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Database: UniProt
Entry: R0HWE8_9BRAS
LinkDB: R0HWE8_9BRAS
Original site: R0HWE8_9BRAS 
ID   R0HWE8_9BRAS            Unreviewed;      1162 AA.
AC   R0HWE8;
DT   26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT   26-JUN-2013, sequence version 1.
DT   24-JAN-2024, entry version 57.
DE   RecName: Full=Phytochrome {ECO:0000256|PIRNR:PIRNR000084};
GN   ORFNames=CARUB_v10012844mg {ECO:0000313|EMBL:EOA29755.1};
OS   Capsella rubella.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Camelineae; Capsella.
OX   NCBI_TaxID=81985 {ECO:0000313|EMBL:EOA29755.1, ECO:0000313|Proteomes:UP000029121};
RN   [1] {ECO:0000313|Proteomes:UP000029121}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Monte Gargano {ECO:0000313|Proteomes:UP000029121};
RX   PubMed=23749190; DOI=10.1038/ng.2669;
RA   Slotte T., Hazzouri K.M., Agren J.A., Koenig D., Maumus F., Guo Y.L.,
RA   Steige K., Platts A.E., Escobar J.S., Newman L.K., Wang W., Mandakova T.,
RA   Vello E., Smith L.M., Henz S.R., Steffen J., Takuno S., Brandvain Y.,
RA   Coop G., Andolfatto P., Hu T.T., Blanchette M., Clark R.M., Quesneville H.,
RA   Nordborg M., Gaut B.S., Lysak M.A., Jenkins J., Grimwood J., Chapman J.,
RA   Prochnik S., Shu S., Rokhsar D., Schmutz J., Weigel D., Wright S.I.;
RT   "The Capsella rubella genome and the genomic consequences of rapid mating
RT   system evolution.";
RL   Nat. Genet. 45:831-835(2013).
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.
CC       {ECO:0000256|PIRNR:PIRNR000084}.
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; KB870807; EOA29755.1; -; Genomic_DNA.
DR   RefSeq; XP_006296857.1; XM_006296795.1.
DR   AlphaFoldDB; R0HWE8; -.
DR   STRING; 81985.R0HWE8; -.
DR   GeneID; 17893021; -.
DR   KEGG; crb:17893021; -.
DR   eggNOG; ENOG502QRNS; Eukaryota.
DR   OrthoDB; 1770905at2759; -.
DR   Proteomes; UP000029121; 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; 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; 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; 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:UP000029121};
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          242..413
FT                   /note="Phytochrome chromophore attachment site"
FT                   /evidence="ECO:0000259|PROSITE:PS50046"
FT   DOMAIN          642..713
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   DOMAIN          776..828
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   DOMAIN          924..1143
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   REGION          1..44
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        15..44
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         347
FT                   /ligand="phytochromobilin"
FT                   /ligand_id="ChEBI:CHEBI:189064"
FT                   /note="covalent"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000084-50"
SQ   SEQUENCE   1162 AA;  128253 MW;  2B521326AF7A7634 CRC64;
     MASGGSGGGR VGEGAASSSR TTNNRRGEQA QSSGTKSLRP QESVSKAIQQ YTVDARLHAV
     FEQSGESGKS FDYSQSLKTT TYGSSVPEQQ ITAYLSRIQR GGYIQPFGCM IAVDESSFGI
     IGYSQNAREM LGLMPQSVPS LEKPEILAMG TDVRSLFTSS SSILLERAFV AREITLLNPV
     WIHSKYTGKP FYAILHRIDV GVVIDLEPAR TEDPALSIAG AVQSQKLAVR AISQLQALPG
     GDIKLLCDTV VESVRDLTGY DRVMVYKFHE DEHGEVVAES KRDDLEPYIG LHYPATDIPQ
     ASRFLFKQNR VRMIVDCHAT PVLVVQDDRL TQSMCLVGST LRAPHGCHSQ YMANMGSIAS
     LAMAVIINGN EEDGSNVASG RSSMRLWGLV VCHHTSSRCI PFPLRYACEF LMQAFGLQLN
     MELQLALQMS EKRVLRTQTL LCDMLLRDSP AGIVTQSPSI MDLVKCDGAA FLYHGKYYPL
     GVAPSEVQIK YVVEWLLANH ADSTGLSTDS LGDAGYPGAA ALGDAVCGMA VAYITKRDFL
     FWFRSHTAKE IKWGGAKHHP EDKDDGQRMH PRSSFKAFLE VVKSRSQPWE TAEMDAIHSL
     QLILRDSFKE SEAAMNSKTG DGVVQPYRDM AGEQGIDELG AVAREMVRLI ETATVPIFAV
     DAGGCINGWN AKIAELTGLS VEEAMGKSLV SDLIYKENEE TVNKLLSRAL RGDEDKNVEV
     KLKTFTPELQ GKAVFVVVNA CSSKDYLNNI VGVCFVGQDV TGQKIVMDKF INIQGDYKAI
     VHSPNPLIPP IFAADENTCC LEWNTAMEKL TGWSRSEVVG KMLVGEVFGS CCKLKGPDAL
     TKFMIVLHNA IGGQETDKFP FPFFDRDGKF VQALLTANKR VSLEGKVIGA FCFLQIPSPE
     LQQALAVQRR QDTECFAKAK ELAYICQVIK NPLSGMRFAN SLLEATDLNE DQKQFLETSV
     SCEKQISRIV GDMDLESIED GSFELKRAEF FLGSVINAIV SQAMFLLRDR GLQLIRDIPE
     EIKSIAVYGD QIRIQQLLAE FLLSIIRYAP SQEWVEIHLS QVSKQMADGF TAIRTEFRMA
     CPGEGLPPEL VRDMFHSSRW TSPEGLGLSV CRKILKLMNG EVQYIRESER SYFLIILELP
     GPRKRPLSTA SGSGDMMLMM PY
//
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