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Database: UniProt
Entry: A0A0C1QY98_9CYAN
LinkDB: A0A0C1QY98_9CYAN
Original site: A0A0C1QY98_9CYAN 
ID   A0A0C1QY98_9CYAN        Unreviewed;       472 AA.
AC   A0A0C1QY98;
DT   01-APR-2015, integrated into UniProtKB/TrEMBL.
DT   01-APR-2015, sequence version 1.
DT   27-MAR-2024, entry version 32.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
DE   Flags: Fragment;
GN   ORFNames=DA73_0229470 {ECO:0000313|EMBL:KIE08663.1};
OS   Tolypothrix bouteillei VB521301.
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Tolypothrichaceae;
OC   Tolypothrix.
OX   NCBI_TaxID=1479485 {ECO:0000313|EMBL:KIE08663.1};
RN   [1] {ECO:0000313|EMBL:KIE08663.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=VB521301 {ECO:0000313|EMBL:KIE08663.1};
RX   PubMed=25700407;
RA   Chandrababunaidu M.M., Singh D., Sen D., Bhan S., Das S., Gupta A.,
RA   Adhikary S.P., Tripathy S.;
RT   "Draft Genome Sequence of Tolypothrix boutellei Strain VB521301.";
RL   Genome Announc. 3:e00001-15(2015).
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   -!- 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:KIE08663.1}.
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DR   EMBL; JHEG02000058; KIE08663.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0C1QY98; -.
DR   STRING; 1479485.DA73_0229470; -.
DR   OrthoDB; 5401154at2; -.
DR   GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR   CDD; cd00082; HisKA; 1.
DR   Gene3D; 1.10.287.130; -; 1.
DR   Gene3D; 3.30.450.40; -; 1.
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; IPR003661; HisK_dim/P.
DR   InterPro; IPR036097; HisK_dim/P_sf.
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; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   PRINTS; PR00344; BCTRLSENSOR.
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; 1.
DR   SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR   PROSITE; PS50109; HIS_KIN; 1.
PE   4: Predicted;
KW   Coiled coil {ECO:0000256|SAM:Coils}; Kinase {ECO:0000313|EMBL:KIE08663.1};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Serine/threonine-protein kinase {ECO:0000313|EMBL:KIE08663.1};
KW   Transferase {ECO:0000313|EMBL:KIE08663.1}.
FT   DOMAIN          222..472
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   COILED          179..210
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:KIE08663.1"
SQ   SEQUENCE   472 AA;  52655 MW;  6AA818750CFFF803 CRC64;
     ITTTSSKINA SLTFDILTVV KASQALSGEI VLERLLKKLM HLVRENAGAQ KVVFAIEKDN
     KLLVEGYLSE DGEAMVCQSQ SINSLTLLPK TLITYVQRTH EPLVLDNASH NQQFNSDPYI
     ITHQPKSILV LPIFYQSNIV GILYLENNLT KGAFTHDRVE VLQILAAQAA ISLENANFYN
     TLETRVAQRT QELQNTLEEL QRTQLQMIQN EKMSSLGQLV AGIAHEINNP INFIYGNLTH
     ISNYTQSLLT LVDIYLENPS ISLSAILEKA EEIDLEYIRA DLPKLLNSLQ TGASRIRDIV
     QSLRNFSRLD EAAIKAVDVH QGIDNTLMIL SSKLEGIKVI KEYANLPLVN CYAAELNQVF
     MHLLTNAVDA IEESSVLDRN LLRNEKGEIR IRTELRQHNQ VAISIKDNGI GMTAQVQNKM
     CDPFFTTKPV GKGNGLGLSI SYQIVVEKHG GRLICHSVPG ESTEFTLLLP CR
//
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