ID A0A251P156_PRUPE Unreviewed; 1134 AA.
AC A0A251P156;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=Phytochrome {ECO:0008006|Google:ProtNLM};
DE Flags: Fragment;
GN ORFNames=PRUPE_6G302500 {ECO:0000313|EMBL:ONI04095.1};
OS Prunus persica (Peach) (Amygdalus persica).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Rosales; Rosaceae; Amygdaloideae; Amygdaleae; Prunus.
OX NCBI_TaxID=3760 {ECO:0000313|EMBL:ONI04095.1, ECO:0000313|Proteomes:UP000006882};
RN [1] {ECO:0000313|EMBL:ONI04095.1, ECO:0000313|Proteomes:UP000006882}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nemared {ECO:0000313|Proteomes:UP000006882};
RX PubMed=23525075; DOI=10.1038/ng.2586;
RA Verde I., Abbott A.G., Scalabrin S., Jung S., Shu S., Marroni F.,
RA Zhebentyayeva T., Dettori M.T., Grimwood J., Cattonaro F., Zuccolo A.,
RA Rossini L., Jenkins J., Vendramin E., Meisel L.A., Decroocq V.,
RA Sosinski B., Prochnik S., Mitros T., Policriti A., Cipriani G., Dondini L.,
RA Ficklin S., Goodstein D.M., Xuan P., Del Fabbro C., Aramini V., Copetti D.,
RA Gonzalez S., Horner D.S., Falchi R., Lucas S., Mica E., Maldonado J.,
RA Lazzari B., Bielenberg D., Pirona R., Miculan M., Barakat A., Testolin R.,
RA Stella A., Tartarini S., Tonutti P., Arus P., Orellana A., Wells C.,
RA Main D., Vizzotto G., Silva H., Salamini F., Schmutz J., Morgante M.,
RA Rokhsar D.S.;
RT "The high-quality draft genome of peach (Prunus persica) identifies unique
RT patterns of genetic diversity, domestication and genome evolution.";
RL Nat. Genet. 45:487-494(2013).
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. {ECO:0000256|ARBA:ARBA00002479}.
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}.
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DR EMBL; CM007656; ONI04095.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A251P156; -.
DR EnsemblPlants; ONI04095; ONI04095; PRUPE_6G302500.
DR Gramene; ONI04095; ONI04095; PRUPE_6G302500.
DR eggNOG; ENOG502QRSA; Eukaryota.
DR Proteomes; UP000006882; Chromosome g6.
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: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; 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; 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; 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; 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; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF55781; GAF domain-like; 2.
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|PIRSR:PIRSR000084-
KW 50}; Photoreceptor protein {ECO:0000256|ARBA:ARBA00022543};
KW Receptor {ECO:0000256|ARBA:ARBA00023170};
KW Reference proteome {ECO:0000313|Proteomes:UP000006882};
KW Sensory transduction {ECO:0000256|ARBA:ARBA00022606};
KW Transcription {ECO:0000256|ARBA:ARBA00023163};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015}.
FT DOMAIN 218..391
FT /note="Phytochrome chromophore attachment site"
FT /evidence="ECO:0000259|PROSITE:PS50046"
FT DOMAIN 617..687
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 750..802
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 901..1118
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT REGION 1..22
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"
FT /evidence="ECO:0000256|PIRSR:PIRSR000084-50"
FT NON_TER 1134
FT /evidence="ECO:0000313|EMBL:ONI04095.1"
SQ SEQUENCE 1134 AA; 125434 MW; 9D0595A5CE570376 CRC64;
MSSSRPSDSS TNSGRSRHSA RIIAQTTVDA KLHADFEESG SSFDYSNSVR VSGSVGRDQQ
PRSDKVTTAY LHHIQKGKLI QPFGCLLALD EKTFKVIAYS ENAPEMLTMV SHAVPSVGDY
PVLGVGTDIR TIFTAPSASA LHKALGFGEV SLLNPILVHC KTSGKPFYAI THRVTGSLII
DFEPVKPYEV PMTAAGALQS YKLAAKAIAR LQSLPSGSME RLCDTMVQEV FELTGYDRVM
AYKFHDDDHG EVVSEITKPG LEPYLGLHYP STDIPQASRF LFMKNKVRMI VDCCAKQVKV
LQDEKLPFDL TLCGSTLRSP HSCHLQYMKN MESIASLVMA VVVNEGDDEV ASPDSVQPQK
RKRLWGLVVC HNTSPRFVPF PLRYACEFLA QVFAIHVNKE IELEDQMVEK NILRTQTLLC
DMLLRDAPLG IVSQSPNIMD LVKCDGAALL YKSKIWRLGI TPSDFQLHDI ASWLAEYHMD
STGLSTDSLY DAGFPGALAL GDVVCGMAAV RITSKDMLFW FRSHTAAEIR WGGAKHESGE
KDDGWRMHPR SSFKAFLEVV KSRSLPWKDF EMDAIHSLQL ILRNAFKDVE TVDVNPNAIH
VKLSDLKIEG MQELEAVTSE MVRLIETATV PILAVDVDGL VNGWNTKISE LTGLSVDKAI
GNHLLSLVED SSTKMVKRML DLALHGKEEQ NIQFEIKTHG SRSDLGPISL VVNACASRDI
RENVVGVCFV AQDITGQKTV MDKFTRIEGD YKAIVQNPNP LIPPIFGTDE FGWCSEWNPA
MTKLTGWKRE EVIDKMLLGE VFGINMACCP LKSQEAFVNL GIVLNHAMTG QVSEKVPFGF
SARSGKHIEC LLCVSKKLDS EGSVTGVFCF LQLASPELQQ ALHVQRLSEQ TAVKRSKELS
YIKRQIRNPL AGIMFSRKMM EGTELGTEQK QLLHTSAQCQ HQLNKILDDS DLDTIIDGYL
DLEMVEFTLH EVLLASVSQV MIKSNAKSIQ IVHDAAEEIM NETLYGDSLR LQQVLADFLA
VSINFMPTGG QLTIAANLTK DQLGQSVHLV HLELRITHAG GGIPEGLLNQ MFGNDIAISE
EGIGLLVSSR LVKLMNGDIR YLREAGKATF IISVELAAAH KLRSSITRSD SRHE
//
