ID Q3M4I4_TRIV2 Unreviewed; 1795 AA. AC Q3M4I4; DT 25-OCT-2005, integrated into UniProtKB/TrEMBL. DT 25-OCT-2005, sequence version 1. DT 27-MAR-2024, entry version 123. DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438}; DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438}; GN OrderedLocusNames=Ava_4504 {ECO:0000313|EMBL:ABA24102.1}; 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:ABA24102.1, 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; ABA24102.1; -; Genomic_DNA. DR STRING; 240292.Ava_4504; -. DR KEGG; ava:Ava_4504; -. DR eggNOG; COG0515; Bacteria. DR eggNOG; COG3899; Bacteria. DR eggNOG; COG4191; Bacteria. DR HOGENOM; CLU_000445_34_0_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; IPR036097; HisK_dim/P_sf. 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; SM00388; HisKA; 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; 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; PS50011; PROTEIN_KINASE_DOM; 1. DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1. PE 4: Predicted; KW Kinase {ECO:0000313|EMBL:ABA24102.1}; KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553}; KW Serine/threonine-protein kinase {ECO:0000313|EMBL:ABA24102.1}; KW Transferase {ECO:0000313|EMBL:ABA24102.1}. FT DOMAIN 14..279 FT /note="Protein kinase" FT /evidence="ECO:0000259|PROSITE:PS50011" FT DOMAIN 1539..1795 FT /note="Histidine kinase" FT /evidence="ECO:0000259|PROSITE:PS50109" SQ SEQUENCE 1795 AA; 200798 MW; AAE5361B2DD69205 CRC64; MSATVDTTVL LSGYQLIEQL YHGSKTLVYR GIRRKESVAQ PVVIKLLQRD YPSFSELLQF RNQYTITKNL NIPGVVRPSS LEPYGNSYAL VMEDFGGVSL GTYSQTHSLS LVDVLAIAIQ LANILHDLYQ NRVIHKDIKP ANLLIHPDTK KIQLIDFSIA SLLPKETEAV KHPKVLEGTL PYLAPEQTGR MNRGIDYRSD FYAFGVTLFE MLTGQLPFIS DDPLELVHCH IAKPAPSVCA LRPEIPSVIG EIIGKLMAKN AEDRYQSALG LQYDLQNCLE QLQNTGKIEA FEIATRDICD RFLIPEKLYG REEEVATLLT AFERVSNGNS ELMLVAGFSG IGKTAVVNEV HKPIVEKRGY FIKGKFDQFN RSTPFSAFVQ AFRDLIGQLL SESDEQLQTW KTQLLQALGE NGQVIIEVIP ELERIIGEQP PARELSGNAA QNRFKLLFQN FIHVFTKPEH PLVIFLDDLQ WADSASLNLM QGLIAESKIG YLLLLGAYRD HEVYPAHPLM LTLEAIEKTG ATINTITLQP LSLTSLNQLI TDTLNCTATL AQPLTKLVNQ KTQGNPFFAT QFLKALYQDE LIYFDLVTGY WQCDLVQVKA AALTDDVVEF MALQLQKLPP VTQDILKLAA CIGNQFDLNT LAIVSEISPA ETSTILWKAL QEELILPLSE TYKFFQSSPH QTTGDCQITI SYKFFHDRVQ QAAYSLIPQE QKTATHLRIG QLLLTHTPET ELENRIFDIV NQLNVGVAYL TDQPEKQRLL ELNLMAGRKA KVATAYVVAV DYLNTAIKLL EEDSWQNQYE LTLSLYDLVA ETEYLNTNFP TSELLVREIL VNAKHTLDKI KAYEIQIQAY TAQNKLIEAI NIGREVLGLL GIDLPEDGNI ETIITEHGRL KSLFGERLIE DLVNLPELTD LQQGAALRIL CGLFAPIYLA KPMLLPLKIF TMVKICIQYG NSPQSAIAYS LYGLFLCASE EIADGYQFGQ LAMTVLDKFN AQELRSKVYL TFALFIKHWQ DSINSTLNIF LEGLKSGLDT GDLEYVGYCA NCYAQFLFWT GQNLEIAEAE ANKYCALMQD LKQDVSLIWG NTWRQTVMNL QAKVDNPQML VGECFDETVT LPALISSRNT NGICYVYLAK LFLAYLLGAD EQAIKYASLF EEYEQGAAGL LIVPLKNFYQ SLSILSLYPK LDTEQQSRHL EKITNNQQKM QNWADHAPLN YQHKFYLVAA EKHRVLDEKT AAIELYDQAI ALAKTNGYIQ EAALANELAA KFYLDWGKEK VAAAYMQEAY YCYAHWGSLA KTNDLESRYP QLLRPILQQV IHPLSILETF ASLTSSVHST RHQSSSSTSI NHMLDFAALL QVSQAISSTI QLDKLLQTMT ETVLENSGAD YCALILCQEG EWQVKVIANS QQTSLQSTPL ENNPTVPVKL IQYVKNTLET VVIHDLKTEI PGVMSNYLDQ HHPKSVLCLP LVNQGNLSAI LYLENQVTSD VFTSDRLLVL KFLSSQAVIA LENARLYHQV QKTLEDLQQA QVQIVQSEKM SALGNLVAGV AHEINNPVGC IVGNIGAAQE YINDLLGVID LYGEKFPQPG TEIEDELQAI DLEYLREDLP KLIRAMKDGS DRIKAISESL RTFSRADSDQ KQPFNLHDGL ESTLLILRHR LKANQYRPAI EVITEYGNLP LVKCFPGQLN QVFMNILANA IDALDESNPG YSFTEIEANP NRIIIRTTVA GEQIKIAISD NGHGIPEEVK AKIFDHLFTT KGVGKGTGLG LAIAHQIIVE KHGGAIAVNS QPGIGTEFLL TLPIS //