ID   PSAF_CYAPA              Reviewed;         186 AA.
AC   P48115;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 1.
DT   03-AUG-2022, entry version 70.
DE   RecName: Full=Photosystem I reaction center subunit III;
DE   AltName: Full=PSI-F;
DE   Flags: Precursor;
GN   Name=psaF;
OS   Cyanophora paradoxa.
OG   Plastid; Cyanelle.
OC   Eukaryota; Glaucocystophyceae; Cyanophoraceae; Cyanophora.
OX   NCBI_TaxID=2762;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UTEX LB 555 / Pringsheim;
RA   Stirewalt V.L., Michalowski C.B., Loeffelhardt W., Bohnert H.J.,
RA   Bryant D.A.;
RT   "Nucleotide sequence of the cyanelle DNA from Cyanophora paradoxa.";
RL   Plant Mol. Biol. Rep. 13:327-332(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UTEX LB 555 / Pringsheim;
RA   Loeffelhardt W., Stirewalt V.L., Michalowski C.B., Annarella M.,
RA   Farley J.Y., Schluchter W.M., Chung S., Newmann-Spallart C., Steiner J.M.,
RA   Jakowitsch J., Bohnert H.J., Bryant D.A.;
RT   "The complete sequence of the cyanelle genome of Cyanophora paradoxa: the
RT   genetic complexity of a primitive plastid.";
RL   (In) Schenk H.E.A., Herrmann R., Jeon K.W., Mueller N.E., Schwemmler W.
RL   (eds.);
RL   Eukaryotism and symbiosis, pp.40-48, Springer-Verlag, Heidelberg (1997).
CC   -!- FUNCTION: Probably participates in efficiency of electron transfer from
CC       plastocyanin to P700 (or cytochrome c553 in algae and cyanobacteria).
CC       This plastocyanin-docking protein contributes to the specific
CC       association of plastocyanin to PSI.
CC   -!- SUBCELLULAR LOCATION: Plastid, cyanelle thylakoid membrane
CC       {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Note=The
CC       soluble domain is associated with the lumenal side of the thylakoid
CC       membrane. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the PsaF family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; U30821; AAA81184.1; -; Genomic_DNA.
DR   PIR; T06841; T06841.
DR   RefSeq; NP_043153.1; NC_001675.1.
DR   PDB; 7DR0; EM; 3.30 A; F=1-186.
DR   PDB; 7DR1; EM; 3.20 A; F=1-186.
DR   PDB; 7DR2; EM; 3.80 A; aF/bF/cF/dF=1-186.
DR   PDBsum; 7DR0; -.
DR   PDBsum; 7DR1; -.
DR   PDBsum; 7DR2; -.
DR   AlphaFoldDB; P48115; -.
DR   SMR; P48115; -.
DR   GeneID; 801569; -.
DR   GO; GO:0033115; C:cyanelle thylakoid membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0009538; C:photosystem I reaction center; IEA:InterPro.
DR   GO; GO:0015979; P:photosynthesis; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.8.110; -; 1.
DR   InterPro; IPR003666; PSI_PsaF.
DR   InterPro; IPR036577; PSI_PsaF_sf.
DR   PANTHER; PTHR34939; PTHR34939; 1.
DR   Pfam; PF02507; PSI_PsaF; 1.
DR   SUPFAM; SSF81536; SSF81536; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Cyanelle; Membrane; Photosynthesis; Photosystem I; Plastid;
KW   Signal; Thylakoid; Transmembrane; Transmembrane helix.
FT   SIGNAL          1..25
FT                   /evidence="ECO:0000255"
FT   CHAIN           26..186
FT                   /note="Photosystem I reaction center subunit III"
FT                   /id="PRO_0000207751"
FT   TRANSMEM        105..125
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        144..164
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   186 AA;  20673 MW;  D938E6923DD27179 CRC64;
     MRKLFLLMFC LSGLILTTDI RPVRADVAGL IPCSQSDAFE RRLKNTTQRL ENRLKKYEPG
     SAPAEALQKQ IDKTQQRFDK YRNSGLLCGA DGLPHLITDG RWSHAGEFTI PGLLFLYIAG
     FIGWSGRSYL QAVAASDNST EKEIIIDIPV ALQSVSKGFV WPLAALQEFS SGKLTARDEE
     ITISPR