ID A0A3B6HUE1_WHEAT Unreviewed; 1166 AA.
AC A0A3B6HUE1;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=Phytochrome {ECO:0000256|PIRNR:PIRNR000084};
GN ORFNames=CFC21_052021 {ECO:0000313|EMBL:KAF7042405.1};
OS Triticum aestivum (Wheat).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Pooideae; Triticodae; Triticeae; Triticinae; Triticum.
OX NCBI_TaxID=4565 {ECO:0000313|EnsemblPlants:TraesCS4A02G122500.2};
RN [1] {ECO:0000313|EMBL:KAF7042405.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Leaf {ECO:0000313|EMBL:KAF7042405.1};
RX PubMed=29069494;
RA Zimin A.V., Puiu D., Hall R., Kingan S., Clavijo B.J., Salzberg S.L.;
RT "The first near-complete assembly of the hexaploid bread wheat genome,
RT Triticum aestivum.";
RL Gigascience 6:1-7(2017).
RN [2] {ECO:0000313|EnsemblPlants:TraesCS4A02G122500.2}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Chinese Spring
RC {ECO:0000313|EnsemblPlants:TraesCS4A02G122500.2};
RX PubMed=30115783; DOI=10.1126/science.aar7191;
RG International wheat genome sequencing consortium (IWGSC);
RT "Shifting the limits in wheat research and breeding using a fully annotated
RT reference genome.";
RL Science 361:EAAR7191-EAAR7191(2018).
RN [3] {ECO:0000313|EnsemblPlants:TraesCS4A02G122500.2}
RP IDENTIFICATION.
RG EnsemblPlants;
RL Submitted (OCT-2018) to UniProtKB.
RN [4] {ECO:0000313|EMBL:KAF7042405.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Leaf {ECO:0000313|EMBL:KAF7042405.1};
RA Zimin A.V., Puiu D., Shumante A., Alonge M., Salzberg S.L.;
RT "The second near-complete assembly of the hexaploid bread wheat (Triticum
RT aestivum) genome.";
RL Submitted (MAR-2020) 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. {ECO:0000256|ARBA:ARBA00002479}.
CC -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}.
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, ECO:0000256|PIRNR:PIRNR000084}.
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; CM022220; KAF7042405.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3B6HUE1; -.
DR SMR; A0A3B6HUE1; -.
DR STRING; 4565.A0A3B6HUE1; -.
DR PaxDb; 4565-Traes_4AS_1F3163292-1; -.
DR EnsemblPlants; TraesCS4A02G122500.2; TraesCS4A02G122500.2; TraesCS4A02G122500.
DR Gramene; TraesCS4A02G122500.2; TraesCS4A02G122500.2; TraesCS4A02G122500.
DR Gramene; TraesCS4A03G0251700.2; TraesCS4A03G0251700.2.CDS; TraesCS4A03G0251700.
DR Gramene; TraesKAR4A01G0093550.1; cds.TraesKAR4A01G0093550.1; TraesKAR4A01G0093550.
DR Gramene; TraesRN4A0100254500.2; TraesRN4A0100254500.2; TraesRN4A0100254500.
DR Gramene; TraesRN4B0100534400.1; TraesRN4B0100534400.1; TraesRN4B0100534400.
DR OrthoDB; 1770905at2759; -.
DR Proteomes; UP000019116; Chromosome 4A.
DR Proteomes; UP000815260; Chromosome 4A.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
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; cd16932; HATPase_Phy-like; 1.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd00130; PAS; 2.
DR Gene3D; 1.10.287.130; -; 1.
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; IPR036097; HisK_dim/P_sf.
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_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; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
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|PIRNR:PIRNR000084};
KW Photoreceptor protein {ECO:0000256|ARBA:ARBA00022543,
KW ECO:0000256|PIRNR:PIRNR000084};
KW Receptor {ECO:0000256|ARBA:ARBA00023170, ECO:0000256|PIRNR:PIRNR000084};
KW Reference proteome {ECO:0000313|Proteomes:UP000019116};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Sensory transduction {ECO:0000256|ARBA:ARBA00022606,
KW ECO:0000256|PIRNR:PIRNR000084};
KW Transcription {ECO:0000256|ARBA:ARBA00023163,
KW ECO:0000256|PIRNR:PIRNR000084};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015,
KW ECO:0000256|PIRNR:PIRNR000084}.
FT DOMAIN 254..427
FT /note="Phytochrome chromophore attachment site"
FT /evidence="ECO:0000259|PROSITE:PS50046"
FT DOMAIN 656..727
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 790..842
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 938..1158
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT REGION 1..48
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..35
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 359
FT /ligand="phytochromobilin"
FT /ligand_id="ChEBI:CHEBI:189064"
FT /note="covalent"
FT /evidence="ECO:0000256|PIRSR:PIRSR000084-50"
SQ SEQUENCE 1166 AA; 127680 MW; E8C4359DFDFFB203 CRC64;
MASGSRATPT RSPSSARPAA PHQNHTQSSG GSTSRAGGGG GGAAGSAAAT ESVSKAVAQY
TLDAGLHAVF EQSGASGRSF DYSQSLLAPP TPSSEQQIAA YLSRIQRGGH IQPFGCTLAV
ADDSSFRLLA FSENAADLLD LSPHHSVPSL DSSAAPPPVS LGADARLLFS PSSGVLLERA
FAAREISLLN PLWIHSRVSS KPFYAILHRI DVGVVIDLEP ARTEDPALSI AGAVQSQKLA
VRAISRLQAL PGGDVKLLCD TVVEHVRELT GYDRVMVYKF HDDEHGEVLA ESRRGDLEPY
LGLHYPATDI PQASRFLFRQ NRVRMIADCH AAAVRVIQDP AMPQPLCLVG STLRSPHGCH
AQYMANMGSI ASLVMAVIIS SGGEDEHNMT RGVIPSAMKL WGLVVCHHTS PRCIPFPLRY
ACEFLMQAFG LQLNMELQLA HQLSEKHILR TQTLLCDMLL RDSPTGIVTQ SPSIMDLVKC
DGAALFYHGK YYPLGVTPTE AQIKDIIEWL TVCHGDSTGL STDSLADAGY PGATALGDAV
CGMAVAYITP SDYLFWFRSH TAKEIKWGGA KHHPEDKDDG QRMHPRSSFK AFLEVVKSRS
LPWENAEMDA IHSLQLILRD SFRDAGEGTS NSKAIVNGQV QLGELELRGI DELSSVAREM
VRLIETATVP IFAVDTYGCI NGWNAKVAEL TGLTVEEAMG KSLVKDLIFK ESEEIVEKLL
SQALKGEEGT NVEIKLKTFG SEQSKGPIFV IVNACSSRDY TKSIVGVCFV GQDITGQKVV
MDKFVNIQGD YKAIVHNPNP LIPPIFASDE NICCSEWNTA MEKLTGWSRG EVVGKLLVGE
VFGNCCRLKG PDALTKFMIV LHNAIGGQDS EKSPFSFFDK NGKYVQALLT ANTRSKMDGE
TIGAFCFLQI ASPELQQAFE IQRQQEKKCY ARMKELAYIC QEIKNPLSGI RFTNSLLEMT
DLKDDQRQFL ETSAACEKQM SKIVKDASLQ SIEDGSLVLE KGEFSLGNVM NAVVSQVMIL
LRERDLQLIR DIPDEIKEAS AYGDQYRIQQ VLSDFLLSMV RFAPTENGWV EIQVRPNVKQ
NSDGTETMLF LFRFACPGEG LPPDIVQDMF SNARWTTQEG IGLSVCRKIL KLMGGEVQYI
RESERSFFLI VLELPQPLRS ESRDRS
//