PHYA_SORBI
ID PHYA_SORBI Reviewed; 1131 AA.
AC P93526;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=Phytochrome a;
GN Name=PHYA; OrderedLocusNames=Sb03g017600;
OS Sorghum bicolor (Sorghum) (Sorghum vulgare).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC Panicoideae; Andropogonodae; Andropogoneae; Sorghinae; Sorghum.
OX NCBI_TaxID=4558;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=9046599; DOI=10.1104/pp.113.2.611;
RA Childs K.L., Miller F.R., Cordonnier-Pratt M.-M., Pratt L.H., Morgan P.W.,
RA Mullet J.E.;
RT "The Sorghum bicolor photoperiod sensitivity gene, Ma3, encodes a
RT phytochrome B.";
RL Plant Physiol. 113:611-619(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 (By similarity). {ECO:0000250}.
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; U56729; AAB41397.1; -; mRNA.
DR AlphaFoldDB; P93526; -.
DR SMR; P93526; -.
DR STRING; 4558.Sb01g009920.2; -.
DR eggNOG; ENOG502QRSA; Eukaryota.
DR HOGENOM; CLU_010418_0_0_1; -.
DR ExpressionAtlas; P93526; baseline and differential.
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; 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; 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 a"
FT /id="PRO_0000171987"
FT DOMAIN 219..404
FT /note="GAF"
FT DOMAIN 620..690
FT /note="PAS 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00140"
FT DOMAIN 750..834
FT /note="PAS 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00140"
FT DOMAIN 904..1124
FT /note="Histidine kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 324
FT /ligand="phytochromobilin"
FT /ligand_id="ChEBI:CHEBI:189064"
FT /note="covalent, via 1 link"
FT /evidence="ECO:0000250"
SQ SEQUENCE 1131 AA; 125049 MW; 90E174FC6CD31C5D CRC64;
MSSSRPAHSS SSSSRTRQSS QARILAQTTL DAELNAEYEE SGDSFDYSKL VEAQRSTPSE
QQGRSGKVIA YLQHIQRGKL IQPFGCLLAL DEKSFRVIAF SENAPEMLTT VSHAVPNVDD
PPKLGIGTNV RSLFTDPGAT ALQKALGFAD VSLLNPILVQ CKTSGKPFYA IVHRATGCLV
VDFEPVKPTE FPATAAGALQ SYKLAAKAIS KIQSLPGGSM EALCNTVVKE VFELTGYDRV
MAYKFHEDEH GEVFAEITKP GIEPYLGLHY PATDIPQAAR FLFMKNKVRM ICDCRAKSVK
IIEDEALSID ISLCGSTLRA PHSCHLQYME NMNSIASLVM AVVVNENEED DEPGPEQPPQ
QQKKKRLWGL IVCHHESPRY VPFPLRYACE FLAQVFAVHV NKEFELEKQI REKSILRMQT
MLSDMLFKEA SPLSIVSGSP NIMDLVKCDG AALLYGDKVW RLQTAPTESQ IRDIAFWLSE
VHGDSTGLST DSLQDAGYPG AASLGDMICG MAVAKITSKD ILFWFRSHTA AEIKWGGAKH
DPSDKDDNRR MHPRLSFKAF LEVVKMKSLP WSDYEMDAIH SLQLILRGTL NDALKPVQAS
GLDNQIGDLK LDGLAELQAV TSEMVRLMET ATVPILAVDG NGLVNGWNQK VAELSGLRVD
EAIGRHILTL VEDSSVSIVQ RMLYLALQGK EEKEVRFELK THGSKRDDGP VILVVNACAS
RDLHDHVVGV CFVAQDMTVH KLVMDKFTRV EGDYKAIIHN PNPLIPPIFG ADQFGWCSEW
NVAMTKLTGW HRDEVIDKML LGEVFDSSNA SCLLKSKDDF VRLCIIINSA LAGEEAENAP
FGLFDRNGKY IECLLSVNRK VNADGVVTGV FCFIHVPSDD LQHALHVQQA SEQTAQRRLK
AFSYMRHAIN KPLSGMLYSR ETLKSTGLNE EQMRQVHVAD SCHRQLNKIL ADLDQDNITD
KSSCLDLDMA EFVLEDVVVS AVSQVLIGCQ GKGIRVACNL PERFMKQKVY GDGIRLQQIL
SDFLFVSVKF SPVGGSVDIS SKLTKNSIGE NLHLIDFELR IKHQGAGVPA EILSQMYEED
NKEPSEEGLS LLVSRNLLRL MNGNIRHIRE AGMSTFILTA ELAAAPSAVG Q