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Database: UniProt
Entry: A0A1R3GK68_9ROSI
LinkDB: A0A1R3GK68_9ROSI
Original site: A0A1R3GK68_9ROSI 
ID   A0A1R3GK68_9ROSI        Unreviewed;      1124 AA.
AC   A0A1R3GK68;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   27-MAR-2024, entry version 34.
DE   RecName: Full=Phytochrome {ECO:0000256|PIRNR:PIRNR000084};
GN   ORFNames=COLO4_34612 {ECO:0000313|EMBL:OMO58495.1};
OS   Corchorus olitorius.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Malvales; Malvaceae; Grewioideae; Apeibeae; Corchorus.
OX   NCBI_TaxID=93759 {ECO:0000313|EMBL:OMO58495.1, ECO:0000313|Proteomes:UP000187203};
RN   [1] {ECO:0000313|Proteomes:UP000187203}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. O-4 {ECO:0000313|Proteomes:UP000187203};
RA   Alam M., Haque M.S., Islam M.S., Emdad E.M., Islam M.M., Ahmed B.,
RA   Halim A., Hossen Q.M.M., Hossain M.Z., Ahmed R., Khan M.M., Islam R.,
RA   Rashid M.M., Khan S.A., Rahman M.S., Alam M., Yahiya A.S., Khan M.S.,
RA   Azam M.S., Haque T., Lashkar M.Z.H., Akhand A.I., Morshed G., Roy S.,
RA   Uddin K.S., Rabeya T., Hossain A.S., Chowdhury A., Snigdha A.R.,
RA   Mortoza M.S., Matin S.A., Hoque S.M.E., Islam M.K., Roy D.K., Haider R.,
RA   Moosa M.M., Elias S.M., Hasan A.M., Jahan S., Shafiuddin M., Mahmood N.,
RA   Shommy N.S.;
RT   "Corchorus olitorius genome sequencing.";
RL   Submitted (SEP-2013) 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   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:OMO58495.1}.
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DR   EMBL; AWUE01022414; OMO58495.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1R3GK68; -.
DR   STRING; 93759.A0A1R3GK68; -.
DR   OrthoDB; 1770905at2759; -.
DR   Proteomes; UP000187203; Unassembled WGS sequence.
DR   GO; GO:0043231; C:intracellular membrane-bounded organelle; IEA:UniProt.
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:UP000187203};
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          220..388
FT                   /note="Phytochrome chromophore attachment site"
FT                   /evidence="ECO:0000259|PROSITE:PS50046"
FT   DOMAIN          613..684
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   DOMAIN          747..799
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   DOMAIN          895..1091
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   REGION          1..20
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         325
FT                   /ligand="phytochromobilin"
FT                   /ligand_id="ChEBI:CHEBI:189064"
FT                   /note="covalent"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000084-50"
SQ   SEQUENCE   1124 AA;  125065 MW;  F22A1091497CA05C CRC64;
     MRAFHGHAAG QAHHQPLHHQ AESISKAIAQ YTVDARLHAV FEQSGESGKS FDYSQSVKTT
     TQSVPEQQIT AYLSKIQRGG HIQPFGCMIA VDEPSFRVIA YSENAREMLG ITPQSVPNLE
     KIEVLTIGTD VRTLFTPSSI ILLEKAFGAR EITLLNPVWI HSKNSGKPFY AILHRIDVGI
     VIDLEPARTE DPALSIAGAV QSQKLAVRAI SQLQSLPGGD IKLLCDTVVE SVRELTGYDR
     VMVYKFHEDE HGEVVAESKR PDLDPYIGLH YPATDIPQAS RFLFKQNRVR MIVDCHATPV
     RVIQDDGLMQ PLCLVGSTLR APHGCHAQYM ANMGSIASLA MAVIINGNDE EAIGGRNSMR
     LWGLVVCHHT SARCIPFPLR YACEFLMQAF GLQLNMELQL GSQMSEKRVL RTQTLLCDML
     LRDSPTGIVT QSPSIMDLVK CDGAALYYQG KYYPLGVTPA EAQIKDIVEW LLAFHGDSTG
     LSTDSLADAG YPGAASLGDA VCGMAVAYIT KRDFLFWFRS HTAKEIKWGG AKHHPEDKDD
     GQRMHPRSSF KAFLEVVKSR SLPWENAEMD AIHSLQLILR DSFKDAEASN SKAVVHAHLG
     ELELQGVDEL SSVAREMVRL IETATAPIFA VDVEGRINGW NAKVAELTGL SVEEAMGKSL
     VHDLVYKEYQ ETVDKLLSRA LQGEEDKNVE IKLRTIGSED TKKAIYVVVN ACSSKDYTNN
     IVGVCFVGQD VTGQKVVMDK FIHIQGDYKA IVHSPNPLIP PIFASDENTC CLEWNTAMEK
     LTGWSRGEII GKLLVGEVFG SCCRLKGPDA LTKFMIVLHS AIGGQEADKF PFSFFDRNGK
     FVQALLTANK RVNMEGQVVG AFCFLQIASA ELQQALKVQR QQEKKCFARM KELTYICQEI
     KSPLSGIRFT NSLLEATELT EDQKQFLETS AACEKQMLKI IRDVDLEIIE DGSMELEKAE
     FYLGSVINAV VSQVMLLLRE RNLQLIRDIP EEIKTLAVYG DQARIQQVLA DFLLNMVRYA
     PSAEGWVEIH VRPALKRISD GLTTARTEFR MVCPGEGLPP ELVQDMFHSS RWMTQEGLGL
     SMCRKILKLM NVVKDHNDAD CTALYELYSV IQQAELNIDN YRML
//
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