ID A0A218Q7S9_9CYAN Unreviewed; 1180 AA.
AC A0A218Q7S9;
DT 27-SEP-2017, integrated into UniProtKB/TrEMBL.
DT 27-SEP-2017, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=NIES3585_39870 {ECO:0000313|EMBL:GAX37941.1};
OS Nodularia sp. NIES-3585.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Aphanizomenonaceae;
OC Nodularia.
OX NCBI_TaxID=1973477 {ECO:0000313|EMBL:GAX37941.1, ECO:0000313|Proteomes:UP000198352};
RN [1] {ECO:0000313|EMBL:GAX37941.1, ECO:0000313|Proteomes:UP000198352}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NIES-3585 {ECO:0000313|EMBL:GAX37941.1,
RC ECO:0000313|Proteomes:UP000198352};
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 -!- 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:GAX37941.1}.
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DR EMBL; BDUB01000001; GAX37941.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A218Q7S9; -.
DR OrthoDB; 453200at2; -.
DR Proteomes; UP000198352; Unassembled WGS sequence.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd00075; HATPase; 1.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd00130; PAS; 5.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 2.10.70.100; -; 1.
DR Gene3D; 3.10.580.10; CBS-domain; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 3.30.450.20; PAS domain; 5.
DR InterPro; IPR000644; CBS_dom.
DR InterPro; IPR046342; CBS_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; IPR001610; PAC.
DR InterPro; IPR000014; PAS.
DR InterPro; IPR000700; PAS-assoc_C.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR013656; PAS_4.
DR InterPro; IPR013655; PAS_fold_3.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR NCBIfam; TIGR00229; sensory_box; 6.
DR PANTHER; PTHR43304:SF1; PAC DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR43304; PHYTOCHROME-LIKE PROTEIN CPH1; 1.
DR Pfam; PF00571; CBS; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF08447; PAS_3; 3.
DR Pfam; PF08448; PAS_4; 1.
DR Pfam; PF13426; PAS_9; 2.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00116; CBS; 1.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00086; PAC; 5.
DR SMART; SM00091; PAS; 5.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF54631; CBS-domain pair; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 6.
DR PROSITE; PS51371; CBS; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50113; PAC; 6.
DR PROSITE; PS50112; PAS; 5.
PE 4: Predicted;
KW CBS domain {ECO:0000256|PROSITE-ProRule:PRU00703};
KW Kinase {ECO:0000313|EMBL:GAX37941.1};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Transferase {ECO:0000313|EMBL:GAX37941.1}.
FT DOMAIN 16..71
FT /note="CBS"
FT /evidence="ECO:0000259|PROSITE:PS51371"
FT DOMAIN 227..279
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 312..382
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 385..438
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 439..493
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 512..563
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 560..602
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 631..683
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 686..729
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 756..808
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 809..883
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 885..937
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 955..1171
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
SQ SEQUENCE 1180 AA; 132848 MW; 7D51E3632EFB0A74 CRC64;
MQALPQIPWL QCFKSIIDFD PVTVDPETSV LDAVFLMANH GVSVLVVSVS QVVGWLTQKY
VVQLLASGVD LKTTKISEVM QTIKVTLKFA EFQSTTNVFS LLQPHSWEIL LVIDDHNQLI
GIITPDSICQ AIAKPEEKTQ DKSSQTPAER LHLLESAMLN TNDAILMTEA DALDEPFVPR
IVSDRAALLQ ADRLYENLRE NLLDSNHPLD RHGCIGVLDN LLLGKNLNVE FRILRSSGEV
RWICAKTFPV NNQKGELYRF AGIAEDITEL KQTQAALTQV NQELEMRVTE RTITLTQLNQ
QLISEITERQ ISEERFRFMA ESIPQQVWIA QANGELEYVN QRAVDYFVCS SEQLLGVGWQ
QWIHPDDLPD TLSGWQQSLR TGQPHEAEFR CLRGSDQTYR WHLIRALPMR DQEGKIINWF
GTNTDIDDHV STEMTLRQTQ QQLQAILDNS PAVIYLIDTN GKNLLVNRKY QQLLNLSQNQ
IIGKTLHEIW PDDLADEFDT NNRQVILDGV ALETEEIVPL KDGLHTYLSN KFPLKDANGL
LYAVGGISTD ITQRKLAEES LLRFRKAIES TSDAVLIGDI TGAAIYVNPA FIEQYEYTLE
ELQAAGGCRV IFEHSGVYEK ISATVKMTQS WRGEVTFRAS SGRLVQVYLR SDAIKDATGK
GVGTICIYTD ITQRKRTEEG LRLRDRAIAA SSNGIIIADA SLPHSPIIYV NPAFERMTGY
CAAEVIGRNF CSFQSADINQ SGLKELSAAM DAGINCTVTL SNYRKDGSLL WNELSISPVY
DVAGKLTHYI TIQTNITERK QAETALLVSQ QRLQYLLSSS PAVIYTTTTT GDLSSTFISE
NVSTMTGYKA GEIVENSSFW STHIHPEDLS YVCAEISQAL EKQDYTLEYR FLHQDGTYRW
LYDKGKLVRD EAGNPLEFVG YLADITEHKQ LEQELKVALE NEKELNELKS RFVSMTSHEF
RTPLSTILSS SELLEHYSHK WTVEKQLTHL HRIQAAVKRM TEMLNDVLVI GKAEAGKLEY
RPKFFDLVEY CRDLLSEAQM NQNNMCRVNF TSQYESVPCC MDEKLLGHIL NNLLSNAIKY
SPDEGIIQFT LACQNGEAIF QIQDQGIGIP QEDIPHLFES FHRARNVGNI LGTGLGLAIV
KNCVDLHQGK ISVSSTLEAG TVFTVILPLN NHINIGVKND
//
