ID   Q8YQX0_NOSS1            Unreviewed;      2021 AA.
AC   Q8YQX0;
DT   01-MAR-2002, integrated into UniProtKB/TrEMBL.
DT   01-MAR-2002, sequence version 1.
DT   27-MAR-2024, entry version 141.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   OrderedLocusNames=all3691 {ECO:0000313|EMBL:BAB75390.1};
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:BAB75390.1, ECO:0000313|Proteomes:UP000002483};
RN   [1] {ECO:0000313|EMBL:BAB75390.1, 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};
CC   -!- SIMILARITY: In the N-terminal section; belongs to the phytochrome
CC       family. {ECO:0000256|ARBA:ARBA00006402}.
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DR   EMBL; BA000019; BAB75390.1; -; Genomic_DNA.
DR   PIR; AD2267; AD2267.
DR   STRING; 103690.gene:10495733; -.
DR   KEGG; ana:all3691; -.
DR   eggNOG; COG0457; Bacteria.
DR   eggNOG; COG0515; Bacteria.
DR   eggNOG; COG2203; Bacteria.
DR   eggNOG; COG3899; Bacteria.
DR   eggNOG; COG4191; Bacteria.
DR   Proteomes; UP000002483; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-EC.
DR   CDD; cd14014; STKc_PknB_like; 1.
DR   Gene3D; 1.10.287.130; -; 1.
DR   Gene3D; 3.30.450.40; -; 2.
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; IPR036097; HisK_dim/P_sf.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR016132; Phyto_chromo_attachment.
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; 2.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00065; GAF; 2.
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; 2.
DR   SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 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; PS50046; PHYTOCHROME_2; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   3: Inferred from homology;
KW   Kinase {ECO:0000313|EMBL:BAB75390.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002483};
KW   Transferase {ECO:0000313|EMBL:BAB75390.1}.
FT   DOMAIN          19..304
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   DOMAIN          1569..1708
FT                   /note="Phytochrome chromophore attachment site"
FT                   /evidence="ECO:0000259|PROSITE:PS50046"
FT   DOMAIN          1758..2015
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
SQ   SEQUENCE   2021 AA;  228572 MW;  3AE028C04782C1B0 CRC64;
     MESVKMNTYV DLAIAIPGYF ILEEIYHGSK TVVYRAVREA DQQPVVIKLL KREYPTFSEL
     LQFRNQYAIA KNLKIPGIVN LYSLEPYRNS YAMVMEDFGG ISLRDYAQQQ SLSLTEILTI
     TIQLADILHH IYQQRIIHKD IKPANILINP ETKQVKLIDF SIASLLPRET QNIISPNILE
     GTLAYLSPEQ TGRMNRGIDY RSDFYSLGVS LFELLTGELP FTTDDPMELV HCHIAKQPDK
     FTIPFSCQRR YANRFSNGGE STKLPNEETI PQVVGEIVMK LMAKNAEDRY QNALGLKYDL
     EKCLAELQET GKVEYFTIGS RDVCDRFIIP DKLYGREAEI ETLLAAFNRV SLGATELMLV
     AGFSGIGKTA VINEVHKPIV RQRGYFIQGK FDQFQRNIPF SAFVQAFRNL MGQLLTESDT
     QIQQWRSKIL EAVGKNGQVI IEVIPELELI IGKQPAAPKL SGTSLQNRFN LLFKKFTQVF
     TSAEHPLVIF LDDLQWADSG SLKLIQLLMN DTGYLLLIGA YRDNEVNPAH PLMLTVNEIG
     KNNGTIKKID LAPLNQLKVN TLVAETLKCS EETAQSLALL VFQKTQGNPF FTTQFLKALH
     QDNLIQFNYD LGCWQCDIAQ VNHQALTDDV LAFMASQLKR LPRATQEVLQ LAACIGNQFD
     LETLAIVWES SPMKTAACLW KALQEGLIIP QSEVYKFFVG QEQEIDHAQT TEIVTYKFLH
     DRVQQAAYCL IPEAERAIAH HHIGQLLLQK ISPAAREEHI FEIVNQLNYG ITLITQQSER
     DELAQLNLNA AQKARAATAY QASREYADTS MTLLGETAWQ RQYQLTLTIH ELAAEIALLC
     GDVEQMNQLI ETVVNHAKCP LDRVQVYQVK IQALTSRNEL LEAIATGKSF LQELGVSLPD
     HPTPEDVQQA REEINRLIGD RLLGEFINLP KMTDPEKLAI MQISSSLIPA CYMTGSLLYL
     LIVPLQVKLS LQFGNSLFSA HGYVSYAFHL STTWQNMALA QQLGQIAYQL ASEPEAKNIR
     AATFIVLGGY FYHCTSHLQD TLPIIQEGCI AGLETGNLEF FGYNVQNFGM NAYWSGESLS
     EFASQMCTYH QQLLDFNLVT SANHCFVYWE SALILLGKSA DEISLRQDAY AEKIVTEALA
     SNDLWRLFQF YLYRLVLNFL LADPRAKQDA EKARQYLTGC MGSVAEPIFY FYDSLTALAE
     LHQSPAGRDS QWQRVRENQA ILDKWADHAP MNYLHKWQLV AAETHRLLEQ KTEAMEFYEM
     AIKGAKENKY LRDEALANEL AAKFYLDWGK EKVAAVYMQE AYYCYARWEA KAKTNDLEKR
     YPQLLQPILQ ERQFKFNFQE TIAVPGTSSS TLSSTLGSTS ISDTLDFASI LKAAQVISTS
     LELDELITNL TEIILENSGA KKSALLLPQE DIWQIKAMTL SNFQPNSSES TQTILESQPL
     ETCEDIPKNI IYYVKNTQQT VVIDNLQTDI PGLIGEYMLQ HQPQSVFCTP MMNQGHLVGI
     LYLENRLTRG VFTSDRLEVI RLLSAQAAVS LEKARLYQES QTKAQQLKQS LKQQKILFNV
     VNQMRQSLDL NAIFCVVTQN IRRILDVDRV GIYQFHLDVN YEYGEFVAED VSPAFPSALA
     VKVQDHCFGE NYANLYKQGR ICAITDVQSS EILDCHRQIL AQFHVRASLV VPIMQEEELW
     GLLCIHQCDR PRQWEPLEMQ FAQQVGAQMG IALKQTDLLI QTQKQATQLE HTLQHLQQTQ
     LQLVQNEKMS ALGNLVAGVA HEMNNPLGFI AVSLQHTQPT FADIMEHLKL YQESLPHPGD
     KILHHAAQID LDYILEDLPK LIEAMVMACD RLKNISTSLR TFSRADKDYK IPFNIHKGID
     STILILKHRL KANDKRPAIE VITEYGNLPH IECFPGQLNQ VFMNILANAI DALEDANNGL
     SYAEITANNN RIIIRTTQVN NHVRISITDN GIGMSEELKQ HIFEHLFTTK GVEKGTGLGL
     AIARQIVVEK HGGAIEVNSQ LGQGTEFVII FPITAESANK Y
//