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Database: UniProt
Entry: K9X150_9NOST
LinkDB: K9X150_9NOST
Original site: K9X150_9NOST 
ID   K9X150_9NOST            Unreviewed;       998 AA.
AC   K9X150;
DT   06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2013, sequence version 1.
DT   24-JAN-2024, entry version 54.
DE   SubName: Full=Bacteriophytochrome (Light-regulated signal transduction histidine kinase) {ECO:0000313|EMBL:AFZ25472.1};
GN   ORFNames=Cylst_3320 {ECO:0000313|EMBL:AFZ25472.1};
OS   Cylindrospermum stagnale PCC 7417.
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Nostocaceae;
OC   Cylindrospermum.
OX   NCBI_TaxID=56107 {ECO:0000313|EMBL:AFZ25472.1, ECO:0000313|Proteomes:UP000010475};
RN   [1] {ECO:0000313|EMBL:AFZ25472.1, ECO:0000313|Proteomes:UP000010475}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PCC 7417 {ECO:0000313|EMBL:AFZ25472.1,
RC   ECO:0000313|Proteomes:UP000010475};
RG   US DOE Joint Genome Institute;
RA   Gugger M., Coursin T., Rippka R., Tandeau De Marsac N., Huntemann M.,
RA   Wei C.-L., Han J., Detter J.C., Han C., Tapia R., Chen A., Kyrpides N.,
RA   Mavromatis K., Markowitz V., Szeto E., Ivanova N., Pagani I., Pati A.,
RA   Goodwin L., Nordberg H.P., Cantor M.N., Hua S.X., Woyke T., Kerfeld C.A.;
RT   "Finished chromosome of genome of Cylindrospermum stagnale PCC 7417.";
RL   Submitted (JUN-2012) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the phytochrome
CC       family. {ECO:0000256|ARBA:ARBA00006402}.
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DR   EMBL; CP003642; AFZ25472.1; -; Genomic_DNA.
DR   RefSeq; WP_015208721.1; NC_019757.1.
DR   AlphaFoldDB; K9X150; -.
DR   STRING; 56107.Cylst_3320; -.
DR   KEGG; csg:Cylst_3320; -.
DR   PATRIC; fig|56107.3.peg.3637; -.
DR   eggNOG; COG0745; Bacteria.
DR   eggNOG; COG4251; Bacteria.
DR   HOGENOM; CLU_000445_50_1_3; -.
DR   OrthoDB; 9760752at2; -.
DR   Proteomes; UP000010475; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR   GO; GO:0009881; F:photoreceptor activity; IEA:UniProtKB-KW.
DR   GO; GO:0009584; P:detection of visible light; IEA:InterPro.
DR   GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR   CDD; cd16922; HATPase_EvgS-ArcB-TorS-like; 1.
DR   CDD; cd00082; HisKA; 1.
DR   CDD; cd17546; REC_hyHK_CKI1_RcsC-like; 1.
DR   Gene3D; 1.10.287.130; -; 1.
DR   Gene3D; 3.30.450.270; -; 1.
DR   Gene3D; 3.30.450.40; -; 1.
DR   Gene3D; 3.40.50.2300; -; 1.
DR   Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR   Gene3D; 3.30.450.20; PAS domain; 1.
DR   InterPro; IPR011006; CheY-like_superfamily.
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; IPR036097; HisK_dim/P_sf.
DR   InterPro; IPR035965; PAS-like_dom_sf.
DR   InterPro; IPR013654; PAS_2.
DR   InterPro; IPR016132; Phyto_chromo_attachment.
DR   InterPro; IPR001294; Phytochrome.
DR   InterPro; IPR013515; Phytochrome_cen-reg.
DR   InterPro; IPR043150; Phytochrome_PHY_sf.
DR   InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR   PANTHER; PTHR45339; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE J; 1.
DR   PANTHER; PTHR45339:SF1; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE J; 1.
DR   Pfam; PF01590; GAF; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF00512; HisKA; 1.
DR   Pfam; PF08446; PAS_2; 1.
DR   Pfam; PF00360; PHY; 1.
DR   Pfam; PF00072; Response_reg; 1.
DR   PRINTS; PR01033; PHYTOCHROME.
DR   SMART; SM00065; GAF; 1.
DR   SMART; SM00387; HATPase_c; 1.
DR   SMART; SM00388; HisKA; 1.
DR   SMART; SM00448; REC; 1.
DR   SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR   SUPFAM; SSF52172; CheY-like; 1.
DR   SUPFAM; SSF55781; GAF domain-like; 2.
DR   SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR   SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 1.
DR   PROSITE; PS50109; HIS_KIN; 1.
DR   PROSITE; PS50046; PHYTOCHROME_2; 1.
DR   PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Chromophore {ECO:0000256|ARBA:ARBA00022991};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:AFZ25472.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW   ProRule:PRU00169}; Photoreceptor protein {ECO:0000256|ARBA:ARBA00022543};
KW   Receptor {ECO:0000256|ARBA:ARBA00022543};
KW   Reference proteome {ECO:0000313|Proteomes:UP000010475};
KW   Sensory transduction {ECO:0000256|ARBA:ARBA00022606};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          152..310
FT                   /note="Phytochrome chromophore attachment site"
FT                   /evidence="ECO:0000259|PROSITE:PS50046"
FT   DOMAIN          539..766
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   DOMAIN          793..909
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000259|PROSITE:PS50110"
FT   MOD_RES         842
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ   SEQUENCE   998 AA;  112939 MW;  88BC40EC5A5628E5 CRC64;
     MENTEVTISE LIDISNCDQE QIHIPGHIQP HGLLLALQEP HLKILQVSEN TNQLFGIPAE
     FLLGQNLTCL LSHEQIKFIT DALTQDNLAF VHLFEIKTEA SKSPHSFLGM LHRSHDVLIL
     ELEPHSSTET SLCLEKYHQL EKAVSSISNA SNLDKLFHII AQEVKNITQF DRVMLYRFEA
     DYSGVVIAED KQSNLESYLG LHYPATDIPT QARKFYYENL LRVIPDINYQ PVKIIPTNHP
     LTDRPLDLSG ALLRSISPLH VEYLQNMGVA ASMSISLINE NRLWGLIACH HYTPKYIDYD
     IRKTCEFIGQ FASLELLHQQ ESLLNFYRQQ VKLIQVQLSQ NLGNKLDYIG NVFQRNESSV
     LNLVRSTGAA ILLEGQLILI GNTPSESDTQ ELVTWLQNQN QQEIYYTDSL PQLYPNARNF
     QDIASGILAI SIILNQRSYH IIWFRPEQIQ IVHWAGNPNK PTSITSDNNL RLTPRKSFEL
     WKETVQEKSL PWQPFAIEVA QEMRNNLMLA ALEFSQMALQ EAAQQAEIAN RAKSHFLAKM
     SHELRTPLNA ILGFTQLITR NGSLSPEDQE NLDIINRSGE HLLILISDVL EMSKIEAGQL
     TLNESYFDLH RLIYSIQEML ALKASDKGLS LVTEIAENVS QFVCGDEGKL RQILINLIGN
     AVKFTIVGYI ALRVSYPSTS SSLATDQGKI VVEFELEDTG PGIAIDDLGL IFEAFVQAKS
     GRQFMQGTGL GLAISRQFAR LMGGDVTVRS ILGHGSTFTC QVQLTQVDTV DVLHPTQPTR
     RVIGLQPGQP NYRILVVEDV PENRQLIVKL LKSVGFEVRA AENGLEAIDI CQEWEPHFIW
     MDIQMPVMDG REATQRIRAI TQRKDLKIIA LTASAFEEDR KAILEIGCDD FVTKPFEETI
     LFDKMAHYLS LRYIYAENNQ QKLPEAKIQY QQLTLSDLQV MPTAWISQVH EAALIIDDTK
     LYELFAQIPE DQHQLADALK NLVENFHVGT IINLTSLP
//
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