ID   PHYB_SOLTU              Reviewed;        1130 AA.
AC   P34094; O24380;
DT   01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT   25-JUL-2003, sequence version 2.
DT   03-AUG-2022, entry version 133.
DE   RecName: Full=Phytochrome B;
GN   Name=PHYB;
OS   Solanum tuberosum (Potato).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Solanales; Solanaceae; Solanoideae; Solaneae; Solanum.
OX   NCBI_TaxID=4113;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=cv. Desiree; TISSUE=Leaf;
RX   PubMed=1450376; DOI=10.1007/bf00046444;
RA   Heyer A., Gatz C.;
RT   "Isolation and characterization of a cDNA-clone coding for potato type B
RT   phytochrome.";
RL   Plant Mol. Biol. 20:589-600(1992).
RN   [2]
RP   SEQUENCE REVISION TO 213-228; 722-723; 856 AND 1058-1065.
RA   Gatz C.;
RL   Submitted (AUG-1997) 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.
CC   -!- SUBUNIT: Homodimer.
CC   -!- PTM: Contains one covalently linked phytochromobilin chromophore.
CC       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the phytochrome family. {ECO:0000305}.
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DR   EMBL; Y14572; CAA74908.1; -; Genomic_DNA.
DR   PIR; S28431; S28431.
DR   AlphaFoldDB; P34094; -.
DR   SMR; P34094; -.
DR   IntAct; P34094; 11.
DR   STRING; 4113.PGSC0003DMT400061712; -.
DR   PRIDE; P34094; -.
DR   eggNOG; ENOG502QRNS; Eukaryota.
DR   InParanoid; P34094; -.
DR   Proteomes; UP000011115; Unassembled WGS sequence.
DR   ExpressionAtlas; P34094; baseline.
DR   GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProt.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0051740; F:ethylene binding; IEA:UniProt.
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:0010105; P:negative regulation of ethylene-activated signaling pathway; IEA:UniProt.
DR   GO; GO:0017006; P:protein-tetrapyrrole linkage; IEA:InterPro.
DR   GO; GO:0009585; P:red, far-red light phototransduction; IEA:InterPro.
DR   GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:InterPro.
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; 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.
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; SSF47384; SSF47384; 1.
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   3: Inferred from homology;
KW   Chromophore; Photoreceptor protein; Receptor; Reference proteome; Repeat;
KW   Sensory transduction; Transcription; Transcription regulation.
FT   CHAIN           1..1130
FT                   /note="Phytochrome B"
FT                   /id="PRO_0000171993"
FT   DOMAIN          227..406
FT                   /note="GAF"
FT   DOMAIN          621..692
FT                   /note="PAS 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00140"
FT   DOMAIN          755..826
FT                   /note="PAS 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00140"
FT   DOMAIN          903..1123
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
FT   REGION          1..25
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         332
FT                   /ligand="phytochromobilin"
FT                   /ligand_id="ChEBI:CHEBI:189064"
FT                   /note="covalent, via 1 link"
FT                   /evidence="ECO:0000250"
FT   VARIANT         687
FT                   /note="N -> T"
FT   VARIANT         695
FT                   /note="K -> N"
FT   VARIANT         794
FT                   /note="R -> K"
FT   VARIANT         839
FT                   /note="P -> T"
SQ   SEQUENCE   1130 AA;  125422 MW;  09D1B8375B609584 CRC64;
     MASGSRTKHS HHSSSQAQSS GTSNVNYKDS ISKAIAQYTA DARLHAVFEQ SGESGKFFDY
     SQSVKTTTQS VPERQITAYL TKIQRGGHIQ PFGCMIAVDE ASFRVIAYSE NACEMLSLTP
     QSVPSLEKCE ILTIGTDVRT LFTPSSSVLL ERAFGAREIT LLNPIWIHSK NSGKPFYAIL
     HRVDVGIVID LEPARTEDPA LSIAGAVQSQ KLAVRAISHL QSLPGGDIKL LCDTVVESVR
     ELTGYDRVMV YKFHEDEHGE VVAESKRSDL EPYIGLHYPA TDIPQASRFL FKQNRVRMIV
     DCHATPVRVT QDESLMQPLC LVGSTLRAPH GCHAQYMANM GSIASLTLAV IINGNDEEAV
     GGGRNSMRLW GLVVGHHTSV RSIPFPLRYA CEFLMQAFGL QLNMELQLAS QLSEKHVLRT
     QTLLCDMLLR DSPPGIVTQS PSIMDLVKCD GAALYYQGKY YPLGVTPTEA QIKDIVEWLL
     AYHGDSTGLS TDSLPDAGYP GAASLGDAVC GMAVAYITSK DFLFWFRSHT AKEIKWGGAK
     HHPEDKDDGQ RMHPRSSFKA FLEVVKSRSS PWENAEMDAI HSLQLILRDS FKDAEASNSK
     AIVHAHLGEM ELQGIDELSS VAREMVRLIE TATAPIFAVD VEGRINGWNA KVAELTGVSV
     EEAMGKSLVH DLVYKESQET AEKLLYNALR GEEDKNVEIK LRTFGAEQLE KAVFVVVNAC
     ASKDYTNNIV GVCFVGQDVT GEKVVMDKFI NIQGDYKAIV HSPNPLIPPI FASDENTCCS
     EWNTAMEKLT GWSRGEIVGK MLVGEIFGSC CRLKGPDAMT KFMIVLHNAI GGQDTDKFPF
     SFFDRNGKYV QALLTANKRV NMEGDTIGAF CFIQIASPEL QQALRVQRQQ EKKCYSQMKE
     LAYICQEIKS PLNGIRFTNS LLEATNLTEN QKQYLETSAA CERQMSKIIR DIDLENIEDG
     SLTLEKEDFF LGSVIDAVVS QVMLLLREKG VQLIRDIPEE IKTLTVHGDQ VRIQQVLADF
     LLNMVRYAPS PDGWVEIQLR PSMMPISDGV TVVHIELRII CPGEGLPPEL VQDMFHSSRW
     VTQEGLGLSM CRKMLKLMNG EIQYIRESER CYFLIILDLP MTRKGPKSVG