ID Q3M5Y6_TRIV2 Unreviewed; 1794 AA. AC Q3M5Y6; DT 25-OCT-2005, integrated into UniProtKB/TrEMBL. DT 25-OCT-2005, sequence version 1. DT 24-JAN-2024, entry version 118. DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438}; DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438}; GN OrderedLocusNames=Ava_3995 {ECO:0000313|EMBL:ABA23600.1}; 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:ABA23600.1, 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; ABA23600.1; -; Genomic_DNA. DR STRING; 240292.Ava_3995; -. DR KEGG; ava:Ava_3995; -. 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:ABA23600.1}; KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553}; KW Serine/threonine-protein kinase {ECO:0000313|EMBL:ABA23600.1}; KW Transferase {ECO:0000313|EMBL:ABA23600.1}. FT DOMAIN 14..274 FT /note="Protein kinase" FT /evidence="ECO:0000259|PROSITE:PS50011" FT DOMAIN 1539..1794 FT /note="Histidine kinase" FT /evidence="ECO:0000259|PROSITE:PS50109" SQ SEQUENCE 1794 AA; 201970 MW; D270539A1B1C1F50 CRC64; MTSTVPQFPE ISGYTITEQI YRGSRTAVYL AIQDNQRLPV VIKVLQREYA TFGELVQFRN QYAIAKNLPI TGIIPPLSLE PFGNGYALVM ADWGGISLET YIQQQPLDLG DILVVAIQLA DILHELQQHR VIHKDIKPAN ILIHPESQQV KLIDFSIASV LPKETQEIQN PNTLEGTLAY LSPEQTGRMN RGIDYRSDFY ALGVTLYQLL TGRLPFLTDD PLELVHCHIA KIATPVHLVN TDVPPTLGAI VAKLMAKNAE DRYQSALGLK HDLDECWSQW KQTGSIAEFE LGQKDLCDRF LIPEKLYGRE TEVQTLLDAF ERVAQGSSEM MLVAGFSGIG KTAVVNEVHK PIVKQRGYFI KGKFDQFNRN IPFSAFVQGF QDLVGQLLSE SDTQLQHWKT QILSTLGENA QVIVELIPEL ERIIGVQPPT RELSGTAAQN RFNLLFQRFI QVFTTPAHPL VMFVDDLQWA DSASLNLIQV LMSESQTGCL LLLGAYRDNE VFAAHPLMLT LNGMEKAGAK IHTITLQPLS FTSLNHLIAD TLHTHALVVQ PLTKLVMQKT LGNPFFATQF LKALHQDQLI TFDPNAGHWQ CDIVQVRDVA LTDDVLELMV QQLQKMPEAT QEILKLAACI GAQFDLTTLA IVSQQSQTEV ATILWKALQE GLILPQSDLY KFYLGESQAI QHTPQETLNY RFLHDRVQQA AYSLILDDQK QVTHLTIGKL LLENSNPSFQ DSHLFAIVHQ LNCGISMITE LEQRYQYAQL NLQAGYKAKD STAYNAALHY FDKGMQFLPT DSWDKNYNLT LLIYESAAEV ALLSCDFKQM DTLIQIVLKN TNDLLEQVKV YEIKLQAYQV QNQQLQAIKI GREILQKLGV ILPESITLSD IQRQVQHTLT KLSNYSLEDL INLPITQDAT ATAAARIMTS LVPSIHQANP LLFPVVACEE VNLSLQYGNS LFSAPGYADF SIIVSSVLNE IEVGYRFGQL ALQLMEKFNE SYVQSIVMFK VAAFNQSNQQ DIRNAIFLLN KSYKVAIETG DSVHALVSTS FRLFYSYLSG DKPLPELLEE VEIYQSKFAT SEHFLTWVHI ISSSIHNFIE LSDNPDCLGS IDAENEKLST LIQENDELAL HLFYLSKLIL SYSFSCFETA IQIADRGLQY LKAGISMPSA PAYYYYDSLT RLKLYFNFQP SSQKEVLRKV DSNQKHLLVY VNAAPMNYQH KYHLVEAVRF QRLGKQAEAI EFFDCAIAGA KANRFIQDEA LANELAAEFY LNWGKDKFAA GYIQEAYYCY SRWGAKAKVT DLETRYPELL RPILQQTMTS TDALTTLMTI AAPAVSVHYD THHTSSSTGV NQVLDFAAIL KASQVLSRTI QLDQLLQKLT QIILHNSGGD RCALLFPNET GEWQVRAIAT PDDVQLIAEP FTNNPNIPVK LIQYVKNNQE TVVIDDLKTD LPVIDDYLRQ RQPKSILCLP LLNQGHLIGI LYLKNRLTRG VFTSDRLLIL NFLCIQAAIS LENARLYQQA QTYARQLEQS QLQMIQSEKM ASLGNLVAGV AHEINNPIGF LNGSIKNGKE YVQDLLGHLA LYQQHYPNPV EAIQDNAKDI DWEFLSEDLP KLLDSMEGAT NRINSISNSL RTFSRADTEY KISANLHEGL DSTLLILKYR LKANEHRPAI QVIQDLGDLP TIKCFPGQLN QVFMNILANA IDMFDEMAQT RLFKELEANP QKITIRTEVI SNQVYIRIRD NGKGITQELQ EKIFDHLFTT KAVGKGTGLG LAIARQIVVE KHGGSLNVWS ELGQGTEFTV QIPV //