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Database: UniProt
Entry: A0A2R5FR93_NOSCO
LinkDB: A0A2R5FR93_NOSCO
Original site: A0A2R5FR93_NOSCO 
ID   A0A2R5FR93_NOSCO        Unreviewed;       909 AA.
AC   A0A2R5FR93;
DT   20-JUN-2018, integrated into UniProtKB/TrEMBL.
DT   20-JUN-2018, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=NIES4072_45070 {ECO:0000313|EMBL:GBG20825.1};
OS   Nostoc commune NIES-4072.
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Nostocaceae; Nostoc.
OX   NCBI_TaxID=2005467 {ECO:0000313|EMBL:GBG20825.1, ECO:0000313|Proteomes:UP000245124};
RN   [1] {ECO:0000313|EMBL:GBG20825.1, ECO:0000313|Proteomes:UP000245124}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NIES-4072 {ECO:0000313|EMBL:GBG20825.1,
RC   ECO:0000313|Proteomes:UP000245124};
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:GBG20825.1}.
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DR   EMBL; BDUD01000001; GBG20825.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2R5FR93; -.
DR   OrthoDB; 474548at2; -.
DR   Proteomes; UP000245124; Unassembled WGS sequence.
DR   GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0009584; P:detection of visible light; IEA:InterPro.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR   Gene3D; 1.10.287.130; -; 1.
DR   Gene3D; 3.30.450.40; -; 3.
DR   Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal 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; IPR016132; Phyto_chromo_attachment.
DR   InterPro; IPR013515; Phytochrome_cen-reg.
DR   InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR   PANTHER; PTHR43065:SF50; HISTIDINE KINASE; 1.
DR   PANTHER; PTHR43065; SENSOR HISTIDINE KINASE; 1.
DR   Pfam; PF01590; GAF; 2.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF00360; PHY; 1.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00065; GAF; 3.
DR   SMART; SM00387; HATPase_c; 1.
DR   SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR   SUPFAM; SSF55781; GAF domain-like; 3.
DR   PROSITE; PS50109; HIS_KIN; 1.
DR   PROSITE; PS50046; PHYTOCHROME_2; 2.
PE   3: Inferred from homology;
KW   Kinase {ECO:0000313|EMBL:GBG20825.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000245124};
KW   Transferase {ECO:0000313|EMBL:GBG20825.1}.
FT   DOMAIN          32..199
FT                   /note="Phytochrome chromophore attachment site"
FT                   /evidence="ECO:0000259|PROSITE:PS50046"
FT   DOMAIN          454..587
FT                   /note="Phytochrome chromophore attachment site"
FT                   /evidence="ECO:0000259|PROSITE:PS50046"
FT   DOMAIN          644..903
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
SQ   SEQUENCE   909 AA;  103469 MW;  976B84772EE3EDEC CRC64;
     MTFTHKPNGL QQSLDQESLL HQMINQIRRS LDLQDILTTT VSQVRLFLGA DRVKVYRFDS
     DGSGEVIAES IHEQRLPSLL GQRFPADDIP QEAREMFLLV GQRSIVDVAN GKIGLSPLQS
     KETGKLLRTN IHYRQVDPCH IQYLKAMGVQ SSLIVPILDC DLQEESAKPK LWGLLVSHHS
     KPRKISKQEL KVLQQVADQV AIAIAQSNLL TAARTKQERE ATINRVTTLL HKLPTVQLQG
     ALEEVITAFN GTGGRLYIEQ SQELYTWGVQ PTLPYELYNN IIEQHPIWQN WMAEFKQGNI
     WATTDLYKEP HLRVLALAFR STQIRGLMVI PIHDREKFIG VLSIFRSEFE TEILWAGRCE
     KNRRQLLPQL SFELWREQKK GQSAQWKPED ISLAQALYDH FSMAIQQQQM FRQVQTLNGN
     LELRVQEQTY ELEKSLLFTK VLKQVTEHIR RTLDLQTTLQ SIVREVRALL NSDRMVIFEL
     KRKSVIVEEI NGNWQSVLGM NAPSDCFPDE YTHLYSQGRV RVISNVSTAS LNDCHRKFLQ
     SLQVQATLIV PINIGIEVWG LLIAHECETP RNWEDAEIDL LQQLGDQAAI AIQQAQLYEQ
     TCNAEAEARN QAAQLEHTLH ELQETQTKLI HTEKMSGLGQ LVAGVAHEIN NPVNFIYANL
     CHASDYTEKI LEILRLYQLH YPQPHSEISA AIKAMDFEFL VEDLPKIMTS MQVGSDRIRS
     IVLSLRSFSR LDEAENKRVD LHEGIDNTLL ILQHRLKGNG EFPGIEVIKD YGNIPRVECY
     AGQMNQVFMN IISNAIDALM GNGSKRDKEN AQYQMPTIHI STRVSADGSR LLIRISDNGS
     GMTEEVKRRI FDPFYTTKPV GKGTGLGLAI SYQIIVEKHG GIMECISEPG QGTEFWIEIP
     VTPPARIDR
//
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