ID A0A251TN39_HELAN Unreviewed; 1139 AA.
AC A0A251TN39;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN Name=AHK2 {ECO:0000313|EMBL:OTG12179.1};
GN ORFNames=HannXRQ_Chr10g0306861 {ECO:0000313|EMBL:OTG12179.1};
OS Helianthus annuus (Common sunflower).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; campanulids; Asterales; Asteraceae; Asteroideae;
OC Heliantheae alliance; Heliantheae; Helianthus.
OX NCBI_TaxID=4232 {ECO:0000313|EMBL:OTG12179.1, ECO:0000313|Proteomes:UP000215914};
RN [1] {ECO:0000313|Proteomes:UP000215914}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. SF193 {ECO:0000313|Proteomes:UP000215914};
RX PubMed=28538728; DOI=10.1038/nature22380;
RA Badouin H., Gouzy J., Grassa C.J., Murat F., Staton S.E., Cottret L.,
RA Lelandais-Briere C., Owens G.L., Carrere S., Mayjonade B., Legrand L.,
RA Gill N., Kane N.C., Bowers J.E., Hubner S., Bellec A., Berard A.,
RA Berges H., Blanchet N., Boniface M.C., Brunel D., Catrice O., Chaidir N.,
RA Claudel C., Donnadieu C., Faraut T., Fievet G., Helmstetter N., King M.,
RA Knapp S.J., Lai Z., Le Paslier M.C., Lippi Y., Lorenzon L., Mandel J.R.,
RA Marage G., Marchand G., Marquand E., Bret-Mestries E., Morien E.,
RA Nambeesan S., Nguyen T., Pegot-Espagnet P., Pouilly N., Raftis F.,
RA Sallet E., Schiex T., Thomas J., Vandecasteele C., Vares D., Vear F.,
RA Vautrin S., Crespi M., Mangin B., Burke J.M., Salse J., Munos S.,
RA Vincourt P., Rieseberg L.H., Langlade N.B.;
RT "The sunflower genome provides insights into oil metabolism, flowering and
RT Asterid evolution.";
RL Nature 546:148-152(2017).
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};
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DR EMBL; CM007899; OTG12179.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A251TN39; -.
DR STRING; 4232.A0A251TN39; -.
DR InParanoid; A0A251TN39; -.
DR OMA; QATFEGC; -.
DR OrthoDB; 5476858at2759; -.
DR Proteomes; UP000215914; Chromosome 10.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR GO; GO:0048856; P:anatomical structure development; IEA:UniProt.
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; 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 Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:OTG12179.1};
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:UP000215914};
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}.
FT TRANSMEM 36..54
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 157..178
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 205..224
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 510..534
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 273..499
FT /note="CHASE"
FT /evidence="ECO:0000259|PROSITE:PS50839"
FT DOMAIN 567..830
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 859..975
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 999..1136
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT MOD_RES 911
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 1049
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1139 AA; 127160 MW; D84F91AC67FA339C CRC64;
MSLNYKISGL NGTSSKMRKV KEPARGCNSV LNWKRLLLFV WVIVVSTGFC LFFLNGVFRT
KIEVTGTCKD NKSLVLVEQF NVSNELLHEL ASSFYKSDQI TALKCTKQLG DKLSTKHEIT
CSLNGVTNME LSGQCPVHDE KAPLVHEKLA REHDNGILKV CMWVLFVIAL CSPISCLWKN
RKGEMKKKEH TQSSSRSAGK WMKKLLVLFV LVGVTVSIWL FWYLNDGIQL RRRETIANMC
DERARMLQDQ FNVSMNHVHA LAILVSTFYH GKQPPAIDQK TFGEYTERTS FERPLTSGVA
YALRVRHSER EKFEKEHGWT IKKMDTEDQD QTLAQDCDPA NLDPSPIQDE YAPVILSQET
VSHIVSIDMM SGKEDRENIL RARASGKGVL TSPFKLLKSN HLGVVLTFAV YNTHLHQDAT
PEQRINATVG YLGASYDVPS LVEKLLHQLA SKQTIVVNVY DTTNASAAIN MYGPEEIDTG
FLHISSLDFG DPSRKHEMRC RFKQRPPPPW TAILASGGVL IITFLLGHIF YAAINRIAAV
EHDYRKMMEL KHRAEAADVA KSQFLATVSH EIRTPMNGVL GMLQMLMDTN LDAKQLDFAQ
TAHASGKDLI KLINEVLDQA KIESGRLELE EVPFELRTIL DNVVSLLSTK SQEKGIELAV
YVSNQLPEVV VGDPGRFRQI ITNLVENSLK FTHDRGHIFV SVHLADEVTD ENYMKIFNGS
KSNAVCNTLS GLPVVDRKKS WENFENLSRK DINESEQIKI LVTVEDTGVG IPIKAQSSIF
TPFMQADSST SRTYGGTGIG LSISKRLVGL MNGEIGFVSE PGTGSTFSFT GVFMKKETCS
LDTVLQQYHP DTSEFRGLRA LVIDQKNIRA EVTRYHLERM GISVTITSDF DSAQSSQSPI
DSAVFAMVLI DQEVWDKKSG LAFLRGLKSS TKLFLLANSV SPAIQDEIQS ANMVATVVPK
PLRLSILISC FQETISVGNT SFLARRKPST LGTLLRNKRI LVVDDNIVNR RVAEGALKKY
GAIVICVDSG KAALEKLKPP HSFHACFMDL QMPEMDGFEA TRQIRRLESM VNEQIESGEV
SIEMFGNAGH WHTPILAMTA DVIQATDEEC MKCGMDGYVS KPFEEEQLYS AAACFFESG
//
