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PSAC_ANTAG
ID   PSAC_ANTAG              Reviewed;          81 AA.
AC   Q85AC1;
DT   25-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   03-AUG-2022, entry version 89.
DE   RecName: Full=Photosystem I iron-sulfur center;
DE            EC=1.97.1.12;
DE   AltName: Full=9 kDa polypeptide;
DE   AltName: Full=PSI-C;
DE   AltName: Full=Photosystem I subunit VII;
DE   AltName: Full=PsaC;
GN   Name=psaC;
OS   Anthoceros angustus (Hornwort) (Anthoceros formosae).
OG   Plastid; Chloroplast.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Anthocerotophyta;
OC   Anthocerotopsida; Anthocerotidae; Anthocerotales; Anthocerotaceae;
OC   Anthoceros.
OX   NCBI_TaxID=48387;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND RNA EDITING.
RX   PubMed=12527781; DOI=10.1093/nar/gkg155;
RA   Kugita M., Kaneko A., Yamamoto Y., Takeya Y., Matsumoto T., Yoshinaga K.;
RT   "The complete nucleotide sequence of the hornwort (Anthoceros formosae)
RT   chloroplast genome: insight into the earliest land plants.";
RL   Nucleic Acids Res. 31:716-721(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND RNA EDITING.
RC   TISSUE=Thallus;
RX   PubMed=12711687; DOI=10.1093/nar/gkg327;
RA   Kugita M., Yamamoto Y., Fujikawa T., Matsumoto T., Yoshinaga K.;
RT   "RNA editing in hornwort chloroplasts makes more than half the genes
RT   functional.";
RL   Nucleic Acids Res. 31:2417-2423(2003).
CC   -!- FUNCTION: Apoprotein for the two 4Fe-4S centers FA and FB of
CC       photosystem I (PSI); essential for photochemical activity. FB is the
CC       terminal electron acceptor of PSI, donating electrons to ferredoxin.
CC       The C-terminus interacts with PsaA/B/D and helps assemble the protein
CC       into the PSI complex. Required for binding of PsaD and PsaE to PSI. PSI
CC       is a plastocyanin-ferredoxin oxidoreductase, converting photonic
CC       excitation into a charge separation, which transfers an electron from
CC       the donor P700 chlorophyll pair to the spectroscopically characterized
CC       acceptors A0, A1, FX, FA and FB in turn (By similarity). {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=hnu + oxidized [2Fe-2S]-[ferredoxin] + reduced [plastocyanin]
CC         = oxidized [plastocyanin] + reduced [2Fe-2S]-[ferredoxin];
CC         Xref=Rhea:RHEA:30407, Rhea:RHEA-COMP:10000, Rhea:RHEA-COMP:10001,
CC         Rhea:RHEA-COMP:10039, Rhea:RHEA-COMP:10040, ChEBI:CHEBI:29036,
CC         ChEBI:CHEBI:30212, ChEBI:CHEBI:33737, ChEBI:CHEBI:33738,
CC         ChEBI:CHEBI:49552; EC=1.97.1.12;
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; Evidence={ECO:0000250};
CC       Note=Binds 2 [4Fe-4S] clusters. Cluster 2 is most probably the
CC       spectroscopically characterized electron acceptor FA and cluster 1 is
CC       most probably FB. {ECO:0000250};
CC   -!- SUBUNIT: The eukaryotic PSI reaction center is composed of at least 11
CC       subunits. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane
CC       {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Stromal side
CC       {ECO:0000250}.
CC   -!- RNA EDITING: Modified_positions=4 {ECO:0000269|PubMed:12527781,
CC       ECO:0000269|PubMed:12711687}, 16 {ECO:0000269|PubMed:12527781,
CC       ECO:0000269|PubMed:12711687}, 22 {ECO:0000269|PubMed:12527781,
CC       ECO:0000269|PubMed:12711687}, 26 {ECO:0000269|PubMed:12527781,
CC       ECO:0000269|PubMed:12711687}, 38 {ECO:0000269|PubMed:12527781,
CC       ECO:0000269|PubMed:12711687}, 59 {ECO:0000269|PubMed:12527781,
CC       ECO:0000269|PubMed:12711687}, 62 {ECO:0000269|PubMed:12527781,
CC       ECO:0000269|PubMed:12711687}; Note=The nonsense codons at positions 17
CC       and 39 are modified to sense codons.;
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DR   EMBL; AB086179; BAC55402.1; -; Genomic_DNA.
DR   EMBL; AB087486; BAC55502.1; -; mRNA.
DR   RefSeq; NP_777465.1; NC_004543.1.
DR   AlphaFoldDB; Q85AC1; -.
DR   SMR; Q85AC1; -.
DR   GeneID; 2553392; -.
DR   GO; GO:0009535; C:chloroplast thylakoid membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0009522; C:photosystem I; IEA:UniProtKB-KW.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0009055; F:electron transfer activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0009773; P:photosynthetic electron transport in photosystem I; IEA:InterPro.
DR   HAMAP; MF_01303; PSI_PsaC; 1.
DR   InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR   InterPro; IPR017900; 4Fe4S_Fe_S_CS.
DR   InterPro; IPR017491; PSI_PsaC.
DR   TIGRFAMs; TIGR03048; PS_I_psaC; 1.
DR   PROSITE; PS00198; 4FE4S_FER_1; 2.
DR   PROSITE; PS51379; 4FE4S_FER_2; 2.
PE   2: Evidence at transcript level;
KW   4Fe-4S; Chloroplast; Electron transport; Iron; Iron-sulfur; Membrane;
KW   Metal-binding; Oxidoreductase; Photosynthesis; Photosystem I; Plastid;
KW   Repeat; RNA editing; Thylakoid; Transport.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250"
FT   CHAIN           2..81
FT                   /note="Photosystem I iron-sulfur center"
FT                   /id="PRO_0000061968"
FT   DOMAIN          2..31
FT                   /note="4Fe-4S ferredoxin-type 1"
FT   DOMAIN          39..68
FT                   /note="4Fe-4S ferredoxin-type 2"
FT   BINDING         11
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         14
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         17
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         21
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         48
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         51
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         54
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         58
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   81 AA;  8819 MW;  D7E6FE0B815FE678 CRC64;
     MAHSVKIYDT CIGCTQCVRA CPTDVLEMIS WDGCKANQIA SAPRTEDCVG CKRCESACPT
     DFLSVRVYLG SETTRSMGLA Y
 
 
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