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Database: UniProt
Entry: A0A061GL48_THECC
LinkDB: A0A061GL48_THECC
Original site: A0A061GL48_THECC 
ID   A0A061GL48_THECC        Unreviewed;      1127 AA.
AC   A0A061GL48;
DT   03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT   03-SEP-2014, sequence version 1.
DT   24-JAN-2024, entry version 60.
DE   RecName: Full=Phytochrome {ECO:0000256|PIRNR:PIRNR000084};
GN   ORFNames=TCM_029563 {ECO:0000313|EMBL:EOY27809.1};
OS   Theobroma cacao (Cacao) (Cocoa).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Malvales; Malvaceae; Byttnerioideae; Theobroma.
OX   NCBI_TaxID=3641 {ECO:0000313|EMBL:EOY27809.1, ECO:0000313|Proteomes:UP000026915};
RN   [1] {ECO:0000313|EMBL:EOY27809.1, ECO:0000313|Proteomes:UP000026915}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Matina 1-6 {ECO:0000313|Proteomes:UP000026915};
RX   PubMed=23731509; DOI=10.1186/gb-2013-14-6-r53;
RA   Motamayor J.C., Mockaitis K., Schmutz J., Haiminen N., Iii D.L.,
RA   Cornejo O., Findley S.D., Zheng P., Utro F., Royaert S., Saski C.,
RA   Jenkins J., Podicheti R., Zhao M., Scheffler B.E., Stack J.C., Feltus F.A.,
RA   Mustiga G.M., Amores F., Phillips W., Marelli J.P., May G.D., Shapiro H.,
RA   Ma J., Bustamante C.D., Schnell R.J., Main D., Gilbert D., Parida L.,
RA   Kuhn D.N.;
RT   "The genome sequence of the most widely cultivated cacao type and its use
RT   to identify candidate genes regulating pod color.";
RL   Genome Biol. 14:R53.1-R53.24(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. 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; CM001884; EOY27809.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A061GL48; -.
DR   STRING; 3641.A0A061GL48; -.
DR   EnsemblPlants; EOY27809; EOY27809; TCM_029563.
DR   Gramene; EOY27809; EOY27809; TCM_029563.
DR   eggNOG; ENOG502R3WG; Eukaryota.
DR   InParanoid; A0A061GL48; -.
DR   OMA; IMRESIQ; -.
DR   Proteomes; UP000026915; Chromosome 6.
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; 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; 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:UP000026915};
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          230..391
FT                   /note="Phytochrome chromophore attachment site"
FT                   /evidence="ECO:0000259|PROSITE:PS50046"
FT   DOMAIN          616..687
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   DOMAIN          690..746
FT                   /note="PAC"
FT                   /evidence="ECO:0000259|PROSITE:PS50113"
FT   DOMAIN          750..828
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   DOMAIN          898..1116
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   REGION          1..27
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        9..27
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         336
FT                   /ligand="phytochromobilin"
FT                   /ligand_id="ChEBI:CHEBI:189064"
FT                   /note="covalent"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000084-50"
SQ   SEQUENCE   1127 AA;  125727 MW;  16B8620D99D38A78 CRC64;
     MVLESGERAK RPQQQQQPNT ALSSSAASNM KPINKGKAIA QYNADAGLMA EFEQSGVSGK
     SFNYSRSVIY APRSVPEEQI TAYLSRIQRG GLIQPFGCMI AIEEPTFRII SYSENCFELL
     GLRLDTEDES KALKGLIGID ARSLFTPASG PSLAKAAASR EISLLNPIWV YSRSTQKPFY
     AILHRIDVGI VIDLEPARSG DPALSLAGAV HSQKLAVRAI ARLQSLPGGD IGVLCDTVVE
     DVQKLTGYDR VMVYKFHDDD DHGEVVSEIR RSDLEPYLGL HYPAIDIPQA ARFLFKQNRV
     RMICDCHANP VKVIQSDELK QPLCLVNSTL RSPHGCHRQY MANMGSIASL VMAVIINGND
     STKLWGLVVC HHTSPRYVPF PLRYACEFLM QAFGLQLYLE LQLASQLAEK KILRTQTLLC
     DMLLRDAPFG IVTQSPNIMD LVKCDGAALY YNGKCWLLGV TPTESQVKDI AEWLLSTHED
     STGLSTDSLA GAGYPGAALL GDAVCGMATA RITSKDFLFW FRSHTAKEVK WGGAKHHPED
     KDDGGRMHPR SSFNAFLEVV KSRSLPWEIP EINAIHSLQL IMRDSFQGME DSGSKGLVYA
     RQNDTEMQGM GELSSVTYEM VRLIETATAP IFGVNTAGLI NGWNAKIAEL TGLQADDAMG
     RSLVNEVVHE DSHEVIANLL RRALHGEEDK NVELKLRNFG LNRQNSVVYI VVNACTSRDY
     TNDVVGVCFV GQDITSEKVV MDKFIRLQGD YRAIIQSLSP LIPPIFASDE NACCSEWNAA
     LEKLTGWSRS EVIGKMLPGE IFGELCQLKG QDTLTRFTIL LYQGISGQDT EKFPFGFFDR
     KGKFLEVFLT ANKRTDADGN IIGCFCFLQV IVPDLQQATE GHKQEDKEFF TKLKQLVYMR
     QEMKNPLNGI RFTHKLLETT AISENQKQFL ETSDACERQI LAIIEDMDLG SIEDSMELSM
     EEFLLGNVLD AVISQVMILL GERNLQLFHE IPEEIKRQSL YGDRIRLQLV LSDFLLSVVH
     HAPSPDGWVE IRISPGLKLI QDGNEFVRLQ FRMTHPGKGL PSTLIQDVFE EGNQPTTQEG
     LGLNLSRKLL NKMNGHVHYV REHSKCYFLI DLEIRTRKGR QKASQAE
//
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