ID F8RSL7_9POAL Unreviewed; 62 AA.
AC F8RSL7;
DT 21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT 21-SEP-2011, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE RecName: Full=Photosystem II reaction center protein Z {ECO:0000256|ARBA:ARBA00021665, ECO:0000256|RuleBase:RU003472};
DE Flags: Fragment;
GN Name=psbZ {ECO:0000313|EMBL:AEJ10200.1};
OS Flagellaria indica.
OG Plastid {ECO:0000313|EMBL:AEJ10200.1}.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Flagellariaceae;
OC Flagellaria.
OX NCBI_TaxID=13529 {ECO:0000313|EMBL:AEJ10200.1};
RN [1] {ECO:0000313|EMBL:AEJ10200.1}
RP NUCLEOTIDE SEQUENCE.
RA Givnish T.J., Ames M., McNeal J.R., McKain M.J., Steele P.R.,
RA dePamphilis C.W., Graham S.W., Pires J.C., Stevenson D.W., Zomlefer W.B.,
RA Briggs B.G., Duvall M.R., Moore M.J., Heaney J.M., Soltis D.E.,
RA Soltis P.S., Thiele K., Leebens-Mack J.H.;
RT "Assembling the Tree of the Monocotyledons: Plastome Sequence Phylogeny and
RT Evolution of Poales.";
RL Ann. Mo. Bot. Gard. 97:584-616(2010).
CC -!- FUNCTION: Controls the interaction of photosystem II (PSII) cores with
CC the light-harvesting antenna, regulates electron flow through the 2
CC photosystem reaction centers. PSII is a light-driven water
CC plastoquinone oxidoreductase, using light energy to abstract electrons
CC from H(2)O, generating a proton gradient subsequently used for ATP
CC formation. {ECO:0000256|RuleBase:RU003472}.
CC -!- SUBUNIT: PSII is composed of 1 copy each of membrane proteins PsbA,
CC PsbB, PsbC, PsbD, PsbE, PsbF, PsbH, PsbI, PsbJ, PsbK, PsbL, PsbM, PsbT,
CC PsbY, PsbZ, Psb30/Ycf12, at least 3 peripheral proteins of the oxygen-
CC evolving complex and a large number of cofactors. It forms dimeric
CC complexes. {ECO:0000256|ARBA:ARBA00038734}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the PsbZ family. {ECO:0000256|ARBA:ARBA00008367,
CC ECO:0000256|RuleBase:RU003472}.
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DR EMBL; HQ180824; AEJ10200.1; -; Genomic_DNA.
DR AlphaFoldDB; F8RSL7; -.
DR GO; GO:0009539; C:photosystem II reaction center; IEA:InterPro.
DR GO; GO:0009536; C:plastid; IEA:UniProtKB-KW.
DR GO; GO:0015979; P:photosynthesis; IEA:UniProtKB-KW.
DR GO; GO:0042549; P:photosystem II stabilization; IEA:InterPro.
DR Gene3D; 1.10.287.740; Photosystem II PsbZ, reaction centre; 1.
DR HAMAP; MF_00644; PSII_PsbZ; 1.
DR InterPro; IPR002644; PSII_PsbZ.
DR InterPro; IPR036512; PSII_PsbZ_sf.
DR NCBIfam; TIGR03043; PS_II_psbZ; 1.
DR PANTHER; PTHR34971; PHOTOSYSTEM II REACTION CENTER PROTEIN Z; 1.
DR PANTHER; PTHR34971:SF2; PHOTOSYSTEM II REACTION CENTER PROTEIN Z; 1.
DR Pfam; PF01737; Ycf9; 1.
DR SUPFAM; SSF161055; PsbZ-like; 1.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Photosynthesis {ECO:0000256|ARBA:ARBA00022531,
KW ECO:0000256|RuleBase:RU003472};
KW Photosystem II {ECO:0000256|ARBA:ARBA00023276,
KW ECO:0000256|RuleBase:RU003472}; Plastid {ECO:0000313|EMBL:AEJ10200.1};
KW Reaction center {ECO:0000256|ARBA:ARBA00022469,
KW ECO:0000256|RuleBase:RU003472};
KW Thylakoid {ECO:0000256|ARBA:ARBA00023078, ECO:0000256|RuleBase:RU003472};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU003472};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 44..61
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT NON_TER 62
FT /evidence="ECO:0000313|EMBL:AEJ10200.1"
SQ SEQUENCE 62 AA; 6544 MW; 7A5C74B47F76C3C5 CRC64;
MTIAFQLAVF ALIATSSVLL ISVPVVFASS EGWSNNKNVV FSGTSLWIGL VFLVAILNSL
VS
//
