PHY_PICAB
ID PHY_PICAB Reviewed; 1136 AA.
AC Q40762;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=Phytochrome;
OS Picea abies (Norway spruce) (Picea excelsa).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Pinopsida; Pinidae; Conifers I; Pinales; Pinaceae; Picea.
OX NCBI_TaxID=3329;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=10480390; DOI=10.1023/a:1006204318499;
RA Clapham D.H., Kolukisaoglu H.U., Larsson C.T., Qamaruddin M., Ekberg I.,
RA Wiegmann-Eirund C., Schneider-Poetsch H.A., von Arnold S.;
RT "Phytochrome types in Picea and Pinus. Expression patterns of PHYA-Related
RT types.";
RL Plant Mol. Biol. 40:669-678(1999).
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. {ECO:0000250}.
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; U60264; AAB03339.1; -; mRNA.
DR PIR; T14842; T14842.
DR AlphaFoldDB; Q40762; -.
DR SMR; Q40762; -.
DR PRIDE; Q40762; -.
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; 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; 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..1136
FT /note="Phytochrome"
FT /id="PRO_0000171983"
FT DOMAIN 231..414
FT /note="GAF"
FT DOMAIN 629..699
FT /note="PAS 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00140"
FT DOMAIN 762..833
FT /note="PAS 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00140"
FT DOMAIN 913..1132
FT /note="Histidine kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
FT REGION 1..28
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 336
FT /ligand="phytochromobilin"
FT /ligand_id="ChEBI:CHEBI:189064"
FT /note="covalent, via 1 link"
FT /evidence="ECO:0000250"
SQ SEQUENCE 1136 AA; 126066 MW; 07A4E01498453E93 CRC64;
MSTTRPRAAT HSASSGSVSR SSKHSARVIT QTPVDAKLQA EFEGSVHSFD YTKSIDISGD
SSSVPSETVK AYLQRLQKEM LIQPFGCVLA VEEGSCAVVG YSENAPEMLD VVGGAHAVPS
IGGQQQEGGG GGGGLLRIGM DARTLFKPAS AAALQKAATF ADMHLVNPIF VRCNRSGKPF
YAILNRIDAG LVIDFEPVMP SDVPVSAAGA LQSYKLAAKA ISRLQSLPGG DIRLLCDTVV
QEVRELTGYD RVMAYRFHED EHGEVVAEMR RPDLEPYLGL HYPATDIPQA SRFLFMKNRV
RMICDCCAPP VNVIQDKRLR QPLSLCGSTL RAPHGCHAQY MANMGSIASL VMSVTTNENG
DDSEGGGQQQ PQNRRKLWGL VVCHHTSPRV IPFPLRYACE FLMQVFGIQL NKEVELAAQL
REKHILRVQP VLCDMLLRDA PVGIVSQTPN IMDLVKCDGA ALLYGKRLWL LGTTPTEAQI
LDIADWLLEH HRDSTGLSTD SLAEAGYPGA ASLGDAVCGI AAARITSKDF LFWFRSHTAK
EIIWGGAKHD PNDKDDGRRM HPRSSFKAFL EVVKRRSLPW EDVEMDAIHS LQLILRDSFH
DIDDSDSKTM IHARLNDLRL QGIDELSAVT NEMVRLIETA TVPILAIDSN GLVNGWNTKA
AELTGLLADE VIGRPLIDLV QHDSVEIVKK MLYLALQGEE EQNVEIKLKT FGIQEEKGPV
VLIVNACSSR DLEENVVGVC FVAQDVTWQR IAMDKFTHLQ GDYRAIVQNP NPLIPPIFGA
DEYGYCSEWN PAMEKLTGWK REEVIGKMLV GEVFGIHRMS CQLKGQDGLT KLRIVLNNAM
AGKETEKFPF SFFDRHGKNT EALLSANKRT DAEGIITGVF CFLHVTSTEL QQALQVQRMA
EQAAMDRLKE LAYIRQEIRN PLYGIIFTRK LMESTDLSEE QKQIVQTSAL CQRQLVKVLD
DADLESIEDG YLELDTIEFT LGTVLDAVVS QGMILSREKG LQLIRDSPEE IKTMCLYGDQ
LRLQQILSNF LINALRFSTS EGWVGNKVVP TKRHLGSGVN VMHMEFRITH SGQGIPEELI
KEMFVHNQDM FQEGLGLYMC QQLVKIMNGD VQYLREAGRS SFIINVEFPL AQTDKQ
