PHY_ADICA
ID PHY_ADICA Reviewed; 1118 AA.
AC P42496; O80419;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2000, sequence version 2.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=Phytochrome 1;
GN Name=PHY1;
OS Adiantum capillus-veneris (Maidenhair fern).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Polypodiopsida; Polypodiidae; Polypodiales; Pteridineae; Pteridaceae;
OC Vittarioideae; Adiantum.
OX NCBI_TaxID=13818;
RN [1]
RP NUCLEOTIDE SEQUENCE.
RA Okamoto H., Hirano Y., Abe H., Tomizawa K., Furuya M., Wada M.;
RT "The deduced amino sequence of phytochrome from Adiantum includes consensus
RT motifs present in phytochrome B from seed plants.";
RL Plant Cell Physiol. 34:1329-1334(1993).
RN [2]
RP SEQUENCE REVISION TO 28; 93-97; 310; 345 AND 1044.
RA Nozue K., Fukuda S., Kanegae T., Wada M.;
RL Submitted (JUL-1998) to the EMBL/GenBank/DDBJ databases.
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; AB016168; BAA31856.1; -; mRNA.
DR EMBL; AB016151; BAA31710.1; -; Genomic_DNA.
DR AlphaFoldDB; P42496; -.
DR SMR; P42496; -.
DR PRIDE; P42496; -.
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..1118
FT /note="Phytochrome 1"
FT /id="PRO_0000171961"
FT DOMAIN 212..391
FT /note="GAF"
FT DOMAIN 606..677
FT /note="PAS 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00140"
FT DOMAIN 740..811
FT /note="PAS 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00140"
FT DOMAIN 887..1110
FT /note="Histidine kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 317
FT /ligand="phytochromobilin"
FT /ligand_id="ChEBI:CHEBI:189064"
FT /note="covalent, via 1 link"
FT /evidence="ECO:0000250"
SQ SEQUENCE 1118 AA; 123825 MW; 27C218F61F4B9333 CRC64;
MSSTRHSYSS GGSGKSKHGR RIAQTSADAK LYAAYEESSE SGSFDYSQSV SAGKEGISSQ
LVTAYLQRMQ RGGLVQQFGC LIAVEEETFR VLAYGANAPE MLDVATQAVP TMGQYSRLCI
GADVRTLLSP ASASALDRVI GVVDVSMFNP ITVQSRSSGK PFYAILHRND VGLVIDLEPI
RPDDASITGG ALQSHKLAAK AIARLQSLPG GDIGLLCDSV VEEVHELTGF DRVMAYKFHE
DEHGEVVAEI RRTDLEPYIG LHYPATDIPQ AARFLFMKNR VRMICDCRLP PVKLIQDKTL
SQPMSLTGSK LRAPHGCHTQ YMANMNSISS LVMAVIVNDS DDDSPGHSSQ GIKLWGLVVC
HHTSPRYVPF PVRSACEFLM QVFSLQLNME VGMAAQVREK HILRTQTLLC DMLLRDAPIG
IVSQSPNIMD LVTCDGAALY YGKKCWLLGT TPTEAQIVDI AAWLLDCHKD STGLSTDSLA
KTGYPEASCL GDAVCGLAAA KITATDFLFW FRSHTAKEVR WGGARHDPEE RDDGRRMHPR
SSFKAFLEVV KQQSLPWEDV EMDAIHSLQL ILRGSFQDID DSNTKTMIHA RLNDLKLQGL
DELSTVASEM VRLIETATAP ILAVDGQGLI NGWNGKVAEL TGLSFETAMG KSLAKELVHE
ESKTIVERVL HLALEGEEEQ DIEIHLRTYD QHKQKGVVIL IVNTCCSRDV SNNVVGVCFV
GQDVTGQKLV LDRFIRIQGD YKAIVQSLNP LIPPIFGADE YGFCSEWNAA MEKLSNWRRE
EVLGKMLVGE IFGLQMVCCR LQGQDVVTKL MIVLNDAVNG QESEKFPLVF YDRNGRRVEA
LLIASKRTDA DGRITGVFCF LHTASPELLQ ALIIKRAKEK VDKELSYVKE ELKKPLEGLA
FTRTVLEGTN LTIEQRQLIK TNAWCERQLR KILEDDLNNI EEGYMDLEMS EFFMGSVIDA
VISQGMAASR GKGVQILTEI PNDVKLMCLF GDQARLQQVL ADLLFCAINH ATTTNEDEKD
WVTIKVSRTK TRLDDGVHLM HFEFRISHSG QGISEALVEE MTNKSQKWTP EGLAISISCT
LIRLMNGDVK YTTDAGNKCF LVTIQFPLAH RDDATSVR
