ID   PHYB_ARATH              Reviewed;        1172 AA.
AC   P14713; Q6S4P0;
DT   01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1990, sequence version 1.
DT   24-JAN-2024, entry version 210.
DE   RecName: Full=Phytochrome B {ECO:0000303|PubMed:2606345};
DE   AltName: Full=Protein LONG HYPOCOTYL 3 {ECO:0000303|PubMed:8453299};
DE   AltName: Full=Protein OUT OF PHASE 1 {ECO:0000303|PubMed:12177480};
GN   Name=PHYB {ECO:0000303|PubMed:2606345};
GN   Synonyms=HY3 {ECO:0000303|PubMed:8453299}, OOP1
GN   {ECO:0000303|PubMed:12177480};
GN   OrderedLocusNames=At2g18790 {ECO:0000312|Araport:AT2G18790};
GN   ORFNames=MSF3.17 {ECO:0000312|EMBL:AAD08948.1};
OS   Arabidopsis thaliana (Mouse-ear cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX   NCBI_TaxID=3702;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=2606345; DOI=10.1101/gad.3.11.1745;
RA   Sharrock R.A., Quail P.H.;
RT   "Novel phytochrome sequences in Arabidopsis thaliana: structure, evolution,
RT   and differential expression of a plant regulatory photoreceptor family.";
RL   Genes Dev. 3:1745-1757(1989).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=cv. Landsberg erecta;
RX   PubMed=8453299; DOI=10.1105/tpc.5.2.147;
RA   Reed J.W., Nagpal P., Poole D.S., Furuya M., Chory J.;
RT   "Mutations in the gene for the red/far-red light receptor phytochrome B
RT   alter cell elongation and physiological responses throughout Arabidopsis
RT   development.";
RL   Plant Cell 5:147-157(1993).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS 9-GLY--ARG-12 DEL; GLU-19;
RP   ILE-143; VAL-980 AND LEU-1072.
RC   STRAIN=cv. Kas-1;
RX   PubMed=15238539; DOI=10.1534/genetics.103.024810;
RA   Wolyn D.J., Borevitz J.O., Loudet O., Schwartz C., Maloof J., Ecker J.R.,
RA   Berry C.C., Chory J.;
RT   "Light-response quantitative trait loci identified with composite interval
RT   and eXtreme array mapping in Arabidopsis thaliana.";
RL   Genetics 167:907-917(2004).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=10617197; DOI=10.1038/45471;
RA   Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA   Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA   Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA   Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA   Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA   Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA   Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT   "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL   Nature 402:761-768(1999).
RN   [5]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Columbia;
RX   PubMed=27862469; DOI=10.1111/tpj.13415;
RA   Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA   Town C.D.;
RT   "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT   genome.";
RL   Plant J. 89:789-804(2017).
RN   [6]
RP   INTERACTION WITH ADO1.
RX   PubMed=11260718; DOI=10.1038/35068589;
RA   Jarillo J.A., Capel J., Tang R.-H., Yang H.-Q., Alonso J.M., Ecker J.R.,
RA   Cashmore A.R.;
RT   "An Arabidopsis circadian clock component interacts with both CRY1 and
RT   phyB.";
RL   Nature 410:487-490(2001).
RN   [7]
RP   FUNCTION, AND INTERACTION WITH FYPP3.
RX   PubMed=12468726; DOI=10.1105/tpc.005306;
RA   Kim D.-H., Kang J.-G., Yang S.-S., Chung K.-S., Song P.-S., Park C.-M.;
RT   "A phytochrome-associated protein phosphatase 2A modulates light signals in
RT   flowering time control in Arabidopsis.";
RL   Plant Cell 14:3043-3056(2002).
RN   [8]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RC   STRAIN=cv. Columbia;
RX   PubMed=12177480; DOI=10.1104/pp.003418;
RA   Salome P.A., Michael T.P., Kearns E.V., Fett-Neto A.G., Sharrock R.A.,
RA   McClung C.R.;
RT   "The out of phase 1 mutant defines a role for PHYB in circadian phase
RT   control in Arabidopsis.";
RL   Plant Physiol. 129:1674-1685(2002).
RN   [9]
RP   FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH PAPP5.
RX   PubMed=15707897; DOI=10.1016/j.cell.2004.12.019;
RA   Ryu J.S., Kim J.-I., Kunkel T., Kim B.C., Cho D.S., Hong S.H., Kim S.-H.,
RA   Fernandez A.P., Kim Y., Alonso J.M., Ecker J.R., Nagy F., Lim P.O.,
RA   Song P.-S., Schaefer E., Nam H.G.;
RT   "Phytochrome-specific type 5 phosphatase controls light signal flux by
RT   enhancing phytochrome stability and affinity for a signal transducer.";
RL   Cell 120:395-406(2005).
RN   [10]
RP   INTERACTION WITH PKS4.
RX   PubMed=18390804; DOI=10.1104/pp.108.118166;
RA   Schepens I., Boccalandro H.E., Kami C., Casal J.J., Fankhauser C.;
RT   "PHYTOCHROME KINASE SUBSTRATE4 modulates phytochrome-mediated control of
RT   hypocotyl growth orientation.";
RL   Plant Physiol. 147:661-671(2008).
RN   [11]
RP   INTERACTION WITH PTAC12/HMR/PAP5, AND MUTAGENESIS OF TYR-276.
RC   STRAIN=cv. Columbia;
RX   PubMed=22895253; DOI=10.1101/gad.193219.112;
RA   Galvao R.M., Li M., Kothadia S.M., Haskel J.D., Decker P.V.,
RA   Van Buskirk E.K., Chen M.;
RT   "Photoactivated phytochromes interact with HEMERA and promote its
RT   accumulation to establish photomorphogenesis in Arabidopsis.";
RL   Genes Dev. 26:1851-1863(2012).
RN   [12]
RP   INTERACTION WITH CRYA.
RX   PubMed=22577138; DOI=10.1074/jbc.m112.360545;
RA   Hughes R.M., Vrana J.D., Song J., Tucker C.L.;
RT   "Light-dependent, dark-promoted interaction between Arabidopsis
RT   cryptochrome 1 and phytochrome B proteins.";
RL   J. Biol. Chem. 287:22165-22172(2012).
RN   [13]
RP   INTERACTION WITH VOZ1 AND VOZ2.
RX   PubMed=22904146; DOI=10.1105/tpc.112.101915;
RA   Yasui Y., Mukougawa K., Uemoto M., Yokofuji A., Suzuri R., Nishitani A.,
RA   Kohchi T.;
RT   "The phytochrome-interacting VASCULAR PLANT ONE-ZINC FINGER1 and VOZ2
RT   redundantly regulate flowering in Arabidopsis.";
RL   Plant Cell 24:3248-3263(2012).
RN   [14]
RP   TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND REVIEW.
RX   PubMed=23708772; DOI=10.1007/s10059-013-0135-5;
RA   Jeong J., Choi G.;
RT   "Phytochrome-interacting factors have both shared and distinct biological
RT   roles.";
RL   Mol. Cells 35:371-380(2013).
RN   [15]
RP   INTERACTION WITH PHL, AND SUBCELLULAR LOCATION.
RX   PubMed=24127609; DOI=10.1073/pnas.1310631110;
RA   Endo M., Tanigawa Y., Murakami T., Araki T., Nagatani A.;
RT   "PHYTOCHROME-DEPENDENT LATE-FLOWERING accelerates flowering through
RT   physical interactions with phytochrome B and CONSTANS.";
RL   Proc. Natl. Acad. Sci. U.S.A. 110:18017-18022(2013).
RN   [16]
RP   INTERACTION WITH PIF4 AND PIF5.
RX   PubMed=26724867; DOI=10.1016/j.cell.2015.12.018;
RA   Pedmale U.V., Huang S.S., Zander M., Cole B.J., Hetzel J., Ljung K.,
RA   Reis P.A., Sridevi P., Nito K., Nery J.R., Ecker J.R., Chory J.;
RT   "Cryptochromes interact directly with PIFs to control plant growth in
RT   limiting blue light.";
RL   Cell 164:233-245(2016).
RN   [17]
RP   FUNCTION, MUTAGENESIS OF TYR-276, AND INDUCTION BY TEMPERATURE.
RC   STRAIN=cv. Columbia;
RX   PubMed=27789797; DOI=10.1126/science.aaf6005;
RA   Jung J.-H., Domijan M., Klose C., Biswas S., Ezer D., Gao M., Khattak A.K.,
RA   Box M.S., Charoensawan V., Cortijo S., Kumar M., Grant A., Locke J.C.W.,
RA   Schaefer E., Jaeger K.E., Wigge P.A.;
RT   "Phytochromes function as thermosensors in Arabidopsis.";
RL   Science 354:886-889(2016).
RN   [18]
RP   COMPLEX WITH PHYTOCHROMOBILIN.
RX   PubMed=28376244; DOI=10.1002/1873-3468.12642;
RA   Velazquez Escobar F., Buhrke D., Fernandez Lopez M., Shenkutie S.M.,
RA   von Horsten S., Essen L.O., Hughes J., Hildebrandt P.;
RT   "Structural communication between the chromophore-binding pocket and the N-
RT   terminal extension in plant phytochrome phyB.";
RL   FEBS Lett. 591:1258-1265(2017).
RN   [19]
RP   X-RAY CRYSTALLOGRAPHY (3.40 ANGSTROMS) OF 90-624 IN COMPLEX WITH
RP   PHYTOCHROMOBILIN, AND HOMODIMERIZATION.
RX   PubMed=24982198; DOI=10.1073/pnas.1403096111;
RA   Burgie E.S., Bussell A.N., Walker J.M., Dubiel K., Vierstra R.D.;
RT   "Crystal structure of the photosensing module from a red/far-red light-
RT   absorbing plant phytochrome.";
RL   Proc. Natl. Acad. Sci. U.S.A. 111:10179-10184(2014).
RN   [20]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RC   STRAIN=cv. Columbia;
RX   PubMed=30635559; DOI=10.1038/s41467-018-08059-z;
RA   Qiu Y., Li M., Kim R.J.-A., Moore C.M., Chen M.;
RT   "Daytime temperature is sensed by phytochrome B in Arabidopsis through a
RT   transcriptional activator HEMERA.";
RL   Nat. Commun. 10:140-140(2019).
RN   [21]
RP   FUNCTION, AND INTERACTION WITH UNE10/PIF8.
RC   STRAIN=cv. Columbia;
RX   PubMed=31732705; DOI=10.1105/tpc.19.00515;
RA   Oh J., Park E., Song K., Bae G., Choi G.;
RT   "PHYTOCHROME INTERACTING FACTOR8 inhibits phytochrome a-mediated far-red
RT   light responses in Arabidopsis.";
RL   Plant Cell 32:186-205(2020).
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 morphogenetic responses, whereas reconversion of
CC       Pfr 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. Involved in the flowering time regulation. Involved in light-
CC       regulated circadian phase control that triggers stomatal aperture,
CC       stomatal conductance, and CO(2) assimilation. Implicated in red light
CC       perception, and, to a lower extent, in blue light signaling
CC       (PubMed:12177480). Controls thermomorphogenesis in the daytime and
CC       regulates temperature responses by associating with the promoters of
CC       key target genes in a temperature-dependent manner and subsequently
CC       repressing their expression in a PIF4-dependent manner (temperature-
CC       responsive transcriptional regulator); this process requires
CC       PTAC12/HMR/PAP5 (transcriptional activator) (PubMed:27789797,
CC       PubMed:30635559). Thermal timer that integrates temperature information
CC       over the course of the night (PubMed:27789797). Detabilizes UNE10/PIF8
CC       in red light (PubMed:31732705). {ECO:0000269|PubMed:12177480,
CC       ECO:0000269|PubMed:12468726, ECO:0000269|PubMed:15707897,
CC       ECO:0000269|PubMed:27789797, ECO:0000269|PubMed:30635559,
CC       ECO:0000269|PubMed:31732705}.
CC   -!- SUBUNIT: Homodimer (PubMed:24982198). Interacts with ADO1 and PKS4.
CC       Stabilized by interactions with PAPP5 and FYPP3 which are enhanced in
CC       the phosphorylated Pfr form. Interacts with VOZ1 and VOZ2
CC       (PubMed:11260718, PubMed:12468726, PubMed:15707897, PubMed:18390804,
CC       PubMed:22904146). Binds, via its photosensory domain, to
CC       PTAC12/HMR/PAP5 when photoactivated; this interaction stimulates its
CC       localization to photobodies (PubMed:22895253). Interacts with CRY1
CC       specifically when in the dark/far-red (Pr) state, but not when red
CC       light-activated (Pfr) (PubMed:22577138). Interacts with PIF4 and PIF5
CC       in response to low blue light (LBL) (PubMed:26724867). Component of a
CC       red light-dependent nuclear complex made of PHL, PHYB and CO. Interacts
CC       directly with PHL (PubMed:24127609). Binds to UNE10/PIF8 when red
CC       light-activated (Pfr) (PubMed:31732705). {ECO:0000269|PubMed:11260718,
CC       ECO:0000269|PubMed:12468726, ECO:0000269|PubMed:15707897,
CC       ECO:0000269|PubMed:18390804, ECO:0000269|PubMed:22577138,
CC       ECO:0000269|PubMed:22895253, ECO:0000269|PubMed:22904146,
CC       ECO:0000269|PubMed:24127609, ECO:0000269|PubMed:24982198,
CC       ECO:0000269|PubMed:26724867, ECO:0000269|PubMed:31732705}.
CC   -!- INTERACTION:
CC       P14713; O82798: ARR4; NbExp=3; IntAct=EBI-300727, EBI-625213;
CC       P14713; Q96524: CRY2; NbExp=3; IntAct=EBI-300727, EBI-531555;
CC       P14713; P14713: PHYB; NbExp=3; IntAct=EBI-300727, EBI-300727;
CC       P14713; P14714: PHYC; NbExp=5; IntAct=EBI-300727, EBI-624366;
CC       P14713; P42497: PHYD; NbExp=6; IntAct=EBI-300727, EBI-624382;
CC       P14713; P42498: PHYE; NbExp=5; IntAct=EBI-300727, EBI-624404;
CC       P14713; Q8GZM7: PIF1; NbExp=3; IntAct=EBI-300727, EBI-630400;
CC       P14713; O80536: PIF3; NbExp=22; IntAct=EBI-300727, EBI-625701;
CC       P14713; Q8W2F3-2: PIF4; NbExp=3; IntAct=EBI-300727, EBI-625732;
CC       P14713; Q9SWI1: PKS1; NbExp=2; IntAct=EBI-300727, EBI-626200;
CC       P14713; Q9SGQ0: VOZ1; NbExp=4; IntAct=EBI-300727, EBI-6306928;
CC       P14713; Q9SLB9: VOZ2; NbExp=4; IntAct=EBI-300727, EBI-6306942;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15707897}. Nucleus,
CC       nucleoplasm {ECO:0000269|PubMed:15707897}. Nucleus speckle
CC       {ECO:0000269|PubMed:15707897}. Nucleus {ECO:0000269|PubMed:24127609}.
CC       Note=Cytoplasmic in darkness, but translocated to the nucleus upon
CC       illumination, when associated with PAPP5 into speckles.
CC       {ECO:0000269|PubMed:15707897}.
CC   -!- TISSUE SPECIFICITY: Expressed in fruits, flowers, leaves, stems,
CC       seedlings and roots. {ECO:0000269|PubMed:23708772}.
CC   -!- DEVELOPMENTAL STAGE: Accumulates progressively in maturating seeds to
CC       reach a peak in dry seeds (PubMed:23708772). Expressed upon seed
CC       imbibition (PubMed:23708772). {ECO:0000269|PubMed:23708772}.
CC   -!- INDUCTION: Inactivation is proportional to temperature in the dark.
CC       {ECO:0000269|PubMed:27789797}.
CC   -!- PTM: Contains one covalently linked phytochromobilin chromophore.
CC       {ECO:0000269|PubMed:24982198, ECO:0000269|PubMed:28376244}.
CC   -!- DISRUPTION PHENOTYPE: Reduced temperature responses in light
CC       (PubMed:30635559). In oop1, defects in circadian timing with altered
CC       phase; early timing of the peak (acrophase) of multiple circadian
CC       rhythms such as leaf movement, CO(2) assimilation and light-induced
CC       gene expression. Strong photoperception defect in red light leading to
CC       long hypocotyls; this phenotype is increased when blue lights are
CC       combined to red lights. Increased sensitivity to SO(2). Elongated
CC       internodes before the transition to flowering when grown in short day
CC       conditions. {ECO:0000269|PubMed:12177480, ECO:0000269|PubMed:30635559}.
CC   -!- SIMILARITY: Belongs to the phytochrome family. {ECO:0000305}.
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DR   EMBL; X17342; CAA35222.1; -; mRNA.
DR   EMBL; L09262; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AY466496; AAR32737.1; -; Genomic_DNA.
DR   EMBL; AC005724; AAD08948.1; -; Genomic_DNA.
DR   EMBL; CP002685; AEC06808.1; -; Genomic_DNA.
DR   PIR; B33473; FKMUB.
DR   RefSeq; NP_179469.1; NM_127435.4.
DR   PDB; 4OUR; X-ray; 3.40 A; A/B=90-624.
DR   PDB; 7RZW; EM; 3.30 A; A/B=1-1172.
DR   PDBsum; 4OUR; -.
DR   PDBsum; 7RZW; -.
DR   AlphaFoldDB; P14713; -.
DR   EMDB; EMD-24780; -.
DR   EMDB; EMD-28870; -.
DR   EMDB; EMD-28871; -.
DR   EMDB; EMD-28872; -.
DR   SMR; P14713; -.
DR   BioGRID; 1751; 70.
DR   DIP; DIP-31742N; -.
DR   IntAct; P14713; 19.
DR   MINT; P14713; -.
DR   STRING; 3702.P14713; -.
DR   iPTMnet; P14713; -.
DR   PaxDb; 3702-AT2G18790-1; -.
DR   ProteomicsDB; 234908; -.
DR   EnsemblPlants; AT2G18790.1; AT2G18790.1; AT2G18790.
DR   GeneID; 816394; -.
DR   Gramene; AT2G18790.1; AT2G18790.1; AT2G18790.
DR   KEGG; ath:AT2G18790; -.
DR   Araport; AT2G18790; -.
DR   TAIR; AT2G18790; PHYB.
DR   eggNOG; ENOG502QPNJ; Eukaryota.
DR   HOGENOM; CLU_010418_0_0_1; -.
DR   InParanoid; P14713; -.
DR   OrthoDB; 1770905at2759; -.
DR   PhylomeDB; P14713; -.
DR   PRO; PR:P14713; -.
DR   Proteomes; UP000006548; Chromosome 2.
DR   ExpressionAtlas; P14713; baseline and differential.
DR   GO; GO:0005829; C:cytosol; IDA:TAIR.
DR   GO; GO:0016604; C:nuclear body; IDA:TAIR.
DR   GO; GO:0016607; C:nuclear speck; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR   GO; GO:0031516; F:far-red light photoreceptor activity; IDA:TAIR.
DR   GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR   GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR   GO; GO:1990841; F:promoter-specific chromatin binding; IDA:UniProtKB.
DR   GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
DR   GO; GO:0031517; F:red light photoreceptor activity; IDA:TAIR.
DR   GO; GO:0009883; F:red or far-red light photoreceptor activity; IMP:TAIR.
DR   GO; GO:0043565; F:sequence-specific DNA binding; IDA:UniProtKB.
DR   GO; GO:0009687; P:abscisic acid metabolic process; IMP:TAIR.
DR   GO; GO:0006325; P:chromatin organization; IMP:TAIR.
DR   GO; GO:0010617; P:circadian regulation of calcium ion oscillation; IMP:TAIR.
DR   GO; GO:0009584; P:detection of visible light; IEA:InterPro.
DR   GO; GO:0009649; P:entrainment of circadian clock; IMP:TAIR.
DR   GO; GO:0009630; P:gravitropism; IMP:TAIR.
DR   GO; GO:0009867; P:jasmonic acid mediated signaling pathway; IMP:TAIR.
DR   GO; GO:0045892; P:negative regulation of DNA-templated transcription; IDA:UniProtKB.
DR   GO; GO:0009640; P:photomorphogenesis; IMP:TAIR.
DR   GO; GO:0015979; P:photosynthesis; IMP:TAIR.
DR   GO; GO:0009638; P:phototropism; IMP:TAIR.
DR   GO; GO:0017012; P:protein-phytochromobilin linkage; IDA:UniProtKB.
DR   GO; GO:0010161; P:red light signaling pathway; IMP:TAIR.
DR   GO; GO:0031347; P:regulation of defense response; IMP:TAIR.
DR   GO; GO:2000028; P:regulation of photoperiodism, flowering; IMP:TAIR.
DR   GO; GO:0010029; P:regulation of seed germination; IMP:TAIR.
DR   GO; GO:0009409; P:response to cold; IMP:TAIR.
DR   GO; GO:0010218; P:response to far red light; IMP:TAIR.
DR   GO; GO:0010244; P:response to low fluence blue light stimulus by blue low-fluence system; IDA:UniProtKB.
DR   GO; GO:0010202; P:response to low fluence red light stimulus; IMP:TAIR.
DR   GO; GO:0009266; P:response to temperature stimulus; IMP:UniProtKB.
DR   GO; GO:0010374; P:stomatal complex development; IMP:TAIR.
DR   GO; GO:0010148; P:transpiration; IMP:TAIR.
DR   CDD; cd16932; HATPase_Phy-like; 1.
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; 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; 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.
DR   Genevisible; P14713; AT.
PE   1: Evidence at protein level;
KW   3D-structure; Chromophore; Cytoplasm; DNA-binding; Nucleus;
KW   Photoreceptor protein; Phytochrome signaling pathway; Receptor;
KW   Reference proteome; Repeat; Repressor; Sensory transduction; Transcription;
KW   Transcription regulation.
FT   CHAIN           1..1172
FT                   /note="Phytochrome B"
FT                   /id="PRO_0000171963"
FT   DOMAIN          252..433
FT                   /note="GAF"
FT                   /evidence="ECO:0000305"
FT   DOMAIN          652..723
FT                   /note="PAS 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00140"
FT   DOMAIN          786..857
FT                   /note="PAS 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00140"
FT   DOMAIN          934..1153
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
FT   REGION          1..54
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        22..54
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         357
FT                   /ligand="phytochromobilin"
FT                   /ligand_id="ChEBI:CHEBI:189064"
FT                   /note="covalent"
FT                   /evidence="ECO:0000269|PubMed:24982198,
FT                   ECO:0007744|PDB:4OUR"
FT   VARIANT         9..12
FT                   /note="Missing (in strain: cv. Kas-1)"
FT                   /evidence="ECO:0000269|PubMed:15238539"
FT   VARIANT         19
FT                   /note="E -> K (in strain: cv. Kas-1)"
FT                   /evidence="ECO:0000269|PubMed:15238539"
FT   VARIANT         143
FT                   /note="I -> L (in strain: cv. Kas-1)"
FT                   /evidence="ECO:0000269|PubMed:15238539"
FT   VARIANT         980
FT                   /note="V -> I (in strain: cv. Kas-1)"
FT                   /evidence="ECO:0000269|PubMed:15238539"
FT   VARIANT         1072
FT                   /note="L -> V (in strain: cv. Kas-1)"
FT                   /evidence="ECO:0000269|PubMed:15238539"
FT   MUTAGEN         276
FT                   /note="Y->H: In YHB; constitutively active and stronger
FT                   interaction with PTAC12/HMR/PAP5 in the dark. Constitutive
FT                   warm-temperature response with the warm-temperature
FT                   transcriptome derepressed at low temperatures."
FT                   /evidence="ECO:0000269|PubMed:22895253,
FT                   ECO:0000269|PubMed:27789797"
FT   TURN            98..100
FT                   /evidence="ECO:0007829|PDB:4OUR"
FT   HELIX           105..110
FT                   /evidence="ECO:0007829|PDB:7RZW"
FT   STRAND          112..114
FT                   /evidence="ECO:0007829|PDB:4OUR"
FT   STRAND          119..124
FT                   /evidence="ECO:0007829|PDB:7RZW"
FT   TURN            125..128
FT                   /evidence="ECO:0007829|PDB:7RZW"
FT   STRAND          129..132
FT                   /evidence="ECO:0007829|PDB:7RZW"
FT   HELIX           137..140
FT                   /evidence="ECO:0007829|PDB:7RZW"
FT   HELIX           163..166
FT                   /evidence="ECO:0007829|PDB:7RZW"
FT   HELIX           169..179
FT                   /evidence="ECO:0007829|PDB:7RZW"
FT   TURN            185..187
FT                   /evidence="ECO:0007829|PDB:7RZW"
FT   STRAND          189..197
FT                   /evidence="ECO:0007829|PDB:7RZW"
FT   STRAND          200..203
FT                   /evidence="ECO:0007829|PDB:7RZW"
FT   STRAND          209..218
FT                   /evidence="ECO:0007829|PDB:7RZW"
FT   HELIX           224..226
FT                   /evidence="ECO:0007829|PDB:4OUR"
FT   HELIX           231..246
FT                   /evidence="ECO:0007829|PDB:7RZW"
FT   HELIX           253..268
FT                   /evidence="ECO:0007829|PDB:7RZW"
FT   STRAND          271..278
FT                   /evidence="ECO:0007829|PDB:7RZW"
FT   STRAND          284..289
FT                   /evidence="ECO:0007829|PDB:7RZW"
FT   HELIX           305..307
FT                   /evidence="ECO:0007829|PDB:4OUR"
FT   HELIX           310..319
FT                   /evidence="ECO:0007829|PDB:7RZW"
FT   STRAND          321..323
FT                   /evidence="ECO:0007829|PDB:7RZW"
FT   STRAND          327..329
FT                   /evidence="ECO:0007829|PDB:4OUR"
FT   STRAND          332..334
FT                   /evidence="ECO:0007829|PDB:7RZW"
FT   HELIX           356..365
FT                   /evidence="ECO:0007829|PDB:7RZW"
FT   STRAND          368..377
FT                   /evidence="ECO:0007829|PDB:7RZW"
FT   STRAND          395..406
FT                   /evidence="ECO:0007829|PDB:7RZW"
FT   HELIX           412..455
FT                   /evidence="ECO:0007829|PDB:7RZW"
FT   HELIX           461..465
FT                   /evidence="ECO:0007829|PDB:7RZW"
FT   STRAND          466..468
FT                   /evidence="ECO:0007829|PDB:7RZW"
FT   TURN            470..473
FT                   /evidence="ECO:0007829|PDB:7RZW"
FT   STRAND          477..486
FT                   /evidence="ECO:0007829|PDB:7RZW"
FT   STRAND          488..492
FT                   /evidence="ECO:0007829|PDB:7RZW"
FT   HELIX           496..508
FT                   /evidence="ECO:0007829|PDB:7RZW"
FT   STRAND          514..519
FT                   /evidence="ECO:0007829|PDB:7RZW"
FT   HELIX           521..524
FT                   /evidence="ECO:0007829|PDB:7RZW"
FT   HELIX           529..532
FT                   /evidence="ECO:0007829|PDB:7RZW"
FT   HELIX           534..536
FT                   /evidence="ECO:0007829|PDB:7RZW"
FT   STRAND          538..544
FT                   /evidence="ECO:0007829|PDB:7RZW"
FT   TURN            545..547
FT                   /evidence="ECO:0007829|PDB:7RZW"
FT   STRAND          548..554
FT                   /evidence="ECO:0007829|PDB:7RZW"
FT   STRAND          560..566
FT                   /evidence="ECO:0007829|PDB:7RZW"
FT   STRAND          587..591
FT                   /evidence="ECO:0007829|PDB:7RZW"
FT   HELIX           601..620
FT                   /evidence="ECO:0007829|PDB:7RZW"
FT   STRAND          780..783
FT                   /evidence="ECO:0007829|PDB:7RZW"
FT   STRAND          785..787
FT                   /evidence="ECO:0007829|PDB:7RZW"
FT   STRAND          790..792
FT                   /evidence="ECO:0007829|PDB:7RZW"
FT   STRAND          801..804
FT                   /evidence="ECO:0007829|PDB:7RZW"
FT   STRAND          809..813
FT                   /evidence="ECO:0007829|PDB:7RZW"
FT   HELIX           815..821
FT                   /evidence="ECO:0007829|PDB:7RZW"
FT   HELIX           825..828
FT                   /evidence="ECO:0007829|PDB:7RZW"
FT   TURN            833..835
FT                   /evidence="ECO:0007829|PDB:7RZW"
FT   HELIX           836..839
FT                   /evidence="ECO:0007829|PDB:7RZW"
FT   TURN            840..842
FT                   /evidence="ECO:0007829|PDB:7RZW"
FT   HELIX           849..862
FT                   /evidence="ECO:0007829|PDB:7RZW"
FT   STRAND          866..874
FT                   /evidence="ECO:0007829|PDB:7RZW"
FT   STRAND          880..889
FT                   /evidence="ECO:0007829|PDB:7RZW"
FT   STRAND          893..896
FT                   /evidence="ECO:0007829|PDB:7RZW"
FT   STRAND          900..905
FT                   /evidence="ECO:0007829|PDB:7RZW"
FT   HELIX           909..919
FT                   /evidence="ECO:0007829|PDB:7RZW"
FT   TURN            920..924
FT                   /evidence="ECO:0007829|PDB:7RZW"
FT   TURN            926..928
FT                   /evidence="ECO:0007829|PDB:7RZW"
FT   HELIX           929..938
FT                   /evidence="ECO:0007829|PDB:7RZW"
FT   HELIX           940..953
FT                   /evidence="ECO:0007829|PDB:7RZW"
FT   HELIX           960..982
FT                   /evidence="ECO:0007829|PDB:7RZW"
FT   STRAND          987..990
FT                   /evidence="ECO:0007829|PDB:7RZW"
FT   STRAND          998..1000
FT                   /evidence="ECO:0007829|PDB:7RZW"
FT   HELIX           1003..1006
FT                   /evidence="ECO:0007829|PDB:7RZW"
FT   TURN            1007..1013
FT                   /evidence="ECO:0007829|PDB:7RZW"
FT   HELIX           1014..1019
FT                   /evidence="ECO:0007829|PDB:7RZW"
FT   STRAND          1023..1027
FT                   /evidence="ECO:0007829|PDB:7RZW"
FT   STRAND          1037..1039
FT                   /evidence="ECO:0007829|PDB:7RZW"
FT   HELIX           1041..1057
FT                   /evidence="ECO:0007829|PDB:7RZW"
FT   STRAND          1064..1068
FT                   /evidence="ECO:0007829|PDB:7RZW"
FT   STRAND          1071..1075
FT                   /evidence="ECO:0007829|PDB:7RZW"
FT   STRAND          1077..1079
FT                   /evidence="ECO:0007829|PDB:7RZW"
FT   STRAND          1081..1085
FT                   /evidence="ECO:0007829|PDB:7RZW"
FT   STRAND          1092..1094
FT                   /evidence="ECO:0007829|PDB:7RZW"
FT   HELIX           1098..1104
FT                   /evidence="ECO:0007829|PDB:7RZW"
FT   HELIX           1113..1127
FT                   /evidence="ECO:0007829|PDB:7RZW"
FT   STRAND          1130..1135
FT                   /evidence="ECO:0007829|PDB:7RZW"
FT   STRAND          1137..1139
FT                   /evidence="ECO:0007829|PDB:7RZW"
FT   STRAND          1141..1148
FT                   /evidence="ECO:0007829|PDB:7RZW"
SQ   SEQUENCE   1172 AA;  129331 MW;  7B5348CB1091B813 CRC64;
     MVSGVGGSGG GRGGGRGGEE EPSSSHTPNN RRGGEQAQSS GTKSLRPRSN TESMSKAIQQ
     YTVDARLHAV FEQSGESGKS FDYSQSLKTT TYGSSVPEQQ ITAYLSRIQR GGYIQPFGCM
     IAVDESSFRI IGYSENAREM LGIMPQSVPT LEKPEILAMG TDVRSLFTSS SSILLERAFV
     AREITLLNPV WIHSKNTGKP FYAILHRIDV GVVIDLEPAR TEDPALSIAG AVQSQKLAVR
     AISQLQALPG GDIKLLCDTV VESVRDLTGY DRVMVYKFHE DEHGEVVAES KRDDLEPYIG
     LHYPATDIPQ ASRFLFKQNR VRMIVDCNAT PVLVVQDDRL TQSMCLVGST LRAPHGCHSQ
     YMANMGSIAS LAMAVIINGN EDDGSNVASG RSSMRLWGLV VCHHTSSRCI PFPLRYACEF
     LMQAFGLQLN MELQLALQMS EKRVLRTQTL LCDMLLRDSP AGIVTQSPSI MDLVKCDGAA
     FLYHGKYYPL GVAPSEVQIK DVVEWLLANH ADSTGLSTDS LGDAGYPGAA ALGDAVCGMA
     VAYITKRDFL FWFRSHTAKE IKWGGAKHHP EDKDDGQRMH PRSSFQAFLE VVKSRSQPWE
     TAEMDAIHSL QLILRDSFKE SEAAMNSKVV DGVVQPCRDM AGEQGIDELG AVAREMVRLI
     ETATVPIFAV DAGGCINGWN AKIAELTGLS VEEAMGKSLV SDLIYKENEA TVNKLLSRAL
     RGDEEKNVEV KLKTFSPELQ GKAVFVVVNA CSSKDYLNNI VGVCFVGQDV TSQKIVMDKF
     INIQGDYKAI VHSPNPLIPP IFAADENTCC LEWNMAMEKL TGWSRSEVIG KMIVGEVFGS
     CCMLKGPDAL TKFMIVLHNA IGGQDTDKFP FPFFDRNGKF VQALLTANKR VSLEGKVIGA
     FCFLQIPSPE LQQALAVQRR QDTECFTKAK ELAYICQVIK NPLSGMRFAN SLLEATDLNE
     DQKQLLETSV SCEKQISRIV GDMDLESIED GSFVLKREEF FLGSVINAIV SQAMFLLRDR
     GLQLIRDIPE EIKSIEVFGD QIRIQQLLAE FLLSIIRYAP SQEWVEIHLS QLSKQMADGF
     AAIRTEFRMA CPGEGLPPEL VRDMFHSSRW TSPEGLGLSV CRKILKLMNG EVQYIRESER
     SYFLIILELP VPRKRPLSTA SGSGDMMLMM PY
//