ID   PHYA_CUCPE              Reviewed;        1124 AA.
AC   P06592;
DT   01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1988, sequence version 1.
DT   03-AUG-2022, entry version 127.
DE   RecName: Full=Phytochrome A;
GN   Name=PHYA; Synonyms=PHY;
OS   Cucurbita pepo (Vegetable marrow) (Summer squash).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Cucurbitales; Cucurbitaceae; Cucurbiteae; Cucurbita.
OX   NCBI_TaxID=3663;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=3557123; DOI=10.1016/0378-1119(86)90072-7;
RA   Sharrock R.A., Lissemore J.L., Quail P.H.;
RT   "Nucleotide and amino acid sequence of a Cucurbita phytochrome cDNA clone:
RT   identification of conserved features by comparison with Avena
RT   phytochrome.";
RL   Gene 47:287-295(1986).
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; M15265; AAA33115.1; -; mRNA.
DR   PIR; S00099; FKPUZ.
DR   AlphaFoldDB; P06592; -.
DR   SMR; P06592; -.
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; 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; 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..1124
FT                   /note="Phytochrome A"
FT                   /id="PRO_0000171972"
FT   DOMAIN          218..400
FT                   /note="GAF"
FT   DOMAIN          616..686
FT                   /note="PAS 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00140"
FT   DOMAIN          749..820
FT                   /note="PAS 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00140"
FT   DOMAIN          900..1119
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
FT   REGION          1..24
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          39..64
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         323
FT                   /ligand="phytochromobilin"
FT                   /ligand_id="ChEBI:CHEBI:189064"
FT                   /note="covalent, via 1 link"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   1124 AA;  125082 MW;  D78BDBB153F3911B CRC64;
     MSTSRPSQSS SNSGRSRHST RIIAQTSVDA NVQADFEESG NSFDYSSSVR VTSDVSGDQQ
     PRSDKVTTAY LHHIQKGKLI QPFGCLLALD DKTFKVIAYS ENAPEMLTMV SHAVPSMGDY
     PVLGIGTDVR TIFTAPSASA LLKALGFGEV TLLNPILVHC KTSGKPFYAI VHRVTGSLII
     DFEPVKPYEG PVTAAGALQS YKLAAKAITR LQSLPSGSMA RLCDTMVQEV FELTGYDRVM
     AYKFHDDDHG EVISEVAKPG LQPYLGLHYP ATDIPQAARF LFMKNKVRMI VDCRAKHLKV
     LQDEKLQFDL TLCGSTLRAP HSCHLQYMEN MNSIASLVMA VVVNEGDEEN EGPALQQQKR
     KRLWGLVVCH NSSPRFVPFP LRYACEFLAQ VFAIHVNKEL ELENQIIEKN ILRTQTLLCD
     MLMRDAPLGI VSRSPNIMDL VKSDGAALLY KKKIWRLGLT PNDFQLLDIA SWLSEYHMDS
     TGLSTDSLYD AGYPGAIALG DEVCGMAAVR ITNNDMIFWF RSHTASEIRW GGAKHEHGQK
     DDARKMHPRS SFKAFLEVVK TRSLPWKDYE MDAIHSLQLI LRNTFKDTDA TEINRKSIQT
     TLGDLKIEGR QELESVTSEM VRLIETATVP ILAVDLDGLI NGWNTKIAEL TGLPVDKAIG
     KHLLTLVEDS SVEVVRKMLF LALQGQEEQN VQFEIKTHGS HIEVGSISLV VNACASRDLR
     ENVVGVFFVA QDITGQKMVM DKFTRLEGDY KAIVQNPNPL IPPIFGSDEF GWCSEWNPAM
     AKLTGWSREE VIDKMLLGEV FGVHKSCCRL KNQEAFVNLG IVLNNAMCGQ DPEKASFGFL
     ARNGMYVECL LCVNKILDKD GAVTGFFCFL QLPSHELQQA LNIQRLCEQT ALKRLRALGY
     IKRQIQNPLS GIIFSRRLLE RTELGVEQKE LLRTSGLCQK QISKVLDESD IDKIIDGFID
     LEMDEFTLHE VLMVSISQVM LKIKGKGIQI VNETPEEAMS ETLYGDSLRL QQVLADFLLI
     SVSYAPSGGQ LTISTDVTKN QLGKSVHLVH LEFRITYAGG GIPESLLNEM FGSEEDASEE
     GFSLLISRKL VKLMNGDVRY MREAGKSSFI ITVELAAAHK SRTT