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Database: UniProt
Entry: A0D7J3_PARTE
LinkDB: A0D7J3_PARTE
Original site: A0D7J3_PARTE 
ID   A0D7J3_PARTE            Unreviewed;       770 AA.
AC   A0D7J3;
DT   28-NOV-2006, integrated into UniProtKB/TrEMBL.
DT   28-NOV-2006, sequence version 1.
DT   27-MAR-2024, entry version 78.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=GSPATT00002052001 {ECO:0000313|EMBL:CAK79010.1};
OS   Paramecium tetraurelia.
OC   Eukaryota; Sar; Alveolata; Ciliophora; Intramacronucleata;
OC   Oligohymenophorea; Peniculida; Parameciidae; Paramecium.
OX   NCBI_TaxID=5888 {ECO:0000313|EMBL:CAK79010.1, ECO:0000313|Proteomes:UP000000600};
RN   [1] {ECO:0000313|EMBL:CAK79010.1, ECO:0000313|Proteomes:UP000000600}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Stock d4-2 {ECO:0000313|EMBL:CAK79010.1,
RC   ECO:0000313|Proteomes:UP000000600};
RX   PubMed=17086204; DOI=10.1038/nature05230;
RG   Genoscope;
RA   Aury J.-M., Jaillon O., Duret L., Noel B., Jubin C., Porcel B.M.,
RA   Segurens B., Daubin V., Anthouard V., Aiach N., Arnaiz O., Billaut A.,
RA   Beisson J., Blanc I., Bouhouche K., Camara F., Duharcourt S., Guigo R.,
RA   Gogendeau D., Katinka M., Keller A.-M., Kissmehl R., Klotz C., Koll F.,
RA   Le Moue A., Lepere C., Malinsky S., Nowacki M., Nowak J.K., Plattner H.,
RA   Poulain J., Ruiz F., Serrano V., Zagulski M., Dessen P., Betermier M.,
RA   Weissenbach J., Scarpelli C., Schachter V., Sperling L., Meyer E.,
RA   Cohen J., Wincker P.;
RT   "Global trends of whole-genome duplications revealed by the ciliate
RT   Paramecium tetraurelia.";
RL   Nature 444:171-178(2006).
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DR   EMBL; CT868318; CAK79010.1; -; Genomic_DNA.
DR   RefSeq; XP_001446407.1; XM_001446370.1.
DR   AlphaFoldDB; A0D7J3; -.
DR   STRING; 5888.A0D7J3; -.
DR   EnsemblProtists; CAK79010; CAK79010; GSPATT00002052001.
DR   GeneID; 5032192; -.
DR   KEGG; ptm:GSPATT00002052001; -.
DR   eggNOG; KOG0519; Eukaryota.
DR   HOGENOM; CLU_358824_0_0_1; -.
DR   InParanoid; A0D7J3; -.
DR   Proteomes; UP000000600; Partially assembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
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   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:SF28; PEROXIDE STRESS-ACTIVATED HISTIDINE KINASE MAK2; 1.
DR   PANTHER; PTHR43719; TWO-COMPONENT HISTIDINE 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   Membrane {ECO:0000256|SAM:Phobius};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW   ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000000600};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        37..57
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        104..124
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          304..527
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   DOMAIN          636..756
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000259|PROSITE:PS50110"
FT   MOD_RES         690
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ   SEQUENCE   770 AA;  88765 MW;  D7FF9E8D655ED7C3 CRC64;
     MNSCIKSIGN AKILQIMLIA DSLLIHIQSY LISNYNYLII ALSLTCFHGI VLTFEHFLKG
     KNKLFNSLFN AFKGVAQIIV HYLLEQNWLI FAGIQLVCLL KQDVLHVNYV SSIFFITQIF
     CVAFSKKDFI IIGVIRTVFN YLFISQIFRI EKQNKLIQLE NLLKHIQHNE FCLLDSNFNP
     IFQLQFFNEL KGEQVVGGQE FYNQTRIITP RDNTTNLIRD MPSNFEDEMK QTLSIQEILY
     HVKKSKVHLK KKLYYQLNNS NYNISIENIL LDDYNSIVMI QKNKQFENSQ SSNKINFMIK
     TVRKVSHDMR NPLNAIINMQ MCLKDYIDQE LVLKYLKPSL NSCHLLLNLI NDILDQAQVE
     NKKLKLVYKK FNLEKLICKT ISIFDSLKDK KDINITFNYD SKLPILVNSD KFRIRQIIMN
     LLSNAIKYTR PSGEVYIDCS ESSQRKNFIR ISIQDTGYGI KPENLQYLFK EYSKIEDGEN
     QNLNPFGVGL GLMISNELAK LLSNNGIQVQ SEFGIGSKFY FEIENKQLPP EDISESQLLI
     NHQNGLPSLD VHFFTGLNSQ KSPTISLALP QIESSKKIIL KKSQKTITLM NNSVHNLTKH
     KGKNDEKSIA RKSSLSAKQV EMLIQKWYVS TNYKPPVLIV DDDEINILVL QYLLEQMDIS
     SDSAMNGMTC LQKFVERQND GISYQLVFLD INMPVMDGYE LAKKLIQIDP LIILIACSGD
     ASDQHQLEQC KQSGILGCIL KPILKNNLKE LLVKLSEGIK HDSQQFSYYC
//
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