ID   A0A220NH95_9POAL        Unreviewed;       353 AA.
AC   A0A220NH95;
DT   25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT   25-OCT-2017, sequence version 1.
DT   28-MAR-2018, entry version 5.
DE   RecName: Full=Photosystem II protein D1 {ECO:0000256|HAMAP-Rule:MF_01379, ECO:0000256|RuleBase:RU004332};
DE            Short=PSII D1 protein {ECO:0000256|HAMAP-Rule:MF_01379};
DE            EC=1.10.3.9 {ECO:0000256|HAMAP-Rule:MF_01379};
DE   AltName: Full=Photosystem II Q(B) protein {ECO:0000256|HAMAP-Rule:MF_01379};
GN   Name=psbA {ECO:0000256|HAMAP-Rule:MF_01379,
GN   ECO:0000313|EMBL:ASJ66532.1};
OS   Hakonechloa macra.
OG   Plastid; Chloroplast {ECO:0000313|EMBL:ASJ66532.1}.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae;
OC   PACMAD clade; Arundinoideae; Molinieae; Hakonechloa.
OX   NCBI_TaxID=29678 {ECO:0000313|EMBL:ASJ66532.1};
RN   [1] {ECO:0000313|EMBL:ASJ66532.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Teisher97 {ECO:0000313|EMBL:ASJ66532.1}, and Teisher99
RC   {ECO:0000313|EMBL:ASJ66615.1};
RX   PubMed=28645142;
RA   Teisher J.K., McKain M.R., Schaal B.A., Kellogg E.A.;
RT   "Polyphyly of Arundinoideae (Poaceae) and evolution of the twisted
RT   geniculate lemma awn.";
RL   Ann. Bot. 0:0-0(2017).
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. {ECO:0000256|HAMAP-Rule:MF_01379}.
CC   -!- CATALYTIC ACTIVITY: 2 H(2)O + 2 plastoquinone + 4 light = O(2) + 2
CC       plastoquinol. {ECO:0000256|HAMAP-Rule:MF_01379}.
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. D1
CC       provides most of the ligands for the Mn4-Ca-O5 cluster of the
CC       oxygen-evolving complex (OEC). There is also a Cl(-1) ion
CC       associated with D1 and D2, which is required for oxygen evolution.
CC       The PSII complex binds additional chlorophylls, carotenoids and
CC       specific lipids. {ECO:0000256|HAMAP-Rule:MF_01379};
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_01379}.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane
CC       {ECO:0000256|HAMAP-Rule:MF_01379}; Multi-pass membrane protein
CC       {ECO:0000256|HAMAP-Rule:MF_01379}.
CC   -!- PTM: C-terminally processed by CtpA; processing is essential to
CC       allow assembly of the oxygen-evolving complex and thus
CC       photosynthetic growth. {ECO:0000256|HAMAP-Rule:MF_01379}.
CC   -!- PTM: Tyr-161 forms a radical intermediate that is referred to as
CC       redox-active TyrZ, YZ or Y-Z. {ECO:0000256|HAMAP-Rule:MF_01379}.
CC   -!- MISCELLANEOUS: 2 of the reaction center chlorophylls (ChlD1 and
CC       ChlD2) are entirely coordinated by water. {ECO:0000256|HAMAP-
CC       Rule:MF_01379}.
CC   -!- MISCELLANEOUS: Herbicides such as atrazine, BNT, diuron or ioxynil
CC       bind in the Q(B) binding site and block subsequent electron
CC       transfer. {ECO:0000256|HAMAP-Rule:MF_01379}.
CC   -!- SIMILARITY: Belongs to the reaction center PufL/M/PsbA/D family.
CC       {ECO:0000256|HAMAP-Rule:MF_01379, ECO:0000256|RuleBase:RU004331}.
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DR   EMBL; MF035984; ASJ66532.1; -; Genomic_DNA.
DR   EMBL; MF035985; ASJ66615.1; -; Genomic_DNA.
DR   SMR; A0A220NH95; -.
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:0009523; C:photosystem II; IEA:UniProtKB-KW.
DR   GO; GO:0016168; F:chlorophyll binding; IEA:UniProtKB-UniRule.
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-UniRule.
DR   GO; GO:0016682; F:oxidoreductase activity, acting on diphenols and related substances as donors, oxygen as acceptor; IEA:UniProtKB-UniRule.
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   GO; GO:0009635; P:response to herbicide; IEA:UniProtKB-KW.
DR   CDD; cd09289; Photosystem-II_D1; 1.
DR   Gene3D; 1.20.85.10; -; 1.
DR   HAMAP; MF_01379; PSII_PsbA_D1; 1.
DR   InterPro; IPR036854; Photo_II_D1/D2_sf.
DR   InterPro; IPR000484; Photo_RC_L/M.
DR   InterPro; IPR005867; PSII_D1.
DR   PANTHER; PTHR33149; PTHR33149; 1.
DR   Pfam; PF00124; Photo_RC; 1.
DR   PRINTS; PR00256; REACTNCENTRE.
DR   SUPFAM; SSF81483; SSF81483; 1.
DR   TIGRFAMs; TIGR01151; psbA; 1.
DR   PROSITE; PS00244; REACTION_CENTER; 1.
PE   3: Inferred from homology;
KW   Calcium {ECO:0000256|HAMAP-Rule:MF_01379};
KW   Chlorophyll {ECO:0000256|HAMAP-Rule:MF_01379};
KW   Chloroplast {ECO:0000313|EMBL:ASJ66532.1};
KW   Chromophore {ECO:0000256|HAMAP-Rule:MF_01379};
KW   Electron transport {ECO:0000256|HAMAP-Rule:MF_01379,
KW   ECO:0000256|RuleBase:RU004332};
KW   Herbicide resistance {ECO:0000256|HAMAP-Rule:MF_01379};
KW   Iron {ECO:0000256|HAMAP-Rule:MF_01379, ECO:0000256|RuleBase:RU004332};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_01379};
KW   Manganese {ECO:0000256|HAMAP-Rule:MF_01379};
KW   Membrane {ECO:0000256|HAMAP-Rule:MF_01379,
KW   ECO:0000256|RuleBase:RU004332, ECO:0000256|SAM:Phobius};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_01379,
KW   ECO:0000256|RuleBase:RU004332};
KW   Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_01379};
KW   Photosynthesis {ECO:0000256|HAMAP-Rule:MF_01379,
KW   ECO:0000256|RuleBase:RU004332};
KW   Photosystem II {ECO:0000256|HAMAP-Rule:MF_01379,
KW   ECO:0000256|RuleBase:RU004332};
KW   Plastid {ECO:0000313|EMBL:ASJ66532.1};
KW   Thylakoid {ECO:0000256|HAMAP-Rule:MF_01379};
KW   Transmembrane {ECO:0000256|HAMAP-Rule:MF_01379,
KW   ECO:0000256|RuleBase:RU004332, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|HAMAP-Rule:MF_01379,
KW   ECO:0000256|SAM:Phobius};
KW   Transport {ECO:0000256|HAMAP-Rule:MF_01379,
KW   ECO:0000256|RuleBase:RU004332}.
FT   INIT_MET      1      1       Removed. {ECO:0000256|HAMAP-Rule:
FT                                MF_01379}.
FT   PROPEP      345    353       {ECO:0000256|HAMAP-Rule:MF_01379}.
FT                                /FTId=PRO_5011319609.
FT   TRANSMEM     29     55       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM     76     97       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    109    129       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    141    161       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    167    186       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    198    218       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    273    295       Helical. {ECO:0000256|SAM:Phobius}.
FT   REGION      264    265       Quinone (B). {ECO:0000256|HAMAP-Rule:
FT                                MF_01379}.
FT   METAL       118    118       Magnesium (chlorophyll-a ChlzD1 axial
FT                                ligand); via tele nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_01379}.
FT   METAL       170    170       Calcium-manganese-oxide [Ca-4Mn-5O];
FT                                calcium. {ECO:0000256|HAMAP-Rule:
FT                                MF_01379}.
FT   METAL       170    170       Calcium-manganese-oxide [Ca-4Mn-5O];
FT                                manganese 4. {ECO:0000256|HAMAP-Rule:
FT                                MF_01379}.
FT   METAL       189    189       Calcium-manganese-oxide [Ca-4Mn-5O];
FT                                manganese 1. {ECO:0000256|HAMAP-Rule:
FT                                MF_01379}.
FT   METAL       198    198       Magnesium (chlorophyll-a PD1 axial
FT                                ligand); via tele nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_01379}.
FT   METAL       215    215       Iron; shared with heterodimeric partner;
FT                                via tele nitrogen. {ECO:0000256|HAMAP-
FT                                Rule:MF_01379}.
FT   METAL       272    272       Iron; shared with heterodimeric partner;
FT                                via tele nitrogen. {ECO:0000256|HAMAP-
FT                                Rule:MF_01379}.
FT   METAL       332    332       Calcium-manganese-oxide [Ca-4Mn-5O];
FT                                manganese 1; via tele nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_01379}.
FT   METAL       333    333       Calcium-manganese-oxide [Ca-4Mn-5O];
FT                                manganese 3. {ECO:0000256|HAMAP-Rule:
FT                                MF_01379}.
FT   METAL       333    333       Calcium-manganese-oxide [Ca-4Mn-5O];
FT                                manganese 4. {ECO:0000256|HAMAP-Rule:
FT                                MF_01379}.
FT   METAL       342    342       Calcium-manganese-oxide [Ca-4Mn-5O];
FT                                manganese 1. {ECO:0000256|HAMAP-Rule:
FT                                MF_01379}.
FT   METAL       342    342       Calcium-manganese-oxide [Ca-4Mn-5O];
FT                                manganese 2. {ECO:0000256|HAMAP-Rule:
FT                                MF_01379}.
FT   METAL       344    344       Calcium-manganese-oxide [Ca-4Mn-5O];
FT                                calcium; via carboxylate.
FT                                {ECO:0000256|HAMAP-Rule:MF_01379}.
FT   METAL       344    344       Calcium-manganese-oxide [Ca-4Mn-5O];
FT                                manganese 2; via carboxylate.
FT                                {ECO:0000256|HAMAP-Rule:MF_01379}.
FT   BINDING     126    126       Pheophytin D1. {ECO:0000256|HAMAP-Rule:
FT                                MF_01379}.
FT   BINDING     215    215       Quinone (B). {ECO:0000256|HAMAP-Rule:
FT                                MF_01379}.
FT   SITE        161    161       Tyrosine radical intermediate.
FT                                {ECO:0000256|HAMAP-Rule:MF_01379}.
FT   SITE        190    190       Stabilizes free radical intermediate.
FT                                {ECO:0000256|HAMAP-Rule:MF_01379}.
FT   SITE        344    345       Cleavage; by CtpA. {ECO:0000256|HAMAP-
FT                                Rule:MF_01379}.
FT   MOD_RES       2      2       N-acetylthreonine. {ECO:0000256|HAMAP-
FT                                Rule:MF_01379}.
FT   MOD_RES       2      2       Phosphothreonine. {ECO:0000256|HAMAP-
FT                                Rule:MF_01379}.
SQ   SEQUENCE   353 AA;  38935 MW;  AA6BFB4FBFCE1C79 CRC64;
     MTAILERRES TSLWGRFCNW ITSTENRLYI GWFGVLMIPT LLTATSVFII AFIAAPPVDI
     DGIREPVSGS LLYGNNIISG AIIPTSAAIG LHFYPIWEAA SVDEWLYNGG PYELIVLHFL
     LGVACYMGRE WELSFRLGMR PWIAVAYSAP VAAATAVFLI YPIGQGSFSD GMPLGISGTF
     NFMIVFQAEH NILMHPFHML GVAGVFGGSL FSAMHGSLVT SSLIRETTEN ESANEGYKFG
     QEEETYNIVA AHGYFGRLIF QYASFNNSRS LHFFLAAWPV VGIWFTALGI STMAFNLNGF
     NFNQSVVDSQ GRVINTWADI INRANLGMEV MHERNAHNFP LDLAALEVPS LNG
//