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Database: UniProt
Entry: Q6XFQ2_MAIZE
LinkDB: Q6XFQ2_MAIZE
Original site: Q6XFQ2_MAIZE 
ID   Q6XFQ2_MAIZE            Unreviewed;      1166 AA.
AC   Q6XFQ2;
DT   05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2004, sequence version 1.
DT   27-MAR-2024, entry version 147.
DE   RecName: Full=Phytochrome {ECO:0000256|PIRNR:PIRNR000084};
GN   Name=phyB2 {ECO:0000313|EMBL:AAP06789.1};
GN   Synonyms=100381811 {ECO:0000313|EnsemblPlants:Zm00001eb396030_P001};
GN   ORFNames=ZEAMMB73_Zm00001d047632 {ECO:0000313|EMBL:AQL07142.1};
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:AAP06789.1};
RN   [1] {ECO:0000313|EMBL:AAP06789.1}
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:Zm00001eb396030_P001, ECO:0000313|Proteomes:UP000007305}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. B73 {ECO:0000313|EnsemblPlants:Zm00001eb396030_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|EMBL:AQL07142.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Seedling {ECO:0000313|EMBL:AQL07142.1};
RG   Maize Genome Sequencing Project;
RA   Ware D.;
RT   "Update maize B73 reference genome by single molecule sequencing
RT   technologies.";
RL   Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases.
RN   [4] {ECO:0000313|EnsemblPlants:Zm00001eb396030_P001}
RP   IDENTIFICATION.
RC   STRAIN=cv. B73 {ECO:0000313|EnsemblPlants:Zm00001eb396030_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}.
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DR   EMBL; AY234828; AAP06789.1; -; Genomic_DNA.
DR   EMBL; CM000785; AQL07142.1; -; Genomic_DNA.
DR   RefSeq; NP_001168077.1; NM_001174606.1.
DR   AlphaFoldDB; Q6XFQ2; -.
DR   SMR; Q6XFQ2; -.
DR   IntAct; Q6XFQ2; 5.
DR   STRING; 4577.Q6XFQ2; -.
DR   PaxDb; 4577-GRMZM2G092174_P01; -.
DR   EnsemblPlants; Zm00001eb396030_T001; Zm00001eb396030_P001; Zm00001eb396030.
DR   GeneID; 100381811; -.
DR   Gramene; Zm00001eb396030_T001; Zm00001eb396030_P001; Zm00001eb396030.
DR   KEGG; zma:100381811; -.
DR   eggNOG; ENOG502QRNS; Eukaryota.
DR   HOGENOM; CLU_010418_0_0_1; -.
DR   InParanoid; Q6XFQ2; -.
DR   OrthoDB; 1770905at2759; -.
DR   Proteomes; UP000007305; Chromosome 9.
DR   ExpressionAtlas; Q6XFQ2; baseline and differential.
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; 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; 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; 2.
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   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:Q6XFQ2};
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          252..424
FT                   /note="Phytochrome chromophore attachment site"
FT                   /evidence="ECO:0000259|PROSITE:PS50046"
FT   DOMAIN          653..724
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   DOMAIN          787..839
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   DOMAIN          935..1155
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        13..27
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         357
FT                   /ligand="phytochromobilin"
FT                   /ligand_id="ChEBI:CHEBI:189064"
FT                   /note="covalent"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000084-50"
SQ   SEQUENCE   1166 AA;  128300 MW;  5B89C21E3B68EAE0 CRC64;
     MASDSRPPKR SPSARRVAPR HAHHHHSQSS GGSTSRAGAG GGGGGAAATE SVSKAVAQYN
     LDARLHAVFE QSGASGRSFD YSQSLRAPPT PSSEQQIAAY LSRIQRGGHI QPLGCTLAVA
     DDSSFRLLAF SENAADLLDL SPHHSVPSLD SVALPPVSLG ADARLYFSPS SAVLLERAFA
     AREISLLNPL WIHSRASSKP FYAILHRIDV GVVIDLEPAR TEDPALSIAG AVQSQKLAVR
     AISRLQALPG GDVKLLCDTV VEHVRELTGY DRVMVYKFHE DEHGEVVAES RRDNLEPYLG
     LHYPATDIPQ ASRFLFQQNR VRMIADCHAI PVRVIQDPGL SQQLCLVGST LRAPHGCHAQ
     YMANMGSIAS LVMAVIISSG GDDERTGRGA ISSSMKLWGL VVCHHTSPRC IPFPLRYACE
     FLMQAFGLQL NMELQLAHQL SEKHILRTQT LLCDMLLRDS PAGIITQSPS VMDLVKCDGA
     ALYYRGKYYP LGVTPTESQI KDIIEWLTVC HGDSTGLSTD SLADAGYLGA VALGDAVCGM
     AVAYITPSDY LFWFRSHTAK EIKWGGAKHH PEDKDDGQRM HPRSSFKAFL EVVKSRSLSW
     ENAEMDAIHS LQLILRDSFR DAAEGTSNSK AIVNGQRQLG ELELRGINEL SSVAREMVRL
     IETATVPIFA VDTDGCINGW NAKIAELTGL SVEEAMGKSL VNDLIFKECD DIVEKLLSRA
     LRGEEDKNVE IKLKTFGSEQ SKGAIFVIVN ACSSRDYTQN IVGVCFVGQD VTGQKVVMDK
     FINIQGDYKA IVHNPNPLLP PIFASDENTS CSEWNTAMEK LTGWSREEVV GKFLIGEVFG
     NCCRLKGPDA LTKFMVVIHN AIEGHDSEKF PFSFFDKNGK YVQALLTANT RSKMDGKSIG
     AFCFLQIASA EIQQAFEIQR QQEKKCYARM KELAYICQEI KNPLSGIRFT NSLLQMTDLN
     DDQRQFLETS SACEKQMSKI VKDASLKSIE DGSLVLEKSE FSLGDVMNAV VSQTMSLLRE
     RDLQLIRDIP DEIKDASAYG DQFRIQQVLA DFLLSMAQSA PSENGWVEIQ VRPNVKQNYD
     GTDTELFIFR FACPGEGLPA DIVQDMFSNS QWSTQEGVGL STCRKILKLM GGEVQYIRES
     ERSFFLIVLE LPQPRLAAGR ENQLIC
//
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