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Database: UniProt
Entry: A0A1D6HJP3_MAIZE
LinkDB: A0A1D6HJP3_MAIZE
Original site: A0A1D6HJP3_MAIZE 
ID   A0A1D6HJP3_MAIZE        Unreviewed;       709 AA.
AC   A0A1D6HJP3;
DT   30-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   30-NOV-2016, sequence version 1.
DT   27-MAR-2024, entry version 36.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=ZEAMMB73_Zm00001d017977 {ECO:0000313|EMBL:AQK74680.1};
OS   Zea mays (Maize).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC   Panicoideae; Andropogonodae; Andropogoneae; Tripsacinae; Zea.
OX   NCBI_TaxID=4577 {ECO:0000313|EMBL:AQK74680.1};
RN   [1] {ECO:0000313|EMBL:AQK74680.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Seedling {ECO:0000313|EMBL:AQK74680.1};
RG   Maize Genome Sequencing Project;
RA   Ware D.;
RT   "Update maize B73 reference genome by single molecule sequencing
RT   technologies.";
RL   Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Cytokinin receptor related to bacterial two-component
CC       regulators. Functions as a histidine kinase and transmits the stress
CC       signal to a downstream MAPK cascade. {ECO:0000256|ARBA:ARBA00002427}.
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   -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004651};
CC       Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}.
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DR   EMBL; CM000781; AQK74680.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1D6HJP3; -.
DR   OMA; FDHETHE; -.
DR   ExpressionAtlas; A0A1D6HJP3; baseline and differential.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR   GO; GO:0009736; P:cytokinin-activated signaling pathway; IEA:UniProtKB-KW.
DR   CDD; cd16922; HATPase_EvgS-ArcB-TorS-like; 1.
DR   CDD; cd00082; HisKA; 1.
DR   CDD; cd06223; PRTases_typeI; 1.
DR   CDD; cd17546; REC_hyHK_CKI1_RcsC-like; 1.
DR   Gene3D; 1.10.287.130; -; 1.
DR   Gene3D; 3.40.50.2300; -; 1.
DR   Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR   InterPro; IPR011006; CheY-like_superfamily.
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; IPR000836; PRibTrfase_dom.
DR   InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR   InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR   PANTHER; PTHR43719:SF65; HISTIDINE KINASE 6-RELATED; 1.
DR   PANTHER; PTHR43719; TWO-COMPONENT HISTIDINE KINASE; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF00512; HisKA; 1.
DR   Pfam; PF00072; Response_reg; 1.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00387; HATPase_c; 1.
DR   SMART; SM00388; HisKA; 1.
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; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR   PROSITE; PS50109; HIS_KIN; 1.
DR   PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE   4: Predicted;
KW   Cytokinin signaling pathway {ECO:0000256|ARBA:ARBA00022864};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:AQK74680.1};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
SQ   SEQUENCE   709 AA;  78331 MW;  EF651B764DFCE1E1 CRC64;
     MVLYGPSSLD EQVPFLHVSM LDFGDPFRKH EMRCRYRQKL PMPWSAITNP LGTFVIWMLL
     GYSIAAAYSR YDKVTEDCRK MEELKTQAEA ADVAKSQFLA TVSHEIRTPM NGVLGMLDML
     LGTDLTMTQK DYAQTAQMCG RALITLINDV LDRAKIEAGK LELEAVPFDL RSLMDDVVSL
     FSSKSREKCI ELAVFVCDNV PKVVIGDPWR FRQILTNLVG NAVKFTERGH VFVRVCLAEN
     SNVEANQVLH GAMNGKGGRV ESTTNGAFNT LSGFEAADRR NSWQYFKLLL SDKESLLDDL
     EGENSNQSDS NHVTLAISIE DTGVGIPLQA QDRVFTPFMQ ADSSTSRNYG GTGIGLSISK
     CLAELMGGQI SFTSHPSVGS TFTFSATLKH SYKDISVDSS RSLTEALPTA FKGMKAILVD
     GRPVRSAVTR YHLKRLGILL QVVNNMNAVV KAFPGQNGAT GSREKASILF IESDFWRPET
     DVQLLNHLRE QKNGQLSDGH KVVLLVTSEA DKDKYGSIFD IVMCKPIRAS TIASSIQQLL
     KVEIAERKDN QNRPSFLRSL LVGKNILVVD DNKVNLRVAA AALKKYGANV SCVESGKDAI
     SLLQPPHRFD ACFMDVQMPE MDGFEATGQI RQMELKANEE RKNKLASIEG STTAEYHLPV
     LAMTADVIQA TYEECIKSGM DGYVSKPFDE EQLYQAVSRL VVGTTDSAV
//
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