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Database: UniProt
Entry: A0A0P8DT34_9CYAN
LinkDB: A0A0P8DT34_9CYAN
Original site: A0A0P8DT34_9CYAN 
ID   A0A0P8DT34_9CYAN        Unreviewed;       693 AA.
AC   A0A0P8DT34;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   24-JAN-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=HLUCCO16_02975 {ECO:0000313|EMBL:KPQ40383.1};
OS   Phormidium sp. OSCR.
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Oscillatoriophycideae;
OC   Oscillatoriales; Oscillatoriaceae; Phormidium.
OX   NCBI_TaxID=1666905 {ECO:0000313|EMBL:KPQ40383.1, ECO:0000313|Proteomes:UP000050461};
RN   [1] {ECO:0000313|EMBL:KPQ40383.1, ECO:0000313|Proteomes:UP000050461}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OSCR {ECO:0000313|EMBL:KPQ40383.1};
RA   Nelson W.C., Romine M.F., Lindemann S.R.;
RT   "Identification and resolution of microdiversity through metagenomic
RT   sequencing of parallel consortia.";
RL   Submitted (SEP-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}.
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:KPQ40383.1}.
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DR   EMBL; LJZT01000005; KPQ40383.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0P8DT34; -.
DR   STRING; 1666905.HLUCCO16_02975; -.
DR   PATRIC; fig|1666905.3.peg.411; -.
DR   Proteomes; UP000050461; 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; IPR016132; Phyto_chromo_attachment.
DR   InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR   PANTHER; PTHR43711:SF26; SENSOR HISTIDINE KINASE RCSC; 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.
DR   PROSITE; PS50046; PHYTOCHROME_2; 1.
PE   3: Inferred from homology;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553}.
FT   DOMAIN          257..409
FT                   /note="Phytochrome chromophore attachment site"
FT                   /evidence="ECO:0000259|PROSITE:PS50046"
FT   DOMAIN          443..668
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   REGION          669..693
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          416..443
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   693 AA;  77724 MW;  12F892CD5F5C14F9 CRC64;
     MNVKTSVLED LLQAQPHLRS QTYFKSSLIA LSHAMEDQVL AGENSPLVIA SFQKERFYRM
     EASRYKRIAQ ASEHVYVLAA PESDFSNQSG HYETIAFSGD EPLSQEWNLV ILSPNYGTCL
     VCQEQNIPEG ETRWLGETSL EIDTARRFEG IWSFDHDLSR FVAEQLLQRI LHYRPELADK
     VAQARRNYGL DGQPLEPQVT PVVEPLGMNP GPFAERLITY LQAGQYKLIK AYRSIAAQEE
     QERLVNSITT AIRQSLDPQE ILKVAVRELG EVLDVCRCLV YRCKETDATA TIVHEYAAPG
     IQSLVGETWA LLDNPLFQEA IERQSGVFLE DTEHPQQTRM ESLASLLEQP TARDWLAQQV
     QRWKIGAWLM MPILYRGKLL GILELHHCQG CAHHWSNDEV ALVNTIAIQM GTGLIQAETY
     AHLEDLNQQL EALERTRSNL IAITGHELRT PLSTIQICLE SLASEPDMPE ELQKVMLNTA
     LVDAERLREL VQDFLTLSRF ESGRVEWNLE PLSLQECIDL AMSGVRARYG GEYGGESLPE
     LVVDIPPDLP LVQADGEWLV QVLGKLLDNA CKFTPSGGSI TVQATPMGYR LLKVTVADTG
     RGIEPARVED IFERFYQEEG ALRRTTGGTG LGLAICRQAV QRWGGQVWAE SEGKDRGSRF
     HFTIPRLDDE ATSSSTSSLA GGLSALPKRR RSR
//
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