SYNY3:PHY1

Species (Taxon ID)	Synechocystis sp. (strain PCC 6803 / Kazusa). (1111708)
Gene Name(s)	cph1
Protein Name(s)	Phytochrome-like protein cph1 Bacteriophytochrome cph1 Light-regulated histidine kinase 1
External Links
UniProt	Q55168
EMBL	BA000022
PIR	S74389
RefSeq	NP_442237.1 YP_005652297.1 YP_007452113.1
PDB	2VEA 3ZQ5
PDBsum	2VEA 3ZQ5
ProteinModelPortal	Q55168
IntAct	Q55168
MINT	MINT-8375044
STRING	1148.slr0473
EnsemblBacteria	BAA10307
GeneID	952560
KEGG	syn:slr0473
PATRIC	23842112
eggNOG	COG4251
HOGENOM	HOG000030537
InParanoid	Q55168
KO	K11354
OMA	CAQEPIQ
OrthoDB	EOG6G4VQG
PhylomeDB	Q55168
BRENDA	2.7.13.3
EvolutionaryTrace	Q55168
Proteomes	UP000001425
GO	GO:0016020 GO:0005524 GO:0042802 GO:0000155 GO:0004673 GO:0009883 GO:0009584 GO:0018106 GO:0046777 GO:0018298 GO:0009585 GO:0006355 GO:0009639
Gene3D	1.10.287.130 3.30.450.40 3.30.565.10
InterPro	IPR003661 IPR003018 IPR029016 IPR003594 IPR000014 IPR013654 IPR016132 IPR001294 IPR013515 IPR005467 IPR009082
Pfam	PF01590 PF02518 PF00512 PF08446 PF00360
PRINTS	PR01033
SMART	SM00065 SM00387 SM00388 SM00091
SUPFAM	SSF47384 SSF55781 SSF55785 SSF55874
PROSITE	PS50109 PS50046

Annotations

Qualifier	GO ID	GO term name	Reference	ECO ID	ECO term name	with/from	Aspect	Notes	Status
	GO:0004673	protein histidine kinase activity	PMID:9278513^[1]	ECO:0000250		UniProtKB:	F	Fig 1B: shows sequence homology between prokaryotic Cph1 and collection of 21 eukaryotic phytochromes	complete
involved_in	GO:0046777	protein autophosphorylation	PMID:9278513^[1]	ECO:0000314	direct assay evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0018298	protein-chromophore linkage	PMID:15641769^[2]	ECO:0000314	direct assay evidence used in manual assertion		P	Seeded From UniProt	complete
enables	GO:0009883	red or far-red light photoreceptor activity	PMID:15641769^[2]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
involved_in	GO:0009639	response to red or far red light	PMID:9278513^[1]	ECO:0000314	direct assay evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0009585	red, far-red light phototransduction	PMID:15641769^[2]	ECO:0000314	direct assay evidence used in manual assertion		P	Seeded From UniProt	complete
enables	GO:0004673	protein histidine kinase activity	PMID:9278513^[1]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
enables	GO:0042802	identical protein binding	PMID:9278513^[1]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:Q55168	F	Seeded From UniProt	complete
enables	GO:0042802	identical protein binding	PMID:22641032^[3]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:Q55168	F	Seeded From UniProt	complete
enables	GO:0042802	identical protein binding	PMID:16844775^[4]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:Q55168	F	Seeded From UniProt	complete
enables	GO:0042802	identical protein binding	PMID:15641769^[2]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:Q55168	F	Seeded From UniProt	complete
enables	GO:0042802	identical protein binding	PMID:12741847^[5]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:Q55168	F	Seeded From UniProt	complete
enables	GO:0042802	identical protein binding	PMID:11532008^[6]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:Q55168	F	Seeded From UniProt	complete
involved_in	GO:0000160	phosphorelay signal transduction system	GO_REF:0000108	ECO:0000366	evidence based on logical inference from automatic annotation used in automatic assertion	GO:0000155	P	Seeded From UniProt	complete
involved_in	GO:0018106	peptidyl-histidine phosphorylation	GO_REF:0000108	ECO:0000364	evidence based on logical inference from manual annotation used in automatic assertion	GO:0004673	P	Seeded From UniProt	complete
involved_in	GO:0018106	peptidyl-histidine phosphorylation	GO_REF:0000108	ECO:0000366	evidence based on logical inference from automatic annotation used in automatic assertion	GO:0004673	P	Seeded From UniProt	complete
involved_in	GO:0023014	signal transduction by protein phosphorylation	GO_REF:0000108	ECO:0000366	evidence based on logical inference from automatic annotation used in automatic assertion	GO:0000155	P	Seeded From UniProt	complete
enables	GO:0000155	phosphorelay sensor kinase activity	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR003661 InterPro:IPR036097	F	Seeded From UniProt	complete
involved_in	GO:0006355	regulation of transcription, DNA-templated	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR001294 InterPro:IPR013515 InterPro:IPR013654	P	Seeded From UniProt	complete
involved_in	GO:0007165	signal transduction	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR003661 InterPro:IPR036097	P	Seeded From UniProt	complete
involved_in	GO:0009584	detection of visible light	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR001294 InterPro:IPR013515	P	Seeded From UniProt	complete
involved_in	GO:0018298	protein-chromophore linkage	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR013515 InterPro:IPR016132	P	Seeded From UniProt	complete
enables	GO:0004673	protein histidine kinase activity	GO_REF:0000003	ECO:0000501	evidence used in automatic assertion	EC:2.7.13.3	F	Seeded From UniProt	complete
enables	GO:0000166	nucleotide binding	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0547	F	Seeded From UniProt	complete
enables	GO:0016740	transferase activity	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0808	F	Seeded From UniProt	complete
involved_in	GO:0016310	phosphorylation	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0418	P	Seeded From UniProt	complete
involved_in	GO:0018298	protein-chromophore linkage	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0157	P	Seeded From UniProt	complete
involved_in	GO:0050896	response to stimulus	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0716	P	Seeded From UniProt	complete
enables	GO:0009881	photoreceptor activity	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0600	F	Seeded From UniProt	complete
enables	GO:0016301	kinase activity	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0418	F	Seeded From UniProt	complete
enables	GO:0005524	ATP binding	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0067	F	Seeded From UniProt	complete
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Notes

References

See Help:References for how to manage references in GONUTS.

↑ ^1.0 ^1.1 ^1.2 ^1.3 ^1.4 Yeh, KC et al. (1997) A cyanobacterial phytochrome two-component light sensory system. Science 277 1505-8 PubMed GONUTS page
↑ ^2.0 ^2.1 ^2.2 ^2.3 Esteban, B et al. (2005) Light-induced conformational changes of cyanobacterial phytochrome Cph1 probed by limited proteolysis and autophosphorylation. Biochemistry 44 450-61 PubMed GONUTS page
↑ Eisenhardt, BD & Forreiter, C (2012) Insights in small Heat Shock Protein/client interaction by combined protection analysis of two different client proteins. FEBS Lett. 586 1772-7 PubMed GONUTS page
↑ Miller, AE et al. (2006) Single-molecule dynamics of phytochrome-bound fluorophores probed by fluorescence correlation spectroscopy. Proc. Natl. Acad. Sci. U.S.A. 103 11136-41 PubMed GONUTS page
↑ Otto, H et al. (2003) Dimerization and inter-chromophore distance of Cph1 phytochrome from Synechocystis, as monitored by fluorescence homo and hetero energy transfer. Biochemistry 42 5885-95 PubMed GONUTS page
↑ Lamparter, T et al. (2001) Phytochrome Cph1 from the cyanobacterium Synechocystis PCC6803. Purification, assembly, and quaternary structure. Eur. J. Biochem. 268 4720-30 PubMed GONUTS page

[PMID:9278513-1] 1.0 ^1.1 ^1.2 ^1.3 ^1.4 Yeh, KC et al. (1997) A cyanobacterial phytochrome two-component light sensory system. Science 277 1505-8 PubMed GONUTS page

[PMID:15641769-2] 2.0 ^2.1 ^2.2 ^2.3 Esteban, B et al. (2005) Light-induced conformational changes of cyanobacterial phytochrome Cph1 probed by limited proteolysis and autophosphorylation. Biochemistry 44 450-61 PubMed GONUTS page

[PMID:22641032-3] Eisenhardt, BD & Forreiter, C (2012) Insights in small Heat Shock Protein/client interaction by combined protection analysis of two different client proteins. FEBS Lett. 586 1772-7 PubMed GONUTS page

[PMID:16844775-4] Miller, AE et al. (2006) Single-molecule dynamics of phytochrome-bound fluorophores probed by fluorescence correlation spectroscopy. Proc. Natl. Acad. Sci. U.S.A. 103 11136-41 PubMed GONUTS page

[PMID:12741847-5] Otto, H et al. (2003) Dimerization and inter-chromophore distance of Cph1 phytochrome from Synechocystis, as monitored by fluorescence homo and hetero energy transfer. Biochemistry 42 5885-95 PubMed GONUTS page

[PMID:11532008-6] Lamparter, T et al. (2001) Phytochrome Cph1 from the cyanobacterium Synechocystis PCC6803. Purification, assembly, and quaternary structure. Eur. J. Biochem. 268 4720-30 PubMed GONUTS page

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SYNY3:PHY1

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