PHYA3_AVESA
ID PHYA3_AVESA Reviewed; 1129 AA.
AC P06593;
DT 01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=Phytochrome A type 3;
DE Short=AP3;
GN Name=PHYA3; Synonyms=PHY3;
OS Avena sativa (Oat).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Pooideae; Poodae; Poeae; Aveninae; Avena.
OX NCBI_TaxID=4498;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=3001642; DOI=10.1093/nar/13.23.8543;
RA Hershey H.P., Barker R.F., Idler K.B., Lissemore J.L., Quail P.H.;
RT "Analysis of cloned cDNA and genomic sequences for phytochrome: complete
RT amino acid sequences for two gene products expressed in etiolated Avena.";
RL Nucleic Acids Res. 13:8543-8559(1985).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2965664; DOI=10.1016/0378-1119(87)90197-1;
RA Hershey H.P., Barker R.F., Idler K.B., Murray M.G., Quail P.H.;
RT "Nucleotide sequence and characterization of a gene encoding the
RT phytochrome polypeptide from Avena.";
RL Gene 61:339-348(1987).
RN [3]
RP PROTEIN SEQUENCE OF 2-13.
RA Grimm R., Kellermann J., Schaefer W., Ruediger W.;
RT "The amino-terminal structure of oat phytochrome.";
RL FEBS Lett. 234:497-499(1988).
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 -!- INTERACTION:
CC P06593; Q43125: CRY1; Xeno; NbExp=2; IntAct=EBI-630413, EBI-300703;
CC -!- PTM: Contains one covalently linked phytochromobilin chromophore.
CC -!- SIMILARITY: Belongs to the phytochrome family. {ECO:0000305}.
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DR EMBL; X03242; CAA26999.1; -; mRNA.
DR EMBL; M18822; AAA76820.1; -; Genomic_DNA.
DR PIR; A29631; A29631.
DR AlphaFoldDB; P06593; -.
DR SMR; P06593; -.
DR IntAct; P06593; 2.
DR iPTMnet; P06593; -.
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; cd16932; HATPase_Phy-like; 1.
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; 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; 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 1: Evidence at protein level;
KW Chromophore; Direct protein sequencing; Photoreceptor protein; Receptor;
KW Repeat; Sensory transduction; Transcription; Transcription regulation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|Ref.3"
FT CHAIN 2..1129
FT /note="Phytochrome A type 3"
FT /id="PRO_0000171967"
FT DOMAIN 217..402
FT /note="GAF"
FT DOMAIN 618..688
FT /note="PAS 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00140"
FT DOMAIN 748..822
FT /note="PAS 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00140"
FT DOMAIN 902..1122
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 322
FT /ligand="phytochromobilin"
FT /ligand_id="ChEBI:CHEBI:189064"
FT /note="covalent, via 1 link"
FT CONFLICT 279
FT /note="L -> F (in Ref. 2; AAA76820)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1129 AA; 124993 MW; 8AC1083533567ACF CRC64;
MSSSRPASSS SSRNRQSSQA RVLAQTTLDA ELNAEYEESG DSFDYSKLVE AQRDGPPVQQ
GRSEKVIAYL QHIQKGKLIQ TFGCLLALDE KSFNVIAFSE NAPEMLTTVS HAVPSVDDPP
RLGIGTNVRS LFSDQGATAL HKALGFADVS LLNPILVQCK TSGKPFYAIV HRATGCLVVD
FEPVKPTEFP ATAAGALQSY KLAAKAISKI QSLPGGSMEV LCNTVVKEVF DLTGYDRVMA
YKFHEDDHGE VFSEITKPGL EPYLGLHYPA TDIPQAARLL FMKNKVRMIC DCRARSIKVI
EAEALPFDIS LCGSALRAPH SCHLQYMENM NSIASLVMAV VVNENEEDDE AESEQPAQQQ
KKKKLWGLLV CHHESPRYVP FPLRYACEFL AQVFAVHVNR EFELEKQLRE KNILKMQTML
SDMLFREASP LTIVSGTPNI MDLVKCDGAA LLYGGKVWRL RNAPTESQIH DIAFWLSDVH
RDSTGLSTDS LHDAGYPGAA ALGDMICGMA VAKINSKDIL FWFRSHTAAE IRWGGAKNDP
SDMDDSRRMH PRLSFKAFLE VVKMKSLPWS DYEMDAIHSL QLILRGTLND ASKPKREASL
DNQIGDLKLD GLAELQAVTS EMVRLMETAT VPILAVDGNG LVNGWNQKAA ELTGLRVDDA
IGRHILTLVE DSSVPVVQRM LYLALQGKEE KEVRFEVKTH GPKRDDGPVI LVVNACASRD
LHDHVVGVCF VAQDMTVHKL VMDKFTRVEG DYKAIIHNPN PLIPPIFGAD EFGWCSEWNA
AMTKLTGWNR DEVLDKMLLG EVFDSSNASC PLKNRDAFVS LCVLINSALA GEETEKAPFG
FFDRSGKYIE CLLSANRKEN EGGLITGVFC FIHVASHELQ HALQVQQASE QTSLKRLKAF
SYMRHAINNP LSGMLYSRKA LKNTDLNEEQ MKQIHVGDNC HHQINKILAD LDQDSITEKS
SCLDLEMAEF LLQDVVVAAV SQVLITCQGK GIRISCNLPE RFMKQSVYGD GVRLQQILSD
FLFISVKFSP VGGSVEISSK LTKNSIGENL HLIDLELRIK HQGLGVPAEL MAQMFEEDNK
EQSEEGLSLL VSRNLLRLMN GDVRHLREAG VSTFIITAEL ASAPTAMGQ
