ID A0A2G5DWG6_AQUCA Unreviewed; 1132 AA.
AC A0A2G5DWG6;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 24-JAN-2024, entry version 29.
DE RecName: Full=Phytochrome {ECO:0000256|PIRNR:PIRNR000084};
GN ORFNames=AQUCO_01400435v1 {ECO:0000313|EMBL:PIA47841.1};
OS Aquilegia coerulea (Rocky mountain columbine).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Ranunculales; Ranunculaceae; Thalictroideae;
OC Aquilegia.
OX NCBI_TaxID=218851 {ECO:0000313|EMBL:PIA47841.1, ECO:0000313|Proteomes:UP000230069};
RN [1] {ECO:0000313|EMBL:PIA47841.1, ECO:0000313|Proteomes:UP000230069}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Goldsmith {ECO:0000313|Proteomes:UP000230069};
RA Hodges S., Kramer E., Nordborg M., Tomkins J., Borevitz J., Derieg N.,
RA Yan J., Mihaltcheva S., Hayes R.D., Rokhsar D.;
RT "WGS assembly of Aquilegia coerulea Goldsmith.";
RL Submitted (SEP-2017) 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; KZ305031; PIA47841.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2G5DWG6; -.
DR STRING; 218851.A0A2G5DWG6; -.
DR InParanoid; A0A2G5DWG6; -.
DR OrthoDB; 1770905at2759; -.
DR Proteomes; UP000230069; Unassembled WGS sequence.
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 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:UP000230069};
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; 125816 MW; 0794BAEC3B327462 CRC64;
MSSGSNIRPE INKNNNTITT TTTTTTTNQT ESVNKAIAQF TVDARLHAVF EQSGESGKPF
DYSQSIRSTT SQSIPEQQIT AYLSRIQRGG HIQPFGCMIS VDESSFRVIA FSENATEMLD
LTPQSVPTLD KPQLLDVGTD VRTLFTQSSV GLLEKAFSAR EITLLNPVWI HSKNSGKPFY
AILHRIDVGI VIDLEPARTE DPALSIAGAV QSQKIAVRAI SRLQSLPGGD IKILCDTVVE
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 VCGMAVAYIT SRDFLFWFRS NTAKEIKWGG
AKHHPEDKDD GHRMHPRSSF KAFLEVVKSR SLPWENAEMD AIHSLQLILR DSFGDAEGSN
SKPLITSPPG DLELQGVDEL SSVAREMVRL IETATAPIFA VDSDGRINGW NAKIAELTGL
SVGEAMGKSL VHELVFKESV EVVDNLLKHA LRGQEDKNVE IKLRKFIPRK PEEAIFVVVN
ACSSRDYTNN IVGVCFVGQD VTSQKVVMDK FIHIQGDYKA IVHNPNPLIP PIFASDENTC
CSEWNTAMEK LTGWDRGEIM GKMLVGEVFG GCCRLKGPDS LTKFMIVLHS AIGGQDTDKF
PFAFFNRDGK YVQALLTANK RANLEGQIIG AFCFLQIASP ELQQALEIQR 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
//
