PSBH_ANTAG
ID PSBH_ANTAG Reviewed; 74 AA.
AC Q85CN0;
DT 15-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
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};
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: 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 -!- RNA EDITING: Modified_positions=23 {ECO:0000269|PubMed:12527781,
CC ECO:0000269|PubMed:12711687}, 53 {ECO:0000269|PubMed:12527781,
CC ECO:0000269|PubMed:12711687}, 54 {ECO:0000269|PubMed:12527781,
CC ECO:0000269|PubMed:12711687}, 60 {ECO:0000269|PubMed:12527781,
CC ECO:0000269|PubMed:12711687};
CC -!- SIMILARITY: Belongs to the PsbH family. {ECO:0000255|HAMAP-
CC Rule:MF_00752}.
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DR EMBL; AB086179; BAC55378.1; -; Genomic_DNA.
DR EMBL; AB087463; BAC55475.1; -; mRNA.
DR RefSeq; NP_777442.1; NC_004543.1.
DR AlphaFoldDB; Q85CN0; -.
DR SMR; Q85CN0; -.
DR GeneID; 2553402; -.
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: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 2: Evidence at transcript level;
KW Chloroplast; Membrane; Phosphoprotein; Photosynthesis; Photosystem II;
KW Plastid; RNA editing; Thylakoid; Transmembrane; Transmembrane helix.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250"
FT CHAIN 2..74
FT /note="Photosystem II reaction center protein H"
FT /id="PRO_0000070497"
FT TRANSMEM 41..61
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00752"
FT MOD_RES 3
FT /note="Phosphothreonine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00752"
SQ SEQUENCE 74 AA; 7923 MW; 115C27B3419B94F9 CRC64;
MATQIIDDTP KTKGRRSGIG NILKPLNSEY GKVAPGWGTT PLMGIAMGLF AVFLVIILEL
YNSSVLLDGV SVSW
