ID Q3M9C0_TRIV2 Unreviewed; 1805 AA. AC Q3M9C0; DT 25-OCT-2005, integrated into UniProtKB/TrEMBL. DT 25-OCT-2005, sequence version 1. DT 27-MAR-2024, entry version 121. DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438}; DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438}; GN OrderedLocusNames=Ava_2803 {ECO:0000313|EMBL:ABA22416.1}; OS Trichormus variabilis (strain ATCC 29413 / PCC 7937) (Anabaena variabilis). OC Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Nostocaceae; OC Trichormus. OX NCBI_TaxID=240292 {ECO:0000313|EMBL:ABA22416.1, ECO:0000313|Proteomes:UP000002533}; RN [1] {ECO:0000313|Proteomes:UP000002533} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29413 / PCC 7937 {ECO:0000313|Proteomes:UP000002533}; RX PubMed=25197444; DOI=10.4056/sigs.3899418; RA Thiel T., Pratte B.S., Zhong J., Goodwin L., Copeland A., Lucas S., Han C., RA Pitluck S., Land M.L., Kyrpides N.C., Woyke T.; RT "Complete genome sequence of Anabaena variabilis ATCC 29413."; RL Stand. Genomic Sci. 9:562-573(2014). 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 --------------------------------------------------------------------------- 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; CP000117; ABA22416.1; -; Genomic_DNA. DR STRING; 240292.Ava_2803; -. DR KEGG; ava:Ava_2803; -. DR eggNOG; COG0515; Bacteria. DR eggNOG; COG3899; Bacteria. DR eggNOG; COG4191; Bacteria. DR HOGENOM; CLU_000445_34_2_3; -. DR Proteomes; UP000002533; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:InterPro. DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro. DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA. DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW. DR CDD; cd00082; HisKA; 1. 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; IPR003661; HisK_dim/P. 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 Coiled coil {ECO:0000256|SAM:Coils}; Kinase {ECO:0000313|EMBL:ABA22416.1}; KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553}; KW Serine/threonine-protein kinase {ECO:0000313|EMBL:ABA22416.1}; KW Transferase {ECO:0000313|EMBL:ABA22416.1}. FT DOMAIN 7..272 FT /note="Protein kinase" FT /evidence="ECO:0000259|PROSITE:PS50011" FT DOMAIN 1544..1801 FT /note="Histidine kinase" FT /evidence="ECO:0000259|PROSITE:PS50109" FT COILED 1508..1535 FT /evidence="ECO:0000256|SAM:Coils" SQ SEQUENCE 1805 AA; 202399 MW; 1FF27416AA647212 CRC64; MLNIPGYTIS EELYDGSRTL VYRAIRQADT LPVVIKLLKN PYPSFSELVQ FRNQYTIAKN LNYPGIIATH SLEPLHNGYQ LVMEDFGGIS VKDYFVHNHY VASLDKFLQI AIALCDILDI LYRQRIIHKD IKPANILINP ETTQVKLIDF SIASLLPRET QTLINPNVLE GTLGYISPEQ TGRMNRGIDH RTDFYSLGAT FYELLTGKLP FPSEDAMELV HCHLAKAPTL VHEINLTIPS VLSDIVNKLM AKNAEDRYQS ALGLKYDLEK CLVQLQETGK IESFPIAQRD VCDRFIIPDK LYGREAEVET LLQAFERVST GNTEMMLVAG FSGIGKTAVV NEVHKPIVRQ RGYFIKGKYD QFQRNIPFSA FVQAFRDLMG QLLTESDAQI QQWKSQILAA VGENGQVIIE VIPELAGIIG QQPPIIELSG TAAQNRFNLL FQKFVQVFKT QEHPLVMFLD DLQWADSASL NLMQLLMSES GGGYLLLIGA YRDNEVSDAH PLMFSLAEIR KAQATINTIT LAPLSQSSLN QLVADTLSCS SAIAQPLTQL VYQKTKGNPF FSTQFIKAIY EDGLITFNGD EGNWQCDIVG VKESSLSDDV VEFMALQLQK LPQTTQNILK FAACIGNKFD LGILAIIWEK SLTETATALW KALQEGLILP QSEVYKFYVD REIQDEVKGS QTVTYKFLHD RVQQAAYSLI PAEQKQYTHF QIGQLLLQGL SQGEQEERIF DIVNQLNMGL DVITSNEQKQ ELAHLNLKAG QKAKLSAAYQ AAYDYCTIGM SVLSPDAWQQ DYPLMYSLHR DASEAAYLCG KFDQAEALYA ETLTYAQAPL DQAIVYRIQM TQYQLQGRNA EAIAIQRQSL QMLGWTIPTQ PEMIQAGLDA EIATVQQFLE QHTIESILAA PKMVDPSIAE MLRILQILFY AAWLDGQSTL ALLALAKMTT LSLQYGNSDM SPFGYAGYGL IANGVFKDCA TAYEFGEMAV QLCEQFDNAD VRGMTNFIFA ADVHSWSRPI READTYYNNA YQYGMEAGNW LTVGFMMMQS GSDRLTYGKH LDDLYAIAQN HAAFLHQIKS LDNLDALTAG VLQPIRHLLG LTKTLFTFDD DDFSEAEYLQ KYANAPYHLS WLYSVKIRHA YLFDQKSTYS DLIPQLSMIE TTISSHAKVP SSVFYVALMH LALAETATEA SERQHHWQAL LPLETSLKRW LKACPENIRH KFLLIQAEKA RIKKQKTKAI ELYEQAISQA QANQYGYEEA LANELAAKFY LDWGKVKIAQ VYMQEACYGY ARWGAKAKAH HLEKTYPQLL KPILQQQRIN FNPLETITFR GATSSTHTTT TSSTNISEIL DFTSVLKGAQ AISGCIELDE LIANLTRIIL ENSGAKKSVL ILPLEETWQV KAITSVNQES SSHTNIQTIL SSQSIEDCQD IPPKIINYVK NTQKPLIIDN CQTDIPGVIG EYMLEHQPKS VLCTPIIHQG HLVGILYLEN ELTSEVFNSE HLQVVNLLSS QAAISLENAR LYQKAQQALQ DLQQAQLQIV QSEKMSALGN LVAGVAHEMN NPLGFIAASL MQAQPIIADI TEHLKLYQEN LPDKIEKIAD HAQEIDLEYI LEDLPKMIES MTMACERLKN ISTSLRTFSR ADRDYKVPFN IHEGIESTIL ILKHRLKANE QRPAIEVVTE YADSPMIECF PGQINQVFMN ILANAIDALD EANMGRSFAE IQANHNKIMI RTLLENQQVK ITIADNGKGM SEEVKAKIFD HLFTTKMVGK GTGLGLAIAQ SIVVEKHGGT LTVNSTLGEG TEFVISLPIL DESQN //