ID Q334C9_POPTN Unreviewed; 1144 AA.
AC Q334C9;
DT 06-DEC-2005, integrated into UniProtKB/TrEMBL.
DT 06-DEC-2005, sequence version 1.
DT 27-MAR-2024, entry version 116.
DE RecName: Full=Phytochrome {ECO:0000256|PIRNR:PIRNR000084};
GN Name=phyB2 {ECO:0000313|EMBL:CAJ21297.1};
OS Populus tremula (European aspen).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Malpighiales; Salicaceae; Saliceae; Populus.
OX NCBI_TaxID=113636 {ECO:0000313|EMBL:CAJ21297.1};
RN [1] {ECO:0000313|EMBL:CAJ21297.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Fra22 {ECO:0000313|EMBL:CAJ21297.1};
RX PubMed=16361240; DOI=10.1534/genetics.105.047522;
RA Ingvarsson P.K., Garcia M.V., Hall D., Luquez V., Jansson S.;
RT "Clinal variation in phyB2, a candidate gene for day-length-induced growth
RT cessation and bud set, across a latitudinal gradient in European aspen
RT (Populus tremula).";
RL Genetics 172:1845-1853(2006).
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, ECO:0000256|PIRNR:PIRNR000084}.
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DR EMBL; AM072296; CAJ21297.1; -; Genomic_DNA.
DR AlphaFoldDB; Q334C9; -.
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; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
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|PIRNR:PIRNR000084};
KW Photoreceptor protein {ECO:0000256|ARBA:ARBA00022543,
KW ECO:0000256|PIRNR:PIRNR000084};
KW Receptor {ECO:0000256|ARBA:ARBA00023170, ECO:0000256|PIRNR:PIRNR000084};
KW Sensory transduction {ECO:0000256|ARBA:ARBA00022606,
KW ECO:0000256|PIRNR:PIRNR000084};
KW Transcription {ECO:0000256|ARBA:ARBA00023163,
KW ECO:0000256|PIRNR:PIRNR000084};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015,
KW ECO:0000256|PIRNR:PIRNR000084}.
FT DOMAIN 231..399
FT /note="Phytochrome chromophore attachment site"
FT /evidence="ECO:0000259|PROSITE:PS50046"
FT DOMAIN 624..695
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 758..810
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 904..1040
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT REGION 1..33
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"
FT /evidence="ECO:0000256|PIRSR:PIRSR000084-50"
SQ SEQUENCE 1144 AA; 127860 MW; 702722469BE11AFB CRC64;
MASQSQRQSN QPAHNQAQSS GTSNMRQHHH PTESVSKAIA QYTVDAQLHA VFEQSGGTGK
SFDYSKSVRT PNQSVPEEQI TAYLSKIQRG GHIQPFGCMI AADEQSFRVI AYSENAKDML
GLTPQSVPSL EKQEILFVGA DVRILFRPSS AVLLEKAFGA REITLLNPIW IHSKNSGKPF
YAILHRIDVG IVIDLEPART EDPALSIAGA VQSQKLAVRA ISQLQSLPGG DIKLLCDTVV
DSVRELTGYD RVMVYKFHED EHGEVVAENK RVDLEPYIGL HYPSTDIPQA SRFLFKQNRV
RMIVDCHAIP VSVIQDEGLM QPLCLVGSTL RAPHGCHAQY MENMGSIASL AMAVIIYGND
EEAIGGRNSM RLWGLVVCHH TSARCIPFPL RYACEFLMQA FGLQLNMELQ LASQLLEKHV
LRTQTLLCDM LLRDSPTGIV TQSPSIMDLV KCDGAALYYQ GQYYPLGVTP TEAQIKDIVE
WLLTLHGDPT GLSTDSLADA GYPGAAFLGD AVCGMAVAYI AERDFLFWFR SHTAKEVKWG
GAKHHPEDKD DGQRMHPRSS FKAFLEVVKS RSLPWENAEM DAIHSLQLIL RDSFRDAEAT
NSKAVVHTQL KDMELQGMDE LSSVAREMVR LIETATAPIF AVDVDGRING WNAKVAELTG
LSVEEAMGKS LVHDLVYKEY EEIVDKLIHR AVKGEEDKNV EIKLRTFCSE HQKKAVFVVV
NACSSKDYMD NIVGVCFVGQ DVTGQKVVMD KYVLIQGDYK AIVHSPNPSI PPIFASDENT
CCLEWNTALE KLTGWSRGEV VGKMLVGEVF GSCCRLKGPD ALTKFMIALH NAIGGIDTDK
LPFSFFDRNE KNVQTLLTAN KRVNMNIIGA FCFLQIVSPE LQPSLKVQKQ QEKKSFARMK
ELAYICQEIK NPLSGIHFTN SLLENTDLTE DQQQFLETSA ACEKQILKII RDIDLESIEN
GSLELEKAEF LLGSVINAVV SQAMLLLRER NLQLLRDIPE EIKTLAVYGD QARIQQVLAD
FLLNMVRYAP SSAGWVEIHV CPTLKQISDG HTLVHTEFRY LERVLQTRML GLQHPLRSFL
NCKLTLVMLH REGMVPKIQF QGLSVCQGRL IWLSFPENTT VALYPLTIWF LLLHRHQSRS
ITHT
//
