ID A0A445DKT5_ARAHY Unreviewed; 1030 AA.
AC A0A445DKT5;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=Ahy_A04g021535 {ECO:0000313|EMBL:RYR63780.1};
OS Arachis hypogaea (Peanut).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC dalbergioids sensu lato; Dalbergieae; Pterocarpus clade; Arachis.
OX NCBI_TaxID=3818 {ECO:0000313|EMBL:RYR63780.1, ECO:0000313|Proteomes:UP000289738};
RN [1] {ECO:0000313|EMBL:RYR63780.1, ECO:0000313|Proteomes:UP000289738}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Fuhuasheng {ECO:0000313|Proteomes:UP000289738};
RC TISSUE=Leaves {ECO:0000313|EMBL:RYR63780.1};
RA Chen X.;
RT "Sequencing of cultivated peanut Arachis hypogaea provides insights into
RT genome evolution and oil improvement.";
RL Submitted (JAN-2019) to the EMBL/GenBank/DDBJ databases.
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: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00169}.
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:RYR63780.1}.
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DR EMBL; SDMP01000004; RYR63780.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A445DKT5; -.
DR OrthoDB; 5476858at2759; -.
DR Proteomes; UP000289738; Chromosome a04.
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; cd16922; HATPase_EvgS-ArcB-TorS-like; 1.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd06223; PRTases_typeI; 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; IPR000836; PRibTrfase_dom.
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; 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};
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:UP000289738};
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 12..32
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 402..421
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 163..389
FT /note="CHASE"
FT /evidence="ECO:0000259|PROSITE:PS50839"
FT DOMAIN 457..725
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 753..872
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 898..1027
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT MOD_RES 948
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1030 AA; 115631 MW; 89D4445BD703CC91 CRC64;
MSLLHVVGFG LKVGHLLWVP CCLIVSFIYL NWFNCNLGIN HNHNCSNNNK WKMGFLGDYD
GKVWLNNWWE KNLGNTCKQY YYKYNSLRRS WWRKLWHAYV VFWIVISSSR FLHMSSEATE
KRKESLVSLC DERARMLQDQ FNVSMNHIQA MSILISTFHH AMDPSAIDQK TFARYTERTA
FERPLTSGVA YAVRVLHSER EQFEKQQGWT IKRMDTLEQN PVQEDDFALE ALEPSPIQEE
YAPVIFAQET IKHVISVDVL SGKEDRQNVL RARESGKGVL TAPFRLLKTN RLGVILTFAV
YKKELPSNAT PDERIQATDG YLGGVFDIES LVEKLLQQLA SKQSVIVNVY DTTNHTDPIA
MYGSDVLGDE FYHVSTLNFG DPFRKHEMHC RFKQKPPWPW EAIHSSVGML VIAVLIGYIL
YATVNRMFIS EDNYNEQMEL KKRAQAADVA KSQFLATVSH EIRTPMNGVL GMLNMLMDTD
LDVTQQEYVR TAQGSGKALV SLINEVLDQA KIDSGKLELE AVVFDLRAIL DDVLLLFSEK
SQGKGVELAV YVSDKVPEQL IGDPGRFRQI ITNLMGNSIK FTEKGHIFVT IHLVEEVVHS
IEVEPQSTSK DTLSGYPVAD IRRSWEGFKA FSQEGPLGSF SSPSSELVNL IVSVEDTGVG
IPLEAQSRIF TPFMQVDPSI SRKHGGTGIG LSISKCLVGR MNGEIGFVSI PNIGSTFTFT
AVFTNGSPNS KEGRTQQINN QPHLASSEFH GTNALVIDPR PIRAKVSRYH LQRLDIRVEL
VSDLDQGLSL ITNGNSAISI VFIEQEVWDR DSSISSHFVN NTRKVDPPKL FILVNSNSSF
RASSVNSGDP FPVVITKPLK ASMLAVTLQR AMGVGNRGNT RNVELPSLSL QHLLRGRRIL
VVDDNSVNRT VAAGALKKYG ADVVCVSSGK DAISKLKPPH QFDACFMDIQ MPEMDGFEAT
RRIRELEHMA SIEDGDGNNS KLRVPILAMT ADVMQATNEE CLKSGMDGYV SKPFEAEQLY
REVSRFFPTS
//
