ID   Q8YWI8_NOSS1            Unreviewed;      1787 AA.
AC   Q8YWI8;
DT   01-MAR-2002, integrated into UniProtKB/TrEMBL.
DT   01-MAR-2002, sequence version 1.
DT   27-MAR-2024, entry version 133.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   OrderedLocusNames=all1625 {ECO:0000313|EMBL:BAB77991.1};
OS   Nostoc sp. (strain PCC 7120 / SAG 25.82 / UTEX 2576).
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Nostocaceae; Nostoc.
OX   NCBI_TaxID=103690 {ECO:0000313|EMBL:BAB77991.1, ECO:0000313|Proteomes:UP000002483};
RN   [1] {ECO:0000313|EMBL:BAB77991.1, ECO:0000313|Proteomes:UP000002483}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PCC 7120 / SAG 25.82 / UTEX 2576
RC   {ECO:0000313|Proteomes:UP000002483};
RX   PubMed=11759840; DOI=10.1093/dnares/8.5.205;
RA   Kaneko T., Nakamura Y., Wolk C.P., Kuritz T., Sasamoto S., Watanabe A.,
RA   Iriguchi M., Ishikawa A., Kawashima K., Kimura T., Kishida Y., Kohara M.,
RA   Matsumoto M., Matsuno A., Muraki A., Nakazaki N., Shimpo S., Sugimoto M.,
RA   Takazawa M., Yamada M., Yasuda M., Tabata S.;
RT   "Complete genomic sequence of the filamentous nitrogen-fixing
RT   cyanobacterium Anabaena sp. strain PCC 7120.";
RL   DNA Res. 8:205-213(2001).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC         [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC         COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC         Evidence={ECO:0000256|ARBA:ARBA00001433};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC         threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC         Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC         EC=2.7.11.1; Evidence={ECO:0000256|ARBA:ARBA00000775};
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; BA000019; BAB77991.1; -; Genomic_DNA.
DR   PIR; AC2009; AC2009.
DR   RefSeq; WP_010995794.1; NZ_RSCN01000013.1.
DR   STRING; 103690.gene:10493642; -.
DR   KEGG; ana:all1625; -.
DR   eggNOG; COG0515; Bacteria.
DR   eggNOG; COG3899; Bacteria.
DR   eggNOG; COG4191; Bacteria.
DR   OrthoDB; 573511at2; -.
DR   Proteomes; UP000002483; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   CDD; cd14014; STKc_PknB_like; 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   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR041664; AAA_16.
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; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR   PANTHER; PTHR43642; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE G; 1.
DR   PANTHER; PTHR43642:SF1; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE G; 1.
DR   Pfam; PF13191; AAA_16; 1.
DR   Pfam; PF01590; GAF; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00065; GAF; 1.
DR   SMART; SM00387; HATPase_c; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR   SUPFAM; SSF55781; GAF domain-like; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS50109; HIS_KIN; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   4: Predicted;
KW   Kinase {ECO:0000313|EMBL:BAB77991.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002483};
KW   Transferase {ECO:0000313|EMBL:BAB77991.1}.
FT   DOMAIN          13..271
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   DOMAIN          1532..1787
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
SQ   SEQUENCE   1787 AA;  201059 MW;  96C87CDD9735267F CRC64;
     MDTANSQPII PGYQISSQIY AGSKSRVYRA TREQDTLTVI IKVLTSEYPS FNELLQFRNQ
     YTISKNLNVT GITHPLSLDV YGNSYILVMK DTGGISLRQY TETAKLTLIE FLAIAIQLTN
     ILHGLHQNRV IHKDIKPANI LINPHTKQVE LIDFSIASLL PKETQEIKSP NILEGTLVYI
     SPEQTGRMNR GVDYRSDFYS LGVTFYELLT GELPFNSNDP MELVHSHIAK QPNKFNPESI
     PQVISDIVMK LMAKNAEDRY QSALGLKHDL ELCLTQLKDT GAIQNFEIGL RDICDRFLIP
     EKLYGRETEV ANLLAAFERV ANGASEMMLV AGFSGIGKTA VINEVHKPIT RQQGYFIKGK
     FDQFNRNIPF SAFVQALRDL MGQLLSESDT QLEQWRTKIL SSVGNNGQIL IEVIPELERV
     IGKQPAALEL SGMAAQNRFN LLFQKFLEVF TTKERPLVMF LDDLQWADSA SLNLIKLLME
     DENYLLLLGA YRDNEVSPVH PFMLTVTELK KTDKTVNTIT LAPLALSDTN QLVSDTLHCP
     TERSLLLTEL IVRKTQGNPF FTTQFLKALH ENEWIIFNRH QGYWECDISQ INALSLTDDV
     VEFMAHQLQK LPSETQQILK LAACIGNQFD LVTLAIVSEQ LQAQTAVALW KALQSGLILP
     QGEVYKFYLS DDQQNLNNQN IKNVTYRFLH DRVQQAAYSL IPDVQKQTTH LNIGTLLLAN
     LSVNEREERI FEIVNHLNIG SKLITQTSQK EELAKLNLLA GTRAKSSTAY SAALAYITAG
     MELLSADCWE IDYHLSLTLF KERAEVEYLN GNFAAAECWL QETIGKAKAP LEKAEVYNMA
     IVQHTLQANY PEAIQAGRQA LALINIDLPD ADFDIVRDAE LAIIQATLKQ RSFSELIDLP
     MMSQPEQKMA IKLLISMGPP TYRSHQRLWS VICAKAVNLC LQYGNTPEIG YIYPAFGGLR
     GYALSNYQGT SELLDVTLQL IQTFNNKSAE SVAYLMIGSS LRHWSHPLSV ATEDYLSSYR
     VGLESSNLQY AAYAFGHNMY CRFYQSVHLE QLFTEIVESL AFSRKYKNQW AIDLFLGGQI
     ILAELMGTTT DISESNYLEQ CRQHKNWQVI CIYNILKSQI LFCSERVEEA FFYSEQAESE
     IINVAPQGLL PYVHHCFIHA LLLLTRYPTL SEQQQQSAWE KISTYQQKLA VWSQNNPVNF
     LHLSCLVQAE MDRVVGNSLG AIENYDRAIA EAKANTYFQE EALANQLAAK FYLDWGKQKI
     ATSYMEEAYY CYAHWGAKAK VDDLEHRYPN LLSPIFQKAA PTVSPLVTLT SIDIPNISIH
     SSTSTSRSSS TRINTALDFA AILKASQSLS STIQLDELLQ QLTQIILHNS GGDRCALILP
     NSRGEWLLRA IATTDFTELC SEPVEGNLNL PVKLIQYVKN TQDIVVIDEL KTDLPVIDEY
     LHQQQPQSVL CLPILNQGNL IGILYLKNCS TRAVFTSDRI LILNFLCTQA AISLENARLY
     QQAQTYAQQL EQSQLHIVQS EKMASLGNLV AGVAHEVNNP IGFLNGSISN AKEYVHDLIG
     HLQLYQQHYS QPVAPIQDNA EEIDLEFLVA DLPKLLNSMT EATKRITSIS TSLRTFSRAD
     TDHTVSADIH EGLDSTIMIL KYRIKANQHR PEIIIQKEYG KIPPVECFPG QLNQVFMNIL
     ANAIDMFDEM AQMHTFTEMQ THPQKITIRT EAISNQVSIR IRDNGKGMSA QVQQKIFDHL
     FTTKGVGKGT GLGLAIARQI ITEKHGGTIK VNSILGEGTE FAIAIPL
//