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Database: UniProt
Entry: A0A0D6KZR3_9CYAN
LinkDB: A0A0D6KZR3_9CYAN
Original site: A0A0D6KZR3_9CYAN 
ID   A0A0D6KZR3_9CYAN        Unreviewed;      1406 AA.
AC   A0A0D6KZR3;
DT   27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT   27-MAY-2015, sequence version 1.
DT   27-MAR-2024, entry version 38.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=FDUTEX481_01135 {ECO:0000313|EMBL:EKF04971.1};
OS   Tolypothrix sp. PCC 7601.
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Tolypothrichaceae;
OC   Tolypothrix.
OX   NCBI_TaxID=1188 {ECO:0000313|EMBL:EKF04971.1, ECO:0000313|Proteomes:UP000032761};
RN   [1] {ECO:0000313|EMBL:EKF04971.1, ECO:0000313|Proteomes:UP000032761}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PCC 7601 / UTEX B 481 {ECO:0000313|Proteomes:UP000032761};
RX   PubMed=25953173;
RA   Yerrapragada S., Shukla A., Hallsworth-Pepin K., Choi K., Wollam A.,
RA   Clifton S., Qin X., Muzny D., Raghuraman S., Ashki H., Uzman A.,
RA   Highlander S.K., Fryszczyn B.G., Fox G.E., Tirumalai M.R., Liu Y., Kim S.,
RA   Kehoe D.M., Weinstock G.M.;
RT   "Extreme Sensory Complexity Encoded in the 10-Megabase Draft Genome
RT   Sequence of the Chromatically Acclimating Cyanobacterium Tolypothrix sp.
RT   PCC 7601.";
RL   Genome Announc. 3:0-0(2015).
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:EKF04971.1}.
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DR   EMBL; AGCR01000005; EKF04971.1; -; Genomic_DNA.
DR   RefSeq; WP_045868099.1; NZ_JH930357.1.
DR   STRING; 1188.FDUTEX481_01135; -.
DR   PATRIC; fig|1188.3.peg.1139; -.
DR   HOGENOM; CLU_252075_0_0_3; -.
DR   OrthoDB; 518094at2; -.
DR   Proteomes; UP000032761; Unassembled WGS sequence.
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; 6.
DR   Gene3D; 1.10.287.130; -; 1.
DR   Gene3D; 2.10.70.100; -; 1.
DR   Gene3D; 3.10.580.10; CBS-domain; 1.
DR   Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR   Gene3D; 3.30.450.20; PAS domain; 8.
DR   InterPro; IPR000644; CBS_dom.
DR   InterPro; IPR046342; CBS_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   NCBIfam; TIGR00229; sensory_box; 6.
DR   PANTHER; PTHR43304:SF1; PAC DOMAIN-CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR43304; PHYTOCHROME-LIKE PROTEIN CPH1; 1.
DR   Pfam; PF00571; CBS; 2.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF00512; HisKA; 1.
DR   Pfam; PF08447; PAS_3; 7.
DR   Pfam; PF08448; PAS_4; 1.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00116; CBS; 2.
DR   SMART; SM00387; HATPase_c; 1.
DR   SMART; SM00388; HisKA; 1.
DR   SMART; SM00086; PAC; 8.
DR   SMART; SM00091; PAS; 6.
DR   SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR   SUPFAM; SSF54631; CBS-domain pair; 1.
DR   SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR   SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 8.
DR   PROSITE; PS51371; CBS; 2.
DR   PROSITE; PS50109; HIS_KIN; 1.
DR   PROSITE; PS50113; PAC; 8.
DR   PROSITE; PS50112; PAS; 5.
PE   4: Predicted;
KW   CBS domain {ECO:0000256|PROSITE-ProRule:PRU00703};
KW   Kinase {ECO:0000313|EMBL:EKF04971.1};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Transferase {ECO:0000313|EMBL:EKF04971.1}.
FT   DOMAIN          10..67
FT                   /note="CBS"
FT                   /evidence="ECO:0000259|PROSITE:PS51371"
FT   DOMAIN          74..134
FT                   /note="CBS"
FT                   /evidence="ECO:0000259|PROSITE:PS51371"
FT   DOMAIN          173..219
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   DOMAIN          222..274
FT                   /note="PAC"
FT                   /evidence="ECO:0000259|PROSITE:PS50113"
FT   DOMAIN          275..347
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   DOMAIN          351..404
FT                   /note="PAC"
FT                   /evidence="ECO:0000259|PROSITE:PS50113"
FT   DOMAIN          485..536
FT                   /note="PAC"
FT                   /evidence="ECO:0000259|PROSITE:PS50113"
FT   DOMAIN          610..665
FT                   /note="PAC"
FT                   /evidence="ECO:0000259|PROSITE:PS50113"
FT   DOMAIN          666..740
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   DOMAIN          738..794
FT                   /note="PAC"
FT                   /evidence="ECO:0000259|PROSITE:PS50113"
FT   DOMAIN          874..926
FT                   /note="PAC"
FT                   /evidence="ECO:0000259|PROSITE:PS50113"
FT   DOMAIN          927..1004
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   DOMAIN          1006..1058
FT                   /note="PAC"
FT                   /evidence="ECO:0000259|PROSITE:PS50113"
FT   DOMAIN          1059..1114
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   DOMAIN          1132..1184
FT                   /note="PAC"
FT                   /evidence="ECO:0000259|PROSITE:PS50113"
FT   DOMAIN          1188..1405
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
SQ   SEQUENCE   1406 AA;  160023 MW;  21CBD6215130235F CRC64;
     MQPLSQTQFL QKCPLTLAPN TSVEFAVQAM NQENSSYVLV VEQHQLVGIF TQRDLVKAIA
     SGVNLSVATL SDVMTDNVIT VKESELGDLF KILRLLKQQQ ISYLPVLDKE GKLVGAIALA
     NMQAALLLEI EHREQVAQTQ PNYQTQLDVI LSSTRTIISR IRLLSAPEFR CEYISPSCQS
     ILGYSPDEFL ADPLLWASRL LPEDQNVILH HIQDAIQSEK ILTIEYPFSH KDGSICWICD
     TFSSEWDEIT QSWQVMSVKT DITQRKQTEE ALRTSEERLQ LALEASGEGV WDWNIITGYL
     YLSPRWCEML GYAADELADD ITTWEQLLHP EDRPWVMDVL QSHLMDSSIP YTFEYRMRTK
     SEGWKWIANY GKVVSRDKNG QALRMAGIHR NVTNRKRAEQ ALQEREAFLR AIGDNIPHSY
     IYQVIRERDG NYRFYYISAG VEATNGFHPT AVLADSSLLY NNLLPEDQLY VSQKQEESAQ
     TMSVFDVQVR EYTPQRDIRW IRLCSTPRHL DDGRICWDGI RLDITEQKLT EERLRKSTAL
     LTEAQQVAQI GNWEYDLATQ KITWTEELFH ILNRDPALLE PSYDENLQIY QPQDAARLHK
     AVETTITTGE SYKLILKRNP RPDGSIRYIE GTGQAEFNAD GQVIRLYGTA QDITERFLAQ
     QSLQKKEEFL SSIYNGVEQC IFVVDVLVDG EISFVDINPA YERLTGISAL DIQGKTLDKL
     LPPEVASLVR QHYQACVTAR ETVTYEECLP ISGQDTWWIT SLTPLLDENS CVYRIVGSST
     NISDRKRLEL ALQASESRLN NILTTANASI VCFRVFANYD WEYEYQSIGS EALFGYTPAE
     IVSDKQMWMS QVFAEDREQV LYPLFEEILA ERTSTIEYRF HHKDGSLRWI SATYSSHRDK
     VANCWIVTGV SIDISDRKRL ELALQASEKR LQNILSTASA SIFSFRISAN QEWEYEYQSA
     ASEIIFGYSP AEILADKKLW ISRVLPEDRK QVMYARFQRS IAEGTNSIEY RFRHKDGAVR
     WISTTYSSVR QEETDTWVVI GVSIDVSSLK LAEEAMRQSE TLFRTLSDSA PVGIFRSDTL
     GTNIYTNPRF QAICGLSLEE SFGDSWLQYI HPEDLAVFWP QWQELATVNL EFCTELRYIR
     PDSTLRFLRI TIVPIISSPH EIIGYVGTIE DITESRAIEK MKNEFISIVS HELRTPLASI
     RGALGLLSSG VLKTQPETAQ QMLDIAYSDT ERLVRLVNDI LDLEHLESNK FSLVKQRCDA
     ATLIRQSVEA LQPLATANNV VLEMSLTSIQ ICVDPDRIMQ TLLNLIGNAI KFSPANSTVT
     LSAEDLSDRI LFKVQDQGRG IPHDMLETIF GRFQQVDASD SRQKGGTGLG LAICRGIVQQ
     HGGTIWAQSV LGEGSIFYFT IPKPEV
//
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