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Database: UniProt
Entry: A0A433UNF5_ANAVA
LinkDB: A0A433UNF5_ANAVA
Original site: A0A433UNF5_ANAVA 
ID   A0A433UNF5_ANAVA        Unreviewed;       834 AA.
AC   A0A433UNF5;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   27-MAR-2024, entry version 16.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=DSM107003_30690 {ECO:0000313|EMBL:RUS95366.1};
OS   Trichormus variabilis SAG 1403-4b.
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Nostocaceae;
OC   Trichormus.
OX   NCBI_TaxID=447716 {ECO:0000313|EMBL:RUS95366.1, ECO:0000313|Proteomes:UP000276103};
RN   [1] {ECO:0000313|EMBL:RUS95366.1, ECO:0000313|Proteomes:UP000276103}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SAG 1403-4b {ECO:0000313|EMBL:RUS95366.1,
RC   ECO:0000313|Proteomes:UP000276103};
RX   PubMed=30590650;
RA   Will S.E., Henke P., Boedeker C., Huang S., Brinkmann H., Rohde M.,
RA   Jarek M., Friedl T., Seufert S., Schumacher M., Overmann J.,
RA   Neumann-Schaal M., Petersen J.;
RT   "Day and night: Metabolic profiles and evolutionary relationships of six
RT   axenic non-marine cyanobacteria.";
RL   Genome Biol. Evol. 0:0-0(2018).
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:RUS95366.1}.
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DR   EMBL; RSCM01000010; RUS95366.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A433UNF5; -.
DR   OrthoDB; 9788063at2; -.
DR   Proteomes; UP000276103; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR   GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR   CDD; cd00082; HisKA; 1.
DR   CDD; cd00130; PAS; 2.
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; 3.30.450.20; PAS domain; 3.
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; IPR013767; PAS_fold.
DR   InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR   NCBIfam; TIGR00229; sensory_box; 2.
DR   PANTHER; PTHR43065:SF10; PEROXIDE STRESS-ACTIVATED HISTIDINE KINASE MAK3; 1.
DR   PANTHER; PTHR43065; SENSOR HISTIDINE KINASE; 1.
DR   Pfam; PF01590; GAF; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF00512; HisKA; 1.
DR   Pfam; PF00989; PAS; 1.
DR   Pfam; PF13188; PAS_8; 1.
DR   Pfam; PF13426; PAS_9; 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   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; SSF55785; PYP-like sensor domain (PAS domain); 3.
DR   PROSITE; PS50109; HIS_KIN; 1.
DR   PROSITE; PS50113; PAC; 3.
DR   PROSITE; PS50112; PAS; 1.
PE   4: Predicted;
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000276103}.
FT   DOMAIN          256..311
FT                   /note="PAC"
FT                   /evidence="ECO:0000259|PROSITE:PS50113"
FT   DOMAIN          390..445
FT                   /note="PAC"
FT                   /evidence="ECO:0000259|PROSITE:PS50113"
FT   DOMAIN          442..512
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   DOMAIN          514..566
FT                   /note="PAC"
FT                   /evidence="ECO:0000259|PROSITE:PS50113"
FT   DOMAIN          579..801
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
SQ   SEQUENCE   834 AA;  94486 MW;  6A27E1A8B7513A30 CRC64;
     MRLPVSNNEA ARLEALRQYD ILDTEPEQTF DDLAFLAAQI CDAPIALINF IDTNRQWFKA
     KVGLDVQEMP RDAGFCPICL QQGDVLIIPD TLLDERFATA DIVTSELHVR FYVGVPLIVS
     GGEVIGTLCV VDQVPRQISS KQLQALQSIS RLIVRQLEVR RNLVELARIN IEYKQAQKAL
     YQSESTLHSF FESAPMMMGI VELVDNDILH IADNPVTAKF LGLTPEAMQN RLAREMGAEN
     SNLKHWINYY RQAELTQTPV RFEHSLETPQ GITWLSATVS AIANNHGNRQ QFAYIVEDIT
     ERKLAEDELR WQEALLRSMN SVSPLGFYVV DNRTDDILYF NDRFCEIWQI EHLKDGMEIR
     ELKNQDIIPD CCKLILDIPS FAASCQPLQD ESNLSVIEDE IGFNDGRIIR RFSTQIRNKS
     DQYFGRLYIF EDITARKQVE QKLREQAALL NMTTNAIIVI DLNNKILLWN KSAEKLYGWK
     AEEVIDQNAR ELWVEETVAQ EIEIYQTVLM SGSWQGELNK ITKFDTEIIV ESHWTLVHDE
     HNQAKSILVI DTDITQKKQL EQQFLRAQRM DSIGTLASGI AHDLNNVLSP ILMSAYLLKN
     KYHEPQAQQI ISIIETNAKR GANLVKQVLS FAKGIKGEHT VIQVKYLISE MQQIIEQTFP
     KSITVHTEIQ QNLFPVCGDI TQLDQVLINL CLNARDAMPN GGTLTISADN IWIDETSAKM
     HLDAQVGSYI VIKVIDTGLG IPSKILNRIF EPFFTTKEFG KGTGLGLSTV IGIIKGHNGF
     ITVSSSLNKG TEFQVYLPAI YTPENQSVKQ VEMLTGNGEW VLLVDDEASI QEIT
//
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