ID A0A0A0K6F8_CUCSA Unreviewed; 1119 AA.
AC A0A0A0K6F8;
DT 07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT 07-JAN-2015, sequence version 1.
DT 24-JAN-2024, entry version 43.
DE RecName: Full=Phytochrome {ECO:0000256|PIRNR:PIRNR000084};
GN ORFNames=Csa_7G031720 {ECO:0000313|EMBL:KGN43411.1};
OS Cucumis sativus (Cucumber).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Cucurbitales; Cucurbitaceae; Benincaseae; Cucumis.
OX NCBI_TaxID=3659 {ECO:0000313|EMBL:KGN43411.1, ECO:0000313|Proteomes:UP000029981};
RN [1] {ECO:0000313|EMBL:KGN43411.1, ECO:0000313|Proteomes:UP000029981}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. 9930 {ECO:0000313|Proteomes:UP000029981};
RX PubMed=19881527; DOI=10.1038/ng.475;
RA Huang S., Li R., Zhang Z., Li L., Gu X., Fan W., Lucas W.J., Wang X.,
RA Xie B., Ni P., Ren Y., Zhu H., Li J., Lin K., Jin W., Fei Z., Li G.,
RA Staub J., Kilian A., van der Vossen E.A., Wu Y., Guo J., He J., Jia Z.,
RA Ren Y., Tian G., Lu Y., Ruan J., Qian W., Wang M., Huang Q., Li B.,
RA Xuan Z., Cao J., Asan null, Wu Z., Zhang J., Cai Q., Bai Y., Zhao B.,
RA Han Y., Li Y., Li X., Wang S., Shi Q., Liu S., Cho W.K., Kim J.Y., Xu Y.,
RA Heller-Uszynska K., Miao H., Cheng Z., Zhang S., Wu J., Yang Y., Kang H.,
RA Li M., Liang H., Ren X., Shi Z., Wen M., Jian M., Yang H., Zhang G.,
RA Yang Z., Chen R., Liu S., Li J., Ma L., Liu H., Zhou Y., Zhao J., Fang X.,
RA Li G., Fang L., Li Y., Liu D., Zheng H., Zhang Y., Qin N., Li Z., Yang G.,
RA Yang S., Bolund L., Kristiansen K., Zheng H., Li S., Zhang X., Yang H.,
RA Wang J., Sun R., Zhang B., Jiang S., Wang J., Du Y., Li S.;
RT "The genome of the cucumber, Cucumis sativus L.";
RL Nat. Genet. 41:1275-1281(2009).
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; CM002928; KGN43411.1; -; Genomic_DNA.
DR RefSeq; XP_004144620.1; XM_004144572.2.
DR AlphaFoldDB; A0A0A0K6F8; -.
DR STRING; 3659.A0A0A0K6F8; -.
DR EnsemblPlants; KGN43411; KGN43411; Csa_7G031720.
DR GeneID; 101211915; -.
DR Gramene; KGN43411; KGN43411; Csa_7G031720.
DR KEGG; csv:101211915; -.
DR eggNOG; ENOG502QT1B; Eukaryota.
DR OMA; NFGCRVK; -.
DR OrthoDB; 1770905at2759; -.
DR Proteomes; UP000029981; Chromosome 7.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
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; 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; 3.
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; 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; 2.
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; 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; 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:UP000029981};
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 219..388
FT /note="Phytochrome chromophore attachment site"
FT /evidence="ECO:0000259|PROSITE:PS50046"
FT DOMAIN 613..683
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 746..798
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 896..1115
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT BINDING 324
FT /ligand="phytochromobilin"
FT /ligand_id="ChEBI:CHEBI:189064"
FT /note="covalent"
FT /evidence="ECO:0000256|PIRSR:PIRSR000084-50"
SQ SEQUENCE 1119 AA; 125104 MW; E4EE009B58630256 CRC64;
MSSTSTNKTV CSKTSFDRSK HGAHVVAQTP IDAKLHVDFE GSERLFDYSA SVDFNAACST
SNVHASTVQS YLLNIQRGSL VQPFGCMIAV DGENLSVLAY SENAPEMLDL APHAVPNIEQ
QEALTFGTDV RTLFRSPGAA ALQKAADFKE VNLLNPILVH CRTSGKPFYA ILHRVDVGLI
IDLEPVNPAD VPVTAAGALK SYKLAAKAIS KLQNLQSGNI SLLCEVLVKE VSDLTGYDRV
MVYKFHDDEH GEVVAECCRS DLEPYFGLHY PATDIPQASR FLFLKNKVRM ICDCLAPPVK
VLQDRRLAQP LSLCGSALRA PHGCHARYMM NMGSIASLVM SITINENDSE SENDQEKDRK
LWGLVVCHHT SPRFVPFPLR YACEFLIQVF GIQINKEVEL QAQLKEKHIL RIQTVLCDML
LRDAPVGIVT QSPNIMDLVK CDGAALYFRK KFWSLGVTPT EAQIRNIADW LLKDHSGSTG
LSTDSLTEAG FYGASALGDE ICGMAAVRIT SKDFLFWFRS HMAKEIRWGG AKHDPSDEDD
GRKMHPRSSF KAFLEVVKRR SQPWEDVEMD AIHSLQLILR GSLQDEIEEE CKVITTVPPV
DEKTQQLDEL RVITNEMVRL IETAAVPILA VDVFGKINGW NSKATELTGL AIQEAIGMPL
VDCVVNDSVK VVKKMLSLAI QGIEEKNVEI KLKTFGTAVQ NGPVILEVNS CCSRDLNNNV
VGISFIGQDV TKQKLVMNQY TQIQGDYTGI MRNPSALIPP IFMADGEGRC LEWNDAMEKL
SGFRRVEMTN RMLLGEVFTL ENFGCRVKDH TLTKLRIILH RVISGQDTEK FLFRFCDREG
NYVESLLTAS KRTDTEGTVT GVFFFLHVAS PELQYALEMQ RISEQATAEN LHKLAYLRQE
IRKPLDGIAL MQNLISSSDL SIEQKQLIKL NTLSREQLHK IVHDTDIQSI EECYMETNCS
EFNLGDVLDV VTNQTMTLSQ EREVKIICES LADVSSLHLY GDNLRLQQVL SEFLTNTLLF
TCKESSVIFK ATPRKERIGK GIHIVHLELR ITHPTPGIPA HLIQEMFDDN NDSSKEGLGL
YISQKLVKIM NGTVQYLREA ETSSFIILIE FPLVEHVAR
//
