PHYB_ARATH
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 03-AUG-2022, entry version 203.
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},
GN OOP1 {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=10.2307/3869581;
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, 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 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 [15]
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 [16]
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 [17]
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 [18]
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).
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). Regulates temperature responses by associating with
CC the promoters of key target genes in a temperature-dependent manner and
CC subsequently repressing their expression probably in a PIF4-dependent
CC manner. Thermal timer that integrates temperature information over the
CC course of the night (PubMed:27789797). {ECO:0000269|PubMed:12177480,
CC ECO:0000269|PubMed:12468726, ECO:0000269|PubMed:15707897,
CC ECO:0000269|PubMed:27789797}.
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 PTAC12/HMR
CC when photoactivated; this interaction stimulates its localization to
CC photobodies (PubMed:22895253). Interacts with CRY1 specifically when in
CC the dark/far-red (Pr) state, but not when red light-activated (Pfr)
CC (PubMed:22577138). Interacts with PIF4 AND PIF5 in response to low blue
CC light (LBL) (PubMed:26724867). Component of a red light-dependent
CC nuclear complex made of PHL, PHYB and CO. Interacts directly with PHL
CC (PubMed:24127609). {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}.
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 -!- 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: 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}.
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 SMR; P14713; -.
DR BioGRID; 1751; 68.
DR DIP; DIP-31742N; -.
DR IntAct; P14713; 19.
DR MINT; P14713; -.
DR STRING; 3702.AT2G18790.1; -.
DR iPTMnet; P14713; -.
DR PaxDb; P14713; -.
DR PRIDE; P14713; -.
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; locus:2005515; AT2G18790.
DR eggNOG; ENOG502QPNJ; Eukaryota.
DR HOGENOM; CLU_010418_0_0_1; -.
DR InParanoid; P14713; -.
DR OrthoDB; 59136at2759; -.
DR PhylomeDB; P14713; -.
DR PRO; PR:P14713; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; P14713; baseline and differential.
DR Genevisible; P14713; AT.
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 transcription, DNA-templated; 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; -; 1.
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.
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; SSF55785; SSF55785; 3.
DR SUPFAM; SSF55874; SSF55874; 1.
DR TIGRFAMs; TIGR00229; sensory_box; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50112; PAS; 2.
DR PROSITE; PS00245; PHYTOCHROME_1; 1.
DR PROSITE; PS50046; PHYTOCHROME_2; 1.
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, via 1 link"
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 in the dark. Constitutive warm-
FT 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..109
FT /evidence="ECO:0007829|PDB:4OUR"
FT STRAND 112..114
FT /evidence="ECO:0007829|PDB:4OUR"
FT STRAND 118..123
FT /evidence="ECO:0007829|PDB:4OUR"
FT TURN 125..127
FT /evidence="ECO:0007829|PDB:4OUR"
FT STRAND 129..134
FT /evidence="ECO:0007829|PDB:4OUR"
FT HELIX 137..140
FT /evidence="ECO:0007829|PDB:4OUR"
FT HELIX 163..165
FT /evidence="ECO:0007829|PDB:4OUR"
FT HELIX 169..180
FT /evidence="ECO:0007829|PDB:4OUR"
FT HELIX 184..187
FT /evidence="ECO:0007829|PDB:4OUR"
FT STRAND 189..197
FT /evidence="ECO:0007829|PDB:4OUR"
FT STRAND 200..207
FT /evidence="ECO:0007829|PDB:4OUR"
FT STRAND 209..218
FT /evidence="ECO:0007829|PDB:4OUR"
FT HELIX 224..246
FT /evidence="ECO:0007829|PDB:4OUR"
FT HELIX 253..268
FT /evidence="ECO:0007829|PDB:4OUR"
FT STRAND 271..278
FT /evidence="ECO:0007829|PDB:4OUR"
FT STRAND 284..289
FT /evidence="ECO:0007829|PDB:4OUR"
FT HELIX 305..307
FT /evidence="ECO:0007829|PDB:4OUR"
FT HELIX 310..318
FT /evidence="ECO:0007829|PDB:4OUR"
FT STRAND 321..325
FT /evidence="ECO:0007829|PDB:4OUR"
FT STRAND 327..329
FT /evidence="ECO:0007829|PDB:4OUR"
FT STRAND 332..336
FT /evidence="ECO:0007829|PDB:4OUR"
FT HELIX 356..365
FT /evidence="ECO:0007829|PDB:4OUR"
FT STRAND 368..378
FT /evidence="ECO:0007829|PDB:4OUR"
FT STRAND 394..406
FT /evidence="ECO:0007829|PDB:4OUR"
FT HELIX 412..448
FT /evidence="ECO:0007829|PDB:4OUR"
FT STRAND 473..475
FT /evidence="ECO:0007829|PDB:4OUR"
FT STRAND 477..480
FT /evidence="ECO:0007829|PDB:4OUR"
FT HELIX 496..506
FT /evidence="ECO:0007829|PDB:4OUR"
FT STRAND 516..519
FT /evidence="ECO:0007829|PDB:4OUR"
FT HELIX 529..531
FT /evidence="ECO:0007829|PDB:4OUR"
FT STRAND 538..541
FT /evidence="ECO:0007829|PDB:4OUR"
FT STRAND 551..554
FT /evidence="ECO:0007829|PDB:4OUR"
FT STRAND 561..566
FT /evidence="ECO:0007829|PDB:4OUR"
FT STRAND 587..590
FT /evidence="ECO:0007829|PDB:4OUR"
FT HELIX 601..616
FT /evidence="ECO:0007829|PDB:4OUR"
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
