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Database: UniProt
Entry: A0DXR2_PARTE
LinkDB: A0DXR2_PARTE
Original site: A0DXR2_PARTE 
ID   A0DXR2_PARTE            Unreviewed;       854 AA.
AC   A0DXR2;
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=GSPATT00021453001 {ECO:0000313|EMBL:CAK87829.1};
OS   Paramecium tetraurelia.
OC   Eukaryota; Sar; Alveolata; Ciliophora; Intramacronucleata;
OC   Oligohymenophorea; Peniculida; Parameciidae; Paramecium.
OX   NCBI_TaxID=5888 {ECO:0000313|EMBL:CAK87829.1, ECO:0000313|Proteomes:UP000000600};
RN   [1] {ECO:0000313|EMBL:CAK87829.1, ECO:0000313|Proteomes:UP000000600}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Stock d4-2 {ECO:0000313|EMBL:CAK87829.1,
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; CT868640; CAK87829.1; -; Genomic_DNA.
DR   RefSeq; XP_001455226.1; XM_001455189.1.
DR   AlphaFoldDB; A0DXR2; -.
DR   STRING; 5888.A0DXR2; -.
DR   EnsemblProtists; CAK87829; CAK87829; GSPATT00021453001.
DR   GeneID; 5041011; -.
DR   KEGG; ptm:GSPATT00021453001; -.
DR   eggNOG; KOG0519; Eukaryota.
DR   HOGENOM; CLU_016833_0_0_1; -.
DR   InParanoid; A0DXR2; -.
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        18..36
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        42..63
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        114..132
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          450..674
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   DOMAIN          723..852
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000259|PROSITE:PS50110"
FT   MOD_RES         784
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ   SEQUENCE   854 AA;  99833 MW;  170C7CC467D615D6 CRC64;
     MGRAEKFRCL DNTNVKNLLI FFNSSIIFAQ IIENLIISRG PFIMTCLIFV LVMLIYQALS
     FYFRAMRIQL IIYSQYFMLT LFSVELQIDT YFLIFQQLSI FDTVFFNRNE KNKIVQNILF
     FGAIVINTYV FLRVGFHNLY FTDLIKALCQ SFLLKLLLYH FRQEHDVSLK EIQKLNNQEL
     EPSDPRVGNV ECEPQDASKL FKTFDVVPEG IIILEKNGKE DFTIKYSNSA AKYLVDADDH
     DQMLSELLDL RSVSPKQKSE EHLYKYSFSI QSQQSVKRNS FKIIPKQQSH IKSAFKISQQ
     LILENQSSSQ KQEFQFPPVQ IIFPGAQTKT ENINHPNSPS IHYATQHKKS LDEIDSFHFL
     LTQIWVQLHT LVKEKILNYQ NQPLYYIHES NPFVTNITKY QKKQCLDLKV YSAIHYNKPL
     LVIILRDVNH KDYIKVLKDY NSQKSKTLSF VSHEFRTPLT CIIQMLEEVI ENRNNLNLSD
     QQLIQSALDN SKYILNLSND LLDLAQIRAG KFKIRNAIFD LRSLLKECLK MFEIQAMKKN
     IQLNYYYDMS LPTEIWSDLN RIRQITVNLI GNALKFTLEG SITLRAYQDG VNEICIEVKD
     TGVGMREEDQ PKLFKAFAKI ENKEASQMNA QGVGLGLLIS NSIATQLNSE QRGLGFRSAY
     QEGTTFCFLV TNNKSTYIDE IENYEDSRKD IDFDLETKLN DFRRQSQNEK KFILQKNYCA
     CPQILLVEDN QFNVDSFLLK FHRTFKSLVK IDYTITGQLA EQKVQQRFLK QQHICHPYKL
     IFMDVELPIQ NGIVTSKNIK NYYRAMNATV TIVGCSGYAE EKEKKECLQY MDDYIVKPVP
     KQELERIMTS YFFK
//
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