ID A0A0D6AF24_9CHRO Unreviewed; 655 AA.
AC A0A0D6AF24;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 27-MAR-2024, entry version 45.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=GM3708_1490 {ECO:0000313|EMBL:BAQ61084.1};
OS Geminocystis sp. NIES-3708.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Oscillatoriophycideae;
OC Chroococcales; Geminocystaceae; Geminocystis.
OX NCBI_TaxID=1615909 {ECO:0000313|EMBL:BAQ61084.1, ECO:0000313|Proteomes:UP000060542};
RN [1] {ECO:0000313|EMBL:BAQ61084.1, ECO:0000313|Proteomes:UP000060542}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NIES-3708 {ECO:0000313|EMBL:BAQ61084.1,
RC ECO:0000313|Proteomes:UP000060542};
RA Hirose Y.;
RT "Geminocystis sp. NIES-3708 complete genome sequence.";
RL Submitted (MAR-2015) 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 -!- SIMILARITY: In the N-terminal section; belongs to the phytochrome
CC family. {ECO:0000256|ARBA:ARBA00006402}.
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DR EMBL; AP014815; BAQ61084.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0D6AF24; -.
DR STRING; 1615909.GM3708_1490; -.
DR KEGG; gee:GM3708_1490; -.
DR PATRIC; fig|1615909.3.peg.1518; -.
DR Proteomes; UP000060542; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd00075; HATPase; 1.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd00130; PAS; 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; 3.30.450.20; PAS domain; 1.
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; IPR000014; PAS.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR013655; PAS_fold_3.
DR InterPro; IPR016132; Phyto_chromo_attachment.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR NCBIfam; TIGR00229; sensory_box; 1.
DR PANTHER; PTHR43711:SF24; SENSOR HISTIDINE KINASE RPPB; 1.
DR PANTHER; PTHR43711; TWO-COMPONENT HISTIDINE KINASE; 1.
DR Pfam; PF01590; GAF; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF08447; PAS_3; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00065; GAF; 1.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00091; PAS; 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; SSF55785; PYP-like sensor domain (PAS domain); 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50112; PAS; 1.
DR PROSITE; PS50046; PHYTOCHROME_2; 1.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|SAM:Coils}; Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000060542};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 6..28
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 64..227
FT /note="Phytochrome chromophore attachment site"
FT /evidence="ECO:0000259|PROSITE:PS50046"
FT DOMAIN 297..367
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 439..655
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT COILED 238..269
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 655 AA; 76096 MW; 5523A0EA929D7DB8 CRC64;
MNLFNFFNPL ITVISFYCFI VLIGFYLLKR EINLRREAEF ILKQKAKRER LIHQITHQIR
LSLNIEEVLN TTVTEVRSFL QTDRVIIFRL WDNGTGSAIT ENVRSPYPQI LGKTFPEEVF
PQEYHQAYIE GKTRAINDIE QTDVEDCLAE FVKQFGVKAK LVVPIIQDIR NRNLENQDES
RVNSTPILSI DSTPCSYLWG LLIAHQCSQP RIWEDEEIEL MKQLATQVAI AIQQSELHTQ
LQQLNTELEE RVQQRTEELA LTNESLKAEI IEREKTEAAL RHTNHTLESL IKALRHSEER
FRQVVENALD IITIIDQNGT IHYQSPSVEK VLGYTFAEFI QENFFSYIHP DEIANIRSSI
ADALEDNPIV RPIEFRCRNK QREWHHLEAI TQKFIDYVPE TRIVITSRDI SERKRLKEVH
KALEREKELN IVKTRFFSMA SHEFRTPLST VLAAAQVLEN ATTHSHNPQK QLRNLHRIQN
AVKNMVQLLD DILTINRAET GNLEFNPQPL ALENFCRQFM EEIKLSTNTQ HHLKFICQGK
RIDVCLDEKL LRSILANLLS NAIKYSPQNS SIYLYLIFHS DKIQIKVRDK GVGISPEDMR
EIFEPFYRGQ NVRHLTGTGL GLVVVKKCVD LHSGSITIRS QMNKGTTVKI ILPYN
//
