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Database: UniProt
Entry: A0A3B6HUE1_WHEAT
LinkDB: A0A3B6HUE1_WHEAT
Original site: A0A3B6HUE1_WHEAT 
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}.
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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
//
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