ID A0A453H8S4_AEGTS Unreviewed; 1130 AA.
AC A0A453H8S4;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=Phytochrome {ECO:0000256|PIRNR:PIRNR000084};
OS Aegilops tauschii subsp. strangulata (Goatgrass).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Pooideae; Triticodae; Triticeae; Triticinae; Aegilops.
OX NCBI_TaxID=200361 {ECO:0000313|EnsemblPlants:AET4Gv20107700.2, ECO:0000313|Proteomes:UP000015105};
RN [1] {ECO:0000313|Proteomes:UP000015105}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. AL8/78 {ECO:0000313|Proteomes:UP000015105};
RX PubMed=25035499; DOI=10.1126/science.1250092;
RG International Wheat Genome Sequencing Consortium,;
RA Marcussen T., Sandve S.R., Heier L., Spannagl M., Pfeifer M.,
RA Jakobsen K.S., Wulff B.B., Steuernagel B., Mayer K.F., Olsen O.A.;
RT "Ancient hybridizations among the ancestral genomes of bread wheat.";
RL Science 345:1250092-1250092(2014).
RN [2] {ECO:0000313|Proteomes:UP000015105}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. AL8/78 {ECO:0000313|Proteomes:UP000015105};
RX PubMed=29158546; DOI=10.1038/s41477-017-0067-8;
RA Zhao G., Zou C., Li K., Wang K., Li T., Gao L., Zhang X., Wang H., Yang Z.,
RA Liu X., Jiang W., Mao L., Kong X., Jiao Y., Jia J.;
RT "The Aegilops tauschii genome reveals multiple impacts of transposons.";
RL Nat. Plants 3:946-955(2017).
RN [3] {ECO:0000313|EnsemblPlants:AET4Gv20107700.2}
RP IDENTIFICATION.
RG EnsemblPlants;
RL Submitted (MAR-2019) to UniProtKB.
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 -!- PTM: Contains one covalently linked phytochromobilin chromophore.
CC {ECO:0000256|PIRSR:PIRSR000084-50}.
CC -!- SIMILARITY: Belongs to the phytochrome family.
CC {ECO:0000256|ARBA:ARBA00008235, ECO:0000256|PIRNR:PIRNR000084}.
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DR AlphaFoldDB; A0A453H8S4; -.
DR STRING; 200361.A0A453H8S4; -.
DR EnsemblPlants; AET4Gv20107700.1; AET4Gv20107700.1; AET4Gv20107700.
DR EnsemblPlants; AET4Gv20107700.2; AET4Gv20107700.2; AET4Gv20107700.
DR EnsemblPlants; AET4Gv20107700.4; AET4Gv20107700.4; AET4Gv20107700.
DR Gramene; AET4Gv20107700.1; AET4Gv20107700.1; AET4Gv20107700.
DR Gramene; AET4Gv20107700.2; AET4Gv20107700.2; AET4Gv20107700.
DR Gramene; AET4Gv20107700.4; AET4Gv20107700.4; AET4Gv20107700.
DR OMA; YLHHIQR; -.
DR OrthoDB; 1770905at2759; -.
DR Proteomes; UP000015105; Chromosome 4D.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR GO; GO:0009881; F:photoreceptor activity; IEA:UniProtKB-KW.
DR GO; GO:0042803; F:protein homodimerization activity; IEA:InterPro.
DR GO; GO:0009584; P:detection of visible light; IEA:InterPro.
DR GO; GO:0009585; P:red, far-red light phototransduction; IEA:InterPro.
DR GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd00130; PAS; 2.
DR Gene3D; 3.30.450.270; -; 1.
DR Gene3D; 3.30.450.40; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 3.30.450.20; PAS domain; 3.
DR InterPro; IPR003018; GAF.
DR InterPro; IPR029016; GAF-like_dom_sf.
DR InterPro; IPR003594; HATPase_C.
DR InterPro; IPR036890; HATPase_C_sf.
DR InterPro; IPR005467; His_kinase_dom.
DR InterPro; IPR003661; HisK_dim/P.
DR InterPro; IPR000014; PAS.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR013654; PAS_2.
DR InterPro; IPR013767; PAS_fold.
DR InterPro; IPR016132; Phyto_chromo_attachment.
DR InterPro; IPR001294; Phytochrome.
DR InterPro; IPR012129; Phytochrome_A-E.
DR InterPro; IPR013515; Phytochrome_cen-reg.
DR InterPro; IPR043150; Phytochrome_PHY_sf.
DR NCBIfam; TIGR00229; sensory_box; 1.
DR PANTHER; PTHR47876; OS08G0260000 PROTEIN; 1.
DR PANTHER; PTHR47876:SF3; PHYTOCHROME 1; 1.
DR Pfam; PF01590; GAF; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF00989; PAS; 2.
DR Pfam; PF08446; PAS_2; 1.
DR Pfam; PF00360; PHY; 1.
DR PIRSF; PIRSF000084; Phytochrome; 1.
DR PRINTS; PR01033; PHYTOCHROME.
DR SMART; SM00065; GAF; 1.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00091; PAS; 2.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF55781; GAF domain-like; 2.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 3.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50112; PAS; 2.
DR PROSITE; PS50046; PHYTOCHROME_2; 1.
PE 3: Inferred from homology;
KW Chromophore {ECO:0000256|ARBA:ARBA00022991, ECO:0000256|PIRNR:PIRNR000084};
KW Photoreceptor protein {ECO:0000256|ARBA:ARBA00022543,
KW ECO:0000256|PIRNR:PIRNR000084};
KW Receptor {ECO:0000256|ARBA:ARBA00023170, ECO:0000256|PIRNR:PIRNR000084};
KW Reference proteome {ECO:0000313|Proteomes:UP000015105};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Sensory transduction {ECO:0000256|ARBA:ARBA00022606,
KW ECO:0000256|PIRNR:PIRNR000084};
KW Transcription {ECO:0000256|ARBA:ARBA00023163,
KW ECO:0000256|PIRNR:PIRNR000084};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015,
KW ECO:0000256|PIRNR:PIRNR000084}.
FT DOMAIN 218..393
FT /note="Phytochrome chromophore attachment site"
FT /evidence="ECO:0000259|PROSITE:PS50046"
FT DOMAIN 619..689
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 749..829
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 903..1123
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT REGION 1..30
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 323
FT /ligand="phytochromobilin"
FT /ligand_id="ChEBI:CHEBI:189064"
FT /note="covalent"
FT /evidence="ECO:0000256|PIRSR:PIRSR000084-50"
SQ SEQUENCE 1130 AA; 124969 MW; 49DCE2F5A38E6A60 CRC64;
MSSSMPASSS SSRNRQSTQE RVLAQTTLDA QLNAEFEESS DSFDYSKLVE AQRDTPTVLQ
EGRSEKVIAY LQHIQRGKMI QSFGCLLALD EKSFNVIAFS ENAPEMLTTV SHAVPSVDDP
PRLDIGTNVR SLFTDQGATA LHKALGFADV SLLNPILVQC KSSGKPFYAI VHRATGCLVV
DFEPVNPTEF PATAAGALQS YKLAAKAISK IQALPGGSME LLCNTVVKEV FELTGYDRVM
AYKFHEDNHG EVFAEITKPG LEPYLGLHYP ATDIPQAARF LFMKNKVRMI CDVRARSIKV
IEDEALPFDI SLCGSALRAA HSCHLQYMEN MNSIASLVMA VVVNENEEDD EVGSEQPAQQ
QKKKILWGLV VCHHESPRYV PFPLRYACEF LAQVFAVHVN KEFEVQKQLR EKSILRMQTI
LSDMLFKEAS PLTIVSGAPN IMDLIKCDGA ALLYGGKVWR LGNAPTESQI RDLALWLSEV
HMDSTGLSTE SLHDAGYPGA SALGDMVCGM AVAKINSNDI LFWFRSHTAK EIRWGGAKND
PSDQDDSRRM HPRLSFKAFL EVVKMKSLAW TDSEMDAIHS LQLILRGTVD GVVKPTGKAS
LDEQIGDLKL DGLAELQAVT SEMVRLMETA TVPILAVDGN GLVNGWNQKA AELTGLRVDD
AIGRHILTLV EESSVSVVQR MLYLALQGKE EKEVRFEVKT HGPKRDDGPV ILVVNACASR
DLHDDVVGVC FVAQDMTVHK LVMDKFTRVE GDYKAIIHNP NPLIPPIFGA DEFGWCCEWN
AAMTKLTGWH KEEVLDKMLL GEVFDSRNAS CLLKNKDAFV SLCAVINSGL AGKETEKAPF
GFFNRSGKYT ECLLSVNRRQ NEDGLITGVF CFIHIPSHEL QQALQVQQAS EQASLKRLKA
FSYMRHAINN PLSGMLYSRK ALKNTDLNEE QMRQIHVSDN CHHQLNKILA DLDQDSIMEK
SSCLDLEMAE FALQDVVVAA VSQVLIACEG KGIRVSCNLP ERFMKKLIYG DGVRLQQILS
DFLSISVKFS PVGGSIEISA KATKNSIGEN LHLIDLDLRI KHHGLGVPAE LMAQMFEEDD
TQQSEEGLGL LVSRNLLRLM NGDVRHLREA GMSIFILTAE LACGPTAMEH
//
