ID A0A1S2XYV6_CICAR Unreviewed; 1124 AA.
AC A0A1S2XYV6;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE RecName: Full=Phytochrome {ECO:0000256|PIRNR:PIRNR000084};
GN Name=LOC101506511 {ECO:0000313|RefSeq:XP_004495828.1,
GN ECO:0000313|RefSeq:XP_004495829.1};
OS Cicer arietinum (Chickpea) (Garbanzo).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC NPAAA clade; Hologalegina; IRL clade; Cicereae; Cicer.
OX NCBI_TaxID=3827 {ECO:0000313|Proteomes:UP000087171, ECO:0000313|RefSeq:XP_004495829.1};
RN [1] {ECO:0000313|RefSeq:XP_004495828.1, ECO:0000313|RefSeq:XP_004495829.1}
RP IDENTIFICATION.
RC TISSUE=Etiolated seedlings {ECO:0000313|RefSeq:XP_004495828.1,
RC ECO:0000313|RefSeq:XP_004495829.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
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 RefSeq; XP_004495828.1; XM_004495771.2.
DR RefSeq; XP_004495829.1; XM_004495772.3.
DR STRING; 3827.A0A1S2XYV6; -.
DR PaxDb; 3827-XP_004495828-1; -.
DR GeneID; 101506511; -.
DR KEGG; cam:101506511; -.
DR eggNOG; ENOG502QRSA; Eukaryota.
DR OrthoDB; 1770905at2759; -.
DR Proteomes; UP000087171; Chromosome Ca4.
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:0009585; P:red, far-red light phototransduction; IEA:InterPro.
DR GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
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; 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; 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; 1.
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; 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; 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:UP000087171};
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 218..391
FT /note="Phytochrome chromophore attachment site"
FT /evidence="ECO:0000259|PROSITE:PS50046"
FT DOMAIN 617..687
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 750..802
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 901..1120
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 323
FT /ligand="phytochromobilin"
FT /ligand_id="ChEBI:CHEBI:189064"
FT /note="covalent"
FT /evidence="ECO:0000256|PIRSR:PIRSR000084-50"
SQ SEQUENCE 1124 AA; 124106 MW; 135227286BCA2FEA CRC64;
MSTSRPSQSS TNSGRSRHSA RIIAQTTVDA KLHATFEESS SSFDYSSSVR VSGSVDGDHQ
PRSNKVTTAY LNHIQRGKQI QPFGCLLALD EKTCKVVAYS ENAPEMLTMV SHAVPSVGDH
PALGIGTDIR TIFTAPSASA LQKALGFAEV SLLNPILVHC KTSGKPFYAI IHRVTGSLII
DFEPVKPYEV PMNAAGALQS YKLAAKAITR LQSLPSGSME RLCDTMVQEV FELTGYDRVM
AYKFHEDDHG EVIAEIAKPG LEPYLGLHYP ATDIPQAARF LFMKNKVRMI VDCHAKHVKV
LQDEKLPFDL TLCGSTLRAP HSCHLQYMAN MDSIASLVMA VVVNDSDEDS DSTDAVHPQK
KKRLWGLVVC HNTTPRFVPF PLRYACEFLA QVFAIHVNKE IELEYQILEK NILRTQTLLC
DMLMRDAPLG IVSQSPNIMD LVKCDGAALL YKNNLWILGV TPSESKIREI ALWMSEYHTD
STGLSTDSLS DAGFPGALSV GDTVCGMAAV RITPKDIVFW FRSHTAAEIR WGGAKHEPSE
QDDGRKMHPR SSFKAFLEVV KARSLPWKDF EMDAIHSLQL ILRNASKDTE SVDLNTKAIN
TRLNDLKIEG MQELEAVTSE MVRLIETATV PILAVDVDGM VNGWNIKIAE LTGLPVDEAI
GKHLLTLVED SSSDIVKKML NLALQGEEEK NVQFEIKTHA SKMDSGPISL IVNACASKDL
RDNVVGVCFV AQDITAQKTV MDKFTRIEGD YKAIVQNPNP LIPPIFGTDE FGWCCEWNQA
MIKLTGWKRE EVMDKMLLGE VFGTQMACCR LKNQEAFVNF GIVLNKAMTG FETQKVAFGF
FARNGKYVEC LLSVSKKLDA EGLVTGVFCF LQLASPELQQ ALHIQRLSEQ TALKRLKVLH
YMKRQIRNPL SGIVFSSKML EGTDLGTEQK RLLSASAQCQ RQLSKILDDS DLDSIIDGYL
DLEMAEFTLH EVLVTALSQV VTRSNTKGIR IVNDVAEHIA METLYGDSLR LQQVLADFLL
ISINSSPNGG QVVIAASLTK EQLGKSVHLV NLELSITHGG SGVAEALLNE MFGNNVLESE
EGISLHISRK LLKLMNGDVR YLKEAGKSSF ILSVELAAAH KLKG
//
