ID K4A547_SETIT Unreviewed; 1101 AA.
AC K4A547;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 27-MAR-2024, entry version 66.
DE RecName: Full=Phytochrome {ECO:0008006|Google:ProtNLM};
OS Setaria italica (Foxtail millet) (Panicum italicum).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC Panicoideae; Panicodae; Paniceae; Cenchrinae; Setaria.
OX NCBI_TaxID=4555 {ECO:0000313|EnsemblPlants:KQK91177, ECO:0000313|Proteomes:UP000004995};
RN [1] {ECO:0000313|EnsemblPlants:KQK91177, ECO:0000313|Proteomes:UP000004995}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Yugu1 {ECO:0000313|EnsemblPlants:KQK91177,
RC ECO:0000313|Proteomes:UP000004995};
RX PubMed=22580951; DOI=10.1038/nbt.2196;
RA Bennetzen J.L., Schmutz J., Wang H., Percifield R., Hawkins J.,
RA Pontaroli A.C., Estep M., Feng L., Vaughn J.N., Grimwood J., Jenkins J.,
RA Barry K., Lindquist E., Hellsten U., Deshpande S., Wang X., Wu X.,
RA Mitros T., Triplett J., Yang X., Ye C.Y., Mauro-Herrera M., Wang L., Li P.,
RA Sharma M., Sharma R., Ronald P.C., Panaud O., Kellogg E.A., Brutnell T.P.,
RA Doust A.N., Tuskan G.A., Rokhsar D., Devos K.M.;
RT "Reference genome sequence of the model plant Setaria.";
RL Nat. Biotechnol. 30:555-561(2012).
RN [2] {ECO:0000313|EnsemblPlants:KQK91177}
RP IDENTIFICATION.
RC STRAIN=Yugu1 {ECO:0000313|EnsemblPlants:KQK91177};
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 -!- 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}.
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DR EMBL; AGNK02006015; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; K4A547; -.
DR EnsemblPlants; KQK91177; KQK91177; SETIT_033968mg.
DR Gramene; KQK91177; KQK91177; SETIT_033968mg.
DR Proteomes; UP000004995; Chromosome IX.
DR ExpressionAtlas; K4A547; 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: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; 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; 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; 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; 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; SM00388; HisKA; 1.
DR SMART; SM00091; PAS; 2.
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|PIRSR:PIRSR000084-
KW 50}; Photoreceptor protein {ECO:0000256|ARBA:ARBA00022543};
KW Receptor {ECO:0000256|ARBA:ARBA00023170};
KW Reference proteome {ECO:0000313|Proteomes:UP000004995};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Sensory transduction {ECO:0000256|ARBA:ARBA00022606};
KW Transcription {ECO:0000256|ARBA:ARBA00023163};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015}.
FT DOMAIN 262..434
FT /note="Phytochrome chromophore attachment site"
FT /evidence="ECO:0000259|PROSITE:PS50046"
FT DOMAIN 663..734
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 797..875
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 945..1101
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT REGION 1..56
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..15
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 367
FT /ligand="phytochromobilin"
FT /ligand_id="ChEBI:CHEBI:189064"
FT /note="covalent"
FT /evidence="ECO:0000256|PIRSR:PIRSR000084-50"
SQ SEQUENCE 1101 AA; 120475 MW; 8A839D78CAFD98EE CRC64;
MASGSRATPT RSPSSARPAA PRHAHHHHHS QSSGGSTTSQ TGGGGGGGGG GGGAATAATE
SVSKAVAQYN LDARLHAVFE QSGASGRSFD YSQSLRAPPT PSSEQQIAAY LSRIQRGGHI
QPFGCTLAVA DDSSFRLLAF SENAADLLDL SPHHSVPSLD SAAPPPVSLG ADARLLFSPS
SAVLMEGAFA AREISLLNPL WIHSRVSAKP FYAILHRIDI GVVIDLEPAR TEDPALSIAG
AVQSQKLAVR AISRLQALPG GDVKLLCDTV VEHVRELTGY DRVMVYRFHE DEHGEVVAEC
RRDNLEPYLG LHYPATDIPQ ASRFLFRQNR VRMIADCHAT PVRVIQDPGL SQPLCLVGST
LRAPHGCHAQ YMANMGSIAS LVMAVIISSG GDDEQTTRGG ISSAMKLWGL VVCHHTSPRF
IPFPLRYACE FLMQAFGLQL NMELQLAHQL SEKHILRTQT LLCDMLLRDS PTGIVTQSPS
IMDLVKCDGA ALYYHGKYYP LGVTPTESQI KDIIEWLTVC HGDSTGLSTD SLADAGYHGA
AALGDAVCGM AVAYITPSDY LFWFRSHTAK EIKWGGAKHH PEDKDDGQRM HPRSSFKAFL
EVVKSRSLPW ENAEMDAIHS LQLILRDSFR DVAEGTSNSK AIINGQVQLG ELELRGINEL
SSVAREMVRL IETATVPIFA VDTDGCINGW NAKIAELTGL SVEEAMGKSL VNDLIFKESE
EIVEKLLSRA LRGEEDKNVE IKLKTFGPEQ SKGPIFVIVN ACSSRDYTKN IVGVCFVGQD
VTGQKVVMDK FVNIQGDYKA IVHNPNPLIP PIFASDENTC CSEWNTAMEK LTGWSRSEVV
GKLLIGEVFG NICRLKGPDA LTKFMVVLHN AIGGDDYEKF PFSFFDKNGK YVQALLTANT
RSKTDSKSIG AFCFLQIASA ELQQAFEIQR QQEKKCYARM KELAYICQEI KNPLSGIRFT
NSLLQMTDLN DDQRQFLETS SACEKQMSKI VKDASLQSIE DGSLVLEKGE FSLGSVMNAV
VSQAMILLRE RDIQLIRDIP DEIKDASAYG DQYRIQQVLS EFLLSMVQFA PAENGWVEIQ
VRPNVKQNSD GTNTALFMFR Y
//
