PETD_ADICA
ID PETD_ADICA Reviewed; 159 AA.
AC Q85FJ2;
DT 05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 2.
DT 25-MAY-2022, entry version 73.
DE RecName: Full=Cytochrome b6-f complex subunit 4 {ECO:0000255|HAMAP-Rule:MF_01344};
DE AltName: Full=17 kDa polypeptide {ECO:0000255|HAMAP-Rule:MF_01344};
GN Name=petD {ECO:0000255|HAMAP-Rule:MF_01344};
OS Adiantum capillus-veneris (Maidenhair fern).
OG Plastid; Chloroplast.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Polypodiopsida; Polypodiidae; Polypodiales; Pteridineae; Pteridaceae;
OC Vittarioideae; Adiantum.
OX NCBI_TaxID=13818;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12755170; DOI=10.1093/dnares/10.2.59;
RA Wolf P.G., Rowe C.A., Sinclair R.B., Hasebe M.;
RT "Complete nucleotide sequence of the chloroplast genome from a
RT leptosporangiate fern, Adiantum capillus-veneris L.";
RL DNA Res. 10:59-65(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND RNA EDITING.
RC TISSUE=Frond;
RX PubMed=15363849; DOI=10.1016/j.gene.2004.06.018;
RA Wolf P.G., Rowe C.A., Hasebe M.;
RT "High levels of RNA editing in a vascular plant chloroplast genome:
RT analysis of transcripts from the fern Adiantum capillus-veneris.";
RL Gene 339:89-97(2004).
CC -!- FUNCTION: Component of the cytochrome b6-f complex, which mediates
CC electron transfer between photosystem II (PSII) and photosystem I
CC (PSI), cyclic electron flow around PSI, and state transitions.
CC {ECO:0000255|HAMAP-Rule:MF_01344}.
CC -!- SUBUNIT: The 4 large subunits of the cytochrome b6-f complex are
CC cytochrome b6, subunit IV (17 kDa polypeptide, petD), cytochrome f and
CC the Rieske protein, while the 4 small subunits are petG, petL, petM and
CC petN. The complex functions as a dimer (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane
CC {ECO:0000255|HAMAP-Rule:MF_01344}; Multi-pass membrane protein
CC {ECO:0000255|HAMAP-Rule:MF_01344}.
CC -!- RNA EDITING: Modified_positions=36 {ECO:0000269|PubMed:15363849}, 99
CC {ECO:0000269|PubMed:15363849}, 142 {ECO:0000269|PubMed:15363849}, 160
CC {ECO:0000269|PubMed:15363849}; Note=The stop codon at position 160 is
CC created by RNA editing.;
CC -!- SIMILARITY: Belongs to the cytochrome b family. PetD subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_01344}.
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DR EMBL; AY178864; AAP29421.2; -; Genomic_DNA.
DR RefSeq; NP_848090.2; NC_004766.1.
DR AlphaFoldDB; Q85FJ2; -.
DR SMR; Q85FJ2; -.
DR GeneID; 807421; -.
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:0045158; F:electron transporter, transferring electrons within cytochrome b6/f complex of photosystem II activity; IEA:UniProtKB-UniRule.
DR GO; GO:0045156; F:electron transporter, transferring electrons within the cyclic electron transport pathway of photosynthesis activity; IEA:InterPro.
DR GO; GO:0009767; P:photosynthetic electron transport chain; IEA:InterPro.
DR CDD; cd00290; cytochrome_b_C; 1.
DR HAMAP; MF_01344; Cytb6_f_subIV; 1.
DR InterPro; IPR005798; Cyt_b/b6_C.
DR InterPro; IPR036150; Cyt_b/b6_C_sf.
DR InterPro; IPR005870; Cyt_b6/f_cplx_suIV.
DR Pfam; PF00032; Cytochrom_B_C; 1.
DR PIRSF; PIRSF000033; B6f_17K; 1.
DR SUPFAM; SSF81648; SSF81648; 1.
DR TIGRFAMs; TIGR01156; cytb6/f_IV; 1.
DR PROSITE; PS51003; CYTB_CTER; 1.
PE 2: Evidence at transcript level;
KW Chloroplast; Electron transport; Membrane; Photosynthesis; Plastid;
KW RNA editing; Thylakoid; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..159
FT /note="Cytochrome b6-f complex subunit 4"
FT /id="PRO_0000061842"
FT TRANSMEM 35..55
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01344"
FT TRANSMEM 94..114
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01344"
FT TRANSMEM 130..150
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01344"
SQ SEQUENCE 159 AA; 17188 MW; 3ABA58E9E45F33E5 CRC64;
MGVKKPDLND PVLRAKLAKG MGHNYYGEPA WPNDLLYIFP VVILGTVACT VGLAVLEPSM
VGEPANPFAT PLEILPEWYF FPVFQILRTV PNKLLGVLLM ASVPAGLLTV PFLENVNKFQ
NPFRRPVATT VFAIGTVAAI WLGIGATLPI EGSLTLGLF