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Database: UniProt
Entry: Q334A0_POPTN
LinkDB: Q334A0_POPTN
Original site: Q334A0_POPTN 
ID   Q334A0_POPTN            Unreviewed;      1146 AA.
AC   Q334A0;
DT   06-DEC-2005, integrated into UniProtKB/TrEMBL.
DT   06-DEC-2005, sequence version 1.
DT   08-NOV-2023, entry version 113.
DE   RecName: Full=Phytochrome {ECO:0000256|PIRNR:PIRNR000084};
GN   Name=phyB2 {ECO:0000313|EMBL:CAJ21326.1};
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:CAJ21326.1};
RN   [1] {ECO:0000313|EMBL:CAJ21326.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=SweN107 {ECO:0000313|EMBL:CAJ21326.1};
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.
CC       {ECO:0000256|PIRNR:PIRNR000084}.
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; AM072325; CAJ21326.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q334A0; -.
DR   GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProt.
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: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|PIRNR:PIRNR000084};
KW   Transcription regulation {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          906..1042
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   1146 AA;  127996 MW;  F9029ACE82BA35ED CRC64;
     MASQSQRQSN QPAHNQAQSS GTSNMRQHHH PTESVSKAIA QYTVDAQLHA VFEQSGGTGK
     SFDYSKSVRT PNQSVPEEQI TAYLSKIQRG GHIQPFGCMI AADEQSFRVI AYSENAKDML
     GLTPQSVPSL EKQEILFVGA DVRILFRPSS AVLLEKAFGA REITLLNPIW IHSKNSGKPF
     YAILHRIDVG IVIDLEPART EDPALSITGA VQSQKLAVRA ISQLQSLPGG DIKLLCDTVV
     DSVRGLTGYD RVMVYKFHED EHGEVVAENK RVDLEPYIGL HYPSTDIPQA SRFLFKQNRV
     RMIVDCHAIP VSVIQDEGLM QPLCLVGSTL RAPHGCHAQY MENMGSIASL AMAVIIYGND
     EEAIGGRNSM RLWGLVVCHH TSARCIPFPL RYACEFLMQA FGLQLNMELQ LASQLLEKHV
     LRTQTLLCDM LLRDSHTGIV TQSPSIMDLV KCDGAALYYQ GQYYPLGVTP TEAQIKDIVE
     WLLTLHGDPT GLSTDSLADA GYPGAAFLGD AVCGMAVAYI AERDFLFWFR SHTAKEVKWG
     GAKHHPEDKD DGQRMHPRSS FKAFLEVVKS RSLPWENAEM DAIHSLQLIL RDSFRDAEAT
     NSKAVVHNQL KDMELQGMDE LSSVAREMVR LIETATAPIF AVDVEGRING WNAKVAELTG
     LSVEEAMGKS LVHDLVYKEY EEIVDKLIHR AVKGEEDKNV EIKLRTFCSE HQKKAVFVVV
     NACSSKDYMD NIVGVCFVGQ DVTGQKVVMD KYVLIQGDYK AIVHSPNPSI PPIFASDENT
     CCLEWNTALE KLTGWSRGEV VGKMLVGEVF GSCCKLKGPD ALTKFMIALH NAIGGIDTDK
     LPFSFFDRNE KNVQTLLTAN KRVNIKGDII GAFCFLQIAS PELQPSLKVQ KQQEKKSFAR
     MKELAYICQE IKNPLSGIHF TNSLLENTDL TEDQQQFLET SAACEKQILK IIRDIDLESI
     ENGSLELEKA EFLLGSVINA VVSQAMLLLR ERNLQLLRDI PEEIKTLAVY GDQARIQQVL
     ADFLLNMVIY TQSSAGWVEI HVCPTLKQIS DGHTLVHTEF RYLERVLQTR MLGLQHPPRS
     FLNCKLTLVK LHREGMVPKI QFQGLSVCQG RLIWLSFPEN TTVALYPLTI WFLLLHRHQS
     RSITHT
//
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