ID D9HPC4_9ASPA Unreviewed; 394 AA.
AC D9HPC4;
DT 05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2010, sequence version 1.
DT 22-FEB-2023, entry version 35.
DE SubName: Full=Phytochrome C {ECO:0000313|EMBL:ADI49652.1};
DE Flags: Fragment;
GN Name=PhyC {ECO:0000313|EMBL:ADI49652.1};
OS Polystachya caloglossa.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Asparagales; Orchidaceae;
OC Epidendroideae; Vandeae; Polystachyinae; Polystachya.
OX NCBI_TaxID=687598 {ECO:0000313|EMBL:ADI49652.1};
RN [1] {ECO:0000313|EMBL:ADI49652.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=20525745; DOI=10.1093/aob/mcq092;
RA Russell A., Samuel R., Klejna V., Barfuss M.H., Rupp B., Chase M.W.;
RT "Reticulate evolution in diploid and tetraploid species of Polystachya
RT (Orchidaceae) as shown by plastid DNA sequences and low-copy nuclear
RT genes.";
RL Ann. Bot. 106:37-56(2010).
CC -!- FUNCTION: Regulatory photoreceptor which exists in two forms that are
CC reversibly interconvertible by light: the Pr form that absorbs
CC maximally in the red region of the spectrum and the Pfr form that
CC absorbs maximally in the far-red region. Photoconversion of Pr to Pfr
CC induces an array of morphogenic responses, whereas reconversion of Pfr
CC to Pr cancels the induction of those responses. Pfr controls the
CC expression of a number of nuclear genes including those encoding the
CC small subunit of ribulose-bisphosphate carboxylase, chlorophyll A/B
CC binding protein, protochlorophyllide reductase, rRNA, etc. It also
CC controls the expression of its own gene(s) in a negative feedback
CC fashion. {ECO:0000256|ARBA:ARBA00002479}.
CC -!- SIMILARITY: Belongs to the phytochrome family.
CC {ECO:0000256|ARBA:ARBA00008235}.
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DR EMBL; HM018518; ADI49652.1; -; Genomic_DNA.
DR AlphaFoldDB; D9HPC4; -.
DR GO; GO:0009881; F:photoreceptor activity; IEA:UniProtKB-KW.
DR GO; GO:0009584; P:detection of visible light; IEA:InterPro.
DR GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR Gene3D; 3.30.450.270; -; 1.
DR Gene3D; 3.30.450.40; -; 1.
DR InterPro; IPR003018; GAF.
DR InterPro; IPR029016; GAF-like_dom_sf.
DR InterPro; IPR016132; Phyto_chromo_attachment.
DR InterPro; IPR013516; Phyto_chromo_BS.
DR InterPro; IPR001294; Phytochrome.
DR InterPro; IPR013515; Phytochrome_cen-reg.
DR InterPro; IPR043150; Phytochrome_PHY_sf.
DR PANTHER; PTHR43719:SF4; PHYTOCHROME C; 1.
DR PANTHER; PTHR43719; TWO-COMPONENT HISTIDINE KINASE; 1.
DR Pfam; PF01590; GAF; 1.
DR Pfam; PF00360; PHY; 1.
DR PRINTS; PR01033; PHYTOCHROME.
DR SMART; SM00065; GAF; 1.
DR SUPFAM; SSF55781; GAF domain-like; 2.
DR PROSITE; PS00245; PHYTOCHROME_1; 1.
DR PROSITE; PS50046; PHYTOCHROME_2; 1.
PE 3: Inferred from homology;
KW Chromophore {ECO:0000256|ARBA:ARBA00022991};
KW Photoreceptor protein {ECO:0000256|ARBA:ARBA00022543};
KW Receptor {ECO:0000256|ARBA:ARBA00023170};
KW Sensory transduction {ECO:0000256|ARBA:ARBA00022606}.
FT DOMAIN 45..218
FT /note="Phytochrome chromophore attachment site"
FT /evidence="ECO:0000259|PROSITE:PS50046"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:ADI49652.1"
FT NON_TER 394
FT /evidence="ECO:0000313|EMBL:ADI49652.1"
SQ SEQUENCE 394 AA; 43952 MW; 70F4DBB598239974 CRC64;
INEGLVIDLE PVNPADVPVT AAGALKSYKL AAKAISRLQS LPSGNISLMC DVLVREVSEL
TGYDRVMVYK FHEDEHGEVI AECRLSDLEP YLGLHYPATD IPQASRFLFM KNKVRMICDC
SAQPVKVIQD HRLAQPMSLC GSTLRAPHGC HAQYMANMGS IASLVLSITI SDDDDDDNMQ
DSDRQPKGRK LWGLVVCHHT SPRFVPFPLR YACEFLLQVF GIQLNKEVEL AAQTKEKHML
QMQTVLCDMI LRDSPISIFT HSPNVMDLVK CEGATLYYRK QFWLLGTTPT EAQIKDIIAW
LQEYHNGSTG LSTDSLIEAG YPGADVLGDA VCGMAAIKIT SSDFIIWFRP HTAKEIKWGG
AKDEPAEKEN EFGKMHPRAS FKAFLEVVKH RSLP
//