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Database: UniProt
Entry: A0A0Q3JM94_BRADI
LinkDB: A0A0Q3JM94_BRADI
Original site: A0A0Q3JM94_BRADI 
ID   A0A0Q3JM94_BRADI        Unreviewed;       962 AA.
AC   A0A0Q3JM94;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 42.
DE   RecName: Full=Phytochrome {ECO:0008006|Google:ProtNLM};
GN   Name=100834357 {ECO:0000313|EnsemblPlants:KQK13172};
GN   ORFNames=BRADI_1g08400v3 {ECO:0000313|EMBL:KQK13172.1};
OS   Brachypodium distachyon (Purple false brome) (Trachynia distachya).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Pooideae; Stipodae; Brachypodieae; Brachypodium.
OX   NCBI_TaxID=15368 {ECO:0000313|EMBL:KQK13172.1};
RN   [1] {ECO:0000313|EMBL:KQK13172.1, ECO:0000313|EnsemblPlants:KQK13172}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bd21 {ECO:0000313|EMBL:KQK13172.1,
RC   ECO:0000313|EnsemblPlants:KQK13172};
RX   PubMed=20148030; DOI=10.1038/nature08747;
RG   International Brachypodium Initiative;
RT   "Genome sequencing and analysis of the model grass Brachypodium
RT   distachyon.";
RL   Nature 463:763-768(2010).
RN   [2] {ECO:0000313|EMBL:KQK13172.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Bd21 {ECO:0000313|EMBL:KQK13172.1};
RG   The International Brachypodium Initiative;
RA   Lucas S., Harmon-Smith M., Lail K., Tice H., Grimwood J., Bruce D.,
RA   Barry K., Shu S., Lindquist E., Wang M., Pitluck S., Vogel J.P.,
RA   Garvin D.F., Mockler T.C., Schmutz J., Rokhsar D., Bevan M.W.;
RT   "WGS assembly of Brachypodium distachyon.";
RL   Submitted (JUN-2017) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EnsemblPlants:KQK13172}
RP   IDENTIFICATION.
RC   STRAIN=cv. Bd21 {ECO:0000313|EnsemblPlants:KQK13172};
RG   EnsemblPlants;
RL   Submitted (AUG-2018) 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   -!- SIMILARITY: Belongs to the phytochrome family.
CC       {ECO:0000256|ARBA:ARBA00008235}.
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DR   EMBL; CM000880; KQK13172.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0Q3JM94; -.
DR   EnsemblPlants; KQK13172; KQK13172; BRADI_1g08400v3.
DR   Gramene; KQK13172; KQK13172; BRADI_1g08400v3.
DR   Proteomes; UP000008810; Chromosome 1.
DR   ExpressionAtlas; A0A0Q3JM94; baseline.
DR   GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
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   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; 3.30.450.20; PAS domain; 3.
DR   InterPro; IPR003018; GAF.
DR   InterPro; IPR029016; GAF-like_dom_sf.
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; IPR013516; Phyto_chromo_BS.
DR   InterPro; IPR001294; Phytochrome.
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; PF00512; HisKA; 1.
DR   Pfam; PF00989; PAS; 2.
DR   Pfam; PF08446; PAS_2; 1.
DR   Pfam; PF00360; PHY; 1.
DR   PRINTS; PR01033; PHYTOCHROME.
DR   SMART; SM00065; GAF; 1.
DR   SMART; SM00388; HisKA; 1.
DR   SMART; SM00091; PAS; 2.
DR   SUPFAM; SSF55781; GAF domain-like; 2.
DR   SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 3.
DR   PROSITE; PS50112; PAS; 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   Reference proteome {ECO:0000313|Proteomes:UP000008810};
KW   Sensory transduction {ECO:0000256|ARBA:ARBA00022606};
KW   Transcription {ECO:0000256|ARBA:ARBA00023163};
KW   Transcription regulation {ECO:0000256|ARBA:ARBA00023015}.
FT   DOMAIN          218..391
FT                   /note="Phytochrome chromophore attachment site"
FT                   /evidence="ECO:0000259|PROSITE:PS50046"
FT   DOMAIN          621..691
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   DOMAIN          763..806
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   REGION          1..28
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..17
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   962 AA;  106180 MW;  74DEAE5E89E4CCD3 CRC64;
     MSSSRSNNRA TCSRGSSARS KHSERVVAQT PVDARLHAEF EGSQRRFDYS SSVSAANRSG
     ASTSTAVSAY LQNMQRGRYI QPFGCLLAAH PETFALLAYS ENAAEMLDLT PHAVPTIDQR
     DALTVGVDVR TLFRSQSAVA LHKAAVFGEV NLLNPILVHA RTSGKPFYAI LHRIDVGLVI
     DLEPVNPADV PVTAAGALKS YKLAAKAISR LQSLPSGNLS LLCDVLVREV SELTGYDRVM
     AYKFHEDEHG EVIAECRRSD LEPYLGLHYP ATDIPQASRF LFMKNKVRMI CDCAAVPVKL
     IQDDNLSQPI SLCGSTMRAP HGCHAQYMAN MGSVASLVMS ITINEDEEED GDTGSDQQPK
     GRKLWGLVVC HHSSPRFVPF PLRYACEFLL QVFGIQLNKE VELASQAKER HILRTQTLLC
     DMLLRDAPIG IFTQSPNVMD LVKCDGAALC YRNQIMVLGS TPSEGEIKNI VAWLQEYHDG
     STGLSTDSLV EAGYPGASAL GEIVCGMAAI KISSKGFILW FRSHTAKEIK WGGAKHEPGD
     ADDNGRKMHP RSSFRAFLEV VKWRSVPWED VEMDAIHSLQ LILRGSLQDE DANNNNNVMS
     IVEAPSDDMK KIQGLLELRI VTNEMVRLIE TATAPILAVD IVGNINGWNN KAAEITGLPT
     TEAIGMPLVQ VVHGDSVEVV TQILNSALQG VEEQNLEIKL KTFHHLESNG PVILMVNACC
     SRDLSEKVVG VCFVAQDLTG QKMILDKYTR IQGDYVAIVK NPNELIPPIF MINDLGSCLE
     WNEAMQRITG IKREDAIDKL LIGEVFTLHD YGCRVKDHAT LTKLSILMNT VISGQDPEKL
     PFGFFDADGK CMESLLTANK RTDAEGKITG ALCFLHVASP ELQHALQVQK MSEQAATHSF
     KELTYIRQEL KNPLNGMQFT RNLLEPSELT EEQRQLLASN VLCQEQLKKI LHDNDLEGIE
     QW
//
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