ID   A0A0A0PFU7_9ROSI        Unreviewed;       353 AA.
AC   A0A0A0PFU7;
DT   04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT   04-FEB-2015, sequence version 1.
DT   18-JAN-2017, entry version 9.
DE   RecName: Full=Photosystem II D2 protein {ECO:0000256|HAMAP-Rule:MF_01383, ECO:0000256|RuleBase:RU004333};
DE            Short=PSII D2 protein {ECO:0000256|HAMAP-Rule:MF_01383};
DE            EC=1.10.3.9 {ECO:0000256|HAMAP-Rule:MF_01383};
DE   AltName: Full=Photosystem Q(A) protein {ECO:0000256|HAMAP-Rule:MF_01383};
GN   Name=psbD {ECO:0000256|HAMAP-Rule:MF_01383,
GN   ECO:0000313|EMBL:AHH80571.1};
OS   Erodium gruinum.
OG   Plastid {ECO:0000313|EMBL:AHH80571.1}.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
OC   Pentapetalae; rosids; malvids; Geraniales; Geraniaceae; Erodium.
OX   NCBI_TaxID=337380 {ECO:0000313|EMBL:AHH80571.1};
RN   [1] {ECO:0000313|EMBL:AHH80571.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Blazier J.C., Jansen R.K.;
RT   "Plastid genome evolution in Erodium.";
RL   Submitted (NOV-2013) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Photosystem II (PSII) is a light-driven water:
CC       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. The D1/D2
CC       (PsbA/PsbA) reaction center heterodimer binds P680, the primary
CC       electron donor of PSII as well as several subsequent electron
CC       acceptors. D2 is needed for assembly of a stable PSII complex.
CC       {ECO:0000256|HAMAP-Rule:MF_01383}.
CC   -!- CATALYTIC ACTIVITY: 2 H(2)O + 2 plastoquinone + 4 light = O(2) + 2
CC       plastoquinol. {ECO:0000256|HAMAP-Rule:MF_01383}.
CC   -!- COFACTOR:
CC       Note=The D1/D2 heterodimer binds P680, chlorophylls that are the
CC       primary electron donor of PSII, and subsequent electron acceptors.
CC       It shares a non-heme iron and each subunit binds pheophytin,
CC       quinone, additional chlorophylls, carotenoids and lipids. There is
CC       also a Cl(-1) ion associated with D1 and D2, which is required for
CC       oxygen evolution. The PSII complex binds additional chlorophylls,
CC       carotenoids and specific lipids. {ECO:0000256|HAMAP-
CC       Rule:MF_01383};
CC   -!- SUBUNIT: PSII is composed of 1 copy each of membrane proteins
CC       PsbA, PsbB, PsbC, PsbD, PsbE, PsbF, PsbH, PsbI, PsbJ, PsbK, PsbL,
CC       PsbM, PsbT, PsbX, PsbY, PsbZ, Ycf12, at least 3 peripheral
CC       proteins of the oxygen-evolving complex and a large number of
CC       cofactors. It forms dimeric complexes. {ECO:0000256|HAMAP-
CC       Rule:MF_01383, ECO:0000256|SAAS:SAAS00266657}.
CC   -!- SUBCELLULAR LOCATION: Cellular thylakoid membrane
CC       {ECO:0000256|HAMAP-Rule:MF_01383}; Multi-pass membrane protein
CC       {ECO:0000256|HAMAP-Rule:MF_01383}.
CC   -!- MISCELLANEOUS: 2 of the reaction center chlorophylls (ChlD1 and
CC       ChlD2) are entirely coordinated by water. {ECO:0000256|HAMAP-
CC       Rule:MF_01383}.
CC   -!- SIMILARITY: Belongs to the reaction center PufL/M/PsbA/D family.
CC       {ECO:0000256|HAMAP-Rule:MF_01383, ECO:0000256|RuleBase:RU004331}.
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DR   EMBL; KF804069; AHH80571.1; -; Genomic_DNA.
DR   RefSeq; YP_009111560.1; NC_025907.1.
DR   GeneID; 22548172; -.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0009523; C:photosystem II; IEA:UniProtKB-KW.
DR   GO; GO:0009536; C:plastid; IEA:UniProtKB-KW.
DR   GO; GO:0042651; C:thylakoid membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016168; F:chlorophyll binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0045156; F:electron transporter, transferring electrons within the cyclic electron transport pathway of photosynthesis activity; IEA:InterPro.
DR   GO; GO:0005506; F:iron ion binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   GO; GO:0009772; P:photosynthetic electron transport in photosystem II; IEA:InterPro.
DR   GO; GO:0018298; P:protein-chromophore linkage; IEA:UniProtKB-KW.
DR   CDD; cd09288; Photosystem-II_D2; 1.
DR   Gene3D; 1.20.85.10; -; 2.
DR   HAMAP; MF_01383; PSII_PsbD_D2; 1.
DR   InterPro; IPR000484; Photo_RC_L/M.
DR   InterPro; IPR005868; PSII_PsbD/D2.
DR   Pfam; PF00124; Photo_RC; 1.
DR   PRINTS; PR00256; REACTNCENTRE.
DR   SUPFAM; SSF81483; SSF81483; 1.
DR   TIGRFAMs; TIGR01152; psbD; 1.
DR   PROSITE; PS00244; REACTION_CENTER; 1.
PE   3: Inferred from homology;
KW   Acetylation {ECO:0000256|HAMAP-Rule:MF_01383};
KW   Chlorophyll {ECO:0000256|HAMAP-Rule:MF_01383};
KW   Chromophore {ECO:0000256|HAMAP-Rule:MF_01383};
KW   Electron transport {ECO:0000256|HAMAP-Rule:MF_01383,
KW   ECO:0000256|RuleBase:RU004333};
KW   Iron {ECO:0000256|HAMAP-Rule:MF_01383, ECO:0000256|RuleBase:RU004333};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_01383};
KW   Membrane {ECO:0000256|HAMAP-Rule:MF_01383,
KW   ECO:0000256|RuleBase:RU004333, ECO:0000256|SAM:Phobius};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_01383,
KW   ECO:0000256|RuleBase:RU004333};
KW   Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_01383};
KW   Phosphoprotein {ECO:0000256|HAMAP-Rule:MF_01383};
KW   Photosynthesis {ECO:0000256|HAMAP-Rule:MF_01383,
KW   ECO:0000256|RuleBase:RU004333};
KW   Photosystem II {ECO:0000256|HAMAP-Rule:MF_01383,
KW   ECO:0000256|RuleBase:RU004333};
KW   Plastid {ECO:0000313|EMBL:AHH80571.1};
KW   Thylakoid {ECO:0000256|HAMAP-Rule:MF_01383};
KW   Transmembrane {ECO:0000256|HAMAP-Rule:MF_01383,
KW   ECO:0000256|RuleBase:RU004333, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|HAMAP-Rule:MF_01383,
KW   ECO:0000256|SAM:Phobius};
KW   Transport {ECO:0000256|HAMAP-Rule:MF_01383,
KW   ECO:0000256|RuleBase:RU004333}.
FT   TRANSMEM     28     50       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    111    129       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    141    161       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    167    185       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    197    217       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    267    292       Helical. {ECO:0000256|SAM:Phobius}.
FT   METAL       118    118       Magnesium (chlorophyll-a ChlzD2, axial
FT                                ligand; peripheral); via tele nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_01383}.
FT   METAL       198    198       Magnesium (chlorophyll-a PD2 axial
FT                                ligand); via tele nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_01383}.
FT   METAL       215    215       Iron; shared with heterodimeric partner;
FT                                via tele nitrogen. {ECO:0000256|HAMAP-
FT                                Rule:MF_01383}.
FT   METAL       269    269       Iron; shared with heterodimeric partner;
FT                                via tele nitrogen. {ECO:0000256|HAMAP-
FT                                Rule:MF_01383}.
FT   BINDING     130    130       Pheophytin D2. {ECO:0000256|HAMAP-Rule:
FT                                MF_01383}.
FT   BINDING     143    143       Pheophytin D2. {ECO:0000256|HAMAP-Rule:
FT                                MF_01383}.
FT   BINDING     215    215       Plastoquinone Q(A). {ECO:0000256|HAMAP-
FT                                Rule:MF_01383}.
FT   BINDING     262    262       Plastoquinone Q(A); via amide nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_01383}.
FT   MOD_RES       2      2       N-acetylthreonine. {ECO:0000256|HAMAP-
FT                                Rule:MF_01383}.
FT   MOD_RES       2      2       Phosphothreonine. {ECO:0000256|HAMAP-
FT                                Rule:MF_01383}.
SQ   SEQUENCE   353 AA;  39515 MW;  30CBC93752867B06 CRC64;
     MTIALGKFTK DENDLFDIMD DWLRRDRFVF VGWSGLLLFP CAYFALGGWF TGTTFVTSWY
     THGLASSYLE GCNFLTAAVS TPANSLAHSL LLLWGPEAQG DLTRWCQLGG LWTFVALHGA
     FGLIGFMLRQ FELARSVQLR PYNAIAFSGP IAVFVSVFLI YPLGQSGWFF APSFGVAAIF
     RFILFFQGFH NWTLNPFHMM GVAGVLGAAL LCAIHGATVE NTLFEDGDGA NTFRAFNPTQ
     AEETYSMVTA NRFWSQIFGV AFSNKRWLHF FMLFVPVTGL WMSALGVVGL ALNLRAYDFV
     SQEIRAAEDP EFETFYTKNI LLNEGIRAWM AAQDQPHENL IFPEEVLPRG NAL
//