ID A0A1U7ZPU2_NELNU Unreviewed; 1013 AA.
AC A0A1U7ZPU2;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN Name=LOC104592867 {ECO:0000313|RefSeq:XP_010250687.1,
GN ECO:0000313|RefSeq:XP_010250688.1};
GN ORFNames=HUJ06_004868 {ECO:0000313|EMBL:DAD34228.1};
OS Nelumbo nucifera (Sacred lotus).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Proteales; Nelumbonaceae; Nelumbo.
OX NCBI_TaxID=4432 {ECO:0000313|Proteomes:UP000189703, ECO:0000313|RefSeq:XP_010250687.1};
RN [1] {ECO:0000313|EMBL:DAD34228.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Leaf {ECO:0000313|EMBL:DAD34228.1};
RX PubMed=32343808;
RA Shi T., Rahmani R.S., Gugger P.F., Wang M., Li H., Zhang Y., Li Z.,
RA Wang Q., Van de Peer Y., Marchal K., Chen J.;
RT "Distinct Expression and Methylation Patterns for Genes with Different
RT Fates following a Single Whole-Genome Duplication in Flowering Plants.";
RL Mol. Biol. Evol. 37:2394-2413(2020).
RN [2] {ECO:0000313|RefSeq:XP_010250687.1, ECO:0000313|RefSeq:XP_010250688.1}
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
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 ---------------------------------------------------------------------------
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; DUZY01000004; DAD34228.1; -; Genomic_DNA.
DR RefSeq; XP_010250687.1; XM_010252385.2.
DR RefSeq; XP_010250688.1; XM_010252386.2.
DR GeneID; 104592867; -.
DR KEGG; nnu:104592867; -.
DR OrthoDB; 5476858at2759; -.
DR Proteomes; UP000189703; Unplaced.
DR Proteomes; UP000607653; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
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: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, ECO:0000313|RefSeq:XP_010250687.1};
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:UP000189703};
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 61..79
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 363..385
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 128..354
FT /note="CHASE"
FT /evidence="ECO:0000259|PROSITE:PS50839"
FT DOMAIN 422..692
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 720..842
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 868..1005
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT MOD_RES 918
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1013 AA; 113690 MW; 1BD82CE71FD7D96C CRC64;
MNWFTNSGVM EKKTGFLLDK GKIWLSWWEN LLAASGWKIH HYYQYIGSKK VHGTTWWRKV
LVAWVVLWIL VSFSVFWYMS SQATEKNKET LASMCDERAR MLQDQFNVSM NHVQALSILV
ATFHHGKNPS VIDQTTFARY TERTAFERPL TSGVAYAVRV LHSEREQFEK QQGWTIKRMD
TLEQTPVQED GNAFEPKEPS PVQEEYAPVI FAQDTISHVV SLDVLSGKED RENVLRARVS
GKAVLSAPFR LLKSNRLGVI LTFAVYKSEL PSNATPNERI QATDGYLGGI FDIESLVEKL
LHQLASKQTI IVNVYDTTNL SHPISMYGPN VTDDRLYHIS TLNFGDPYRK HEMRCRFKQK
PPWPWLAITT SVGILVIALL VGHIFHATVN RIAKVEDDYR KMMELKKRAE AADVAKSQFL
ATVSHEIRTP MNGVLGMMQM LMDTDLDIIQ QDHVRTAQAS GKALVSLINE VLDQAKIESG
KLELEAVRFD IRAILDDVLS LFSGKSQDKG LELAVYISDQ VPEVLIGDPG RFRQIMANLV
GNSIKFTERG HIFVTVHCAE EVMGSIEVET ETSSKNTLSG FPVADRCCSW RAFKTFSQER
PPSPQTFLST SSELINLIVS VEDTGVGIPL EAQSRIFTPF MQVGPSISRT HGGTGIGLSI
SKCLVGLMNG EIGFASKPQV GSTFTFTAVF ANGCSNLKEY NNQQIDNHSK PLSSEFQGMT
ALVVDPRPVR AKVTRYHLQR LGIQVEVVSN LNESLSSISS GTTVIKMILV EKEAWIKDTD
LSNIFINKLR KDYKVDPPKL FLLANSISST KTIAVKCSGY TLNVIMKPLR VSMLAVSLQR
AMGVVNKGNC LNRELPILSL CNLLHGKRIL VVDDNYVNLR VAAGALKKYG ADVICTDSGK
KAIKMLKPPH NFDACFMDIQ MPEMDGFEAT RRIRNLEHAI NDRIRHGIVT METCRNILNW
HVPILAMTAD VIQATHEECL KCGMDGYVSK PFEGEQLYQE VSRFFRSTPT CNQ
//
