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Database: UniProt
Entry: D8T7S3_SELML
LinkDB: D8T7S3_SELML
Original site: D8T7S3_SELML 
ID   D8T7S3_SELML            Unreviewed;      1142 AA.
AC   D8T7S3;
DT   05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2010, sequence version 1.
DT   24-JAN-2024, entry version 85.
DE   RecName: Full=Phytochrome {ECO:0000256|PIRNR:PIRNR000084};
GN   ORFNames=SELMODRAFT_161807 {ECO:0000313|EMBL:EFJ07212.1};
OS   Selaginella moellendorffii (Spikemoss).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Lycopodiopsida; Selaginellales; Selaginellaceae; Selaginella.
OX   NCBI_TaxID=88036 {ECO:0000313|Proteomes:UP000001514};
RN   [1] {ECO:0000313|EMBL:EFJ07212.1, ECO:0000313|Proteomes:UP000001514}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=21551031; DOI=10.1126/science.1203810;
RA   Banks J.A., Nishiyama T., Hasebe M., Bowman J.L., Gribskov M.,
RA   dePamphilis C., Albert V.A., Aono N., Aoyama T., Ambrose B.A., Ashton N.W.,
RA   Axtell M.J., Barker E., Barker M.S., Bennetzen J.L., Bonawitz N.D.,
RA   Chapple C., Cheng C., Correa L.G., Dacre M., DeBarry J., Dreyer I.,
RA   Elias M., Engstrom E.M., Estelle M., Feng L., Finet C., Floyd S.K.,
RA   Frommer W.B., Fujita T., Gramzow L., Gutensohn M., Harholt J., Hattori M.,
RA   Heyl A., Hirai T., Hiwatashi Y., Ishikawa M., Iwata M., Karol K.G.,
RA   Koehler B., Kolukisaoglu U., Kubo M., Kurata T., Lalonde S., Li K., Li Y.,
RA   Litt A., Lyons E., Manning G., Maruyama T., Michael T.P., Mikami K.,
RA   Miyazaki S., Morinaga S., Murata T., Mueller-Roeber B., Nelson D.R.,
RA   Obara M., Oguri Y., Olmstead R.G., Onodera N., Petersen B.L., Pils B.,
RA   Prigge M., Rensing S.A., Riano-Pachon D.M., Roberts A.W., Sato Y.,
RA   Scheller H.V., Schulz B., Schulz C., Shakirov E.V., Shibagaki N.,
RA   Shinohara N., Shippen D.E., Soerensen I., Sotooka R., Sugimoto N.,
RA   Sugita M., Sumikawa N., Tanurdzic M., Theissen G., Ulvskov P., Wakazuki S.,
RA   Weng J.K., Willats W.W., Wipf D., Wolf P.G., Yang L., Zimmer A.D., Zhu Q.,
RA   Mitros T., Hellsten U., Loque D., Otillar R., Salamov A., Schmutz J.,
RA   Shapiro H., Lindquist E., Lucas S., Rokhsar D., Grigoriev I.V.;
RT   "The Selaginella genome identifies genetic changes associated with the
RT   evolution of vascular plants.";
RL   Science 332:960-963(2011).
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   -!- 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; GL377687; EFJ07212.1; -; Genomic_DNA.
DR   RefSeq; XP_002991641.1; XM_002991595.1.
DR   AlphaFoldDB; D8T7S3; -.
DR   STRING; 88036.D8T7S3; -.
DR   EnsemblPlants; EFJ07212; EFJ07212; SELMODRAFT_161807.
DR   GeneID; 9632404; -.
DR   Gramene; EFJ07212; EFJ07212; SELMODRAFT_161807.
DR   KEGG; smo:SELMODRAFT_161807; -.
DR   eggNOG; ENOG502QRNS; Eukaryota.
DR   HOGENOM; CLU_010418_0_0_1; -.
DR   InParanoid; D8T7S3; -.
DR   OMA; FRMACAG; -.
DR   OrthoDB; 1770905at2759; -.
DR   Proteomes; UP000001514; Unassembled WGS sequence.
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; 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; IPR000700; PAS-assoc_C.
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; SSF55785; PYP-like sensor domain (PAS domain); 3.
DR   PROSITE; PS50109; HIS_KIN; 1.
DR   PROSITE; PS50113; PAC; 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:UP000001514};
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..399
FT                   /note="Phytochrome chromophore attachment site"
FT                   /evidence="ECO:0000259|PROSITE:PS50046"
FT   DOMAIN          624..695
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   DOMAIN          698..754
FT                   /note="PAC"
FT                   /evidence="ECO:0000259|PROSITE:PS50113"
FT   DOMAIN          758..810
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   DOMAIN          909..1129
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   BINDING         325
FT                   /ligand="phytochromobilin"
FT                   /ligand_id="ChEBI:CHEBI:189064"
FT                   /note="covalent"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000084-50"
SQ   SEQUENCE   1142 AA;  125452 MW;  5EC9A4C95FFE4CBA CRC64;
     MSTTKLTYSS GSSAKSKHSV RVAQTTADAK LHAVYEESGE SGDSFDYTKS VNATKSTGES
     IPAQAVTAYL QRMQRGGLVQ PFGCMLAVEE GSFRVIAFSD NAGEMLDLMP QSVPSLGAGQ
     QDLLGIGSDA RSLFTPASAS ALEKAAGAID VSMLNPISVH CKTSAKPFYA IVHRIDVGLV
     LDLEPVKASD TSVGSAAGAL QSHKLAAKAI SRLQSLPGGD IGLLCDTVVE EVRELTGYDR
     VMAYKFHDDE HGEVVAEIRR SDLEPYLGLH YPATDIPQAS RFLFMKNRVR MICDCSAAPV
     KISQDKDLRQ PISLAGSTLR APHGCHAQYM GNMGSVASLV MAVIINDNDD EYRSSSGGGG
     GGGAYQQKGR KLWGMVVCHH TSPRSVPFPL RSACEFLMQV FGLQLNMEVE LAAQLREKHI
     LRTQTLLCDM LLRDAPIGIV SQSPNIMDLV KCNGAALYYG KRFWLLGVTP SEAQIKDIAD
     WLLEHHKDST GLSTDSLADA GYPGAASLGD EVCGMAAAKI TAKDFLFWFR SHTAKEIKWG
     GAKHDPDDKD DGRKMHPRSS FKAFLEVVKR RSLPWEDVEM DAIHSLQLIL RGSFHDIDDS
     DTKTMIHARL NDLKLQGMDE LSTVANEMVR LIETATAPIL AVDSSGFING WNAKVAELTG
     LPVTEAMGRS LAKDLVLQES ADMVERLLYL ALQGDEEQNV ELKLKTFGVQ KDKEAVILVV
     NACASRDVSD NVVGVCFVGQ DVTGQKVVMD KFTRIQGDYK AIVQNPNPLI PPIFGADEFG
     YCSEWNPAME KLSGWKREEV LGKMLVGEIF GIQMMYCRLK GQDAVTKFMI VLNSAADGQD
     TEKFPFAFFD RQGKYVEALL TATKRADAEG SITGVFCFLH IASAELQQAL TVQRATEKVA
     LSKLKELAYI RQEIKNPLYG IMFTRTLMET TDLSEDQKQY VETGAVCEKQ IRKILDDMDL
     ESIEDGYLEL DTTEFMMGTV MDAVISQGMI TSKEKNLQLI RETPKEIKAM FLYGDQVRLQ
     QVLADFLLNA IRFTPSSENW VGIKVATSRK RLGGGVHVMH LEFRITHPGV GLPEELVQEM
     FDRGRGMTQE GLGLSMCRKL VKLMNGEVEY LREPGKNFFL VSLELPLAQR DDAGSVKFQA
     SS
//
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