ID C5WN04_SORBI Unreviewed; 996 AA.
AC C5WN04;
DT 01-SEP-2009, integrated into UniProtKB/TrEMBL.
DT 01-SEP-2009, sequence version 1.
DT 27-MAR-2024, entry version 86.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN Name=HK1 {ECO:0000313|EMBL:AHZ44512.1};
GN ORFNames=SORBI_3001G113200 {ECO:0000313|EMBL:EER93561.1};
OS Sorghum bicolor (Sorghum) (Sorghum vulgare).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC Panicoideae; Andropogonodae; Andropogoneae; Sorghinae; Sorghum.
OX NCBI_TaxID=4558 {ECO:0000313|EMBL:EER93561.1, ECO:0000313|Proteomes:UP000000768};
RN [1] {ECO:0000313|EMBL:EER93561.1, ECO:0000313|Proteomes:UP000000768}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. BTx623 {ECO:0000313|Proteomes:UP000000768};
RX PubMed=19189423; DOI=10.1038/nature07723;
RA Paterson A.H., Bowers J.E., Bruggmann R., Dubchak I., Grimwood J.,
RA Gundlach H., Haberer G., Hellsten U., Mitros T., Poliakov A., Schmutz J.,
RA Spannagl M., Tang H., Wang X., Wicker T., Bharti A.K., Chapman J.,
RA Feltus F.A., Gowik U., Grigoriev I.V., Lyons E., Maher C.A., Martis M.,
RA Narechania A., Otillar R.P., Penning B.W., Salamov A.A., Wang Y., Zhang L.,
RA Carpita N.C., Freeling M., Gingle A.R., Hash C.T., Keller B., Klein P.,
RA Kresovich S., McCann M.C., Ming R., Peterson D.G., Mehboob-ur-Rahman,
RA Ware D., Westhoff P., Mayer K.F., Messing J., Rokhsar D.S.;
RT "The Sorghum bicolor genome and the diversification of grasses.";
RL Nature 457:551-556(2009).
RN [2] {ECO:0000313|EMBL:AHZ44512.1}
RP NUCLEOTIDE SEQUENCE.
RA Rakshit S., Ganapathy K., Monika D., Sushma G., Swapna M., Talwar H.,
RA Patil J.;
RL Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:EER93561.1}
RP NUCLEOTIDE SEQUENCE.
RA Paterson A., Mullet J., Bowers J., Bruggmann R., Dubchak I., Grimwood J.,
RA Gundlach H., Haberer G., Hellsten U., Mitros T., Poliakov A., Schmutz J.,
RA Spannagl M., Tang H., Wang X., Wicker T., Bharti A., Chapman J., Feltus F.,
RA Gowik U., Grigoriev I., Lyons E., Maher C., Martis M., Narechania A.,
RA Otillar R., Penning B., Salamov A., Wang Y., Zhang L., Carpita N.,
RA Freeling M., Gingle A., Hash C., Keller B., Klein P., Kresovich S.,
RA Mccann M., Ming R., Peterson D., Rahman M., Ware D., Westhoff P., Mayer K.,
RA Messing J., Sims D., Jenkins J., Shu S., Rokhsar D.;
RT "WGS assembly of Sorghum bicolor.";
RL Submitted (FEB-2017) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0000313|Proteomes:UP000000768}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. BTx623 {ECO:0000313|Proteomes:UP000000768};
RX PubMed=29161754; DOI=10.1111/tpj.13781;
RA McCormick R.F., Truong S.K., Sreedasyam A., Jenkins J., Shu S., Sims D.,
RA Kennedy M., Amirebrahimi M., Weers B.D., McKinley B., Mattison A.,
RA Morishige D.T., Grimwood J., Schmutz J., Mullet J.E.;
RT "The Sorghum bicolor reference genome: improved assembly, gene annotations,
RT a transcriptome atlas, and signatures of genome organization.";
RL Plant J. 93:338-354(2018).
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}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00169}.
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DR EMBL; KJ544884; AHZ44512.1; -; Genomic_DNA.
DR EMBL; KJ544885; AHZ44513.1; -; Genomic_DNA.
DR EMBL; KJ544886; AHZ44514.1; -; Genomic_DNA.
DR EMBL; KJ544887; AHZ44515.1; -; Genomic_DNA.
DR EMBL; KJ544888; AHZ44516.1; -; Genomic_DNA.
DR EMBL; KJ544889; AHZ44517.1; -; Genomic_DNA.
DR EMBL; CM000760; EER93561.1; -; Genomic_DNA.
DR RefSeq; XP_002466563.1; XM_002466518.1.
DR AlphaFoldDB; C5WN04; -.
DR STRING; 4558.C5WN04; -.
DR EnsemblPlants; EER93561; EER93561; SORBI_3001G113200.
DR GeneID; 8060004; -.
DR Gramene; EER93561; EER93561; SORBI_3001G113200.
DR KEGG; sbi:8060004; -.
DR eggNOG; KOG0519; Eukaryota.
DR HOGENOM; CLU_000445_16_4_1; -.
DR InParanoid; C5WN04; -.
DR OMA; DSWGPQM; -.
DR OrthoDB; 5476858at2759; -.
DR Proteomes; UP000000768; Chromosome 1.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0019955; F:cytokine binding; IEA:EnsemblPlants.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:EnsemblPlants.
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:SF51; HISTIDINE KINASE 4; 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, ECO:0000313|EMBL:AHZ44512.1};
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:UP000000768};
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 39..60
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 331..357
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 111..295
FT /note="CHASE"
FT /evidence="ECO:0000259|PROSITE:PS50839"
FT DOMAIN 390..676
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 701..828
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 852..990
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT REGION 1..29
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 902
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 996 AA; 109154 MW; 2459EA438D27CD0B CRC64;
MGVGGGGEAA AASAAPAEEA AAAGKDGEEG TRWTMKEKLI AAAVLLWMLV AATIGVFLHW
SIRHAALRKE EEGLVSMCEE RARMLQDQFA VSVNHVHALA ILVATFHYEK HPPALDQDTF
AEYTARTSFE RPLLSGVAYA QRVEHADREG FERQQGWIIK TMKHEPSPVQ DEYAPVVYSQ
ETVSYIEGLD MMSGEEDREN ILRSRASGKA VLTRPFRLMS NHLGVVLTFP VYHVDLPPDA
KEEERVAATA GYLGGSFDVE SLVENLLRQL AGNQELVVNV YDVTNSSDPL VMYGSEVPLG
IPSPWHICML DFGDPFRKHH MVCRYRNKPP LPWSAISTPS GVFVICMLVG YIVFAAWSRY
DNVKEDCRKM EELKKQAEAA DVAKSQFLAT VSHEIRTPMN GVLGMLDMLL DTDLTSTQRD
FAQTAQVCGK ALISLINEVL DRAKIEAGKL DLESVPFDLR SILDDVIALF SSKSREKGIE
LAVYVSERVP EILLGDPGRF RQIITNLVGN SIKFTERGHI FVQVHLADHS NLATESEVEP
VANGMNGHKD EKTAVATGVS LNTLSGFEAA DSRNSWENFK LLLSYEKNEM PYESVSDKVT
LVVSVEDTGI GIPLDAQAKV FTPFMQADSS TSRTYGGTGI GLSISQCLVE LMGGQINFVS
RPQVGSTFTF TAVLQRCDRS AIGDSKPVML HPLPSSFKGL SALLVDTRPV RATVTKYHLQ
RLGIACDVVA TIDLALGVLS GRNGSSLTST KQPCMLLIES DSWGFKIDVS LRSRLLEMKQ
DGHTNLLPKI ILLAAAESSK LKAHYAVDSV ITKPLKASAL AACLFQTLGI TQSSNERRDN
SGSLHGLLLG KNILVVDDNK VNLRVAAGTL KKFGAKVECV ESGKDALALL QVPYKFHLCL
MDIQMPEMDG FEATQQIRTM EAKANEQAVA CDDSETDGAT RAAKWHLPVL AMTADVIQAT
HEECTKYGMD GYVTKPFEEK QLFQALQKFL DPGMSS
//
