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PETD_ANTAG
ID   PETD_ANTAG              Reviewed;         160 AA.
AC   Q85AY5;
DT   29-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   25-MAY-2022, entry version 75.
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   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: 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=16 {ECO:0000269|PubMed:12527781,
CC       ECO:0000269|PubMed:12711687}, 30 {ECO:0000269|PubMed:12527781,
CC       ECO:0000269|PubMed:12711687}, 36 {ECO:0000269|PubMed:12527781,
CC       ECO:0000269|PubMed:12711687}, 37 {ECO:0000269|PubMed:12527781,
CC       ECO:0000269|PubMed:12711687}, 38 {ECO:0000269|PubMed:12527781,
CC       ECO:0000269|PubMed:12711687}, 40 {ECO:0000269|PubMed:12527781,
CC       ECO:0000269|PubMed:12711687}, 41 {ECO:0000269|PubMed:12527781,
CC       ECO:0000269|PubMed:12711687}, 72 {ECO:0000269|PubMed:12527781,
CC       ECO:0000269|PubMed:12711687}, 85 {ECO:0000269|PubMed:12527781,
CC       ECO:0000269|PubMed:12711687}, 86 {ECO:0000269|PubMed:12527781,
CC       ECO:0000269|PubMed:12711687}, 88 {ECO:0000269|PubMed:12527781,
CC       ECO:0000269|PubMed:12711687}, 89 {ECO:0000269|PubMed:12527781,
CC       ECO:0000269|PubMed:12711687}, 105 {ECO:0000269|PubMed:12527781,
CC       ECO:0000269|PubMed:12711687}, 117 {ECO:0000269|PubMed:12527781,
CC       ECO:0000269|PubMed:12711687}, 121 {ECO:0000269|PubMed:12527781,
CC       ECO:0000269|PubMed:12711687}, 123 {ECO:0000269|PubMed:12527781,
CC       ECO:0000269|PubMed:12711687}, 134 {ECO:0000269|PubMed:12527781,
CC       ECO:0000269|PubMed:12711687}, 161 {ECO:0000269|PubMed:12527781,
CC       ECO:0000269|PubMed:12711687}; Note=The nonsense codons at positions 85
CC       and 121 are modified to sense codons. The stop codon is created by RNA
CC       editing.;
CC   -!- SIMILARITY: Belongs to the cytochrome b family. PetD subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_01344}.
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DR   EMBL; AB086179; BAC55380.1; -; Genomic_DNA.
DR   EMBL; AB087465; BAC55477.1; -; mRNA.
DR   RefSeq; NP_777444.1; NC_004543.1.
DR   AlphaFoldDB; Q85AY5; -.
DR   SMR; Q85AY5; -.
DR   GeneID; 2553386; -.
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..160
FT                   /note="Cytochrome b6-f complex subunit 4"
FT                   /id="PRO_0000061845"
FT   TRANSMEM        36..56
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01344"
FT   TRANSMEM        95..115
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01344"
FT   TRANSMEM        131..151
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01344"
SQ   SEQUENCE   160 AA;  17298 MW;  A3DB6CED07B8937E CRC64;
     MGVTKKPDLS DPVLRAKLAK GMGHNYYGEP AWPNDLLYIF PVVILGTIAC TVGLAVLEPS
     MIGEPANPFA TPLEILPEWY FFPVFQILRT VPNKLLGVLL MAAVPAGLLT VPFLENVNKF
     QNPFRRPVAT TIFLIGTAVA IWLGIGAALP IDKSLTLGLS
 
 
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