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Database: UniProt
Entry: A0A1Z4RN27_9CHRO
LinkDB: A0A1Z4RN27_9CHRO
Original site: A0A1Z4RN27_9CHRO 
ID   A0A1Z4RN27_9CHRO        Unreviewed;       950 AA.
AC   A0A1Z4RN27;
DT   27-SEP-2017, integrated into UniProtKB/TrEMBL.
DT   27-SEP-2017, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=NIES4102_08610 {ECO:0000313|EMBL:BAZ43859.1};
OS   Chondrocystis sp. NIES-4102.
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Oscillatoriophycideae;
OC   Chroococcales; Chroococcaceae; Chondrocystis.
OX   NCBI_TaxID=2005460 {ECO:0000313|EMBL:BAZ43859.1, ECO:0000313|Proteomes:UP000217698};
RN   [1] {ECO:0000313|EMBL:BAZ43859.1, ECO:0000313|Proteomes:UP000217698}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NIES-4102 {ECO:0000313|EMBL:BAZ43859.1,
RC   ECO:0000313|Proteomes:UP000217698};
RA   Hirose Y., Shimura Y., Fujisawa T., Nakamura Y., Kawachi M.;
RT   "Genome sequencing of cyanobaciteial culture collection at National
RT   Institute for Environmental Studies (NIES).";
RL   Submitted (JUN-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}.
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DR   EMBL; AP018281; BAZ43859.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Z4RN27; -.
DR   KEGG; chon:NIES4102_08610; -.
DR   OrthoDB; 418136at2; -.
DR   Proteomes; UP000217698; Chromosome.
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   Gene3D; 1.10.287.130; -; 1.
DR   Gene3D; 2.10.70.100; -; 1.
DR   Gene3D; 3.30.450.40; -; 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; 3.
DR   InterPro; IPR000644; CBS_dom.
DR   InterPro; IPR046342; CBS_dom_sf.
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; IPR016132; Phyto_chromo_attachment.
DR   InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR   NCBIfam; TIGR00229; sensory_box; 2.
DR   PANTHER; PTHR43711:SF1; HISTIDINE KINASE 1; 1.
DR   PANTHER; PTHR43711; TWO-COMPONENT HISTIDINE KINASE; 1.
DR   Pfam; PF00571; CBS; 1.
DR   Pfam; PF01590; GAF; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF00512; HisKA; 1.
DR   Pfam; PF08447; PAS_3; 1.
DR   Pfam; PF08448; PAS_4; 1.
DR   Pfam; PF13426; PAS_9; 1.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00116; CBS; 2.
DR   SMART; SM00065; GAF; 1.
DR   SMART; SM00387; HATPase_c; 1.
DR   SMART; SM00388; HisKA; 1.
DR   SMART; SM00086; PAC; 3.
DR   SMART; SM00091; PAS; 3.
DR   SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR   SUPFAM; SSF54631; CBS-domain pair; 1.
DR   SUPFAM; SSF55781; GAF domain-like; 1.
DR   SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR   SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 3.
DR   PROSITE; PS51371; CBS; 2.
DR   PROSITE; PS50109; HIS_KIN; 1.
DR   PROSITE; PS50113; PAC; 3.
DR   PROSITE; PS50112; PAS; 2.
DR   PROSITE; PS50046; PHYTOCHROME_2; 1.
PE   3: Inferred from homology;
KW   CBS domain {ECO:0000256|PROSITE-ProRule:PRU00703};
KW   Kinase {ECO:0000313|EMBL:BAZ43859.1};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000217698};
KW   Transferase {ECO:0000313|EMBL:BAZ43859.1}.
FT   DOMAIN          7..68
FT                   /note="CBS"
FT                   /evidence="ECO:0000259|PROSITE:PS51371"
FT   DOMAIN          75..134
FT                   /note="CBS"
FT                   /evidence="ECO:0000259|PROSITE:PS51371"
FT   DOMAIN          163..299
FT                   /note="Phytochrome chromophore attachment site"
FT                   /evidence="ECO:0000259|PROSITE:PS50046"
FT   DOMAIN          348..418
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   DOMAIN          427..477
FT                   /note="PAC"
FT                   /evidence="ECO:0000259|PROSITE:PS50113"
FT   DOMAIN          553..605
FT                   /note="PAC"
FT                   /evidence="ECO:0000259|PROSITE:PS50113"
FT   DOMAIN          606..676
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   DOMAIN          678..730
FT                   /note="PAC"
FT                   /evidence="ECO:0000259|PROSITE:PS50113"
FT   DOMAIN          734..950
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
SQ   SEQUENCE   950 AA;  107957 MW;  268CD10B40571A20 CRC64;
     MDIDQCLQPN PITVTPETLL SEAIALMALE QSKDLPACIL IVEVTKILGI LTARDVVRLL
     ALKVNFETTT IGTVMTCPVI TLQNSLVCEQ EYILSLLQQH NISFLPIVKG EQQILGILDT
     KSLFQAWETT PLQQRQVWNQ LKHQYQQTKL LAEITRKIRM SINLDDILQT AVKEVQNLLA
     CDRVLIVKVR FNSTAIPISE AIVPNLPSML GYEITDPLLI GDNLAKYHQG EFLAISDLTL
     AGIALEIQTL LKQFEIKAKL VVPILSQTEL KALLVVHQCR SPRSWQSKEI ELLQQLADQI
     GVALSQAQLL NHLEELVLER TIELTTTNQL LEAEILERKQ TEIALRENQQ KLTGILDHAD
     EAIITINEQQ QIQLFNQGAE KIFGYQVHEI IGKPLDILLP DTYHQIHRQH VNQFNQSPDK
     AHVMTERNCN IYGRRKNGAE FPAEASIAKL QTSEGVLLTV MLKDITERQQ SAAKLQASKT
     LLAKAEKIAK IGSWEYNPAT QQLTWSEELY EILDFPQMQN LPTCAAVVAR IHPEDYLMVK
     KALKQGHREG KAWQFTYRWI LEDEQVKYLE SRGEPTLDSE GKVIKVWGTV MDISDRIRAE
     KSVQRSEEQL RLITDALPIL IAYIDNHKRY RYINRTYETW FGRPRSTLLG LHIQEVVGLD
     NYRHMLPYIE TVLAGRPVIY ENQATDEDGN CYWICGTYIP NFDSQGAVKG FFSMVDDITE
     RKEIERLKSE FISVASHEMR TPLTSIHGVL ELLCAGRLGH LTSSGQTMAN IALKNSDRLV
     RLVNDLLDLE RMTSGRDKIV KSACDSLELI NQAIETLQSQ AQQQQIILET QPQSFKLFAE
     RDRIVQTLIN LINNAIKFSE PNDHVWVTAQ QRQTDILFTV KDQGRGIPKG KIDTIFERFQ
     QVDASDSRDK GGTGLGLAIC RQIVEQHQGK IWVESVYGQG CTFYFTIPQQ
//
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