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Database: UniProt
Entry: A0A0E0B9G2_9ORYZ
LinkDB: A0A0E0B9G2_9ORYZ
Original site: A0A0E0B9G2_9ORYZ 
ID   A0A0E0B9G2_9ORYZ        Unreviewed;      1185 AA.
AC   A0A0E0B9G2;
DT   27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT   27-MAY-2015, 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};
OS   Oryza glumipatula.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Oryzoideae; Oryzeae; Oryzinae; Oryza.
OX   NCBI_TaxID=40148 {ECO:0000313|EnsemblPlants:OGLUM10G07040.1};
RN   [1] {ECO:0000313|EnsemblPlants:OGLUM10G07040.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Wing R.A., Panaud O., Oliveira A.C.;
RT   "Oryza genome evolution.";
RL   Submitted (AUG-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EnsemblPlants:OGLUM10G07040.1}
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}.
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DR   AlphaFoldDB; A0A0E0B9G2; -.
DR   EnsemblPlants; OGLUM10G07040.1; OGLUM10G07040.1; OGLUM10G07040.
DR   Gramene; OGLUM10G07040.1; OGLUM10G07040.1; OGLUM10G07040.
DR   Proteomes; UP000026961; Unassembled WGS sequence.
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; 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; IPR004358; Sig_transdc_His_kin-like_C.
DR   InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR   PANTHER; PTHR43719:SF35; HISTIDINE KINASE 2; 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; PS51257; PROKAR_LIPOPROTEIN; 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:UP000026961};
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        192..212
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        243..260
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        544..567
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          311..535
FT                   /note="CHASE"
FT                   /evidence="ECO:0000259|PROSITE:PS50839"
FT   DOMAIN          603..878
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   DOMAIN          902..1033
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000259|PROSITE:PS50110"
FT   DOMAIN          1057..1185
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000259|PROSITE:PS50110"
FT   MOD_RES         958
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT   MOD_RES         1107
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ   SEQUENCE   1185 AA;  130384 MW;  64B25A55A21BEB2A CRC64;
     MSRVGECGGG GGCGARRGKA AHAGAGAVAG FLGCLLLVWA MGGCGRGCGG GGGEGVRDRV
     EEVAAQFNLS MSKLQALASL LSSPERECIC KSGTINHDNP AHSMPDMSNC RLKNKPSGGN
     QNRLDNVILQ DCCANEDNYD KNNHENNLLQ NAMQQDIGSP TTLWNLCLCD LCIVINGLNV
     QQNNALSCNH GMIFSLSASL GIVVILVVIT IFKRGKQANE LCQHEKLLQT PSVKISRKWS
     KRALLLGVLV GLCSSVWIFS SMHADVVARR IENLENMCDE RARMLQDQFN VSMNHVHALA
     ILVSTFHHGK NPSAIDQKTF EDFTARTTFE RPLMSGVAYA LKVLHSEREL FEQKLGWKIK
     KMETEDQSLV HDYNPEKLQP SPVQDEYAPV IFSQETVKHI ISVDMMSGKE DRDNILRSRA
     TGKGALTAPF PLLKSNHLGV VLTFTVYKYD LPPDATPEER IEATLGYLGA SFDVPSLVER
     LLEQLASKQK IVVRLYDITN HTYPTKMYDS DVIASDDLHI SNIDFGDPTR KHVMQCRFKH
     APSLPWSAIM ISSAVAIIVL LVGYIIYATL NSLEEAEDNY TTMRDLKGRA EAADVAKSQF
     LATVSHEIRT PMNGVLGMLQ MLMDTELDTT QRDFVVTAQE SGKSLINLIN EVLDLAKIES
     GKIELEAVRF DVRDILDNVV SLFSEKSWAK GIELAVLVSD QVPDVLIGDP WRFRQIITNL
     VGNSMKFTEQ GHIFIRVHLI EEVKRKMEAL DDTSPENIEV TANSKNTMPY NTLSGLEVAN
     NRKTLESFRM FKDSSDAIDS VNLLVTVEDT GIGITKDAQT RIFTPFMQAD GSTSRTYGGT
     GIGLSITKRL VELMGGEIGF VSKPGVSSTF SFTAIFKENR KDPGDIKRYC PEPTPPDFQG
     MRALVVDGRC ARAEVTMYHL RRLGIQCDLA ATSESALSAL LESCNSSVKS SLNMVLVDKE
     AWGEDSGLAF FRCLIDLRLK GTLKSWQTMP KFFLLAGSIT PADSDCLRLA GYSNSIRKPL
     RLSTVAACLS KALGVGLTGR QSRDNSLVLR SVLTGKNILV VDDNAVNRIV AAGALKKYGA
     IVTCVDSGKE AISRLQPPHK FDACFMDVQM PEMDGFEATR LVRSVESKIN DMIQAASAKN
     PFGDNNVAKQ KSYAVNREQK FDWTAIYVSF GEFQLNTLNV QALVT
//
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