
AC Q8DJZ6; Q9F1L2;
DT 03-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=Photosystem II reaction center protein I {ECO:0000255|HAMAP-Rule:MF_01316};
DE Short=PSII-I {ECO:0000255|HAMAP-Rule:MF_01316};
DE AltName: Full=PSII 4.4 kDa protein {ECO:0000255|HAMAP-Rule:MF_01316};
GN Name=psbI {ECO:0000255|HAMAP-Rule:MF_01316}; OrderedLocusNames=tsr1074;
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 [GENOMIC DNA].
RA Katoh H., Ikeuchi M.;
RT "Cloning and disruption of the psbI gene from thermophilic
RT Thermosynechococcus (formerly Synechococcus) elongatus BP-1.";
RL Submitted (DEC-2000) to the EMBL/GenBank/DDBJ databases.
RN [2]
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 [3]
RP PROTEIN SEQUENCE OF 1-15, COFACTOR, AND SUBCELLULAR LOCATION.
RX PubMed=17935689; DOI=10.1016/j.bbabio.2007.08.008;
RA Kashino Y., Takahashi T., Inoue-Kashino N., Ban A., Ikeda Y., Satoh K.,
RA Sugiura M.;
RT "Ycf12 is a core subunit in the photosystem II complex.";
RL Biochim. Biophys. Acta 1767:1269-1275(2007).
RN [4]
RP FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RX PubMed=21195048; DOI=10.1016/j.bbabio.2010.12.013;
RA Kawakami K., Umena Y., Iwai M., Kawabata Y., Ikeuchi M., Kamiya N.,
RA Shen J.R.;
RT "Roles of PsbI and PsbM in photosystem II dimer formation and stability
RT studied by deletion mutagenesis and X-ray crystallography.";
RL Biochim. Biophys. Acta 1807:319-325(2011).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (3.50 ANGSTROMS) IN PHOTOSYSTEM II, COFACTOR,
RP 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 [6]
RP X-RAY CRYSTALLOGRAPHY (3.00 ANGSTROMS) IN PHOTOSYSTEM II, COFACTOR,
RP 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 [7]
RP X-RAY CRYSTALLOGRAPHY (2.90 ANGSTROMS) IN PHOTOSYSTEM II, COFACTOR,
RP SUBUNIT, SUBCELLULAR LOCATION, FORMYLATION AT MET-1, MASS SPECTROMETRY, AND
RP TOPOLOGY.
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 [8]
RP X-RAY CRYSTALLOGRAPHY (3.60 ANGSTROMS) IN PHOTOSYSTEM II, FUNCTION,
RP COFACTOR, SUBUNIT, SUBCELLULAR LOCATION, FORMYLATION AT MET-1, AND MASS
RP 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 [9]
RP X-RAY CRYSTALLOGRAPHY (3.20 ANGSTROMS) IN PHOTOSYSTEM II, FUNCTION,
RP 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 [10]
RP X-RAY CRYSTALLOGRAPHY (6.56 ANGSTROMS) IN PHOTOSYSTEM II, COFACTOR,
RP 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 [11]
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 [12]
RP X-RAY CRYSTALLOGRAPHY (5.00 ANGSTROMS) IN PHOTOSYSTEM II, COFACTOR,
RP 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 [13]
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: One of the components of the core complex of photosystem II
CC (PSII). May be required for formation of PSII dimers but not their
CC subsequent stability (PubMed:21195048). PSII is a light-driven
CC water:plastoquinone oxidoreductase that uses light energy to abstract
CC electrons from H(2)O, generating O(2) and a proton gradient
CC subsequently used for ATP formation. It consists of a core antenna
CC complex that captures photons, and an electron transfer chain that
CC converts photonic excitation into a charge separation.
CC {ECO:0000255|HAMAP-Rule:MF_01316, ECO:0000269|PubMed:20558739,
CC ECO:0000269|PubMed:21195048, 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:17935689, 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 -!- SUBUNIT: Cyanobacterial PSII is composed of 1 copy each of membrane
CC proteins PsbA, PsbB, PsbC, PsbD, PsbE, PsbF, PsbH, PsbI, PsbJ, PsbK,
CC PsbL, PsbM, PsbT, PsbX, PsbY, PsbZ, Ycf12, at least 3 peripheral
CC proteins PsbO, PsbU, PsbV and a large number of cofactors. It forms
CC dimeric complexes. {ECO:0000255|HAMAP-Rule:MF_01316,
CC ECO:0000269|PubMed:14764885, ECO:0000269|PubMed:16355230,
CC ECO:0000269|PubMed:19219048, ECO:0000269|PubMed:20558739,
CC ECO:0000269|PubMed:21195048, 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 {ECO:0000255|HAMAP-
CC Rule:MF_01316, ECO:0000269|PubMed:14764885,
CC ECO:0000269|PubMed:16355230, ECO:0000269|PubMed:17935689,
CC ECO:0000269|PubMed:19219048, ECO:0000269|PubMed:20558739,
CC ECO:0000269|PubMed:21195048, ECO:0000269|PubMed:21367867,
CC ECO:0000269|PubMed:22665786, ECO:0000269|PubMed:23413188,
CC ECO:0000269|PubMed:25006873, ECO:0000269|PubMed:25043005}; Single-pass
CC membrane protein {ECO:0000255|HAMAP-Rule:MF_01316,
CC ECO:0000269|PubMed:14764885, ECO:0000269|PubMed:16355230,
CC ECO:0000269|PubMed:17935689, 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 -!- MASS SPECTROMETRY: Mass=4437; Mass_error=4; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:19219048};
CC -!- MASS SPECTROMETRY: Mass=4435; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:20558739};
CC -!- DISRUPTION PHENOTYPE: Decreased yields of PSII dimers with increased
CC PSII monomers, slightly slower photoautotrophic growth, about 20% less
CC oxygen evolution. Formed PSII dimers are stable.
CC {ECO:0000269|PubMed:21195048}.
CC -!- SIMILARITY: Belongs to the PsbI family. {ECO:0000255|HAMAP-
CC Rule:MF_01316}.
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DR EMBL; AB052849; BAB20622.1; -; Genomic_DNA.
DR EMBL; BA000039; BAC08627.1; -; Genomic_DNA.
DR RefSeq; NP_681865.1; NC_004113.1.
DR RefSeq; WP_011056917.1; NC_004113.1.
DR PDB; 1S5L; X-ray; 3.50 A; I/i=1-38.
DR PDB; 2AXT; X-ray; 3.00 A; I/i=1-38.
DR PDB; 3KZI; X-ray; 3.60 A; I=1-38.
DR PDB; 4FBY; X-ray; 6.56 A; I/a=1-38.
DR PDB; 4IXQ; X-ray; 5.70 A; I/i=1-38.
DR PDB; 4IXR; X-ray; 5.90 A; I/i=1-38.
DR PDB; 4PBU; X-ray; 5.00 A; I/i=1-38.
DR PDB; 4PJ0; X-ray; 2.44 A; I/i=1-38.
DR PDB; 4RVY; X-ray; 5.50 A; I/i=1-38.
DR PDB; 4TNH; X-ray; 4.90 A; I/i=1-38.
DR PDB; 4TNI; X-ray; 4.60 A; I/i=1-38.
DR PDB; 4TNJ; X-ray; 4.50 A; I/i=1-38.
DR PDB; 4TNK; X-ray; 5.20 A; I/i=1-38.
DR PDB; 4V62; X-ray; 2.90 A; AI/BI=1-38.
DR PDB; 4V82; X-ray; 3.20 A; AI/BI=1-38.
DR PDB; 5E79; X-ray; 3.50 A; I/i=1-38.
DR PDB; 5E7C; X-ray; 4.50 A; I/i=1-38.
DR PDB; 5H2F; X-ray; 2.20 A; I/i=1-36.
DR PDB; 5KAF; X-ray; 3.00 A; I/i=2-38.
DR PDB; 5KAI; X-ray; 2.80 A; I/i=2-38.
DR PDB; 5MX2; X-ray; 2.20 A; I/i=1-38.
DR PDB; 5TIS; X-ray; 2.25 A; I/i=1-38.
DR PDB; 5ZZN; X-ray; 2.10 A; I/i=1-37.
DR PDB; 6DHE; X-ray; 2.05 A; I/i=1-36.
DR PDB; 6DHF; X-ray; 2.08 A; I/i=1-36.
DR PDB; 6DHG; X-ray; 2.50 A; I/i=1-36.
DR PDB; 6DHH; X-ray; 2.20 A; I/i=1-36.
DR PDB; 6DHO; X-ray; 2.07 A; I/i=1-36.
DR PDB; 6DHP; X-ray; 2.04 A; I/i=1-36.
DR PDB; 6W1O; X-ray; 2.08 A; I/i=1-38.
DR PDB; 6W1P; X-ray; 2.26 A; I/i=1-38.
DR PDB; 6W1Q; X-ray; 2.27 A; I/i=1-38.
DR PDB; 6W1R; X-ray; 2.23 A; I/i=1-38.
DR PDB; 6W1T; X-ray; 2.01 A; I/i=1-38.
DR PDB; 6W1U; X-ray; 2.09 A; I/i=1-38.
DR PDB; 6W1V; X-ray; 2.09 A; I/i=1-38.
DR PDB; 7NHO; EM; 2.66 A; I=1-38.
DR PDB; 7NHP; EM; 2.72 A; I=1-38.
DR PDB; 7NHQ; EM; 2.68 A; I=1-38.
DR PDB; 7RF1; X-ray; 1.89 A; I/i=1-38.
DR PDB; 7RF2; X-ray; 2.08 A; I/i=1-38.
DR PDB; 7RF3; X-ray; 2.26 A; I/i=1-38.
DR PDB; 7RF4; X-ray; 2.27 A; I/i=1-38.
DR PDB; 7RF5; X-ray; 2.23 A; I/i=1-38.
DR PDB; 7RF6; X-ray; 2.01 A; I/i=1-38.
DR PDB; 7RF7; X-ray; 2.09 A; I/i=1-38.
DR PDB; 7RF8; X-ray; 2.09 A; I/i=1-38.
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; 7NHO; -.
DR PDBsum; 7NHP; -.
DR PDBsum; 7NHQ; -.
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; Q8DJZ6; -.
DR SMR; Q8DJZ6; -.
DR DIP; DIP-48494N; -.
DR IntAct; Q8DJZ6; 1.
DR STRING; 197221.22294798; -.
DR EnsemblBacteria; BAC08627; BAC08627; BAC08627.
DR KEGG; tel:tsr1074; -.
DR PATRIC; fig|197221.4.peg.1129; -.
DR eggNOG; ENOG5033CII; Bacteria.
DR EvolutionaryTrace; Q8DJZ6; -.
DR Proteomes; UP000000440; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0009539; C:photosystem II reaction center; IEA:InterPro.
DR GO; GO:0031676; C:plasma membrane-derived thylakoid membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0015979; P:photosynthesis; IEA:UniProtKB-UniRule.
DR HAMAP; MF_01316; PSII_PsbI; 1.
DR InterPro; IPR003686; PSII_PsbI.
DR InterPro; IPR037271; PSII_PsbI_sf.
DR PANTHER; PTHR35772; PTHR35772; 1.
DR Pfam; PF02532; PsbI; 1.
DR SUPFAM; SSF161041; SSF161041; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Formylation; Membrane;
KW Photosynthesis; Photosystem II; Reaction center; Reference proteome;
KW Thylakoid; Transmembrane; Transmembrane helix.
FT CHAIN 1..38
FT /note="Photosystem II reaction center protein I"
FT /id="PRO_0000219660"
FT TOPO_DOM 1..5
FT /note="Lumenal"
FT /evidence="ECO:0000269|PubMed:19219048"
FT TRANSMEM 6..21
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:19219048"
FT TOPO_DOM 22..38
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:19219048"
FT MOD_RES 1
FT /note="N-formylmethionine"
FT /evidence="ECO:0000269|PubMed:19219048,
FT ECO:0000269|PubMed:20558739"
FT HELIX 2..24
FT /evidence="ECO:0007829|PDB:5ZZN"
FT HELIX 27..29
FT /evidence="ECO:0007829|PDB:5ZZN"
FT STRAND 31..34
FT /evidence="ECO:0007829|PDB:5ZZN"
SQ SEQUENCE 38 AA; 4405 MW; 02DDC30594997948 CRC64;
METLKITVYI VVTFFVLLFV FGFLSGDPAR NPKRKDLE
