ID A0A4U6T108_SETVI Unreviewed; 1120 AA.
AC A0A4U6T108;
DT 31-JUL-2019, integrated into UniProtKB/TrEMBL.
DT 31-JUL-2019, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=SEVIR_9G272800v2 {ECO:0000313|EMBL:TKV94128.1};
OS Setaria viridis (Green bristlegrass) (Setaria italica subsp. viridis).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC Panicoideae; Panicodae; Paniceae; Cenchrinae; Setaria.
OX NCBI_TaxID=4556 {ECO:0000313|EMBL:TKV94128.1, ECO:0000313|Proteomes:UP000298652};
RN [1] {ECO:0000313|EMBL:TKV94128.1, ECO:0000313|Proteomes:UP000298652}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. A10 {ECO:0000313|Proteomes:UP000298652};
RA Huang P., Jenkins J., Grimwood J., Barry K., Healey A., Mamidi S.,
RA Sreedasyam A., Shu S., Feldman M., Wu J., Yu Y., Chen C., Johnson J.,
RA Rokhsar D., Baxter I., Schmutz J., Brutnell T., Kellogg E.;
RT "WGS assembly of Setaria viridis.";
RL Submitted (MAR-2019) 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; CM016560; TKV94128.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A4U6T108; -.
DR EnsemblPlants; TKV94128; TKV94128; SEVIR_9G272800v2.
DR Gramene; TKV94128; TKV94128; SEVIR_9G272800v2.
DR Proteomes; UP000298652; Chromosome 9.
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; -; 2.
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; 2.
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:UP000298652};
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 109..128
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 160..183
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 228..453
FT /note="CHASE"
FT /evidence="ECO:0000259|PROSITE:PS50839"
FT DOMAIN 521..796
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 820..950
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 974..1111
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT MOD_RES 875
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 1024
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1120 AA; 124340 MW; 214CF78153265907 CRC64;
MGKSGLIHGG NQVNGMSCIP DSLCIRDKIY DGKQNWLKDA ILQQFCTVQD KYGVNSHAPA
VLEAKFLQNV IQEDISSTTQ GNLHECELCA GMNGVNVVQN IVSSSNHTVM LFLSALFGSI
VVSIVKTIHK RRIQSNKLCE SDKVLQIPSA KISRKWSKRA LLIGVSIGLC SSGCIFLCMY
ADVVARRIEN LANMCDERAR MLQDQFNVSM NHVQALAILV STFHHGKNPS AIDQKTFEDF
TARTTFERPL MSGVAYALKV LHSEREQFEQ QHGWKIKKME AGDQSLVHDY NPEKLEPSPV
QDEYAPVIFS QETVKHIISV DMMSGKEDHD NILRSRATGK GALTSPFKLL KSNHLGVVLT
FTVYKYDLPP NATPEERIHA TLGYLGASFD VPSLVDKLLE QLASKQKIVV RLYDTTNHTS
PIKMYGSDFT VSGDLQHISS IDFGDPTRKH EMHCRFKHEP PLPWSAIIIS AAVAIIVLLV
GHIIYATLNS LEKAEQDYIV MRELKGQAEA ADVAKSQFLA TVSHEIRTPM NGVLGMLQML
MDTELDTTQQ DFVVTAQESG KALINLINEV LDLAKIESGR IELEAVPFDV RDILDNVVSL
FYEKSQAKGI ELAVLVSDQV PDVLIGDPWR FRQIITNLVG NSMKFTERGH IFVQVHLVEE
LKRAGNIFYD VSAQNREVLD DPDNMKLWNT LSGLEVADSW KSLENFRMFK TSTGETDTIN
LVVRVEDTGI GITKNAQLRI FTPFMQADSS TSRTYGGTGI GLSITKRLVE LMGGEIGFTS
KSGVGSTFSF TAIFKENRKG PGDIKRYYFE PTPSDFQGMR ALIIDGRNAR AEITMYHLQR
LGIHCNLVAT TESAFSALLE ACTSSKSNPN MVLVDTEAWG KGSGFAFYRR LVDLQLKGTH
KSSEPMPKIF LLGTSISPAE SDYLRLTGYG DCIRKPLRLS TIAASFRKTL GIGVTRQHNR
DQSSVLQSVL TGKQILVVDD NAVNRKVAAG SLKKYGAIVT CVDSGNDAID MLKPPHTFDA
CFMDVQMPEM DGFEATRLIR SVEKKINDMI QMGEVSADNY GNKPHWHVPI LAMTADVIQA
TFEKCMECGM DGYVSKPFEE QQLYSAVAHF LETGETDPTS
//