ID   A0A2S6CUT2_9CYAN        Unreviewed;       658 AA.
AC   A0A2S6CUT2;
DT   18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT   18-JUL-2018, sequence version 1.
DT   27-MAR-2024, entry version 18.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=CUN59_09670 {ECO:0000313|EMBL:PPJ63523.1};
OS   Cuspidothrix issatschenkoi CHARLIE-1.
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Aphanizomenonaceae;
OC   Cuspidothrix.
OX   NCBI_TaxID=2052836 {ECO:0000313|EMBL:PPJ63523.1, ECO:0000313|Proteomes:UP000239589};
RN   [1] {ECO:0000313|EMBL:PPJ63523.1, ECO:0000313|Proteomes:UP000239589}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CHARLIE-1 {ECO:0000313|EMBL:PPJ63523.1,
RC   ECO:0000313|Proteomes:UP000239589};
RA   Kust A., Mares J., Jokela J., Urajova P., Hajek J., Saurav K., Voracova K.,
RA   Fewer D.P., Haapaniemi E., Permi P., Rehakova K., Sivonen K., Hrouzek P.;
RT   "Discovery of a pederin family compound in a non-symbiotic bloom-forming
RT   cyanobacterium.";
RL   Submitted (FEB-2018) 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   -!- 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:PPJ63523.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; PGEM01000065; PPJ63523.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2S6CUT2; -.
DR   OrthoDB; 524899at2; -.
DR   Proteomes; UP000239589; Unassembled WGS sequence.
DR   GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
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; IPR033415; CHASE6_C.
DR   InterPro; IPR019278; DICT_dom.
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; PTHR43711:SF1; HISTIDINE KINASE 1; 1.
DR   PANTHER; PTHR43711; TWO-COMPONENT HISTIDINE KINASE; 1.
DR   Pfam; PF17150; CHASE6_C; 1.
DR   Pfam; PF10069; DICT; 1.
DR   Pfam; PF01590; GAF; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF00512; HisKA; 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:PPJ63523.1};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000239589};
KW   Transferase {ECO:0000313|EMBL:PPJ63523.1}.
FT   DOMAIN          435..656
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   COILED          408..435
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   658 AA;  74228 MW;  7418F13439B53F5C CRC64;
     MSISTSVLTD LLKSLPYLRP QLYFKASLTA LSHAMEDQVL AATFDQPLII ASFQKERFYR
     QEAHRYQRLA EKSNQIYVLS APETEFADRS EYYEKIDFAP DDALSQEWHL VVVADNYATC
     LVCRESIASG SKNKHIPEMI PSLDMDTARR FEGIWTSEKE VCFKAAELLL NRIEIYRPNL
     AAKVQEVKQR FRIGESIDSL VVNADYKYAC DIDTDPFVQR LVTYLQASQY KLHKAYRSIA
     AQARKERLVN SIGAAIRRSL DPREILQVAA VELGQHLEAC RCLIYRAQAT DSKAIIEHEF
     VNSGVTSVLG QSWELEHNPL FQQVLQQLEG VCVADTLEDY QVKKSPALSS IVRQFGVRSW
     LIEPVLYQGR LLGIVELHNC HFPPHEWQSG ELDLVKAIAT QIGAALIQAE SFANLEELNQ
     QLEALDRTRS NLIAITGHEL RTPLSTIQVC LESLSTEPDM PWELQQVMLN TALADSERMR
     KLVQDFLTLS NLESGRVEWH PESLNLQECI DLALSRLRTR PISEAPPTIK TQIAANLPLI
     RADGDWLVEV LAKLIDNACK FTAPSGSINI KADYNSNQMV EVIISDTGRG IEPNRLEIIF
     DRFYQEEGAL RRTTGGTGLG LAISRQIVNG WSGKIWAESR GKDQGSQFHF TIPIVPGN
//