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Database: UniProt
Entry: A0A367QSN5_9NOSO
LinkDB: A0A367QSN5_9NOSO
Original site: A0A367QSN5_9NOSO 
ID   A0A367QSN5_9NOSO        Unreviewed;      1396 AA.
AC   A0A367QSN5;
DT   07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT   07-NOV-2018, sequence version 1.
DT   27-MAR-2024, entry version 18.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=A6770_26060 {ECO:0000313|EMBL:RCJ26770.1};
OS   Nostoc minutum NIES-26.
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Nostocaceae; Nostoc.
OX   NCBI_TaxID=1844469 {ECO:0000313|EMBL:RCJ26770.1, ECO:0000313|Proteomes:UP000252107};
RN   [1] {ECO:0000313|Proteomes:UP000252107}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Tabuchi Yagui T.R.;
RL   Submitted (APR-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:RCJ26770.1}.
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DR   EMBL; LXQD01000307; RCJ26770.1; -; Genomic_DNA.
DR   Proteomes; UP000252107; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR   CDD; cd16922; HATPase_EvgS-ArcB-TorS-like; 1.
DR   CDD; cd00082; HisKA; 1.
DR   CDD; cd00130; PAS; 3.
DR   CDD; cd17580; REC_2_DhkD-like; 1.
DR   Gene3D; 1.10.287.130; -; 1.
DR   Gene3D; 2.10.70.100; -; 1.
DR   Gene3D; 3.30.450.40; -; 2.
DR   Gene3D; 3.40.50.2300; -; 1.
DR   Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR   Gene3D; 3.30.450.20; PAS domain; 4.
DR   InterPro; IPR011006; CheY-like_superfamily.
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; IPR001610; PAC.
DR   InterPro; IPR000014; PAS.
DR   InterPro; IPR000700; PAS-assoc_C.
DR   InterPro; IPR035965; PAS-like_dom_sf.
DR   InterPro; IPR013656; PAS_4.
DR   InterPro; IPR013655; PAS_fold_3.
DR   InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR   InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR   NCBIfam; TIGR00229; sensory_box; 3.
DR   PANTHER; PTHR43547:SF2; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE C; 1.
DR   PANTHER; PTHR43547; TWO-COMPONENT HISTIDINE KINASE; 1.
DR   Pfam; PF01590; GAF; 2.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF00512; HisKA; 1.
DR   Pfam; PF08447; PAS_3; 1.
DR   Pfam; PF08448; PAS_4; 2.
DR   Pfam; PF13426; PAS_9; 1.
DR   Pfam; PF00072; Response_reg; 1.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00065; GAF; 2.
DR   SMART; SM00387; HATPase_c; 1.
DR   SMART; SM00388; HisKA; 1.
DR   SMART; SM00086; PAC; 2.
DR   SMART; SM00091; PAS; 4.
DR   SMART; SM00448; REC; 1.
DR   SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR   SUPFAM; SSF52172; CheY-like; 1.
DR   SUPFAM; SSF55781; GAF domain-like; 2.
DR   SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR   SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 4.
DR   PROSITE; PS50109; HIS_KIN; 1.
DR   PROSITE; PS50113; PAC; 2.
DR   PROSITE; PS50112; PAS; 2.
DR   PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:RCJ26770.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW   ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000252107};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          109..188
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   DOMAIN          192..244
FT                   /note="PAC"
FT                   /evidence="ECO:0000259|PROSITE:PS50113"
FT   DOMAIN          644..696
FT                   /note="PAC"
FT                   /evidence="ECO:0000259|PROSITE:PS50113"
FT   DOMAIN          711..774
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   DOMAIN          1031..1249
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   DOMAIN          1271..1389
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000259|PROSITE:PS50110"
FT   COILED          63..112
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          381..408
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          681..714
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   MOD_RES         1320
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ   SEQUENCE   1396 AA;  156643 MW;  95F207286B7886A2 CRC64;
     MKRDATGKFI NNWDSETKQR VSISLTSTAW QLLDREAQTR GISRSEVIER VARSLGNDGV
     AQNALLQGQI IEQQQAIAAL ERQKQELESL ERKQAEAERD RLLHELETER AQFEAVLRQM
     PAGVLIADAV SGKLVLANEQ AKQIVGYSYE QSLELEEYEP ITPFEAFHPN GQIYTADEYP
     LVRSLSTGEV VSNEEIELHQ EDGSRIFISA NSAPILDSQE QIIAAIVVFQ DITERKQIAA
     ERDRLLEREQ AARLEAETEH QRLHDILMQL PAMIGIVTGS EHVFEFANPT YLQLTGRTPD
     IIGKSIREVF PELEGQIYFE TLDRVYRTGE AFIRYESPAH WDRNGDGVLE EAFFNCVFPA
     WRDRFGRIQG VLMHSIEVTA QVQARQQVEE LLKNLQHKEE QQQFLIELND AIRAIQDSEE
     IIWRVVCATG QHFQVTRCNY GEVDSSQKYV IIDRDYCNGV ISITGSHHMN SFGTEIIAEL
     KQGKTLVVDD VDADPRTADS GATAFDAIQT KSLLCVPLVK EGQFVALFVL HHVSPRHWTE
     EDVALMEQIA QKTWLAVERS QAEEALRESR ARLQLALMVG RMGTWDWDMQ MNTVTWSDGQ
     FAIMGLQPNQ YQPSYELWLQ SVHPDDLAQT ELSLQQAMLQ KTEYHHEYRT LWADGSLHWT
     EARGQFSYNA QGQPTRMIGV LIDITERKQA EQEREQLLER ERIARTQVEV AQRQLTALFE
     TSPVGIGLLD AEQRFIAINE ALAQINGLTH EQHLGHSIPE IFGQFDPKLV EVFHNIYTTG
     HPFISPSFAV NVPGRSDRSP GYYNVYYLPT KNLNDRVEDV LVYVVDVTER VRLERAQRFL
     AEASAVLGSS LDYQITLERV AQLAVSELAD WCTVHIVEED GSIEQIAVAH TDPAKLQWAH
     QIRQKYPLDL NAPRGAALTL RTGRSDFLAD IPDELLVQAA RDPEHLEILR QVGFKSAMTV
     PLRTQTRILG VITFVSAESG LRYDQVDLQL AEELAHRASL AIDNAQLYRI AQRDRAKAEA
     ANRVKDEFLA VLSHELRSPL NPILGWTKML RSRRLDSTKA DQALETIERN AKLQAELIED
     LLDVSRILQG KMTLNVAPVN LAATIEAAQE IVQLAAEAKS IHIQTTLNPV SGTVAGDMNR
     LQQIVWNLLS NAVKFTPSGG RVEVQLKQVG MYAQIQVKDT GIGISPEFLP HVFEYFQQED
     GTTTRKFGGL GLGLAIVRHL TELHGGTIQA DSPGQNLGAT FTVLLPLNIV EQELSANDNH
     SESGTNLTGI EILVVDDDAD MRDLAEFILT QSGAQVKTAA SAVQALTLLN QSVPNLLLCD
     IGMPEMDGYS LIRQIRKWSP QQGGTIPAIA LTAYAGEINQ QQALTAGFQM HISKPVEPDE
     LVQAIVQLLD PSKTNQ
//
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