ID   Q3MH27_TRIV2            Unreviewed;      1780 AA.
AC   Q3MH27;
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_0083 {ECO:0000313|EMBL:ABA19709.1};
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:ABA19709.1, 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; ABA19709.1; -; Genomic_DNA.
DR   STRING; 240292.Ava_0083; -.
DR   KEGG; ava:Ava_0083; -.
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   Coiled coil {ECO:0000256|SAM:Coils}; Kinase {ECO:0000313|EMBL:ABA19709.1};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Serine/threonine-protein kinase {ECO:0000313|EMBL:ABA19709.1};
KW   Transferase {ECO:0000313|EMBL:ABA19709.1}.
FT   DOMAIN          7..274
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   DOMAIN          1518..1776
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   COILED          1468..1499
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   1780 AA;  201834 MW;  60B9FAA3A2A12CFB CRC64;
     MITLPNYKIL ELIDEGVKTN VYHAISIPDG KLVVIKILKK EYPELKDIAA LKHEYELIKN
     LDIPGVVKAH SFEKYNNYFA IVLEDFDGTC LYKVIQEKKI GLLDFCKIGI QITQALGELH
     QNYIIHKDIK PQNIIVNLET NQVKIIDFSI SSLLFQEKAK LNNPDLLEGT IAYISPEQTG
     RMNRSIDYRT DFYSLGVTFY EMLTGQLPFV VTDPMELVHC HIARQPTKIN ELIPEIPEVV
     SDIIMKLLSK TAEERYQSAF GIKADLEKCL NQLIESNSIT TFIIGQHDYS SQLQIPEKLY
     GRKTEIDILM TAFENVNQGN KELILVAGYS GIGKSALVNE IHKPVIKSRG YFIAGKFEQF
     QRNIPYASVI QAFQELIQQL LTESEQQLAN WREKILEALI PNAQIIIDVI PELELIIGKQ
     PEVPQLGSAE AQNRFNLVMQ KFINVFAQKE HPLVVFLDDL QWADLASLKL IQLLAINSDI
     QYLFLIGAYR DNEVDDSHHL MLVLQEIEQK CIPINIIYCQ NLKITDVCQL VSDTLKSGLE
     ESKELAKLIF HKTAGNPFFV NQLLKFIHQE NLLVFNFITG QWQWYIQYIQ MLDITDNVVD
     LMIGKIQKLK DNTQNIIKIA ACIGNRFNLN TLSCINEKSH NATALDIWEA LQAGLIIPLS
     DNYKLPQLLD DVDVFVIDYK FLHDRVQQAA YALIPDEHKK GIHLNIGRLL LKNINKSLLE
     EKIFDIANQL NMGAELITVP EERYKLASLN LMAGRKAKDS NAYESAVSFL KQGLTLLDID
     CWQNYYELTL DLHVETVESE YLNTNFEEAE PLLATVIANS KNILDTVKVY EKKIQFYVGQ
     NRMREALDLD LQVLEMLGVS LSQTPPTELK IEELINLPEM IDPSKLAAMR ILMTAMPPAY
     LADPALLPLI AFTMIELCLQ YGNSSFAAYA YGFYGLILCG PLKNIESGYR FGKLSLQILN
     QFNAKEIKSK VYALFNIFVR HWKEHIQTTI EPLQEGVKSG LDTGDIEYVG YNGLLVCWHP
     FWSGENLETV EQRLDKYINL AQKIQQEHFT FCLLILKQLI TELKQGLKNE VYLDGDDFND
     SIMQRMAGNI TAIFYAYLAK SMLSYFFKDY SQAVKNAELA QQYEVAVGGT FYLIEYKFYY
     SLGLLALCLN TTSDADIKSA LEKVSENQQQ LKEWADHAPA NNQHKYELVE AEKARVLGQV
     LIAMEYYECA IQGAHKFGYI HEEALAYECA AEFYFSLKRN EFACLYITKA HYGYRHWGAI
     AKARNLESKY PELTAKISNQ YPAGFINTNI TTSTASEKSG GLDLITVIKA SQTLSEVILL
     DNLLEKLMTI LIENAGAQTG ILLLEKAGNL LIEAKASVDK DDITVGQSIP FEDSQQLPIS
     VINFVRRTRK DVVLSDASNE GSFTLDPYIV KHNIKSIICT SILNQGKLIG ILYLENNLIV
     GAFTADRIQI LKLLSSQAAI SLENAQLYAN LEEKIEERTR ELNENNLRLR QTLHELKLTQ
     TQLIQTEKMS SLGQMVAGIA HEINNPVSFI HGNLSHIDNY ANDLLTLIDI YQTIYPEATP
     EIEEFLENID VDFIKEDMPK TLSSMKIGTQ RIREIVLTLR NFSRLDEAEM KAVNIHEGIE
     STLLILQSRL QAKPGKPAIE IIKNYAELPK VECYTGQLNQ VFMNILNNAI DSLEKLNQEH
     NLEEIKTDPS AIAIRTEVVN PDLVAISIKD NGLGMSDSVR KRIFDPFFTT KPIGQGTGLG
     LSISYQIVVD KHRGTIECIS TPGQGAEFII QIPCRQKQVI
//