PHYA_POPTM
ID PHYA_POPTM Reviewed; 1125 AA.
AC O49934;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=Phytochrome A;
GN Name=PHYA;
OS Populus tremuloides (Quaking aspen).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Malpighiales; Salicaceae; Saliceae; Populus.
OX NCBI_TaxID=3693;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=P.tremula X P.tremuloides T89; TISSUE=Leaf;
RA Eriksson M.E., Moritz T.;
RT "Isolation of a cDNA encoding a phytochrome a from Populus tremula x
RT tremuloides.";
RL (er) Plant Gene Register PGR97-186(1997).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AJ001318; CAA04679.1; -; mRNA.
DR PIR; T09835; T09835.
DR AlphaFoldDB; O49934; -.
DR SMR; O49934; -.
DR PRIDE; O49934; -.
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; 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; 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; 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..1125
FT /note="Phytochrome A"
FT /id="PRO_0000171986"
FT DOMAIN 218..401
FT /note="GAF"
FT DOMAIN 617..687
FT /note="PAS 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00140"
FT DOMAIN 750..821
FT /note="PAS 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00140"
FT DOMAIN 901..1117
FT /note="Histidine kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 38..64
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 40..54
FT /note="Polar residues"
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 1125 AA; 124955 MW; 7A4D1CDFCC9BD85F CRC64;
MSSSRPSHSS SNSARSRHSA RIIAQTTVDA KLHADFEESG SSFDYSSSVR VTDSVGGDQP
PRSDKVTTAY LHHIQKGKLI QPFGCLLALD EKTFRVVAYS ENAPELLTMV SHAVPSVGEH
PVLGIGTDIR TIFTAPSASA LQKAMGFGDV SLLNPILVHC KTSGKPFYAI VHRVTGSLII
DFEPVKPYEV PMTAAGALQS YKLAAKAITR LQSLPSGSME RLCDTMVQEV FELTGYDRAM
AYKFHDDDHG EVVSEVTKPG MEPYLGLHYP ATDIPQASRF LFMKNKVRMI VDCHAKHVKV
LQDEKLPFDL TLCGSTLRAP HSCHLQYMEN MNSIASLVMA VVVNDGDEDG DTPDSANPQK
RKRLWGLVVC HNTSPRFVPF PLRYACEFLA QVFAIHVNKE LELENQIVEK NILRTQTLLC
DMLMRDAPLG IVTQSPNIMD LVKCDGAVLF YRNKIWRLGI TPSDLQLQDI AFWLSEYHMD
STGLSTDSLY DAGYPGALAL GDVVCGMAAV RITSKDMLFW FRSQTAAEIR WGGAKHEPGE
KDDGRRMHPR SSFKAFLEVV KTRSLPWKDY EMDAIHSLQL ILRNTFKDIE TMDVDTKTIH
ARLSDLKIEG MQELEAVTSE MVRLIETATV PILAVDVDGL VNGWNTKISE LTGLLVDKAI
GKHLLTLVED SSVDIVKRML FLALQGKEEQ NIQFEIKTHG SKSECGPICL VVNACASRDL
HENVVGVCFV GQDITGQKMV MDKFTRIEGD YKAIVQNRNP LIPPIFGTDE FGWCSEWNPA
MTNLTGWKRE EVLDKMLLGE VFGLNMACCR LKNQEAFVNL GVVLNTAMTG QESEKVSFGF
FARTGKYVEC LLCVSKKLDR EGAVTGVFCF LQLASQELQQ ALHVQRLSEQ TALKRLKALA
YLKKQIWNPL SGIIFSGKMM EGTELGAEQK ELLHTSAQCQ CQLSKILDDS DLDSIIEGYL
DLEMVEFTLR EYYGCYQSSH DEKHEKGIPI INDALKMAET LYGDSIRLQQ VLADFCRCQL
ILTPSGGLLT VSASFFQRPV GAILFILVHS GKLRIRHLGA GIPEALVDQM YGEDTGASVE
GISLVISRKL VKLMNGDVRY MREAGKSSFI ISVELAGGHK SQKRA