ID A0A4S8I613_MUSBA Unreviewed; 923 AA.
AC A0A4S8I613;
DT 31-JUL-2019, integrated into UniProtKB/TrEMBL.
DT 31-JUL-2019, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=Photosystem I P700 chlorophyll a apoprotein A1 {ECO:0000256|ARBA:ARBA00017774};
DE EC=1.97.1.12 {ECO:0000256|ARBA:ARBA00013197};
DE AltName: Full=30S ribosomal protein S14, chloroplastic {ECO:0000256|ARBA:ARBA00035514};
DE AltName: Full=PsaA {ECO:0000256|ARBA:ARBA00031004};
DE AltName: Full=Small ribosomal subunit protein uS14c {ECO:0000256|ARBA:ARBA00035247};
GN ORFNames=C4D60_Mb00t08670 {ECO:0000313|EMBL:THU43320.1};
OS Musa balbisiana (Banana).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Zingiberales; Musaceae; Musa.
OX NCBI_TaxID=52838 {ECO:0000313|EMBL:THU43320.1, ECO:0000313|Proteomes:UP000317650};
RN [1] {ECO:0000313|EMBL:THU43320.1, ECO:0000313|Proteomes:UP000317650}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. DH-PKW {ECO:0000313|Proteomes:UP000317650};
RC TISSUE=Leaves {ECO:0000313|EMBL:THU43320.1};
RA Yao X.;
RT "Genome sequencing of Musa balbisiana reveals subgenome evolution and
RT function divergence in polyploid bananas.";
RL Nat. Plants 0:0-0(2019).
CC -!- FUNCTION: PsaA and PsaB bind P700, the primary electron donor of
CC photosystem I (PSI), as well as the electron acceptors A0, A1 and FX.
CC PSI 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. Oxidized P700 is reduced on
CC the lumenal side of the thylakoid membrane by plastocyanin.
CC {ECO:0000256|ARBA:ARBA00003162}.
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 Evidence={ECO:0000256|ARBA:ARBA00000994};
CC -!- SUBUNIT: The PsaA/B heterodimer binds the P700 chlorophyll special pair
CC and subsequent electron acceptors. PSI 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 eukaryotic
CC PSI reaction center is composed of at least 11 subunits.
CC {ECO:0000256|ARBA:ARBA00026002}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the PsaA/PsaB family.
CC {ECO:0000256|ARBA:ARBA00010598}.
CC -!- SIMILARITY: Belongs to the universal ribosomal protein uS14 family.
CC {ECO:0000256|ARBA:ARBA00009083}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:THU43320.1}.
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; PYDT01000127; THU43320.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A4S8I613; -.
DR STRING; 52838.A0A4S8I613; -.
DR Proteomes; UP000317650; Unassembled WGS sequence.
DR GO; GO:0009522; C:photosystem I; IEA:UniProtKB-KW.
DR GO; GO:1990904; C:ribonucleoprotein complex; IEA:UniProtKB-KW.
DR GO; GO:0005840; C:ribosome; IEA:UniProtKB-KW.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0016168; F:chlorophyll binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro.
DR GO; GO:0015979; P:photosynthesis; IEA:UniProtKB-KW.
DR GO; GO:0006412; P:translation; IEA:InterPro.
DR Gene3D; 1.10.287.1480; -; 1.
DR Gene3D; 1.20.1130.10; Photosystem I PsaA/PsaB; 3.
DR HAMAP; MF_00537; Ribosomal_S14_1; 1.
DR InterPro; IPR001280; PSI_PsaA/B.
DR InterPro; IPR020586; PSI_PsaA/B_CS.
DR InterPro; IPR036408; PSI_PsaA/B_sf.
DR InterPro; IPR001209; Ribosomal_uS14.
DR InterPro; IPR023036; Ribosomal_uS14_bac/plastid.
DR InterPro; IPR018271; Ribosomal_uS14_CS.
DR PANTHER; PTHR30128; OUTER MEMBRANE PROTEIN, OMPA-RELATED; 1.
DR PANTHER; PTHR30128:SF77; PHOTOSYSTEM I P700 CHLOROPHYLL A APOPROTEIN A1; 1.
DR Pfam; PF00223; PsaA_PsaB; 3.
DR Pfam; PF00253; Ribosomal_S14; 1.
DR PRINTS; PR00257; PHOTSYSPSAAB.
DR SUPFAM; SSF57716; Glucocorticoid receptor-like (DNA-binding domain); 1.
DR SUPFAM; SSF81558; Photosystem I subunits PsaA/PsaB; 2.
DR PROSITE; PS00419; PHOTOSYSTEM_I_PSAAB; 2.
DR PROSITE; PS00527; RIBOSOMAL_S14; 1.
PE 3: Inferred from homology;
KW 4Fe-4S {ECO:0000256|ARBA:ARBA00022485};
KW Chlorophyll {ECO:0000256|ARBA:ARBA00022494};
KW Chromophore {ECO:0000256|ARBA:ARBA00022991};
KW Electron transport {ECO:0000256|ARBA:ARBA00022982};
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Photosynthesis {ECO:0000256|ARBA:ARBA00022531};
KW Photosystem I {ECO:0000256|ARBA:ARBA00022836};
KW Plastid {ECO:0000256|ARBA:ARBA00022640};
KW Reference proteome {ECO:0000313|Proteomes:UP000317650};
KW Ribonucleoprotein {ECO:0000256|ARBA:ARBA00023274};
KW Ribosomal protein {ECO:0000256|ARBA:ARBA00022980};
KW Thylakoid {ECO:0000256|ARBA:ARBA00023078};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}; Transport {ECO:0000256|ARBA:ARBA00022448}.
FT TRANSMEM 154..176
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 350..369
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 442..460
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 596..616
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 695..717
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 765..785
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
SQ SEQUENCE 923 AA; 102807 MW; 60597A265B95D5F1 CRC64;
MIIRSPEPEV KIVVDRDPIK TSFEEWARPG HFSRTIAKGP DTTTWIWNLH ADAHDFDSHT
SDLEEISRKV FSAHFGQLSI IFLWLSGMYF HGARFSNYEA WLSDPTHIAP SAQVVWPIVG
QEILNGDVGG GFRGIQITSG FFQIWRASGI TSELQLYCTA IGALVFASLM LFAGWFHYHK
AAPKLAWFQD VESMLNHHLA GLLGLGSLSW AGHQIHVSLP INQFLDAGVD PKEIPLPHEF
ILNRDLLAQL YPSFAEGATP FFTLNWSKYA EFLTFRGGLD PITGGLWLTD IAHHHLAIAI
LFLIAGHMYR TNWGIGHGIK DILEAHKGPF TGQGHKGLYE ILTTSWHAQL SLNLAMLGSL
TIIVAHHMYS MPPYPYLAID YDTAIQLQPI FAQWVQNTHA LAPGITAPGA TASTSLTWGG
GELVAVGGKV ALLPIPLGTA DFLVHHIHAF TIHVTVLILL KGVLFARSSR LIPDKANLGF
RFPCDGPGRG GTCQVSAWDH VFLGLFWMYN AISVSDVWGT ISDQGVVTHI TGGNFAQSSI
TINGWLRDFL WAQASQGNVS QFNESSTYLM GWLRDYNPEQ NEDNVLARML DHKEAIISHL
SWASLFLGFH TLGLYVHNDV MLAFGTPEKQ ILIEPIFAQW IQSAHGKTSY GFDVLLSSTN
GPAFNAGRSI WLPGWLNAVN ENSNSLFLTI GPGDFLVHHA IALGLHTTTL ILVKGALDAR
GSKLMPDKKD FGYSFPCDGP GRGGTCDISA WDAFYLAVFW MLNTIGWDAA VLVIFLLGTH
FIGSFLDVKY HWVGYFLLAL ETHHFMAGIR TVSLIIIGTE HYIMARKSLI QREKKRQKLE
QKYHLIRRSS KKKISKVPSL SEKWEIHGKL QSPPRNSAPI RLHRRCFLTG RPRANYRDFG
LSGHILREMF HACLLPGAIR SSW
//
