ID A0A0D9Z690_9ORYZ Unreviewed; 1129 AA.
AC A0A0D9Z690;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 24-JAN-2024, entry version 42.
DE RecName: Full=Phytochrome {ECO:0000256|PIRNR:PIRNR000084};
OS Oryza glumipatula.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza.
OX NCBI_TaxID=40148 {ECO:0000313|EnsemblPlants:OGLUM03G14900.1};
RN [1] {ECO:0000313|EnsemblPlants:OGLUM03G14900.1}
RP NUCLEOTIDE SEQUENCE.
RA Wing R.A., Panaud O., Oliveira A.C.;
RT "Oryza genome evolution.";
RL Submitted (AUG-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblPlants:OGLUM03G14900.1}
RP IDENTIFICATION.
RG EnsemblPlants;
RL Submitted (APR-2015) to UniProtKB.
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 AlphaFoldDB; A0A0D9Z690; -.
DR EnsemblPlants; OGLUM03G14900.1; OGLUM03G14900.1; OGLUM03G14900.
DR Gramene; OGLUM03G14900.1; OGLUM03G14900.1; OGLUM03G14900.
DR Proteomes; UP000026961; Unassembled WGS sequence.
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; 4.
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; 2.
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:UP000026961};
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 245..390
FT /note="Phytochrome chromophore attachment site"
FT /evidence="ECO:0000259|PROSITE:PS50046"
FT DOMAIN 619..690
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 753..805
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 901..1119
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT REGION 1..53
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..17
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 322
FT /ligand="phytochromobilin"
FT /ligand_id="ChEBI:CHEBI:189064"
FT /note="covalent"
FT /evidence="ECO:0000256|PIRSR:PIRSR000084-50"
SQ SEQUENCE 1129 AA; 123580 MW; 433A21853BC1D542 CRC64;
MASGSRATPT RSPSSARPAA PRHQHHHSQS SGGSTSRAGG GGGGGGGGGG GAAAAESVSK
AVAQYTLDAR LHAVFEQSGA SGRSFDYTQS LRASPTPSSE QQIAAYLSRI QRGGHIQPFG
CTLAVADDSS FRLLAYSENA ADLLDLSPHH SVPSLDSSAV PPPVSLGADA RLLFAPSSAV
LLERAFAARE ISLLNPLWIH SRVSSKPFYA ILHRIDVGVV IDLEPARTED PALSIAGAVQ
SQKLADEHGE VVAESRRSNL EPYIGLHYPA TDIPQASRFL FRQNRVRMIA DCHAAPVRVI
QDPALTQPLC LVGSTLRAPH GCHAQYMANM GSIASLVMAV IISSGGDDDH NIARGSILSA
MKLWGLVVCH HTSPRCIPFP LRYACEFLMQ AFGLQLNMEL QLAHQLSEKH ILRTQTLLCD
MLLRDSPTGI VTQSPSIMDL VKCDGAALYY HGKYYPLGVT PTEVQIKDII EWLTMCHGDS
TGLSTDSLAD AGYPGAAALG DAVSGMAVAY ITPSDYLFWF RSHTAKEIKW GGAKHHPEDK
DDGQRMHPRS SFKAFLEVVK SRSLPWENAE MDAIHSLQLI LRDSFRDSAE GTSNSKAIVN
GQVHLGELEL RGIDELSSVA REMVRLIETA TVPIFAVDTD GCINGWNAKV AELTGLSVEE
AMGKSLVNDL IFKESEETVD KLLSRALRGD EDKNVEIKLK TFGPEQSKGP IFVIVNACSS
RDYTKNIVGV CFVGQDVTGQ KVVMDKFINI QGDYKAIVHN PNPLIPPIFA SDENTCCSEW
NTAMEKLTGW SRGEVVGKLL VGEVFGNCCR LKGPDALTKF MIVLHNAIGG QDCEKFPFSF
FDKNGKYVQA LLTANTRSRM DGEAIGAFCF LQIASPELQQ AFEIQRHHEK KCYARMKELA
YIYQEIKNPL NGIRFTNSLL EMTDLKDDQR QFLETSTACE KQMSKIVKDA SLQSIEDGSL
VLEKGEFSLG SVMNAVVSQV MIQLRERDLQ LIRDIPDEIK EASAYGDQYR IQQVLCDFLL
SMVRFAPAEN GWVEIQVRPN IKQNSDGTDT MLFLFRFACP GEGLPPEIVQ DMFSNSRWTT
QEGIGLSICR KILKLMGGEV QYIRESERSF FHIVLELPQP QQAASRGTS
//
