PHYB_TOBAC
ID PHYB_TOBAC Reviewed; 1132 AA.
AC P29130;
DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1994, sequence version 2.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Phytochrome B;
GN Name=PHYB;
OS Nicotiana tabacum (Common tobacco).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Solanaceae; Nicotianoideae; Nicotianeae;
OC Nicotiana.
OX NCBI_TaxID=4097;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8278560; DOI=10.1104/pp.102.4.1363;
RA Kern R., Gasch A., Deak M., Kay S.A., Chua N.H.;
RT "phyB of tobacco, a new member of the phytochrome family.";
RL Plant Physiol. 102:1363-1364(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 457-1132.
RX PubMed=1498594; DOI=10.2307/3869536;
RA Lopez-Juez E., Nagatani A., Tomizawa K., Deak M., Kern R., Kendrick R.E.,
RA Furuya M.;
RT "The cucumber long hypocotyl mutant lacks a light-stable PHYB-like
RT phytochrome.";
RL Plant Cell 4:241-251(1992).
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; L10114; AAA34092.1; -; Genomic_DNA.
DR EMBL; M65023; AAA34093.1; -; mRNA.
DR PIR; T03668; T03668.
DR AlphaFoldDB; P29130; -.
DR SMR; P29130; -.
DR STRING; 4097.P29130; -.
DR Proteomes; UP000084051; Unplaced.
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 2: Evidence at transcript level;
KW Chromophore; Photoreceptor protein; Receptor; Reference proteome; Repeat;
KW Sensory transduction; Transcription; Transcription regulation.
FT CHAIN 1..1132
FT /note="Phytochrome B"
FT /id="PRO_0000171996"
FT DOMAIN 231..409
FT /note="GAF"
FT DOMAIN 623..694
FT /note="PAS 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00140"
FT DOMAIN 757..828
FT /note="PAS 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00140"
FT DOMAIN 905..1125
FT /note="Histidine kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
FT REGION 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 336
FT /ligand="phytochromobilin"
FT /ligand_id="ChEBI:CHEBI:189064"
FT /note="covalent, via 1 link"
FT /evidence="ECO:0000250"
FT CONFLICT 507
FT /note="L -> S (in Ref. 2; AAA34093)"
FT /evidence="ECO:0000305"
FT CONFLICT 586
FT /note="L -> LQ (in Ref. 2; AAA34093)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1132 AA; 125809 MW; 457F09C024C0F608 CRC64;
MASGSRTKHS HQSGQGQVQA QSSGTSNVNY KDSISKAIAQ YTADARLHAV FEQSGESGKS
FDYSQSIKTT TQSVVPEQQI TAYLTKIQRG GHIQPFGCMI AVDEASFRVI AYSENACEML
SLTPQSVPSL ERPEILTVGT DVRTLFTPSS SVLLERAFGA REITLLNPIW IHSKNSGKPF
YAILHRVDVG IVIDLEPART EDPALSIAGA VQSQKLAVRA ISHLQSLPGG DVKLLCDTVV
ESVRELTGYD RVMVYKFHED EHGEVVAESK IPDLEPYIGL HYPATDIPQA SRFLFKQNRV
RMIVDCHATP VRVVQDESLM QPLCLVGSTL RAPHGCHAQY MANMGSIASL TLAVIINGND
EEAVGGRSSM RLWGLVVGHH TSARCIPFPL RYACEFLMQA FGLQLNMELQ LASQLSEKHV
LRTQTLLCDM LLRDSPTGIV IQSPSIMDLV KCDGAALYCQ GKYYPLGVTP TEAQIKDIVE
WLLTYHGDST GLSTDSLADA GYPGAALLGD AVCGMAVAYI TSKDFLFWFR SHTAKEIKWG
GAKHHPEDKD DGQRMHPRSS FKAFLEVVKS RSLPWENAEM DAIHSLLILR DSFKDAEASN
SKAVVHAQLG EMELQGIDEL SSVAREMVRL IETATAPIFA VDVEGRINGW NAKVAELTDL
SVEEAMGKSL VHDLVHKESQ ETAEKLLFNA LRGEEDKNVE IKLRTFGPEQ LKKAVFVVVN
ACSSKDYTNN IVGVCFVGQD VTGQKVVMDK FIHIQGDYKA IVHSPNPLIP PIFASDENTC
CSEWNTAMEK LTGWSRGEII GKMLVGEIFG SCCRLKGPDA MTKFMIVLHN AIGVQDTDKF
PFSFFDRNGK YVQALLTANK RVNMEGQIIG AFCFIQIASP ELQQALRVQR QQEKKCYSQM
KELAYLCQEI KSPLNGIRFT NSLLEATDLT ENQKQYLETS AACERQMSKI IRDVDLENIE
DGSLTLEKEE FFLGSVIDAV VSQVMLLLRE RSVQLIRDIP EEIKTLTVHG DQVRIQQVLA
DFLLNMVRYA PSPDGWVEIQ LQPNMKQISD EVTVVHIEFR IVCPGEGLPP ELVQDMFHSS
RWVTKEGLGL SMCRKILKLM NGDIQYIRES ERCYFLIILD LPMTRRGSKS LG
