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Database: UniProt
Entry: H6T0J4_9LILI
LinkDB: H6T0J4_9LILI
Original site: H6T0J4_9LILI 
ID   H6T0J4_9LILI            Unreviewed;        39 AA.
AC   H6T0J4;
DT   18-APR-2012, integrated into UniProtKB/TrEMBL.
DT   18-APR-2012, sequence version 1.
DT   13-SEP-2023, entry version 33.
DE   RecName: Full=Cytochrome b559 subunit beta {ECO:0000256|RuleBase:RU004529};
DE   AltName: Full=PSII reaction center subunit VI {ECO:0000256|RuleBase:RU004529};
DE   Flags: Fragment;
GN   Name=psbF {ECO:0000313|EMBL:AFA27573.1};
OS   Renealmia alpinia.
OG   Plastid {ECO:0000313|EMBL:AFA27573.1}.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Zingiberales; Zingiberaceae;
OC   Renealmia.
OX   NCBI_TaxID=199658 {ECO:0000313|EMBL:AFA27573.1};
RN   [1] {ECO:0000313|EMBL:AFA27573.1}
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).
RN   [2] {ECO:0000313|EMBL:AYP34585.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=93-740D {ECO:0000313|EMBL:AYP34585.1};
RX   PubMed=30368769; DOI=.1002/ajb2.1178;
RA   Givnish T.J., Zuluaga A., Spalink D., Soto Gomez M., Lam V.K.Y.,
RA   Saarela J.M., Sass C., Iles W.J.D., de Sousa D.J.L., Leebens-Mack J.,
RA   Chris Pires J., Zomlefer W.B., Gandolfo M.A., Davis J.I., Stevenson D.W.,
RA   dePamphilis C., Specht C.D., Graham S.W., Barrett C.F., Ane C.;
RT   "Monocot plastid phylogenomics, timeline, net rates of species
RT   diversification, the power of multi-gene analyses, and a functional model
RT   for the origin of monocots.";
RL   Am. J. Bot. 105:1888-1910(2018).
CC   -!- FUNCTION: This b-type cytochrome is tightly associated with the
CC       reaction center of photosystem II (PSII). 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:0000256|RuleBase:RU004529}.
CC   -!- SUBUNIT: Heterodimer of an alpha subunit and a beta subunit.
CC       {ECO:0000256|RuleBase:RU004529}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004167}; Single-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004167}. Plastid,
CC       chloroplast thylakoid membrane {ECO:0000256|RuleBase:RU004529}; Single-
CC       pass membrane protein {ECO:0000256|RuleBase:RU004529}.
CC   -!- SIMILARITY: Belongs to the PsbE/PsbF family.
CC       {ECO:0000256|RuleBase:RU004529}.
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DR   EMBL; HQ182067; AFA27573.1; -; Genomic_DNA.
DR   EMBL; MH603438; AYP34585.1; -; Genomic_DNA.
DR   AlphaFoldDB; H6T0J4; -.
DR   SMR; H6T0J4; -.
DR   GO; GO:0009535; C:chloroplast thylakoid membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0009539; C:photosystem II reaction center; IEA:InterPro.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0009767; P:photosynthetic electron transport chain; IEA:InterPro.
DR   HAMAP; MF_00643; PSII_PsbF; 1.
DR   InterPro; IPR006241; PSII_cyt_b559_bsu.
DR   InterPro; IPR006216; PSII_cyt_b559_CS.
DR   InterPro; IPR013081; PSII_cyt_b559_N.
DR   NCBIfam; TIGR01333; cyt_b559_beta; 1.
DR   Pfam; PF00283; Cytochrom_B559; 1.
DR   PIRSF; PIRSF000037; PsbF; 1.
DR   SUPFAM; SSF161045; Cytochrome b559 subunits; 1.
DR   PROSITE; PS00537; CYTOCHROME_B559; 1.
PE   3: Inferred from homology;
KW   Chloroplast {ECO:0000256|RuleBase:RU004529};
KW   Electron transport {ECO:0000256|ARBA:ARBA00022982,
KW   ECO:0000256|RuleBase:RU004529};
KW   Heme {ECO:0000256|ARBA:ARBA00022617, ECO:0000256|RuleBase:RU004529};
KW   Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|RuleBase:RU004529};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU004529};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|RuleBase:RU004529};
KW   Photosynthesis {ECO:0000256|ARBA:ARBA00022531,
KW   ECO:0000256|RuleBase:RU004529};
KW   Photosystem II {ECO:0000256|ARBA:ARBA00023276,
KW   ECO:0000256|RuleBase:RU004529}; Plastid {ECO:0000313|EMBL:AFA27573.1};
KW   Thylakoid {ECO:0000256|ARBA:ARBA00023078};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW   ECO:0000256|RuleBase:RU004529};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|RuleBase:RU004529};
KW   Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU004529}.
FT   TRANSMEM        15..37
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU004529"
FT   DOMAIN          1..29
FT                   /note="Photosystem II cytochrome b559 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00283"
FT   NON_TER         39
FT                   /evidence="ECO:0000313|EMBL:AFA27573.1"
SQ   SEQUENCE   39 AA;  4424 MW;  F61251852D7E1D6F CRC64;
     MTIDRTYPIF TVRWLAVHGL AVPTVSFLGS ISAMQFIQR
//
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