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Database: UniProt
Entry: C9E8M9_AQUFO
LinkDB: C9E8M9_AQUFO
Original site: C9E8M9_AQUFO 
ID   C9E8M9_AQUFO            Unreviewed;      1132 AA.
AC   C9E8M9;
DT   03-NOV-2009, integrated into UniProtKB/TrEMBL.
DT   03-NOV-2009, sequence version 1.
DT   27-MAR-2024, entry version 81.
DE   RecName: Full=Phytochrome {ECO:0000256|PIRNR:PIRNR000084};
OS   Aquilegia formosa (Western columbine).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Ranunculales; Ranunculaceae; Thalictroideae;
OC   Aquilegia.
OX   NCBI_TaxID=223430 {ECO:0000313|EMBL:ACV87354.1};
RN   [1] {ECO:0000313|EMBL:ACV87354.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Gould B., Kramer E.M.;
RT   "Flowering time gene homologs of Aquilegia.";
RL   Submitted (AUG-2009) to the EMBL/GenBank/DDBJ databases.
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   -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}.
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   EMBL; GQ471031; ACV87354.1; -; mRNA.
DR   AlphaFoldDB; C9E8M9; -.
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; cd16932; HATPase_Phy-like; 1.
DR   CDD; cd00082; HisKA; 1.
DR   CDD; cd00130; PAS; 2.
DR   Gene3D; 1.10.287.130; -; 1.
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; IPR036097; HisK_dim/P_sf.
DR   InterPro; IPR000014; PAS.
DR   InterPro; IPR035965; PAS-like_dom_sf.
DR   InterPro; IPR013654; PAS_2.
DR   InterPro; IPR013767; PAS_fold.
DR   InterPro; IPR044767; Phy_HATPase-like.
DR   InterPro; IPR016132; Phyto_chromo_attachment.
DR   InterPro; IPR013516; Phyto_chromo_BS.
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; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR   SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 3.
DR   PROSITE; PS50109; HIS_KIN; 1.
DR   PROSITE; PS50112; PAS; 2.
DR   PROSITE; PS00245; PHYTOCHROME_1; 1.
DR   PROSITE; PS50046; PHYTOCHROME_2; 1.
PE   2: Evidence at transcript level;
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   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          230..398
FT                   /note="Phytochrome chromophore attachment site"
FT                   /evidence="ECO:0000259|PROSITE:PS50046"
FT   DOMAIN          623..694
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   DOMAIN          757..809
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   DOMAIN          905..1125
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         335
FT                   /ligand="phytochromobilin"
FT                   /ligand_id="ChEBI:CHEBI:189064"
FT                   /note="covalent"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000084-50"
SQ   SEQUENCE   1132 AA;  126008 MW;  77E8A0CB1D21C9EB CRC64;
     MSSGSNIRPE INKNNNTITT TTTTTTTNQT ESVNKAIAQF TVDARLHAVF EQSGESGKPF
     DYSQSIRSTT SQSIPEQQIT AYLSRIQRGG HIQPFGCMIS VDESSFRVIA FSENATEMLD
     LTPQSVPTLD KPQLLDVGTD VRTLFTQSSV GLLEKAFSAR EITLLNPVWI HSKNSGKPFY
     AILHKIDVGI VIDLEPARTE DPALSIAGAV QSQKIAVRAI SRLQSLPGGD INILCDTVVE
     NVRDLTGYDR VMVYKFHDDE HGEVVAESKR SDLEPFIGLH YPATDIPQAS RFLFKQNRVR
     MIVDCHATPV HVIQDEALMQ PLCLVGSTLR APHGCHAQYM ANMGSIASLA LAVVINGNDE
     EGTSGRNPMK LWGLVVCHHT SARCIPFPLR HACEFLMQAF GLQLNMELQL ASQLSEKHVL
     RTQTLLCDML LRDSPTGIVT QSPSIMDLVK CDGSALYYKG KFYPIGVTPT EAQMKDIVDW
     LWAYHGDSTG VSTDSLADAG YPGAASLGDA VRGMAVAYIT SRDFLFWFRS NTAKEIKWGG
     AKHHPEDKDD GHRMHPRSSF KAFLEVVKSR SLPWENAEMD AIHSLQLILR DSFRDAEGSN
     SKPLITSPPG DLELQGVDEL SSVAREMVRL IETATAPIFA VDSDGRINGW NAKIAELTGL
     SVGEAMGKSL VHDLVFKESV EVVDNLLKHA FRGQEDKNVE IKLRKFIPRK PEEAIFVVVN
     ARSSRDYTNN IVGVCFVGQD VTSQKVVMDK FIHIQGDYKA IVHNPNPLIP PIFASDENTC
     CSEWNTAMEK LTGWDRGEIM GKMLVGEVFG GCCRLKGPDS LTKFMIVLHS AIGGQDTDKF
     PFAFFNRDGK YVQALLTANK RANLEGQIIG AFCFLQIASP ELQHALEIQR QQEKKCFARV
     KELAYICQEI KNPLSGIRFT NTLLEATDLT EDQKQFLETS AACERQMMKI IKDVDLQNIE
     DGSLELERCD FLLGSVINAV VSQVMILLRE RGLQLIRDIP EEIKTLAVSS DQVRIQQVLA
     DFLLNMVRYA PMPDGWVEIQ VRPNLKQSSD GIELVHLEFR MVCPGEGLPP ELVQDMFHSS
     RWATQEGLGL SMCRKILKLM NGEVQYIRES ERCFFIIILE LPTPQRSLIL SN
//
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