ID A0A0D9YXZ5_9ORYZ Unreviewed; 985 AA.
AC A0A0D9YXZ5;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 27-MAR-2024, entry version 37.
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:OGLUM02G32480.1};
RN [1] {ECO:0000313|EnsemblPlants:OGLUM02G32480.1}
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:OGLUM02G32480.1}
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}.
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; A0A0D9YXZ5; -.
DR EnsemblPlants; OGLUM02G32480.1; OGLUM02G32480.1; OGLUM02G32480.
DR Gramene; OGLUM02G32480.1; OGLUM02G32480.1; OGLUM02G32480.
DR HOGENOM; CLU_000445_16_2_1; -.
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: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; 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 12..31
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 318..345
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 82..309
FT /note="CHASE"
FT /evidence="ECO:0000259|PROSITE:PS50839"
FT DOMAIN 377..666
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 691..817
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 842..977
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT MOD_RES 892
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 985 AA; 109843 MW; 4B8FED8F36373263 CRC64;
MGKPEARSGW RNAAAAAWVL VAVACAAAFH WHLRRETMDR AEERLVSMCE ERARMLQEQF
GVTVNHVHAL AILISTFHFE KFPSAIDQDT FAKYTARTSF ERPLLNGVAY AQRIFHHERE
MFENQQGWIM KTMKRQAAPP QDEYAPVIFS QDTVSYLARI DMMSGEEDRE NILRARATGK
AVLTNPFRLL GSNHLGVVLT FAVYRPGLAA DASVEERVEA TAGCLVVVVS SNQIPTNRYL
GGAFDVESLV ENLLSKLAGN QDIVVNVYDV TNASEPMAMY GPQSPDGKVS LFHVSTLDFG
DPFRAHEMRC RYRQKPPLPW SAITNPLGTF VIWMLVGYII CAAWSRYDKV SEDCRKMEEL
KTQAEAADVA KSQFLATVSH EIRTPMNGVL GMLDMLLGTD LSMTQKDYAQ TAQMCGRALI
TLINDVLDRA KIEAGKLELE AVPFDLRSLM DDVISLFSSK SREKCIELAV FVCDDVPKVV
IGDPWRYRQI LTNLVGNAVK FTERGHVFVR VCLAENSKVE ANQVLNGTMN GKDGKVETTA
NGAFNTLSGF QAADERNNWD YFKLLLSDKE PHMDELECDR SYQNDCDCVT LMISIEDTGV
GIPLHAQDRV FTPFMQADSS TSRNYGGTGI GLSISKCLAE LMGGQISFTS RPFVGSTFTF
SAVLKRSCKD TSSDSKRSLS EALPTAFKGM KAILVDRRPV RGAVTRYHLN RLGIVVKVVN
NLSMGLQTLA GQNGVKESRE KLSMLFIESD IWRPETDILL LNRLHELKNN GQVHELPKLV
LLVTSEADKD RYGSAFDIVM YKPIRASTIA SCLQQLLKVV MPERKDNQNR PSFLRSLLIG
KNILIVDDNK VNLRVAAAAL KKYGAKVHCV ESGKDAVSLL QQPHCFDACF MDVQMPEMDG
FEATRQIRQM EVKANEERKA LDLMEGSTFV ESHLPVLAMT ADVIQATYEE CIKSGMDGYV
SKPFDEEQLY QAVSRLVVGT KESAV
//