ID Q6XFQ0_MAIZE Unreviewed; 1135 AA.
AC Q6XFQ0;
DT 05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2004, sequence version 1.
DT 27-MAR-2024, entry version 136.
DE RecName: Full=Phytochrome {ECO:0000256|PIRNR:PIRNR000084};
GN Name=phyC2 {ECO:0000313|EMBL:AAP06791.1};
GN Synonyms=100192976 {ECO:0000313|EnsemblPlants:Zm00001eb214800_P001};
OS Zea mays (Maize).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC Panicoideae; Andropogonodae; Andropogoneae; Tripsacinae; Zea.
OX NCBI_TaxID=4577 {ECO:0000313|EMBL:AAP06791.1};
RN [1] {ECO:0000313|EMBL:AAP06791.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=15280251; DOI=10.1534/genetics.103.026096;
RA Sheehan M.J., Farmer P.R., Brutnell T.P.;
RT "Structure and expression of maize phytochrome family homeologs.";
RL Genetics 167:1395-1405(2004).
RN [2] {ECO:0000313|EnsemblPlants:Zm00001eb214800_P001, ECO:0000313|Proteomes:UP000007305}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. B73 {ECO:0000313|EnsemblPlants:Zm00001eb214800_P001,
RC ECO:0000313|Proteomes:UP000007305};
RX PubMed=19965430; DOI=10.1126/science.1178534;
RA Schnable P.S., Ware D., Fulton R.S., Stein J.C., Wei F., Pasternak S.,
RA Liang C., Zhang J., Fulton L., Graves T.A., Minx P., Reily A.D.,
RA Courtney L., Kruchowski S.S., Tomlinson C., Strong C., Delehaunty K.,
RA Fronick C., Courtney B., Rock S.M., Belter E., Du F., Kim K., Abbott R.M.,
RA Cotton M., Levy A., Marchetto P., Ochoa K., Jackson S.M., Gillam B.,
RA Chen W., Yan L., Higginbotham J., Cardenas M., Waligorski J., Applebaum E.,
RA Phelps L., Falcone J., Kanchi K., Thane T., Scimone A., Thane N., Henke J.,
RA Wang T., Ruppert J., Shah N., Rotter K., Hodges J., Ingenthron E.,
RA Cordes M., Kohlberg S., Sgro J., Delgado B., Mead K., Chinwalla A.,
RA Leonard S., Crouse K., Collura K., Kudrna D., Currie J., He R.,
RA Angelova A., Rajasekar S., Mueller T., Lomeli R., Scara G., Ko A.,
RA Delaney K., Wissotski M., Lopez G., Campos D., Braidotti M., Ashley E.,
RA Golser W., Kim H., Lee S., Lin J., Dujmic Z., Kim W., Talag J., Zuccolo A.,
RA Fan C., Sebastian A., Kramer M., Spiegel L., Nascimento L., Zutavern T.,
RA Miller B., Ambroise C., Muller S., Spooner W., Narechania A., Ren L.,
RA Wei S., Kumari S., Faga B., Levy M.J., McMahan L., Van Buren P.,
RA Vaughn M.W., Ying K., Yeh C.-T., Emrich S.J., Jia Y., Kalyanaraman A.,
RA Hsia A.-P., Barbazuk W.B., Baucom R.S., Brutnell T.P., Carpita N.C.,
RA Chaparro C., Chia J.-M., Deragon J.-M., Estill J.C., Fu Y., Jeddeloh J.A.,
RA Han Y., Lee H., Li P., Lisch D.R., Liu S., Liu Z., Nagel D.H., McCann M.C.,
RA SanMiguel P., Myers A.M., Nettleton D., Nguyen J., Penning B.W.,
RA Ponnala L., Schneider K.L., Schwartz D.C., Sharma A., Soderlund C.,
RA Springer N.M., Sun Q., Wang H., Waterman M., Westerman R., Wolfgruber T.K.,
RA Yang L., Yu Y., Zhang L., Zhou S., Zhu Q., Bennetzen J.L., Dawe R.K.,
RA Jiang J., Jiang N., Presting G.G., Wessler S.R., Aluru S.,
RA Martienssen R.A., Clifton S.W., McCombie W.R., Wing R.A., Wilson R.K.;
RT "The B73 maize genome: complexity, diversity, and dynamics.";
RL Science 326:1112-1115(2009).
RN [3] {ECO:0000313|EnsemblPlants:Zm00001eb214800_P001}
RP IDENTIFICATION.
RC STRAIN=cv. B73 {ECO:0000313|EnsemblPlants:Zm00001eb214800_P001};
RG EnsemblPlants;
RL Submitted (MAY-2021) 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}.
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; AY234830; AAP06791.1; -; Genomic_DNA.
DR RefSeq; NP_001131622.1; NM_001138150.1.
DR AlphaFoldDB; Q6XFQ0; -.
DR SMR; Q6XFQ0; -.
DR EnsemblPlants; Zm00001eb214800_T001; Zm00001eb214800_P001; Zm00001eb214800.
DR GeneID; 100192976; -.
DR Gramene; Zm00001eb214800_T001; Zm00001eb214800_P001; Zm00001eb214800.
DR KEGG; zma:100192976; -.
DR HOGENOM; CLU_010418_0_0_1; -.
DR OrthoDB; 1770905at2759; -.
DR Proteomes; UP000007305; Chromosome 5.
DR ExpressionAtlas; Q6XFQ0; baseline and differential.
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; 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; 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; 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; SSF55785; PYP-like sensor domain (PAS domain); 3.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50112; PAS; 2.
DR PROSITE; PS50046; PHYTOCHROME_2; 1.
PE 1: Evidence at protein level;
KW Chromophore {ECO:0000256|ARBA:ARBA00022991, ECO:0000256|PIRNR:PIRNR000084};
KW Photoreceptor protein {ECO:0000256|ARBA:ARBA00022543,
KW ECO:0000256|PIRNR:PIRNR000084};
KW Proteomics identification {ECO:0007829|PeptideAtlas:Q6XFQ0};
KW Receptor {ECO:0000256|ARBA:ARBA00023170, ECO:0000256|PIRNR:PIRNR000084};
KW Reference proteome {ECO:0000313|Proteomes:UP000007305};
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 216..389
FT /note="Phytochrome chromophore attachment site"
FT /evidence="ECO:0000259|PROSITE:PS50046"
FT DOMAIN 618..688
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 748..803
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 902..1122
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..23
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 321
FT /ligand="phytochromobilin"
FT /ligand_id="ChEBI:CHEBI:189064"
FT /note="covalent"
FT /evidence="ECO:0000256|PIRSR:PIRSR000084-50"
SQ SEQUENCE 1135 AA; 126071 MW; DB47BC13D197639D CRC64;
MSSPSNNRGT CSRSSSARSK HSARVVAQTP VDAQLHADFE GSQRHFDYSS SVGAANRPSA
STSTVSTYLQ NMQRGRYIQP FGCLLAVHPD TFALLAYSEN APEMLDLTPH AVPTIDQRDA
LTIGADVRTL FRSQSSVALH KAATFGEVNL LNPILVHART SGKPFYAILH RIDVGLVIDL
EPFNPADVPV TAAGALKSYK LAAKAISRLQ SLPSGNLSLL CDVLVREVSE LTGYDRVMAY
KFHEDEHGEV ISECRRSDLE PYLGLHYPAT DIPQASRFLF MKNKMRMICD FSATPVLIIQ
DGSLAQPVSL CGSTLRASHG CHAQYMANMG SVASLVMSVT INDDEEEDGD TDSDQQPKGR
KLWGLVVCHH TSPRFVPFPL RYACEFLLQV FGIQLSKEVE LAAQAKERHI LRTQTLLCDM
LLRDALVGIF TQSPNVMDLV KCDGAALYYQ NQVLVLGSTP SESEIKSIAT WLQENHDGST
GLSTDSLVEA GYPGAAALRE VVCGMVAIKI SSKNFIFWFR SHTTKEIKWS GAKHEPFDAD
DNGRKMHPRS SFKAFLEVVK WRSVPWEDVE MDAIHSLQLI LRDSLQGEDA NRNNIRSIVK
APSDDMKKLQ GLLELRTVTN EMVRLIETAT APVLAVDIAG NINGWNKKAA ELTGLPVMEA
IGRPLIDLVV ADSVEVVKQI LDSALQGIEE QNLEIKLKTF HEQECCGPVI LMINSCCSRD
LSEKVIGVCF VAQDLTRQKM IMDKYTRIQG DYVAIIKNPS ELIPPIFMIN DLGSCLEWNK
AMQKITGMKR EDAINKLLIG EVFTLHDYGC RVKDHATLTK LSILMNAVIS GQDPEKLLFG
FFGTGGKYIE SLLTVNKRTN AEGKITGALC FLHVASPELQ HALEVQKMSE QAATNSFKEL
TYIRQELRNP LNGMQFTYNL LKPSELTEDQ RQLVSSNVLC QDQLKKILHD TDLESIEQCY
METNTVEFNL EEALNTVLMQ GIPLGKEKRI SIERDWPVEV SHMYIYGDNI RLQQVLADYL
ACALQFTQPA EGHIVLQVIP KKENIGSGMQ IAHLEFRIVH PAPGVPEALI QEMFQHNPGV
SREGLGLYIS QKLVKTMSGT LQYLREADTS SFIILIEFPV AQLSSKRSKP SPSKF
//
