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Database: UniProt
Entry: D7DZX5_NOSA0
LinkDB: D7DZX5_NOSA0
Original site: D7DZX5_NOSA0 
ID   D7DZX5_NOSA0            Unreviewed;       443 AA.
AC   D7DZX5;
DT   10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT   10-AUG-2010, sequence version 1.
DT   27-MAR-2024, entry version 66.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   OrderedLocusNames=Aazo_2740 {ECO:0000313|EMBL:ADI64607.1};
OS   Nostoc azollae (strain 0708) (Anabaena azollae (strain 0708)).
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Nostocaceae;
OC   Trichormus.
OX   NCBI_TaxID=551115 {ECO:0000313|EMBL:ADI64607.1, ECO:0000313|Proteomes:UP000001511};
RN   [1] {ECO:0000313|EMBL:ADI64607.1, ECO:0000313|Proteomes:UP000001511}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=0708 {ECO:0000313|EMBL:ADI64607.1,
RC   ECO:0000313|Proteomes:UP000001511};
RX   PubMed=20628610; DOI=10.1371/journal.pone.0011486;
RA   Ran L., Larsson J., Vigil-Stenman T., Nylander J.A., Ininbergs K.,
RA   Zheng W.W., Lapidus A., Lowry S., Haselkorn R., Bergman B.;
RT   "Genome erosion in a nitrogen-fixing vertically transmitted endosymbiotic
RT   multicellular cyanobacterium.";
RL   PLoS ONE 5:E11486-E11486(2010).
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};
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DR   EMBL; CP002059; ADI64607.1; -; Genomic_DNA.
DR   RefSeq; WP_013191623.1; NC_014248.1.
DR   AlphaFoldDB; D7DZX5; -.
DR   STRING; 551115.Aazo_2740; -.
DR   KEGG; naz:Aazo_2740; -.
DR   eggNOG; COG2205; Bacteria.
DR   HOGENOM; CLU_000445_89_2_3; -.
DR   OrthoDB; 9773956at2; -.
DR   Proteomes; UP000001511; Chromosome.
DR   GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR   CDD; cd00075; HATPase; 1.
DR   CDD; cd00082; HisKA; 1.
DR   Gene3D; 1.10.287.130; -; 1.
DR   Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
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; IPR000014; PAS.
DR   InterPro; IPR035965; PAS-like_dom_sf.
DR   InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR   PANTHER; PTHR45453; PHOSPHATE REGULON SENSOR PROTEIN PHOR; 1.
DR   PANTHER; PTHR45453:SF1; PHOSPHATE REGULON SENSOR PROTEIN PHOR; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF00512; HisKA; 1.
DR   Pfam; PF13188; PAS_8; 1.
DR   PRINTS; PR00344; BCTRLSENSOR.
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; 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.
PE   4: Predicted;
KW   Kinase {ECO:0000313|EMBL:ADI64607.1};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001511};
KW   Transferase {ECO:0000313|EMBL:ADI64607.1}.
FT   DOMAIN          197..434
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
SQ   SEQUENCE   443 AA;  50915 MW;  F95EAAADFE1805E2 CRC64;
     MLLLGFVLGL AVGFGFWLWQ QIQLNRYLER VLQPLGSHSG KIGLPLLPCL RQEMSTVKQQ
     HQDLQLSLQT YKELLDFAPL GYLQVDEENQ LLWCNQQARE ILHLHRWEPG QVRLLLELVR
     SYELDQLIEQ TRDWQKPQVR EWIFHPSLDN PKAMLELKPL ALQAFTLPLP QREVGVFLEN
     RQPLLDMNHQ RDRSFSDLAH ELRTPLTSIR LVAETLQTRL EPPLDRWVNR LMQEVDRLIN
     LVQSWLELTE IETNSTMVLN LESVDVRSLI ASVWETIEPL TQNQHLSISY TGTQKICIQA
     DKSRMYQVFV NLLDNSIKYS PADTTIFIEM KVISVNEFIM GDRFSQALEI NIIDSGIGFA
     TTDLPHVFER FYRGDKARHH ESLPEGKTIT AITGSGLGLA IVQQIIIAHG GIIKAMNHPD
     TGGAWIQIQL PEVVANSPRQ DYS
//
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