PHYE_IPONI
ID PHYE_IPONI Reviewed; 1115 AA.
AC P55004;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=Phytochrome E;
GN Name=PHYE;
OS Ipomoea nil (Japanese morning glory) (Pharbitis nil).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Convolvulaceae; Ipomoeeae; Ipomoea.
OX NCBI_TaxID=35883;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Seedling cotyledon;
RA Zheng C.C., O'Neill S.D.;
RL Submitted (JAN-1996) to the EMBL/GenBank/DDBJ databases.
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; U39787; AAA84970.1; -; mRNA.
DR AlphaFoldDB; P55004; -.
DR SMR; P55004; -.
DR PRIDE; P55004; -.
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 2: Evidence at transcript level;
KW Chromophore; Photoreceptor protein; Receptor; Repeat; Sensory transduction;
KW Transcription; Transcription regulation.
FT CHAIN 1..1115
FT /note="Phytochrome E"
FT /id="PRO_0000171982"
FT DOMAIN 213..383
FT /note="GAF"
FT DOMAIN 598..669
FT /note="PAS 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00140"
FT DOMAIN 672..728
FT /note="PAC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00141"
FT DOMAIN 732..803
FT /note="PAS 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00140"
FT DOMAIN 880..1100
FT /note="Histidine kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
FT BINDING 318
FT /ligand="phytochromobilin"
FT /ligand_id="ChEBI:CHEBI:189064"
FT /note="covalent, via 1 link"
FT /evidence="ECO:0000250"
SQ SEQUENCE 1115 AA; 124329 MW; 081A4154EE147800 CRC64;
MENYGKAVTF SSSATSNLNT GKAIAQYNAD AKLMAEFEQS RESGKSFDYS RSVIHAPQNV
TEEEMTAYLS RIQRGGLIQP FGCMLAIEEP SFKIVGFSEN CFDLLGLKSG VEPPERMSLI
GIDARTLFTL SSRASLAKAV ASREISLLNP IWVHSKINQK PFYAVLHRID VGIVIDLEPA
NSADPALLLA GAVQSQKLAV RAISRLQSLP GGDIGTLCDT VVEDVQKLTG YDRVMVYKFH
DDSHGEVVSE IRRSDLEPYL GLHYPATDIP QAARFLFKQN RVRMICDCNA QPVKVLQCEE
LKQPLCLVNS TLRSPHGCHT KYMANMGSIA SLVMAVVINS SESMKLWGLV VCHHTSPRYV
PFPLRYACEF LMQAFSLQLY MELQLASQLA EKKILQTQTL LCDMLLRDAP FGIVTQTPSI
MDLVRCDGAA LYYNGKCWLL GVTPTETQVK DIAEWLLHNH GDSTGLSTDC LSDAGYPGAP
LLGDAVSGMA TARITSKDFL FWFRSHTAKE VKWGGAKHHP EDKDDGGRMH PRSSFIAFLE
VVKSRSLPWE DSEINAIHSL QLIMRDSLQG IGENYMKSVS SPQQNDSDGV RFYELSSMAL
ELVRLVETAT VPIFGVDSSG LINGWNAKIA ELTGLQANVA IGKYLIDDVT HEDSHETFKA
LMCRALQGEE DRNVEVKLLK FGNHPTKEVV YLVVNACTSR DYKNDIIGVC FVGQDITPEK
AVMDKFVRLQ GDYEAIIQSL NPLIPPIFAS DENACCSEWN AAMERLTGLV KCEVIGKRLP
GEIFGGLCRL KGQDALTKFM ILLYQGISGH DTEKLSFGFF DRKGNFIDVF ITANKRTDER
GNIIGCFCFL QTMAVDHPQI SARDIEDDRE CLSTLKEFAY IQQQMKNPLN GIRFTHKLLE
GTVTSDHQKQ FLETSEACEK QILSIIENMD SGGIVDGNRV ELKTEEFVIG NVIDAVVSQV
MIPLKEKNLQ LLHDIPDQIK SLPIYGDQIK LQLVLSDFLL SIVRHAPSPD GWVEIRVSPG
LKLIQDGNVF IHIQFRMTHP GQGLPSALIE DMVRGGTRWT TQEGVVLHLS QKLVRMMNGH
VHYVREQQKC YFLIDLDFKT QKPRSRESSM DTKAD