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Database: UniProt
Entry: A0A061GQ66_THECC
LinkDB: A0A061GQ66_THECC
Original site: A0A061GQ66_THECC 
ID   A0A061GQ66_THECC        Unreviewed;      1017 AA.
AC   A0A061GQ66;
DT   03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT   03-SEP-2014, sequence version 1.
DT   27-MAR-2024, entry version 55.
DE   SubName: Full=Histidine kinase cytokinin receptor isoform 2 {ECO:0000313|EMBL:EOY29254.1};
GN   ORFNames=TCM_036845 {ECO:0000313|EMBL:EOY29254.1};
OS   Theobroma cacao (Cacao) (Cocoa).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Malvales; Malvaceae; Byttnerioideae; Theobroma.
OX   NCBI_TaxID=3641 {ECO:0000313|EMBL:EOY29254.1, ECO:0000313|Proteomes:UP000026915};
RN   [1] {ECO:0000313|EMBL:EOY29254.1, ECO:0000313|Proteomes:UP000026915}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Matina 1-6 {ECO:0000313|Proteomes:UP000026915};
RX   PubMed=23731509; DOI=10.1186/gb-2013-14-6-r53;
RA   Motamayor J.C., Mockaitis K., Schmutz J., Haiminen N., Iii D.L.,
RA   Cornejo O., Findley S.D., Zheng P., Utro F., Royaert S., Saski C.,
RA   Jenkins J., Podicheti R., Zhao M., Scheffler B.E., Stack J.C., Feltus F.A.,
RA   Mustiga G.M., Amores F., Phillips W., Marelli J.P., May G.D., Shapiro H.,
RA   Ma J., Bustamante C.D., Schnell R.J., Main D., Gilbert D., Parida L.,
RA   Kuhn D.N.;
RT   "The genome sequence of the most widely cultivated cacao type and its use
RT   to identify candidate genes regulating pod color.";
RL   Genome Biol. 14:R53.1-R53.24(2013).
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DR   EMBL; CM001887; EOY29254.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A061GQ66; -.
DR   STRING; 3641.A0A061GQ66; -.
DR   EnsemblPlants; EOY29254; EOY29254; TCM_036845.
DR   Gramene; EOY29254; EOY29254; TCM_036845.
DR   eggNOG; KOG0519; Eukaryota.
DR   InParanoid; A0A061GQ66; -.
DR   OMA; HEDACQT; -.
DR   Proteomes; UP000026915; Chromosome 9.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0009927; F:histidine phosphotransfer kinase activity; IBA:GO_Central.
DR   GO; GO:0000155; F:phosphorelay sensor kinase activity; IBA:GO_Central.
DR   GO; GO:0048856; P:anatomical structure development; IEA:UniProt.
DR   GO; GO:0010033; P:response to organic substance; IEA:UniProt.
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; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR   Gene3D; 3.30.450.20; PAS domain; 1.
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; 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   Pfam; PF00072; Response_reg; 1.
DR   PRINTS; PR00344; BCTRLSENSOR.
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; PS50109; HIS_KIN; 1.
DR   PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE   4: Predicted;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:EOY29254.1};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW   ProRule:PRU00169}; Receptor {ECO:0000313|EMBL:EOY29254.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000026915};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          378..677
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   DOMAIN          869..1016
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000259|PROSITE:PS50110"
FT   REGION          521..594
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          770..864
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          92..119
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          188..215
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        525..556
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        778..792
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        794..808
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        809..824
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        840..864
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         918
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ   SEQUENCE   1017 AA;  113869 MW;  AB97377BE50B4CC4 CRC64;
     MVCEMETDQI EDMDVEVLSS MWPEDISNDP GKQFNVEKPG GDQDMLEEVT IVEEPTIVDF
     KHLLELTNYT DKGSSQLAYL VKHWEYKQAN AVRLLREELD NLSRQRQESE LKKLEILEEH
     RFEEERYGGD KRPISILDEV YDIWLEVPRR KNDVVVPSKR VEIDAEYDTV IYWKQRALHF
     EKLLEASIQR EQLLKEKLQE SIKNLERQSS PVEELSQILK RADNFLHFVL QNAPVVIGHQ
     DKELRYRFIY NHFPSLQEED ILGKTDVEIF TGSGVKESQE FKKEVLEKGL PAKREITFET
     ELFGSKTFLI YVEPVFSKAG ETIGINYMGM DVTDQVRKRE KMAKLREEIA VQKAKETELN
     KTIHITEETM RAKQMLATMS HEIRSPLSGV VSMAEILSTT KLDREQRQLL DVMLSSGDLV
     LQLINDILDL SKVESGVMKL EATKFRPREV VKHVLQTAAA SLQKILTLEG HVTDDVPIEV
     IGDVLRIRQI LTNLISNAIK FTHEGKVGIK LYVVPEPPFA KEGSQHVSDG STANQSTTNV
     AKEETCISTS QASSDQKGFH GKKREGPCQN HSLSDKPGTP VMNGTIDGDE EQEELPETTV
     WIRCDVYDTG IGIPENALPT LFKKYMQVSA DHARKYGGTG LGLAICKQLV ELMGGRLTVS
     SRVHCGSTFT FILPYKVSLA CDHSDDLDDL SDMPEHDAAT DDATAGFFQF QPRTLGSLFS
     SNGSSRTQKL MPHNIGYANS HKLNGFADNS YSFPTNNGPT KELAPVEDAC SVAEAVGTSS
     EPEGSFSHSP DPDNESAICR DRHHQNDANA QNKVSTTELS SCSEASREVD AKMKISEPQL
     SPKQEKSDTG SQCTSNSSRE VSNLTSKPKI LLVEDNKINV MVTQSMMKQI GHTIDVVNNG
     IEAVHAVQRC SYDLVLMDVC MPVMDGLQAT RLIRSFEETG NWDAAEKAGI EQPLPSSDSL
     QYLPGCTPPT KRIPIIAMTA NALSESADEC YANGMDSFVS KPVTFQKLKE CLEQYLP
//
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