ID A0A6A6KC30_HEVBR Unreviewed; 980 AA.
AC A0A6A6KC30;
DT 17-JUN-2020, integrated into UniProtKB/TrEMBL.
DT 17-JUN-2020, sequence version 1.
DT 27-MAR-2024, entry version 15.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=GH714_017244 {ECO:0000313|EMBL:KAF2286480.1};
OS Hevea brasiliensis (Para rubber tree) (Siphonia brasiliensis).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Malpighiales; Euphorbiaceae; Crotonoideae; Micrandreae;
OC Hevea.
OX NCBI_TaxID=3981 {ECO:0000313|EMBL:KAF2286480.1, ECO:0000313|Proteomes:UP000467840};
RN [1] {ECO:0000313|EMBL:KAF2286480.1, ECO:0000313|Proteomes:UP000467840}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. GT1 {ECO:0000313|Proteomes:UP000467840};
RC TISSUE=Leaf {ECO:0000313|EMBL:KAF2286480.1};
RX PubMed=31838037; DOI=10.1016/j.molp.2019.10.017;
RA Liu J., Shi C., Shi C.C., Li W., Zhang Q.J., Zhang Y., Li K., Lu H.F.,
RA Shi C., Zhu S.T., Xiao Z.Y., Nan H., Yue Y., Zhu X.G., Wu Y., Hong X.N.,
RA Fan G.Y., Tong Y., Zhang D., Mao C.L., Liu Y.L., Hao S.J., Liu W.Q.,
RA Lv M.Q., Zhang H.B., Liu Y., Hu-Tang G.R., Wang J.P., Wang J.H., Sun Y.H.,
RA Ni S.B., Chen W.B., Zhang X.C., Jiao Y.N., Eichler E.E., Li G.H., Liu X.,
RA Gao L.Z.;
RT "The Chromosome-Based Rubber Tree Genome Provides New Insights into Spurge
RT Genome Evolution and Rubber Biosynthesis.";
RL Mol. Plant 13:336-350(2020).
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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KAF2286480.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; JAAGAX010000017; KAF2286480.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A6A6KC30; -.
DR Proteomes; UP000467840; Chromosome 3.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR GO; GO:0048856; P:anatomical structure development; IEA:UniProt.
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; 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:SF73; HISTIDINE KINASE 3; 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; 1.
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; 1.
PE 4: Predicted;
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000467840};
KW Signal {ECO:0000256|SAM:SignalP};
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 SIGNAL 1..18
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 19..980
FT /note="histidine kinase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5025525338"
FT TRANSMEM 70..90
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 110..132
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 395..417
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 160..386
FT /note="CHASE"
FT /evidence="ECO:0000259|PROSITE:PS50839"
FT DOMAIN 454..700
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 835..972
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT MOD_RES 885
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 980 AA; 109926 MW; 40549D0C922615B2 CRC64;
MLCCWIVSVI SLNWFVNGEI VESKTGLLGD GGKMWLRVWE KISGNSCKMH HHYYQYIGSK
RVRKTWWRRL LVAWVIGWIM VSLWILWYMS SQATEKRKRP LQACVMRGPG CYRISLMSLD
LLSYLSWVLS LLGNDNSKKL IHNLKFAEFA CGFDFGILKL NPEADLRTFA RYTERTAFER
PLTSGVAYAV RVHHSEREQF EKQQGWTIKR MDTLEQNPVH KDDYTPELLE PSPIQEEYAP
VIFAQDTISH VVSLDMLSGK EDRENVLRAR ESGTGVLTAP FRLLKTKRLG VILTFAVYKR
DIPSNATPNE RIQATDGYLG GVFDIELLVE KLLQQLASEQ TIIVDVYDTT NQSHPISMYG
SNVSDDGLQH VSSLNFGDPH RKHEMHCRFK QKPPWQWLAI TTSFGVLVIA LLIGHIFHAT
VNRIAKVEDD YHEMMELKKR AEAADIAKSQ FLATVSHEIR TPMNGVLGML HMLMDTDLDV
TQRDYVRTAQ ASGKALVSLI NEVLDQAKIE SGKLELEDVQ FNLRAILDDV LSLFSDKSQG
KGVEGVPANH HQSHGKFNKR HIFVTVHLVE EVIDSIDIGT EPSSRNTLSG LPIADRRRSW
AGFRAFSQEG SSRTLLPSPP DLINLIVSVE DTGEGIPLES QSRIFTPFMQ VGPSTSRKYG
GTGIGLSISK CLVGLMNGEI GFVSIPKIGT TFTFTAVFAN GCSNLNEYKS HKIGNQSNTI
FSEFQGMTAL VVDPRPVRAK VSRYHIQRLG IHVEVVYDLN QALCSISNEN AVVNMVLIEQ
EVWDRDSSVS ALFVSTIMKI DRDVSPKLFL LANSISSSKT NTATSGVYTL SAIMKPLRAN
DNGVNLKVAA GALKKYGADV VCAESGEKAI KLLTPPHQFD ACFMDIQMPE MDGFEATQKI
RDKEHNFNNS IQNGDASVGT YENVPNWHVP ILAMTADVIQ ATHEECRKCG MDGYVSKPFE
AEQLYREVSR FFQSTSNVIL
//