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Database: UniProt
Entry: A0A2I0VMY4_9ASPA
LinkDB: A0A2I0VMY4_9ASPA
Original site: A0A2I0VMY4_9ASPA 
ID   A0A2I0VMY4_9ASPA        Unreviewed;      1134 AA.
AC   A0A2I0VMY4;
DT   28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT   28-FEB-2018, sequence version 1.
DT   24-JAN-2024, entry version 29.
DE   RecName: Full=Phytochrome {ECO:0000256|PIRNR:PIRNR000084};
GN   Name=PHYC {ECO:0000313|EMBL:PKU64774.1};
GN   ORFNames=MA16_Dca012638 {ECO:0000313|EMBL:PKU64774.1};
OS   Dendrobium catenatum.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Asparagales; Orchidaceae;
OC   Epidendroideae; Malaxideae; Dendrobiinae; Dendrobium.
OX   NCBI_TaxID=906689 {ECO:0000313|EMBL:PKU64774.1, ECO:0000313|Proteomes:UP000233837};
RN   [1] {ECO:0000313|EMBL:PKU64774.1, ECO:0000313|Proteomes:UP000233837}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   TISSUE=The whole plant {ECO:0000313|EMBL:PKU64774.1};
RX   PubMed=26754549; DOI=10.1038/srep19029;
RA   Zhang G.Q., Xu Q., Bian C., Tsai W.C., Yeh C.M., Liu K.W., Yoshida K.,
RA   Zhang L.S., Chang S.B., Chen F., Shi Y., Su Y.Y., Zhang Y.Q., Chen L.J.,
RA   Yin Y., Lin M., Huang H., Deng H., Wang Z.W., Zhu S.L., Zhao X., Deng C.,
RA   Niu S.C., Huang J., Wang M., Liu G.H., Yang H.J., Xiao X.J., Hsiao Y.Y.,
RA   Wu W.L., Chen Y.Y., Mitsuda N., Ohme-Takagi M., Luo Y.B., Van de Peer Y.,
RA   Liu Z.J.;
RT   "The Dendrobium catenatum Lindl. genome sequence provides insights into
RT   polysaccharide synthase, floral development and adaptive evolution.";
RL   Sci. Rep. 6:19029-19029(2016).
RN   [2] {ECO:0000313|EMBL:PKU64774.1, ECO:0000313|Proteomes:UP000233837}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   TISSUE=The whole plant {ECO:0000313|EMBL:PKU64774.1};
RX   PubMed=28902843; DOI=10.1038/nature23897;
RA   Zhang G.Q., Liu K.W., Li Z., Lohaus R., Hsiao Y.Y., Niu S.C., Wang J.Y.,
RA   Lin Y.C., Xu Q., Chen L.J., Yoshida K., Fujiwara S., Wang Z.W., Zhang Y.Q.,
RA   Mitsuda N., Wang M., Liu G.H., Pecoraro L., Huang H.X., Xiao X.J., Lin M.,
RA   Wu X.Y., Wu W.L., Chen Y.Y., Chang S.B., Sakamoto S., Ohme-Takagi M.,
RA   Yagi M., Zeng S.J., Shen C.Y., Yeh C.M., Luo Y.B., Tsai W.C.,
RA   Van de Peer Y., Liu Z.J.;
RT   "The Apostasia genome and the evolution of orchids.";
RL   Nature 549:379-383(2017).
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; KZ503395; PKU64774.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2I0VMY4; -.
DR   STRING; 906689.A0A2I0VMY4; -.
DR   OrthoDB; 1770905at2759; -.
DR   Proteomes; UP000233837; Unassembled WGS sequence.
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; 2.
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; 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; 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:UP000233837};
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          224..397
FT                   /note="Phytochrome chromophore attachment site"
FT                   /evidence="ECO:0000259|PROSITE:PS50046"
FT   DOMAIN          625..695
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
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   REGION          1..22
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         329
FT                   /ligand="phytochromobilin"
FT                   /ligand_id="ChEBI:CHEBI:189064"
FT                   /note="covalent"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000084-50"
SQ   SEQUENCE   1134 AA;  125812 MW;  C04FE75655ED76D0 CRC64;
     MTSKSNKESC SRSSSTRSKH TARVFAQTSL DAKLHAEFED SGQPFDYSIT MGATNRSTSG
     GGGGSSGIPS SSVSAYLQRM QRGQCIQPFG CMVAIDDHTF MIIAYSENAP ELLDLAPHAV
     PNIEQREALT IGMDARTLFR SLSSIALQKA ASFVDVNLLN PILVHCRSSG KPFYAILHRI
     NEGLVIDLEP VNPADVPVTA AGALKSYKLA AKAISRLQSL PSGNISLMCD VLVREVSELT
     GYDRVMVYKF HEDEHGEVIA ECRRSDLEPY LGLHYPATDI PQASRFLFMK NKVRMICDCT
     AHPVKVIQDH RLAQPMSLCG STLRAPHGCH AQYMANMGSI ASLVLSITIN EDDDDENKLD
     SDQQPKGRKL WGLVVCHHTS PRFVPFPLRY ACEFLLQVFG IQLNKEVELA AQTKEKHILR
     TQTVICDMIL RDSPISIFTQ SPNVMDLVKC EGAALYYRKQ FWLLGTTPTE AQIKDIIAWI
     QEYHDGSTGL STDSLREAGY PGADALGDAV CGMAAIKITS SDFIFWFRPH TAKEIKWGGA
     KDEPADVENE FRKMHPRASF KAFLEVVKHR SLPWEDVEMD AIHSLQLIFR GSLKDEIVAV
     ESKSMLQTET YDKRKTQGVE ELRTVTNEMV RLIETATVPI LAVDALGTLN GWNTKAAELT
     GLSIEEAIGM PFINLVEDET SDVARNVLSL ALQGKEENNV EIKLKTFGPK QKDGPVILVV
     NACCSHDLNE NVVGVCFVGQ DMTQHKMVMD KYTRIQGDYT AIIRNPSALI PPIFMIDEYG
     CCSEWNAAMQ EISGLKREDA IDKMLIGEVF TLQGSGCRVK DHDTLTKLKI VLNGVIAGQD
     VEKLLFGFYD AKDKYVEALL SANKKTNAEG KVTGVLCFLH VASPELQHAL QVQRMSEQAA
     MSSLKELAHL RQEIRNPLGG IVFTRNLMEA SELTEQQKKL IRTSALCQEQ LAKILDDADL
     ENIEQCYLEL NMVEFNLGEA LEAVIVQGMD LSRERQVSLV NDSPAEISSM YLYGDNLRLQ
     QVLADFLINA LQFSPRAEGS VVLCATPRKQ NIGTGVQIVH LDVRIIHPAP GIPETLVQEM
     FHQSPGISRE GLGLFLSQKL VKIMNGTVQY LREAERSSFI VLVEFPLVSH TKKR
//
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