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Database: UniProt
Entry: A0A235I775_9NOSO
LinkDB: A0A235I775_9NOSO
Original site: A0A235I775_9NOSO 
ID   A0A235I775_9NOSO        Unreviewed;      1101 AA.
AC   A0A235I775;
DT   25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT   25-OCT-2017, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=CDG76_18305 {ECO:0000313|EMBL:OYD93918.1};
OS   Nostoc sp. 'Peltigera membranacea cyanobiont' 210A.
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Nostocaceae; Nostoc.
OX   NCBI_TaxID=2014529 {ECO:0000313|EMBL:OYD93918.1, ECO:0000313|Proteomes:UP000215440};
RN   [1] {ECO:0000313|EMBL:OYD93918.1, ECO:0000313|Proteomes:UP000215440}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=210A {ECO:0000313|EMBL:OYD93918.1,
RC   ECO:0000313|Proteomes:UP000215440};
RA   Gagunashvili A.N., Andresson O.S.;
RT   "Distinctive characters of Nostoc genomes in cyanolichens.";
RL   Submitted (JUL-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:OYD93918.1}.
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DR   EMBL; NOLJ01000005; OYD93918.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A235I775; -.
DR   OrthoDB; 474548at2; -.
DR   Proteomes; UP000215440; 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; -; 4.
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; 3.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF00360; PHY; 1.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00065; GAF; 4.
DR   SMART; SM00387; HATPase_c; 1.
DR   SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR   SUPFAM; SSF55781; GAF domain-like; 4.
DR   SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR   PROSITE; PS50109; HIS_KIN; 1.
DR   PROSITE; PS50046; PHYTOCHROME_2; 3.
PE   3: Inferred from homology;
KW   Kinase {ECO:0000313|EMBL:OYD93918.1};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Transferase {ECO:0000313|EMBL:OYD93918.1}.
FT   DOMAIN          31..190
FT                   /note="Phytochrome chromophore attachment site"
FT                   /evidence="ECO:0000259|PROSITE:PS50046"
FT   DOMAIN          466..608
FT                   /note="Phytochrome chromophore attachment site"
FT                   /evidence="ECO:0000259|PROSITE:PS50046"
FT   DOMAIN          651..791
FT                   /note="Phytochrome chromophore attachment site"
FT                   /evidence="ECO:0000259|PROSITE:PS50046"
FT   DOMAIN          841..1099
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
SQ   SEQUENCE   1101 AA;  125201 MW;  A2A50FDD86D69577 CRC64;
     MTSNPEQDFS LCRDEESLLR RITNRIRRSL ELEEIITVTT AEVRSLLKTD RVMIYKFHPD
     GSGQVIAESI NKNCLPSLLG LNFPYDDIPS YARELFIKSR VRSVVNVETK EIGQIHLRDL
     DNGETISEEI RYRPVDPCHI EYLTTMGVKS SVVAPILYQD QLWGLLVSHN SEARLISEYE
     LEAIQMVVEQ LSMAIAQSTL HTQVRKTAER EAIVNRIATL LHSLPTIVLQ PALEAAVAAF
     DGVGGRLCIR NEALDVHNGN VTSLTECLIP GNTCIKLYIC GQQPVMPEQT IYPLIEQYSV
     WHEHYKSSKY DVWAISDIYN TPGLRTLQVA FQPTKIRSVL MIPLQYRQQL LGYLSIFRNE
     VDTETLWAGE HEGDQRQQYP RRSFEVWRES KKAQAQKWTV EEIELARNLS KHFASAIQQY
     ELYQQVQTFN ENLEKQVRRR TAELQRTAEQ EQAVFKVIAE IRESLDTNTI FQTTTKEVCQ
     LIKADRVSVY RFDANWGGEF VGDFEAASPY WSNESELGIN TIWNDTYLQD TEGGRYRYNE
     TFAVDDIYKM GFTQCHIDNL EQFQIYAFVL APIFVGQKLW GLLATYQHTG PRQWKASEVN
     FLSQIAAQMG VALQQADLLS QTQQQTLDLQ QAAEQQRVLF EVVAKVRESL NLDAIFQATT
     QEICKSLQAD RVAVYRFEAD WSGEYIAEFV VDNWLKLVGS DTKTVWRDSY LQETQGGRYR
     HNESFAVDDI YEVGHSQCHV AALEQLQARA YAIAPIFIRQ QLWGLLAAYQ NSAPRHWEAS
     EIKFITQIAN QLGVALQQAQ LHNQTKEQAQ KLAQALHDLQ QTQTQLIQTE KMSSLGQLVA
     GVAHEINNPV NFIYGNINHV NDYTQDLLGI LDLYLQNAPN PSSEIRDRAL DIDLEFIIED
     LPKTLSSMKI GVDRIRQIVL GLRNFSRLDE AEKKPVDIHE GIDSTLLILQ HRLKAKPESP
     AIQLVKEYTN LPLVECYAGP LNQVFMNVLS NAIDALEDYT ESQSNSHNSQ ITIRTALGEL
     EGNIKSVVIR IADNGPGIPE AMKAKICDPF FTTKPVGKGT GLGLSISYQI IVDKHGGVFR
     CDSQPGLGTE FWIEIPIKQI D
//
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