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Database: UniProt
Entry: A0A0D9VKS6_9ORYZ
LinkDB: A0A0D9VKS6_9ORYZ
Original site: A0A0D9VKS6_9ORYZ 
ID   A0A0D9VKS6_9ORYZ        Unreviewed;       978 AA.
AC   A0A0D9VKS6;
DT   27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT   27-MAY-2015, sequence version 1.
DT   27-MAR-2024, entry version 40.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
OS   Leersia perrieri.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Oryzoideae; Oryzeae; Oryzinae; Leersia.
OX   NCBI_TaxID=77586 {ECO:0000313|EnsemblPlants:LPERR02G26050.2, ECO:0000313|Proteomes:UP000032180};
RN   [1] {ECO:0000313|EnsemblPlants:LPERR02G26050.2, ECO:0000313|Proteomes:UP000032180}
RP   NUCLEOTIDE SEQUENCE.
RA   Wing R.A.;
RT   "Oryza genome evolution.";
RL   Submitted (AUG-2012) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EnsemblPlants:LPERR02G26050.2, ECO:0000313|Proteomes:UP000032180}
RP   NUCLEOTIDE SEQUENCE.
RA   Yu Y., Lee S., de Baynast K., Wissotski M., Liu L., Talag J.,
RA   Goicoechea J., Angelova A., Jetty R., Kudrna D., Golser W., Rivera L.,
RA   Zhang J., Wing R.;
RL   Submitted (DEC-2013) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EnsemblPlants:LPERR02G26050.2}
RP   IDENTIFICATION.
RG   EnsemblPlants;
RL   Submitted (APR-2015) to UniProtKB.
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   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004651};
CC       Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00169}.
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DR   AlphaFoldDB; A0A0D9VKS6; -.
DR   STRING; 77586.A0A0D9VKS6; -.
DR   EnsemblPlants; LPERR02G26050.1; LPERR02G26050.1; LPERR02G26050.
DR   EnsemblPlants; LPERR02G26050.2; LPERR02G26050.2; LPERR02G26050.
DR   Gramene; LPERR02G26050.1; LPERR02G26050.1; LPERR02G26050.
DR   Gramene; LPERR02G26050.2; LPERR02G26050.2; LPERR02G26050.
DR   eggNOG; KOG0519; Eukaryota.
DR   HOGENOM; CLU_000445_16_3_1; -.
DR   Proteomes; UP000032180; Chromosome 2.
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; 6.10.250.1190; -; 1.
DR   Gene3D; 3.30.450.350; CHASE domain; 1.
DR   Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR   InterPro; IPR006189; CHASE_dom.
DR   InterPro; IPR042240; CHASE_sf.
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; PF03924; CHASE; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF00512; HisKA; 1.
DR   Pfam; PF00072; Response_reg; 1.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM01079; CHASE; 1.
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; 2.
DR   SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR   PROSITE; PS50839; CHASE; 1.
DR   PROSITE; PS50109; HIS_KIN; 1.
DR   PROSITE; PS50110; RESPONSE_REGULATORY; 2.
PE   4: Predicted;
KW   Cytokinin signaling pathway {ECO:0000256|ARBA:ARBA00022864};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW   ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000032180};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius};
KW   Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT   TRANSMEM        310..332
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          89..301
FT                   /note="CHASE"
FT                   /evidence="ECO:0000259|PROSITE:PS50839"
FT   DOMAIN          369..658
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   DOMAIN          683..809
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000259|PROSITE:PS50110"
FT   DOMAIN          834..970
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000259|PROSITE:PS50110"
FT   MOD_RES         884
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ   SEQUENCE   978 AA;  108894 MW;  C1F476777790B0F3 CRC64;
     MGWLPRRSGW MPRRLGWREV ASAAFLLAAV TASAAFHWHM RQETMEKAEE RLVSMCEERA
     RMLQEQFGVT VNHVHALAIL ISTFHFEKSP SAIDQDTFAK YTARTSFERP LLNGVAYAQR
     IFHHEREMFE SQQGWIMKTM KREAAPPQDE YAPVIFSQDS ISYLSRIDMM SGEEDRENIL
     RARATGKAVL TNPFRLLGSN HLGVVLTFAV YRPGLAADAS VEERVEATAG YLGGAFDVES
     LVENLLSKLA GNQDIVVNVY DVTNGSEPMV MYGPQSPDGK VSLFHVSTLD FGDPFRRHEM
     RCRYKQKPPL PWSAITNPLG TFVILMLIGY IAHAAWSRYD KVSEDCRKME ELKTQAEAAD
     VAKSQFLATV SHEIRTPMNG VLGMLDMLLG TDLTMTQKDF AQTAQMCGRA LITLINDVLD
     RAKIEAGKLE LEAVPFDLRS LMDDVISLFS SKSREKCIEL AVFVCDDVPK VVIGDPWRYR
     QILTNLVGNA VKFTERGHVF VRVCLADNSN VGANQVLNGT MNGKDGKVST TANGTFNTLS
     GFQAADERNN WDYFKLLLSD KEPPMDELEC EKSCQNDCDR VNLMISIEDT GVGIPLHAQD
     RVFTPFMQAD SSTSRNYGGT GIGLSISKCL AELMGGQISF TSRPSVGSTF TFSAVLKRSC
     KDTLSDTKRS LSEALPTAFK GMKAILVDGR PVRGAVTRYH LNRLGIVVQV VNSLSMGLQT
     LAGQNGVKES REKLSMLFIE SDIWRPQTDI LLLNHLHELK NNGLVHELPT LVLLVTSEAD
     KDRYGSTFDI VMCKPIRAST IASCLQQLLK VVMPERKENQ NRPSFLRSLL VGKNILIVDD
     NKVNLRVAAA ALKKYGAKVH CVESGKDAIS LLKQQHCFDA CFMDVQMPEM DGFEATRQIR
     QMELKANEER KNALASMDGS TFVEFHLPVL AMTADVIQAT YEECVKSGMD GYVSKPFDEE
     QLYQAVSRLV VGTTESAV
//
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