PSBH_ORYSI
ID PSBH_ORYSI Reviewed; 73 AA.
AC P0C421; P09449; Q6QXZ2; Q6QY56;
DT 29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 29-MAY-2007, sequence version 1.
DT 25-MAY-2022, entry version 70.
DE RecName: Full=Photosystem II reaction center protein H {ECO:0000255|HAMAP-Rule:MF_00752};
DE Short=PSII-H {ECO:0000255|HAMAP-Rule:MF_00752};
DE AltName: Full=Photosystem II 10 kDa phosphoprotein {ECO:0000255|HAMAP-Rule:MF_00752};
GN Name=psbH {ECO:0000255|HAMAP-Rule:MF_00752}; ORFNames=9311092;
OS Oryza sativa subsp. indica (Rice).
OG Plastid; Chloroplast.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX NCBI_TaxID=39946;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. 93-11;
RX PubMed=15122023; DOI=10.1104/pp.103.031245;
RA Tang J., Xia H., Cao M., Zhang X., Zeng W., Hu S., Tong W., Wang J.,
RA Wang J., Yu J., Yang H., Zhu L.;
RT "A comparison of rice chloroplast genomes.";
RL Plant Physiol. 135:412-420(2004).
CC -!- FUNCTION: One of the components of the core complex of photosystem II
CC (PSII), required for its stability and/or assembly. PSII is a light-
CC driven water:plastoquinone oxidoreductase that uses light energy to
CC abstract 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:0000255|HAMAP-Rule:MF_00752}.
CC -!- SUBUNIT: PSII is composed of 1 copy each of membrane proteins PsbA,
CC PsbB, PsbC, PsbD, numerous small proteins, at least 3 peripheral
CC proteins of the oxygen-evolving complex and a large number of
CC cofactors. It forms dimeric complexes. {ECO:0000255|HAMAP-
CC Rule:MF_00752}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane
CC {ECO:0000255|HAMAP-Rule:MF_00752}; Single-pass membrane protein
CC {ECO:0000255|HAMAP-Rule:MF_00752}.
CC -!- PTM: Phosphorylation is a light-dependent reaction catalyzed by a
CC membrane-bound kinase; phosphorylation occurs on Thr residue(s) in the
CC N-terminus of the protein. {ECO:0000255|HAMAP-Rule:MF_00752}.
CC -!- SIMILARITY: Belongs to the PsbH family. {ECO:0000255|HAMAP-
CC Rule:MF_00752}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAS46073.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AY522329; AAS46073.1; ALT_INIT; Genomic_DNA.
DR RefSeq; YP_009161392.1; NC_027678.1.
DR RefSeq; YP_654233.1; NC_008155.1.
DR AlphaFoldDB; P0C421; -.
DR SMR; P0C421; -.
DR STRING; 39946.P0C421; -.
DR PRIDE; P0C421; -.
DR EnsemblPlants; BGIOSGA039463-TA; BGIOSGA039463-PA; BGIOSGA039463.
DR EnsemblPlants; BGIOSGA039485-TA; BGIOSGA039485-PA; BGIOSGA039485.
DR GeneID; 4126896; -.
DR Gramene; BGIOSGA039463-TA; BGIOSGA039463-PA; BGIOSGA039463.
DR Gramene; BGIOSGA039485-TA; BGIOSGA039485-PA; BGIOSGA039485.
DR HOGENOM; CLU_190203_1_0_1; -.
DR OMA; PLMAVFM; -.
DR Proteomes; UP000007015; Chloroplast.
DR GO; GO:0009535; C:chloroplast thylakoid membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0009523; C:photosystem II; IEA:UniProtKB-KW.
DR GO; GO:0009536; C:plastid; IC:Gramene.
DR GO; GO:0042301; F:phosphate ion binding; IEA:InterPro.
DR GO; GO:0015979; P:photosynthesis; IEA:UniProtKB-UniRule.
DR GO; GO:0050821; P:protein stabilization; IEA:InterPro.
DR Gene3D; 1.20.5.880; -; 1.
DR HAMAP; MF_00752; PSII_PsbH; 1.
DR InterPro; IPR001056; PSII_PsbH.
DR InterPro; IPR036863; PSII_PsbH_sf.
DR PANTHER; PTHR34469; PTHR34469; 1.
DR Pfam; PF00737; PsbH; 1.
DR SUPFAM; SSF161025; SSF161025; 1.
PE 3: Inferred from homology;
KW Chloroplast; Membrane; Phosphoprotein; Photosynthesis; Photosystem II;
KW Plastid; Reference proteome; Thylakoid; Transmembrane; Transmembrane helix.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250"
FT CHAIN 2..73
FT /note="Photosystem II reaction center protein H"
FT /id="PRO_0000289666"
FT TRANSMEM 41..61
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00752"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..16
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 3
FT /note="Phosphothreonine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00752"
FT MOD_RES 5
FT /note="Phosphothreonine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00752"
SQ SEQUENCE 73 AA; 7886 MW; BA428A5580BCD4C3 CRC64;
MATQTVEDSS RPGPRQTRVG NLLKPLNSEY GKVAPGWGTT PFMGVAMALF AVFLSIILEI
YNSSVLLDGI LMN
