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Database: UniProt
Entry: D7M2Z3_ARALL
LinkDB: D7M2Z3_ARALL
Original site: D7M2Z3_ARALL 
ID   D7M2Z3_ARALL            Unreviewed;       846 AA.
AC   D7M2Z3;
DT   10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT   10-AUG-2010, sequence version 1.
DT   27-MAR-2024, entry version 60.
DE   RecName: Full=Histidine kinase domain-containing protein {ECO:0000259|PROSITE:PS50109};
GN   ORFNames=ARALYDRAFT_909023 {ECO:0000313|EMBL:EFH47691.1};
OS   Arabidopsis lyrata subsp. lyrata (Lyre-leaved rock-cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX   NCBI_TaxID=81972 {ECO:0000313|Proteomes:UP000008694};
RN   [1] {ECO:0000313|Proteomes:UP000008694}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. MN47 {ECO:0000313|Proteomes:UP000008694};
RX   PubMed=21478890; DOI=10.1038/ng.807;
RA   Hu T.T., Pattyn P., Bakker E.G., Cao J., Cheng J.-F., Clark R.M.,
RA   Fahlgren N., Fawcett J.A., Grimwood J., Gundlach H., Haberer G.,
RA   Hollister J.D., Ossowski S., Ottilar R.P., Salamov A.A., Schneeberger K.,
RA   Spannagl M., Wang X., Yang L., Nasrallah M.E., Bergelson J.,
RA   Carrington J.C., Gaut B.S., Schmutz J., Mayer K.F.X., Van de Peer Y.,
RA   Grigoriev I.V., Nordborg M., Weigel D., Guo Y.-L.;
RT   "The Arabidopsis lyrata genome sequence and the basis of rapid genome size
RT   change.";
RL   Nat. Genet. 43:476-481(2011).
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DR   EMBL; GL348718; EFH47691.1; -; Genomic_DNA.
DR   RefSeq; XP_002871432.1; XM_002871386.1.
DR   AlphaFoldDB; D7M2Z3; -.
DR   STRING; 81972.D7M2Z3; -.
DR   EnsemblPlants; scaffold_601080.1; scaffold_601080.1; scaffold_601080.1.
DR   Gramene; scaffold_601080.1; scaffold_601080.1; scaffold_601080.1.
DR   eggNOG; KOG0519; Eukaryota.
DR   HOGENOM; CLU_336899_0_0_1; -.
DR   Proteomes; UP000008694; Unassembled WGS sequence.
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   Gene3D; 1.10.287.130; -; 1.
DR   Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR   Gene3D; 3.30.450.20; PAS domain; 1.
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; IPR035965; PAS-like_dom_sf.
DR   InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR   PANTHER; PTHR43047:SF68; HISTIDINE KINASE 5; 1.
DR   PANTHER; PTHR43047; TWO-COMPONENT HISTIDINE PROTEIN KINASE; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF00512; HisKA; 1.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00387; HATPase_c; 1.
DR   SMART; SM00388; HisKA; 1.
DR   SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR   SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR   SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 1.
DR   PROSITE; PS50109; HIS_KIN; 1.
PE   4: Predicted;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008694}.
FT   DOMAIN          352..597
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   REGION          795..846
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          88..115
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          720..747
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        815..846
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   846 AA;  96762 MW;  174D22459246A418 CRC64;
     METDQIEEMD VEVLSSMWPE DVGTEADKQF NVEKPAGDLD TLTEVTIEEK PTIADLTRLP
     ELMNSTQQGS SQLTNLVKQW EYMQDNAVRL LREELKNLNR QREEAEAQEL KIIEEYKFES
     NEPENVPVLD ETSDSFRRFR HKKRDEFDTV AYWKPKMLEA STERERRLIE KLSESLKTME
     SQSAPVQELT QNLKKAEGFL HFILQNAPIV MGHQDIDLRY LFIYNKYPSL REQDILGKTD
     VEIFHGGGIK EYQDFKREVL EKGKASKREI TFTTDLFGSK TFLVYVEPVY NKAGEKIGIN
     YMGMEVTEQV DKREKMAKLR EDNAVRKAME SELNKTIHIT EETMRAKQML ATMSHEIRSP
     LSGVVGMAEI LSTTKLDKEQ RQLLNVMISS GDLVLQLIND ILDISKVESG VMKLEATKFR
     PREVVKHVLQ TAAASLKKSL TLEGNIADDV PIEVVGDVLR IRQILTNLIS NAIKFTHEGN
     VGIKLQVISE PSFARDNALN ADTEEHEQNG LTETSVWICC DVWDTGIGIP GKQAKNAIPC
     LFKKYMQASA DHARKYGGTG LGLAICKQLV ELMGGQLTVT SRVNEGSTFT FILPYKVGTS
     DDYSDDQDEF SDMADHHSKP DDTAEGYFQF KPLETDQIEE MDVEVLSSMW PEDVGTEADK
     QFNVEKPAGD LDTLKEVTIE EKLTIADLTR LPELLNSTPQ GSSQLTNLMK QWEYMQHNAV
     RLLREELKNL NRQREEAEAK ELKIIEEYKF ESNEPENVSV LDETSDWFRG FRQKKRDVLV
     DSKKIEIYEE FDSKKVDDEE NSDTVATSTD MNEAVNVEKS KEAEQEEAEV KEEESERRSN
     RNKRPS
//
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