PHY_PINSY
ID PHY_PINSY Reviewed; 1131 AA.
AC Q41046;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=Phytochrome;
OS Pinus sylvestris (Scotch pine).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Pinopsida; Pinidae; Conifers I; Pinales; Pinaceae; Pinus;
OC Pinus subgen. Pinus.
OX NCBI_TaxID=3349;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=PSA 5.1;
RX PubMed=10480390; DOI=10.1023/a:1006204318499;
RA Clapham D.H., Kolukisaoglu H.U., Larsson C.T., Qamaruddin M., Ekberg I.,
RA Wiegmann-Eirund C., Schneider-Poetsch H.A., von Arnold S.;
RT "Phytochrome types in Picea and Pinus. Expression patterns of PHYA-Related
RT types.";
RL Plant Mol. Biol. 40:669-678(1999).
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. {ECO:0000250}.
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; X96738; CAA65510.1; -; mRNA.
DR PIR; T09701; T09701.
DR AlphaFoldDB; Q41046; -.
DR SMR; Q41046; -.
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: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; 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 2: Evidence at transcript level;
KW Chromophore; Photoreceptor protein; Receptor; Repeat; Sensory transduction;
KW Transcription; Transcription regulation.
FT CHAIN 1..1131
FT /note="Phytochrome"
FT /id="PRO_0000171985"
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..30
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"
SQ SEQUENCE 1131 AA; 126255 MW; D63A2008FA9862FB CRC64;
MASNSRHTQS QSTGSNNRRS STNTNTTTNK ATAMAQYNSD ARLLQVFEQS GESGKSFDYT
RSIQVHNRAV PEQQITAYLS RIQRGGRIQP FGCVLAVEET TFRIIAYSEN EEMLDLGAQS
VPSMEKPQQD VLTIGTDVRT LFTAASAHSL EKAAVAQEIS LMNPIWVHCK NSRKPFYAIV
HRIDVGMVID LEPLRTGDAF MSAAGAVQSQ KLAVRAISRL QSLPCGDVGL LCDTVVENVR
ELTGYDRVMV YKFHEDEHGE VVAEIRRSDL EPYLGLHYPA TDIPQASRFL FMQNRVRMIC
DCMATPVKVI QSEELMQPLC LVGSTPSAPH GCHAQYMANM GSIRSLLMAV IINGNDDEGG
GSGRNSMKLW GLVVCHHTSP RAVPFPLRYA CEFLMQALGL QLNMELQLAA QLTEKHILRT
QTLLCDMLLR DAPMGIVTQS PSIKDLVKCD GAALYYGGMC WMLGVTPTEA QIKDIADWLL
EHHGDSTGLS TDSLADAGYP GAASLGDAVC GMASARITSK DFLFWFRSHT AKEMKWGGAK
HHPDDKDDAR RMHPRSSFKA FLEVVKRRSL PWDNVEIDAI HSLQLILRCS FRDIDDSGTK
TMVHSRLNYL RLQGIDELSS VASEMVRLIE TATAPILAVD YNGLVNGWNA KVAELTGLPV
GEAMGMSLVQ DLVFEQSVER VEKMLHNALR GEEEKNVEMM LKTFGPQKEK EAVILVVNAC
SSRDFTDNIV GVCFVGQDVT SQKVVMDKFI RIQGDYRSIV QSPNPLIPPI FASDEYACCS
EWNAAMEKVT GWTHDEVIGK MLVGEIFGGC CRLKGQDAVT KFTIVLHQCN HGQEIEKFPF
AFFDKQGKYV EALLTANKRT DADGRITGSF CFFRIASSEL QHALEVQRQQ EKKCFARLKE
LAYIRQEIKN PLYGMMFTRK LLEETDLSDD QKQFVETSAV CERQMQKVMD DMDLESLEDG
YMELDTAEFI LGTVIDAVVS QGMIVLREKG LQLIREIPGE VKTMRLYGDE VKIQQILADF
LLNVLRFTPS PEGWVAIKVF PTLKQLGGGL HVVHLEFRIT HPGLGLPAEL VQDLFDRSQW
ATQEGVGLSM CRKLLKLMNG DVRYIRESGI CYFLVNVEFP MAQREDAASI K