ID Q3M794_TRIV2 Unreviewed; 1804 AA. AC Q3M794; 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_3535 {ECO:0000313|EMBL:ABA23142.1}; 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:ABA23142.1, 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; ABA23142.1; -; Genomic_DNA. DR STRING; 240292.Ava_3535; -. DR KEGG; ava:Ava_3535; -. 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; 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; 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; 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 Coiled coil {ECO:0000256|SAM:Coils}; Kinase {ECO:0000313|EMBL:ABA23142.1}; KW Serine/threonine-protein kinase {ECO:0000313|EMBL:ABA23142.1}; KW Transferase {ECO:0000313|EMBL:ABA23142.1}. FT DOMAIN 14..273 FT /note="Protein kinase" FT /evidence="ECO:0000259|PROSITE:PS50011" FT DOMAIN 1546..1803 FT /note="Histidine kinase" FT /evidence="ECO:0000259|PROSITE:PS50109" FT COILED 1510..1537 FT /evidence="ECO:0000256|SAM:Coils" SQ SEQUENCE 1804 AA; 202826 MW; 266494E6E703A642 CRC64; MATQQYSNPI ITGYQISSQL YAGSKTRVYR AIREQDQLPV VIKVLASDYP NFQELLQFRN QYTISKNLNV TGIIRPLSLE TYGNGYILVM EDTGGIALRE YIKTAPLPLV EFLAIAIQIT SILQELHLNR VIHKDIKPAN ILIHPQTKQV HLIDFSIASL LPKETQEIRS PNVLEGTLAY ISPEQTGRMN RGIDYRSDFY SLGVTLYELL MGELPFSSDD PMELVYCHIA KTPIALGHQQ HIPLVLSDII MKLMAKNAED RYQSALGLKH DLETCLYQCK NNGKITAFEI GKRDMCDRFL IPEKLYGRET EVKVLLQAFE RVTKGKSEMM LVAGFSGIGK TAVVNEVHKP ITRQQGYFIK GKFDQFNRNL PLSAFVQALR DLMGQLLSES DSQLSKWRTK ILDTVGNNGQ VLIEVIPELE IIIGKQHPAP ELSGIAAQNR FNLLFQKFIA IFSTPKHPLV MFLDDLQWAD TGSLQLIKLL MEDQSYLLLL GAYRDNEVHT AHPLILTVEE LKKAGKTVNK ITLASLTLCD TNHLVADTLH CQAERSHPLT ELIERKTKGN PFFITQFLKA LHEDQLITFN RHQGYWECDI TQINELSLTD DVVKFMAQKL QKFPSKTQDV LKLAACIGNS FDLNTLAIVL EKSAADTADA LWKALQEGLI LPQSEVYKFY LDHDRQDAHV NNSQNVEYRF LHDRVQQAAY SLIPQDQKQA THYQIGQLLL KQISPVAREE RIFELVNQLN YGVALITQQT ERDELAQLNL TACRKARSAT AYQAAHEYIT VGLLLLGEKA WQHQYEITLH LHEFAAEVAS LRGDFAQMEQ FINIVTAQAH TLIEQVNVYR IRIQAYISQN KFAEAIAIAQ KILQQLGVTF AEATTPAVIQ QEIQEIRELI GDRAIADLVH LPIITDEEKV AIVQIASSIM TVAYLSGSPL FPLITLLLVK ISIQYGNTPA TGYIYSTYGV LLCNVLQDVD TATEFGQLAL QIVSKVDAKA TQPQVLLVLA LYILQRKSHV QEILPLLQKG YAIALEVGNL EFAGHHAHNF CSHSFWCGQH LATLQEDARA YSNELEQLNQ ITTANYVRIY WQSTLNLLGF AVHPTILSGE ALQEQEFIPL LIAANDGYGL YIFYLYKLML CYLFGEIETA KSITIKIKDH LMAAAGLFCE PIFYLYDSLI ALAQLRQNSE EVSATLQYVA ENQAKLQRWA QYAPMNHQHK LDLVAAERYR VLGEKTSAIE YYDHAISGAK KSQYIQEEAL SNELAAKFYL DWGKDKVAQI YMQEAYYCYA RWGAKAKIDN LEKLYPQLLK PILQRRQLNL NPLETIAPIN RNTIAVPTDT AGTSSTSISD ILDFTSVLKA AQAISSTIEL EELIVNLTKI ILEISGAKKI VLILPQDNAW YVRAITFISY ENKPEGKIQN ILLLQPIDTC KHIPGTIINY VKNTLETLVI DNYQIDIPGL IDQYLLKHQP KSVLCQPIIK QSNLLGILYL ENQITSGVFT LERLQVINLL SSQAAISLEN ACLYQKAQQA LQDLQAAQLQ IIQSEKMSAL GNLVAGVAHE MNNPLGFITA TLKQAKPTIA DIAEHLRLYQ ANFPNKSAEI INHAEEIDLD YSLEDLPKMI DAMVMASDRL KNISTSLRTF SRADTDHKVS FNVHEGIDST ILILKHRLKA NEQRPAIEVI TDYGNLPQIE CFPGQLNQVF MNILANAIDA LEATNKGQTL EEIKAHPHQI TITTTVNNDQ VKIIIADNGI GMDEQVKQKI FDHLFTTKAV GKGTGLGLAI ARQIVVEKHN GSLFVNSQLG AGTEFVITLP IITR //