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Database: UniProt
Entry: A0A252ECL9_9NOSO
LinkDB: A0A252ECL9_9NOSO
Original site: A0A252ECL9_9NOSO 
ID   A0A252ECL9_9NOSO        Unreviewed;       927 AA.
AC   A0A252ECL9;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=BV372_02230 {ECO:0000313|EMBL:OUL37408.1};
OS   Nostoc sp. T09.
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Nostocaceae; Nostoc.
OX   NCBI_TaxID=1932621 {ECO:0000313|EMBL:OUL37408.1, ECO:0000313|Proteomes:UP000195076};
RN   [1] {ECO:0000313|EMBL:OUL37408.1, ECO:0000313|Proteomes:UP000195076}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=T09 {ECO:0000313|EMBL:OUL37408.1};
RA   Cruz-Morales P., Corona-Gomez J.A., Gutierrez-Garcia K.G., Barona-Gomez F.,
RA   Cibrian-Jaramillo A.;
RT   "Metagenomics of subcommunity co-cultures reveals the complexity of the
RT   cycad coralloid root endophytic microbiome.";
RL   Submitted (JAN-2017) 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:OUL37408.1}.
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DR   EMBL; MTAV01000003; OUL37408.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A252ECL9; -.
DR   OrthoDB; 474548at2; -.
DR   Proteomes; UP000195076; Unassembled WGS sequence.
DR   GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR   GO; GO:0009584; P:detection of visible light; IEA:InterPro.
DR   GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR   CDD; cd00082; HisKA; 1.
DR   Gene3D; 1.10.287.130; -; 1.
DR   Gene3D; 3.30.450.40; -; 3.
DR   Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal 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; IPR016132; Phyto_chromo_attachment.
DR   InterPro; IPR013515; Phytochrome_cen-reg.
DR   InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR   PANTHER; PTHR43065:SF50; HISTIDINE KINASE; 1.
DR   PANTHER; PTHR43065; SENSOR HISTIDINE KINASE; 1.
DR   Pfam; PF01590; GAF; 2.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF00360; PHY; 1.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00065; GAF; 3.
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; 3.
DR   SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR   PROSITE; PS50109; HIS_KIN; 1.
DR   PROSITE; PS50046; PHYTOCHROME_2; 2.
PE   3: Inferred from homology;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000195076}.
FT   DOMAIN          32..200
FT                   /note="Phytochrome chromophore attachment site"
FT                   /evidence="ECO:0000259|PROSITE:PS50046"
FT   DOMAIN          455..591
FT                   /note="Phytochrome chromophore attachment site"
FT                   /evidence="ECO:0000259|PROSITE:PS50046"
FT   DOMAIN          648..902
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   COILED          609..636
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   927 AA;  104996 MW;  12CD3F546934CF1B CRC64;
     MAFTEQPSGL QQTFDPEGLL HRMTNQIRRS LELPEILTAT VAEVRSFLGT DRVMVYRFDS
     DDSGEVIAES IYEQRLPSLL GLHFPANDIP QQSREMFIAA RQRAIVDVAN GKIGLSPLCS
     PQTNEPLETE NIHYRQVDPC HIQYLTALGV QSSLVVPILH RDLKEKSAKP ELWGLLVSHH
     SQARSILPWE LKLLQQITDQ VEIALAQSNL LSEARSQRQQ QALINQIAIL LNQLPTIQFQ
     TALESTITAF GGTGGRLYIE QSRELYTCGE QPQLPHDSKN IVIEQHPVWQ NWIAECKQGQ
     VLAIPDLYKE THLRVLAVGF QPTKIRGILV IPLYYRNSFL GVLSIFRPEF DTEILWAGRC
     DQNQRQRQPQ LSFDVWREQK KGQAPEWKLE DIVLGQALGY HFSMAIQQQQ MYQQVQLLNT
     NLEQRVQEQT GELEKSLLFT KVIKQITEQI RSSLDLKITL QTIVQEVRPL LNSDRVLIYQ
     LSGESDGHVI VEEINGSYPS VLGIKAPPEC FPDEYASLYV QGRVRAINDV STATLSDCHR
     EFLLNLQVQA NLIIPINMGT QLWGLLIAHQ CDRPRNWQDA EIELMLQLAD QAAIAIQQAQ
     LYEQSHTAEN QAKAKAQQLE RTLYELRQTQ TQLIQNEKMS SLGQLVAGVA HEINNPVNFI
     YGNLSYANDY TEQLLKLLRL YQSHYSQPDS EIRSLEKAID VEFVAEDLPK IISSMQVGAD
     RICSIVQSLR NFSRLDEAEH KPVDLHEGID NTLLILQHRL KSTVNFPGVK VVKDYGDLPL
     VRCYAGQMNQ VFMNILSNAL DALQMHADNN QSFIPSICIS TRVSADNSFV LIRIADNGPG
     MTEDVKRRIF DPFFTTKPVG KGTGLGLAIS YQIIVEKHGG IIDCVSEVGK GTEFWMEIAL
     NPQCKVNSQY INSLLPSSER WQVKTNF
//
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