PHYA_ORYSI
ID PHYA_ORYSI Reviewed; 1128 AA.
AC A2XLG5; P10931; Q8LLN7;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 11-SEP-2007, sequence version 2.
DT 03-AUG-2022, entry version 93.
DE RecName: Full=Phytochrome A;
GN Name=PHYA; Synonyms=PHY18; ORFNames=OsI_012908;
OS Oryza sativa subsp. indica (Rice).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX NCBI_TaxID=39946;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=cv. IR36;
RX PubMed=2717416; DOI=10.1093/nar/17.7.2865;
RA Kay S.A., Keith B., Shinozaki K., Chye M.L., Chua N.-H.;
RT "The sequence of the rice phytochrome gene.";
RL Nucleic Acids Res. 17:2865-2866(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. 93-11;
RX PubMed=15685292; DOI=10.1371/journal.pbio.0030038;
RA Yu J., Wang J., Lin W., Li S., Li H., Zhou J., Ni P., Dong W., Hu S.,
RA Zeng C., Zhang J., Zhang Y., Li R., Xu Z., Li S., Li X., Zheng H., Cong L.,
RA Lin L., Yin J., Geng J., Li G., Shi J., Liu J., Lv H., Li J., Wang J.,
RA Deng Y., Ran L., Shi X., Wang X., Wu Q., Li C., Ren X., Wang J., Wang X.,
RA Li D., Liu D., Zhang X., Ji Z., Zhao W., Sun Y., Zhang Z., Bao J., Han Y.,
RA Dong L., Ji J., Chen P., Wu S., Liu J., Xiao Y., Bu D., Tan J., Yang L.,
RA Ye C., Zhang J., Xu J., Zhou Y., Yu Y., Zhang B., Zhuang S., Wei H.,
RA Liu B., Lei M., Yu H., Li Y., Xu H., Wei S., He X., Fang L., Zhang Z.,
RA Zhang Y., Huang X., Su Z., Tong W., Li J., Tong Z., Li S., Ye J., Wang L.,
RA Fang L., Lei T., Chen C.-S., Chen H.-C., Xu Z., Li H., Huang H., Zhang F.,
RA Xu H., Li N., Zhao C., Li S., Dong L., Huang Y., Li L., Xi Y., Qi Q.,
RA Li W., Zhang B., Hu W., Zhang Y., Tian X., Jiao Y., Liang X., Jin J.,
RA Gao L., Zheng W., Hao B., Liu S.-M., Wang W., Yuan L., Cao M.,
RA McDermott J., Samudrala R., Wang J., Wong G.K.-S., Yang H.;
RT "The genomes of Oryza sativa: a history of duplications.";
RL PLoS Biol. 3:266-281(2005).
RN [3]
RP MUTAGENESIS OF N-TERMINAL SERINES.
RX PubMed=1459458; DOI=10.1101/gad.6.12a.2364;
RA Stockhaus J., Nagatani A., Halfter U., Kay S., Furuya M., Chua N.-H.;
RT "Serine-to-alanine substitutions at the amino-terminal region of
RT phytochrome A result in an increase in biological activity.";
RL Genes Dev. 6:2364-2372(1992).
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}.
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; X14172; CAA32375.1; -; Genomic_DNA.
DR EMBL; CM000128; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR PIR; S03728; S03728.
DR AlphaFoldDB; A2XLG5; -.
DR SMR; A2XLG5; -.
DR STRING; 39946.A2XLG5; -.
DR iPTMnet; A2XLG5; -.
DR PRIDE; A2XLG5; -.
DR Proteomes; UP000007015; Chromosome 3.
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 3: Inferred from homology;
KW Chromophore; Photoreceptor protein; Receptor; Reference proteome; Repeat;
KW Sensory transduction; Transcription; Transcription regulation.
FT CHAIN 1..1128
FT /note="Phytochrome A"
FT /id="PRO_0000300859"
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..24
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 1128 AA; 125289 MW; 7DB1823EE704E464 CRC64;
MSSSRPTQCS SSSSRTRQSS RARILAQTTL DAELNAEYEE YGDSFDYSKL VEAQRTTGPE
QQARSEKVIA YLHHIQRAKL IQPFGCLLAL DEKTFNVIAL SENAPEMLTT VSHAVPSVDD
PPKLRIGTNV WSLFTDPGAT ALQKALGFAD VSLLNPILVQ CKTSGKPFYA IVHRATGCLV
VDFEPVKPTE FPATAAGALQ SYKLAAKAIS KIQSLPGGSM EVLCNTVVKE LFDLTGYDRV
MAYKFHEDDH GEVFAEITKP GLEPYLGLHY PATDIPQAAR FLFMKNKVRM ICDCRARSIK
IIEDESLHLD ISLCGSTLRA PHSCHLQYME NMNSIASLVM AVVVNENEDD DEVGADQPAQ
QQKRKKLWGL LVCHHESPRY VPFPLRYACE FLAQVFAVHV NKEFELERQV REKSILRMQT
MLSDMLLRES SPLSIVSGTP NIMDLVKCDG AALLYGGKVW RLQNAPTESQ IRDIAFWLSD
VHRDSTGLST DSLHDAGYPG AAALGDMICG MAVAKINSKD ILFWFRSHTA AEIRWGGAKH
DPSDKDDSRR MHPRLSFKAF LEVVKMKSLP WNDYEMDAIH SLQLILRGTL NDDIKPTRAA
SLDNQVGDLK LDGLAELQAV TSEMVRLMET ATVPILAVDS NGLVNGWNQK VAELTGLRVD
EAIGRHILTV VEESSVPVVQ RMLYLALQGK EEKEVKFEVK THGSKRDDGP VILVVNACAS
RDLHDHVVGV CFVAQDMTVH KLVMDKFTRV EGDYKAIIHN PSPLIPPIFG ADEFGWCSEW
NAAMTKLTGW HRDEVINKML LGEVFDSTNA SCLVKNKDAF VSLCILINSA LAGDETEKAP
FSFFDRNGKY IECLLSVNRK VNADGVITGV FCFIQVPSHE LQHALHVQQA SQQNALTKLK
AYSYMRHAIN NPLSGMLYSR KALKNTGLNE EQMKEVNVAD SCHRQLNKIL SDLDQDSVMN
KSSCLDLEMV EFVLQDVFVA AVSQVLITCQ GKGIRVSCNL PERYMKQTVY GDGVRLQQIL
SDFLFVSVKF SPVGGSVEIS CSLTKNSIGE NLHLIDLELR IKHQGKGVPA DLLSQMYEDD
NKEQSDEGMS LAVSRNLLRL MNGDVRHMRE AGMSTFILSV ELASAPAK
