PHY1_CERPU
ID PHY1_CERPU Reviewed; 1307 AA.
AC P25848; P93100;
DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT 15-JUL-1998, sequence version 3.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=Light-sensor Protein kinase;
DE Includes:
DE RecName: Full=Phytochrome;
DE Includes:
DE RecName: Full=Protein kinase;
DE EC=2.7.11.1;
GN Name=PHY1; Synonyms=PHY;
OS Ceratodon purpureus (Fire moss) (Dicranum purpureum).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Bryophyta;
OC Bryophytina; Bryopsida; Dicranidae; Pseudoditrichales; Ditrichaceae;
OC Ceratodon.
OX NCBI_TaxID=3225;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1463836; DOI=10.1007/bf00028888;
RA Thuemmler F., Dufner M., Kreisl P., Dittrich P.;
RT "Molecular cloning of a novel phytochrome gene of the moss Ceratodon
RT purpureus which encodes a putative light-regulated protein kinase.";
RL Plant Mol. Biol. 20:1003-1017(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 49-550.
RX PubMed=2261981; DOI=10.1016/0014-5793(90)81455-w;
RA Thuemmler F., Beetz A., Ruediger W.;
RT "Phytochrome in lower plants. Detection and partial sequence of a
RT phytochrome gene in the moss Ceratodon purpureus using the polymerase chain
RT reaction.";
RL FEBS Lett. 275:125-129(1990).
RN [3]
RP SEQUENCE REVISION TO C-TERMINUS.
RC STRAIN=WT3;
RA Pasentsis K., Paulo N., Dittrich P., Algarra P., Thuemmler F., Dufner M.,
RA Kreisl P.;
RL Submitted (FEB-1997) 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 -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC EC=2.7.11.1;
CC -!- SUBUNIT: Homodimer.
CC -!- SUBCELLULAR LOCATION: Cell membrane. Note=Located in a fixed position
CC close to the plasma membrane.
CC -!- PTM: Contains one covalently linked phytochromobilin chromophore.
CC {ECO:0000250}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the phytochrome
CC family. {ECO:0000305}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the protein kinase
CC superfamily. Ser/Thr protein kinase family. {ECO:0000305}.
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DR EMBL; U87632; AAB47762.1; -; Genomic_DNA.
DR EMBL; X17084; CAA34936.1; -; Genomic_DNA.
DR PIR; S27396; S27396.
DR AlphaFoldDB; P25848; -.
DR SMR; P25848; -.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0009882; F:blue light photoreceptor activity; IEA:UniProt.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0009584; P:detection of visible light; IEA:InterPro.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:InterPro.
DR Gene3D; 3.30.450.270; -; 1.
DR Gene3D; 3.30.450.40; -; 1.
DR InterPro; IPR003018; GAF.
DR InterPro; IPR029016; GAF-like_dom_sf.
DR InterPro; IPR011009; Kinase-like_dom_sf.
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; IPR016132; Phyto_chromo_attachment.
DR InterPro; IPR013516; Phyto_chromo_BS.
DR InterPro; IPR001294; Phytochrome.
DR InterPro; IPR013515; Phytochrome_cen-reg.
DR InterPro; IPR043150; Phytochrome_PHY.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF01590; GAF; 1.
DR Pfam; PF00989; PAS; 1.
DR Pfam; PF08446; PAS_2; 1.
DR Pfam; PF00360; PHY; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR PRINTS; PR01033; PHYTOCHROME.
DR SMART; SM00065; GAF; 1.
DR SMART; SM00091; PAS; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF55785; SSF55785; 2.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS50113; PAC; 1.
DR PROSITE; PS50112; PAS; 1.
DR PROSITE; PS00245; PHYTOCHROME_1; 1.
DR PROSITE; PS50046; PHYTOCHROME_2; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 3: Inferred from homology;
KW ATP-binding; Cell membrane; Chromophore; Kinase; Membrane;
KW Nucleotide-binding; Photoreceptor protein; Receptor; Sensory transduction;
KW Serine/threonine-protein kinase; Transcription; Transcription regulation;
KW Transferase.
FT CHAIN 1..1307
FT /note="Light-sensor Protein kinase"
FT /id="PRO_0000171970"
FT DOMAIN 215..394
FT /note="GAF"
FT DOMAIN 609..680
FT /note="PAS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00140"
FT DOMAIN 683..739
FT /note="PAC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00141"
FT DOMAIN 1004..1307
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 779..1003
FT /note="Hinge"
FT ACT_SITE 1127
FT /evidence="ECO:0000250"
FT BINDING 320
FT /ligand="phytochromobilin"
FT /ligand_id="ChEBI:CHEBI:189064"
FT /note="covalent, via 1 link"
FT /evidence="ECO:0000250"
FT BINDING 1010..1018
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 1031
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT CONFLICT 513
FT /note="W -> L (in Ref. 2; CAA34936)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1307 AA; 145844 MW; E5E77A9FEF301A5C CRC64;
MSATKKTYSS TTSAKSKHSV RVAQTTADAA LEAVYEMSGD SGDSFDYSKS VGQSAESVPA
GAVTAYLQRM QREGLIQNFG CMVAVEEPNF CVIAYSENAS EFLDLIPQAV PSMGEMDVLG
IGTDIRTLFT PSSSAALEKA AATQDISLLN PITVHCRRSG KPLYAIAHRI DIGIVIDFEA
VKMIDVPVSA AAGALQSHKL AARAITRLQA LPGGDIELLC DTIVEEVREL TGYDRVMAFK
FHEDEHGEVV AEIRRMDLEP YMGLHYPATD IPQASRFLLM KNRVRLIADC YASPVKLIQD
PDIRQPVSLA GSTLRAPHGC HAQYMGNMGS IASLVMAVII NDNEEYSRGA IQRGRKLWGL
VVCQHTSPRT VPFPLRSVCE FLMQVFGMQL NLHVELAAQL REKHILRTQT LLCDMLLRDA
PIGIVSQTPN IMDLVKCDGA ALYYGKRVWL LGTTPTENQI KEIADWLLEH HNDSTGLSTD
SLADANYPGA HLLGDAVCGM AAAKITAKDF LFWFRSHTAT EVKWGGAKHD PDEKDDGRKM
HPRSSFKAFL EVVNKRSPPW EDVEMDAIHS LQLILRGSFR DIADSDTKTM IHARLNDLKL
QGVEERNALA NEMSRVLETA AAPILAVDSR GMINAWNAKI AQVTGLPVEE AMHCSLTKDL
VLDESVVVVE RLLSLALQGE EEQNVEIKLK TFGTQTTERA VILIVNACCS RDASDFVVGV
FFVGQDVTEQ RMFMDRFTRI QGGEKTTVQD PHPLMRPSFD GDEFGRTFKR NSALGGLKDH
ATGSVERLDL YLRRAEECME VMETIPSPKF NNKQCQYLAG KLKAVLQSAS LFLRISHHEH
HELGASIDMG RHVEIFKLLL ALAKEIESFI QGCCKDEWIK AAMTLTNVSE YVSSMGFNLE
LCKIAFCKSC AASGSLTLDQ IEVICKDEAE VVKRNASIDV DTLFAKVIYD LTEKTLSSDQ
NDLAIYLLQR LKRAKPILPS FSSRPSWWNF YDDWSFSEKF FQWIQITGSL GSGSSATVEK
AVWLGTPVAK KTFYGRNNED FKREVEILAE LCHPNITSMF CSPLYRRKCS IIMELMDGDL
LALMQRRLDR NEDHDSPPFS ILEVVDIILQ TSEGMNYLHE KGIIHRDLKS MNILVKSVKV
TKSEIGYVHV KVADFGLSKT KDSSTRYSNQ TWNRGTNRWM APEVINLGYE STEGEISFDG
KVPKYPLKSD VYSFGMVCYE VLTGDVPFPE EKNPNNVKRM VLEGVRPDLP AHCPIELKAL
ITDCWNQDPL KRPSFAVICQ KLKYLKYLLM TGFSSYQDSY PSTEEPS
