PHY_MOUSC
ID PHY_MOUSC Reviewed; 1124 AA.
AC P33529; Q40364;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 2.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=Phytochrome;
GN Name=PHY;
OS Mougeotia scalaris (Green alga) (Sphaerocarpus scalaris).
OC Eukaryota; Viridiplantae; Streptophyta; Zygnemophyceae; Zygnematophycidae;
OC Zygnematales; Zygnemataceae; Mougeotia.
OX NCBI_TaxID=13158;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=B164.80;
RX PubMed=8980511; DOI=10.1007/bf00020200;
RA Winands A., Wagner G.;
RT "Phytochrome of the green alga Mougeotia: cDNA sequence, autoregulation and
RT phylogenetic position.";
RL Plant Mol. Biol. 32:589-597(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 248-435.
RC STRAIN=B164.80;
RX PubMed=1475323; DOI=10.1111/j.1751-1097.1992.tb02232.x;
RA Winands A., Wagner G., Marx S., Schneider-Poetsch H.A.W.;
RT "Partial nucleotide sequence of phytochrome from the zygnematophycean green
RT alga Mougeotia.";
RL Photochem. Photobiol. 56:765-770(1992).
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.
CC -!- SUBUNIT: Homodimer.
CC -!- PTM: Contains one covalently linked phytochromobilin chromophore.
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the phytochrome family. {ECO:0000305}.
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DR EMBL; X95550; CAA64796.1; -; mRNA.
DR EMBL; S52048; AAB24769.1; -; Genomic_DNA.
DR AlphaFoldDB; P33529; -.
DR SMR; P33529; -.
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:0017006; P:protein-tetrapyrrole linkage; IEA:InterPro.
DR GO; GO:0009585; P:red, far-red light phototransduction; IEA:InterPro.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; 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; -; 1.
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.
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; SSF55785; SSF55785; 3.
DR SUPFAM; SSF55874; SSF55874; 1.
DR TIGRFAMs; TIGR00229; sensory_box; 2.
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 2: Evidence at transcript level;
KW Chromophore; Photoreceptor protein; Receptor; Repeat; Sensory transduction;
KW Transcription; Transcription regulation.
FT CHAIN 1..1124
FT /note="Phytochrome"
FT /id="PRO_0000171976"
FT DOMAIN 220..399
FT /note="GAF"
FT DOMAIN 613..684
FT /note="PAS 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00140"
FT DOMAIN 687..743
FT /note="PAC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00141"
FT DOMAIN 747..818
FT /note="PAS 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00140"
FT DOMAIN 895..1116
FT /note="Histidine kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
FT REGION 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 325
FT /ligand="phytochromobilin"
FT /ligand_id="ChEBI:CHEBI:189064"
FT /note="covalent, via 1 link"
FT /evidence="ECO:0000250"
FT CONFLICT 342
FT /note="S -> C (in Ref. 2; AAB24769)"
FT /evidence="ECO:0000305"
FT CONFLICT 381
FT /note="R -> H (in Ref. 2; AAB24769)"
FT /evidence="ECO:0000305"
FT CONFLICT 399
FT /note="V -> A (in Ref. 2; AAB24769)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1124 AA; 123924 MW; A498BBD351AD1771 CRC64;
MSSSKRSQSS GRSSTQTRIQ NRVTQASADA KLSTAFEVSS SSGGDSFDYT KSVTASLNPT
EPLAAKSVTA YLQRMQRGSI IQSFGCMMAV EPGTFRIIAY SENVSEMLGV TPQSVPTGDH
QNAIGIGTDV RSLLSPSSVS VVEKAVAAND VSMMNPIAVY SLATQKLFFA ILHMNDVGLV
IDLEPISSSS DSAMFSAGAV QSHKLAAKAI SRLQSLPGGD ICGLCDVVVE EVRELTGYDR
VMAYKFHDDE HGEVVAEIRR SDLEPYLGLH YPATDIPQAS RFLFIKNRIR MICDCTSPQV
KVVQDSRIPQ EMSLAGSTMR GVHGCHTQYM MNMGSTASLV MSVTINDTNE IAGGPGMKGR
KLWGLIVCHH STPRHIPFPI RSACEFLMQV FGLQLNMEVE LAAQHREKHI LRTQTLLCDM
LLRDAPMGIV SQSPNVMDLV KCDGAALLFG GRCWLLGISP TQEQVKDIAT WLISSHTDTT
GLSTDSLVDA GYPKARELGV DVCGMAAARI TENDFLFWFR GHAQKEVKWA GAKDGGSEED
GSRMHPRSSF KAFLEVVKQR SLPWEDVEMD AIHSLQLILR GSFQDIEDKE DRKIVHARLK
EMHLQGMEEL SSVASEMVRL IETATAPILA VDTAGCVNGW NFKISELTGL SIPEVMGKSL
VKDLTHPSSK DTVEKLLYMA LNGEEEQNVE IRLKTWGMQQ GKGPVILMVN ACASRDVSEK
VVGVCFVAQD VTGEKIVQDK FTRIQGDYTT IVRSHNSLIP PIFGSDESGF CVEWNPAMER
LSGVKREEAI GKMLTRELFG GILRLKNVDG LTKFMIVLNA AMSSHDTDKF PFTFYDRSGK
IVEVLLTTSK RCNSEGVVTG VFCFLHTASS ELQQALTVQK AAERVAEVKA KELAYIRQEI
QNPLDGIHFA RSFMEHTVLS EDQKQLIETS ATCEKQLRRI LADMDLASIE KGYLELETGE
FSMATVMNSV VSQGMIQSTQ KNLQLYCDTP PDFKSLSVFG DQVRLQQVLA DFLLNAVQFT
PPSGWVEIKV EPVVKKLPGG VSVANVDFRV SHPGEGLPED LIDQMFDRAD ARVKSQEGLG
LSICRKLVRL MNGEVQYRRE GERNFFLLQL ELPLAQRDDQ ASMK
