PHY1_SELMA
ID PHY1_SELMA Reviewed; 1134 AA.
AC Q01549;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1993, sequence version 1.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Phytochrome 1;
GN Name=PHY1;
OS Selaginella martensii (Martens's spike moss).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Lycopodiopsida; Selaginellales; Selaginellaceae; Selaginella.
OX NCBI_TaxID=3247;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Spring;
RX PubMed=1475321; DOI=10.1111/j.1751-1097.1992.tb02230.x;
RA Hanelt S., Braun B., Marx S., Schneider-Poetsch H.A.W.;
RT "Phytochrome evolution: a phylogenetic tree with the first complete
RT sequence of phytochrome from a cryptogamic plant (Selaginella martensii
RT spring).";
RL Photochem. Photobiol. 56:751-758(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; X61458; CAA43698.1; -; Genomic_DNA.
DR PIR; S31280; S31280.
DR AlphaFoldDB; Q01549; -.
DR SMR; Q01549; -.
DR PRIDE; Q01549; -.
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; 1.
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; Photoreceptor protein; Receptor; Repeat; Sensory transduction;
KW Transcription; Transcription regulation.
FT CHAIN 1..1134
FT /note="Phytochrome 1"
FT /id="PRO_0000171994"
FT DOMAIN 219..401
FT /note="GAF"
FT DOMAIN 616..687
FT /note="PAS 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00140"
FT DOMAIN 690..746
FT /note="PAC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00141"
FT DOMAIN 750..821
FT /note="PAS 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00140"
FT DOMAIN 901..1121
FT /note="Histidine kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
FT BINDING 324
FT /ligand="phytochromobilin"
FT /ligand_id="ChEBI:CHEBI:189064"
FT /note="covalent, via 1 link"
FT /evidence="ECO:0000250"
SQ SEQUENCE 1134 AA; 124707 MW; 42819B9F4ACC398C CRC64;
MSTTKLTYSS GSSAKSKHSV RVAQTTADAK LHAVYEESGE SGDSFDYSKS INATKSTGET
IPAQAVTAYL QRMQRGGLVQ PFGCMLAVEE GSFRVIAFSD NAGEMLDLMP QSVPSLGSGQ
QDVLTIGTDA RTLFTAAASA LEKAAGAVDL SMLNPIWVQS KTSAKPFYAI VHRIDVGLVM
DLEPVKASDT RVGSAAGALQ SHKLAAKAIS RLQSLPGGDI GLLCDTVVEE VRDVTGYDLV
MAYKFHEDEH GEVVAEIRRS DLEPYLGLHY PATDIPQASR FLFMKNRVRM ICDCSAPPVK
ITQDKELRQP ISLAGSTLRA PHGCHAQYMG NMGSVASLVM AMIINDNDEP SGGGGGGGQH
KGRRLWGLVV CHHTSPRSVP FLRSACEFLM QVFGLQLNME AAVAAHVREK HILRTQTLLC
DMLLRDAPIG IVSQSPNIMD LVKCDGAALY YGKRFWLLGI TPSEAQIKDI AEWLLEHHKD
STGLSTDSLA DAGYPGAASL GDEVCGMAAA KITAKDFLFW FRSHTAKEVK WGGAKHDPDD
KDDGRKMHPR SSFKAFLEVV KRRSLPWEDV EMDAIHSLQL ILRGSFQDID DSDTKTMIHA
RLNDLKLQGM DELSTVANEM VRLIETATAP ILAVDSSGFI NGWNAKVADV TGLPVTEAMG
RSLAKELVLH ESADMVERLL YLALQGDEEQ NVELKLKTFG GQKDKEAVIL VVNACASRDV
SDNVVGVCFV GQDVTGQKVV MDKFTRIQGD YKAIVQNPNP LIPPIFGADE FGYCSEWNPA
MEKLSGWRRE EVLGKMLVGE IFGIQMMYCR LKGQDAVTKF MIVLNSAADG QDTEKFPFAF
FDRQGKYVEA LLTATKRADA EGSITGVFCF LHIASAELQQ ALTVQRATEK VALSKLKELA
YIRQEIKNPL YGIMFTRTLM ETTDLSEDQK QYVETGAVCE KQIRKILDDM DLESIEDGYL
ELDTTEFMMG TVMDAVISQG MITSKEKNLQ LIRETPKEIK AMFLYGDQVR LQQVLADFLL
NAIRFTPSSE NWVGIKVATS RKRLGGVVHV MHLEFRITHP GVGLPEELVQ EMFDRGRGMT
QEGLGLSMCR KLVKLMNGEV EYIREAGKNY FLVSLELPLA QRDDAGSVKF QASS
