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Database: UniProt
Entry: A0A6A6KC30_HEVBR
LinkDB: A0A6A6KC30_HEVBR
Original site: A0A6A6KC30_HEVBR 
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}.
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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
//
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