ID A0A1E5QI61_9CYAN Unreviewed; 687 AA.
AC A0A1E5QI61;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=BH720_15125 {ECO:0000313|EMBL:OEJ74308.1};
OS Desertifilum tharense IPPAS B-1220.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Desertifilales; Desertifilaceae;
OC Desertifilum.
OX NCBI_TaxID=1781255 {ECO:0000313|EMBL:OEJ74308.1, ECO:0000313|Proteomes:UP000095472};
RN [1] {ECO:0000313|EMBL:OEJ74308.1, ECO:0000313|Proteomes:UP000095472}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IPPAS B-1220 {ECO:0000313|EMBL:OEJ74308.1,
RC ECO:0000313|Proteomes:UP000095472};
RA Sinetova M.A., Bolakhan K., Zayadan B.K., Mironov K.S., Ustinova V.,
RA Kupriyanova E.V., Sidorov R.A., Skrypnik A.N., Gogoleva N.E., Gogolev Y.V.,
RA Los D.A.;
RT "Draft genome of thermotolerant cyanobacterium Desertifilum sp. strain
RT IPPAS B-1220.";
RL Submitted (SEP-2016) 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:OEJ74308.1}.
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DR EMBL; MJGC01000067; OEJ74308.1; -; Genomic_DNA.
DR RefSeq; WP_069968055.1; NZ_MJGC01000067.1.
DR AlphaFoldDB; A0A1E5QI61; -.
DR STRING; 1781255.BH720_15125; -.
DR OrthoDB; 524899at2; -.
DR Proteomes; UP000095472; Unassembled WGS sequence.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd00082; HisKA; 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 InterPro; IPR033415; CHASE6_C.
DR InterPro; IPR019278; DICT_dom.
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; IPR004358; Sig_transdc_His_kin-like_C.
DR PANTHER; PTHR43711:SF1; HISTIDINE KINASE 1; 1.
DR PANTHER; PTHR43711; TWO-COMPONENT HISTIDINE KINASE; 1.
DR Pfam; PF17150; CHASE6_C; 1.
DR Pfam; PF10069; DICT; 1.
DR Pfam; PF01590; GAF; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00065; GAF; 1.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 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 PROSITE; PS50109; HIS_KIN; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils}; Kinase {ECO:0000313|EMBL:OEJ74308.1};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000095472};
KW Transferase {ECO:0000313|EMBL:OEJ74308.1}.
FT DOMAIN 433..654
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT REGION 653..687
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 406..433
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 653..667
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 687 AA; 77257 MW; 2229D60A1D4F2F9F CRC64;
MSISTSVLEA LLQAQPQLRS QIYFKPSLIA LSHAMEDQVL AGVGEPLVIA NFQQERFYRQ
EAHRYRRIAA QTPHVYVLAA PETEFKNASG HYETIAFAPT DELKHEWHLV VVGEQYASCL
VCRERDAIAS TPSPEGCKNQ NEWSVLQTSF LEMDQSRRFE GVWTFDRQVS CWVANLLLDR
IVGYRPELAA KVAQAKLKLQ QNLSGFPQAD PGPFAERLVT YLQAGQYKLL KAYSSIAIQE
RKERLINSIT DTIRRSLHLD EILQVATSEL GQALGLCRCM IYRCKATDTA ATISHEFLGS
SALASVAQQT WPLQNHPLFQ EVLEKRSPVW MENTQSSPRL QAVPEILALA QEWQIGSWLM
APVFYNDRLL GLIELHHCGA QTYRWQQDEI ALVEAIATQL GVALIQAEAY ANLEDLNEQL
EALDRTRSNL IAITGHELRT PLSTIQICLE SLAQEPDMPL ELRQVMLNTA LDDAERLREL
VQDFLTLSRL ESGRVEWHPE PLPLGECVDL ALSSVRSRQA EVSLPQITTC LPSELPLVQA
DGEWLVEVLS KLLDNACKFT PTQGQVTIEA QDNQNQMLEV TIGDTGRGIE PNRLEAVFDR
FYQEEGALRR TTGGTGLGLA ICRQIVQNWG GQIWAQSDGK DLGSQFRFTI PIVGNTKAQP
AESASETRQP TRRPRNRTRA KRRTTLK
//
