ID A0A218QJV3_9CYAN Unreviewed; 767 AA.
AC A0A218QJV3;
DT 27-SEP-2017, integrated into UniProtKB/TrEMBL.
DT 27-SEP-2017, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=NIES4075_31880 {ECO:0000313|EMBL:GAX42188.1};
OS Tolypothrix sp. NIES-4075.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Tolypothrichaceae;
OC Tolypothrix.
OX NCBI_TaxID=2005459 {ECO:0000313|EMBL:GAX42188.1, ECO:0000313|Proteomes:UP000198313};
RN [1] {ECO:0000313|EMBL:GAX42188.1, ECO:0000313|Proteomes:UP000198313}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NIES-4075 {ECO:0000313|EMBL:GAX42188.1,
RC ECO:0000313|Proteomes:UP000198313};
RA Hirose Y., Shimura Y., Fujisawa T., Nakamura Y., Kawachi M.;
RT "Genome sequencing of cyanobaciteial culture collection at National
RT Institute for Environmental Studies (NIES).";
RL Submitted (JUN-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + protein L-histidine = ADP + protein N-phospho-L-
CC histidine.; EC=2.7.13.3; Evidence={ECO:0000256|ARBA:ARBA00000085};
CC -!- SIMILARITY: In the N-terminal section; belongs to the phytochrome
CC family. {ECO:0000256|ARBA:ARBA00006402}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:GAX42188.1}.
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DR EMBL; BDUC01000003; GAX42188.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A218QJV3; -.
DR OrthoDB; 9760752at2; -.
DR Proteomes; UP000198313; Unassembled WGS sequence.
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; cd16921; HATPase_FilI-like; 1.
DR CDD; cd00082; HisKA; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.30.450.270; -; 1.
DR Gene3D; 3.30.450.40; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 3.30.450.20; PAS domain; 1.
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 PANTHER; PTHR43304:SF1; PAC DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR43304; PHYTOCHROME-LIKE PROTEIN CPH1; 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 PRINTS; PR01033; PHYTOCHROME.
DR SMART; SM00065; GAF; 1.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 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.
PE 3: Inferred from homology;
KW Chromophore {ECO:0000256|ARBA:ARBA00022991};
KW Kinase {ECO:0000313|EMBL:GAX42188.1};
KW Photoreceptor protein {ECO:0000256|ARBA:ARBA00022543};
KW Receptor {ECO:0000256|ARBA:ARBA00022543};
KW Reference proteome {ECO:0000313|Proteomes:UP000198313};
KW Sensory transduction {ECO:0000256|ARBA:ARBA00022606};
KW Transferase {ECO:0000313|EMBL:GAX42188.1}.
FT DOMAIN 151..309
FT /note="Phytochrome chromophore attachment site"
FT /evidence="ECO:0000259|PROSITE:PS50046"
FT DOMAIN 534..747
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
SQ SEQUENCE 767 AA; 87522 MW; 7B75900C3FF61F80 CRC64;
MTIELPEISI NVTSLKEAPI HISSQIQPHG VLLVLTDDLK ILQTSSNTSK IFGISPERML
EKQLEDLLDS FQVERIKAGL AEENLDLINP TKIWVRKKGD EYVAFDAIFH RNKEGFLILE
LEPTTSQENI PFLSFYHLAR ASINKLEATS NLRDFSQIIV QEVRKVTGFD RVMLYKFDDD
GHGSVIAEEK IESMESYLGL HYPESDIPKP ARKLFVSNSI RLIPDANSQP TQIFPVNNPV
NQRPLDLTNS ILRSASPCHI EYLHNMGVGA SLTISLIKEG KLWGLIACHH QSPKYVSFEL
RKACEFLGRL IFSEISVKEE TEDYDYRMKL TYIQSALIDY MSQEENFIDG LVKHEPNILE
LTSAQGAAVC FGEKCTLIGE TPSEEDLNFL VQWLKNNVDE EVFYTDSLPH IYPDAERYKN
VASGLLAIPI SKRNYVLWFR PEVIQTVNWG GDPNNAFEVN QSQGNVRLCP RKSFELWKET
VRLTSLPWKY VEIKAALELR KAIVNIVLRQ ADELAQLAHD LERSNAELKK FAYVASHDLQ
EPLNQVANYV QLLEMRYHEE LDEDAKEFIN FTVEGVSLMQ TLIDDVLAYS KVDMQAIDFE
LTEVNTALVR ALGSLRGRIG ETKAVITHEE MPSIMADSTQ LMQLFQNLIG NAIKFRSDKL
PEIHIAASRL EDDWLFSVRD NGIGIDPQFS DRIFVIFQRL HTRDEYPGTG MGLAICKKIV
ECHRGRIWVE SQPGEGATFY FTIPVRGRDR ERRNGRKAQN HLFGRGQ
//
