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Database: UniProt
Entry: G6FNC8_9CYAN
LinkDB: G6FNC8_9CYAN
Original site: G6FNC8_9CYAN 
ID   G6FNC8_9CYAN            Unreviewed;      1086 AA.
AC   G6FNC8;
DT   25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT   25-JAN-2012, sequence version 1.
DT   24-JAN-2024, entry version 60.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=FJSC11DRAFT_0375 {ECO:0000313|EMBL:EHC19558.1};
OS   Fischerella thermalis JSC-11.
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Hapalosiphonaceae;
OC   Fischerella.
OX   NCBI_TaxID=741277 {ECO:0000313|EMBL:EHC19558.1, ECO:0000313|Proteomes:UP000004344};
RN   [1] {ECO:0000313|EMBL:EHC19558.1, ECO:0000313|Proteomes:UP000004344}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JSC-11 {ECO:0000313|EMBL:EHC19558.1,
RC   ECO:0000313|Proteomes:UP000004344};
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA   Peters L., Land M.L., Hauser L., Sarkisova S., Bryant D.A., Brown I.,
RA   Woyke T.J.;
RT   "The draft genome of Fischerella sp. JSC-11.";
RL   Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases.
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   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EHC19558.1}.
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DR   EMBL; AGIZ01000001; EHC19558.1; -; Genomic_DNA.
DR   RefSeq; WP_009454192.1; NZ_AGIZ01000001.1.
DR   AlphaFoldDB; G6FNC8; -.
DR   GeneID; 60764623; -.
DR   PATRIC; fig|741277.3.peg.437; -.
DR   Proteomes; UP000004344; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR   CDD; cd00082; HisKA; 1.
DR   CDD; cd00130; PAS; 2.
DR   CDD; cd17580; REC_2_DhkD-like; 1.
DR   Gene3D; 1.10.287.130; -; 1.
DR   Gene3D; 3.30.450.40; -; 1.
DR   Gene3D; 3.40.50.2300; -; 1.
DR   Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR   Gene3D; 3.30.450.20; PAS domain; 3.
DR   InterPro; IPR011006; CheY-like_superfamily.
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; IPR001610; PAC.
DR   InterPro; IPR000014; PAS.
DR   InterPro; IPR000700; PAS-assoc_C.
DR   InterPro; IPR035965; PAS-like_dom_sf.
DR   InterPro; IPR013656; PAS_4.
DR   InterPro; IPR013655; PAS_fold_3.
DR   InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR   InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR   NCBIfam; TIGR00229; sensory_box; 2.
DR   PANTHER; PTHR43547:SF2; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE C; 1.
DR   PANTHER; PTHR43547; TWO-COMPONENT HISTIDINE KINASE; 1.
DR   Pfam; PF01590; GAF; 1.
DR   Pfam; PF02518; HATPase_c; 2.
DR   Pfam; PF00512; HisKA; 1.
DR   Pfam; PF08447; PAS_3; 1.
DR   Pfam; PF08448; PAS_4; 1.
DR   Pfam; PF00072; Response_reg; 1.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00065; GAF; 1.
DR   SMART; SM00387; HATPase_c; 1.
DR   SMART; SM00388; HisKA; 1.
DR   SMART; SM00086; PAC; 2.
DR   SMART; SM00091; PAS; 3.
DR   SMART; SM00448; REC; 1.
DR   SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR   SUPFAM; SSF52172; CheY-like; 1.
DR   SUPFAM; SSF55781; GAF domain-like; 1.
DR   SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR   SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 3.
DR   PROSITE; PS50109; HIS_KIN; 1.
DR   PROSITE; PS50113; PAC; 1.
DR   PROSITE; PS50112; PAS; 2.
DR   PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:EHC19558.1};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW   ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000004344};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius};
KW   Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT   TRANSMEM        12..33
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        45..63
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          86..128
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   DOMAIN          211..289
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   DOMAIN          284..336
FT                   /note="PAC"
FT                   /evidence="ECO:0000259|PROSITE:PS50113"
FT   DOMAIN          654..931
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   DOMAIN          965..1083
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000259|PROSITE:PS50110"
FT   COILED          627..654
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   MOD_RES         1014
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ   SEQUENCE   1086 AA;  120019 MW;  77DBBDFE4B260BCC CRC64;
     MQVITSPTDG GLLARRLLIA ALKVPLITGW LILQGQKAGK YKYEFAISLF AIFQMTIFAI
     IIWENAAAIQ KLSNQRDHAK LALKANTEKL RRFAQSNVIG VLFGDIYGGV SHANDKFLQM
     IGYTRQDLQA GGINWKNITP PEYLPADAQG IAQAKSQGAC IPYEKEYIRR DGSGILVLVG
     YTLVGEKQQE SVAFILDLSG RKKAQAALLQ SEERFRLAVD HMPDVFAIYD AQRRFQFVNA
     AALQHLGKPK EEVIGRTDEE IFPVEITQLY LPSLFKAVET RTTQTTETTI TLPNNGTLTT
     LIKYVPIVDE QGEIYQILAF AEDITVRKQA EEALRNQQKW LEDLLNLMPT PLLLIEPGTA
     RVTFANKAAD EVAGGKFPKA DSAADYQALY YSTDADGNPI PVEQAPGIRV ARGERLDGVE
     LDWHTPTGIR SLLIYADTLP AMHGYPTTCV LTFQDITNLK RVEKALSLGY KRLQLLFGTA
     SDLLSSKEPV ALIESLFQKL AEQIGLDVYF NFLVNENSQI MQLASWHGID EQTAKAANWL
     EIGQGMCGTV AQQRRPISIE NVQESKDPKT ELLRAIGIKT YYGYPLIAQG KLLGTLCFCS
     RTRLQFSQNE MGMMQAVCDQ IAIAIERARL IASLQQQTEQ LQEANRMKDE FLAILSHELR
     SPLNAILGWS QLLRSRKLNE TQITKALETI ERNAKTQTQL IEDLLDISRI IRGKLRLNVR
     TCNLIAIIEA ALDTVRLAAQ AKDIHIRTRF DSKAALVSGD GERLQQVVWN LLSNAIKFTP
     AGGKVEVVLS LVKEETRIRE YRNSESVFDR FSASPRLNIG ASFKASSPLP KLSATMGGTP
     ATQWFPSTSC ETAYAQITVK DTGIGISSEF LPYVFDRFRQ ADSSSTRSHG GLGLGLAIVR
     HLVEMHGGTV DVTSPGKEQG TTFTVKLPLL KSQDSIVHTE ELTVNSQQAN FNCLPISSSV
     LDGVRVLVVD DEADTRDYLT TLLKQSQADV LAVASVPAAL EAVEHWKPDV LVSDIGMPEE
     DGYSLLRKLR SLAPEKGGKI PAAALTAYAR AEDRRRAIQA GFQLHLPKPI DPSELITVVA
     SLVGRT
//
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