PHYA_PETCR
ID PHYA_PETCR Reviewed; 1129 AA.
AC P55141;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=Phytochrome A;
GN Name=PHYA;
OS Petroselinum crispum (Parsley) (Petroselinum hortense).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; campanulids; Apiales; Apiaceae; Apioideae; apioid superclade;
OC Apieae; Petroselinum.
OX NCBI_TaxID=4043;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Hamburger Schnitt;
RX PubMed=7948895; DOI=10.1007/bf00039558;
RA Poppe C., Ehmann B., Frohnmeyer H., Furuya M., Schaefer E.;
RT "Regulation of phytochrome A mRNA abundance in parsley seedlings and cell-
RT suspension cultures.";
RL Plant Mol. Biol. 26:481-486(1994).
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; X75412; CAA53165.1; -; mRNA.
DR PIR; S52631; S52631.
DR AlphaFoldDB; P55141; -.
DR SMR; P55141; -.
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; 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; 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..1129
FT /note="Phytochrome A"
FT /id="PRO_0000171981"
FT DOMAIN 217..399
FT /note="GAF"
FT DOMAIN 622..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 906..1123
FT /note="Histidine kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
FT BINDING 322
FT /ligand="phytochromobilin"
FT /ligand_id="ChEBI:CHEBI:189064"
FT /note="covalent, via 1 link"
FT /evidence="ECO:0000250"
SQ SEQUENCE 1129 AA; 124746 MW; 8F89F9D5B0C23D26 CRC64;
MSSSRPANSS SNPGRANQNA RVVLTTLDAK IHADFEESGN SFDYSSSVRV TSAVGENSSI
QSNKLTTAYL HHIQKGKLIQ PVGCLLAVDE KSFKIMAYSE NAPEMLTMVS HAVPSVGEHP
VLGIGTDVRT IFTAPSAAAL QKAVGFTDIN LLNPILVHCK TSGKPFYAIA HRVTGSLIID
FEPVKPYEVP MTAAGALQSY KLASKAVNRL QALPGGSMER LCDTMVQEVF ELTGYDRVMA
YKFHDDDHGE VTAEVTKPGL EPYFGLHYPA TDVPQAARFL FLKNKVRMIC DCRANSAPVL
QDEKLPFELT LCGSTLRAPH SCHLQYMENM NSIASLVMAV VINDSDEVVE SSDRNSVKSK
KLWGLVVCHN TSPRFVPFPL RYACEFLAQV FAIHVSKELE LENQIVEKNI LRTQTLLCDL
LMRDAPLGIV SQSPNMMDLV KCDGAALLYK NKVYRLGATP SDYQLRDIVS WLTEYHTDST
GLSTDSLYDA GYPGALALGD VVCGMAVVKI TSHDMLFWFR SHAAGHIRWG GAKAEPDENH
DGRKMHPRSS FKAFLEVVKT RSTTWKEFEM DAIHSLQLIL RKALSVEKAV AAQGDEIRSN
TDVIHTKLND LKIEGIQELE AVTSEMVRLI ETATVPIFAV DADEIVNGWN TKIAELTGLP
VDQAMGKHLL TLVEDSSVGT VVFLLALALQ GKEEQGIPFE FKTYGSREDS VPITVVVNAC
ATRGLHDNVV GVCFVAQDVT SQKTIMDKFT RIQGDYKAIV QNPNPLIPPI FGTDEFGWCS
EWNQAMTELS GWRREDVMNK MLLGEIFGIQ TSCCHLKSKE AFVNLGVVLN NALTGQISEK
ICFSFFATDG KYVECLLCAS KKLHGEGTVT GIFCFLQLAS QELQQALHIQ RLTEQTAMKR
LKTLSYLRRQ AKNPLCGINF VREKLEEIGM GEEQTKLFRT SVHCQRHVNK ILDDTDLDSI
IDGYLDLEMS EFRLHDVYVA SRSQVSMRSN GKAIQVVDNF SEEMMSETLY GDSLRLQKVL
ADFMSVCVNL TPVGGHLGIS VTLTEDNLGQ SVQLVHLEFR ITHTGAGVPE EAVSQMFGSD
SETSEEGISL LISRKLVKLM NGDVHYLREA GKSTFIITVE LAAASKRES
