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Database: UniProt
Entry: A0BPY0_PARTE
LinkDB: A0BPY0_PARTE
Original site: A0BPY0_PARTE 
ID   A0BPY0_PARTE            Unreviewed;       779 AA.
AC   A0BPY0;
DT   28-NOV-2006, integrated into UniProtKB/TrEMBL.
DT   28-NOV-2006, sequence version 1.
DT   27-MAR-2024, entry version 80.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=GSPATT00005348001 {ECO:0000313|EMBL:CAK60597.1};
OS   Paramecium tetraurelia.
OC   Eukaryota; Sar; Alveolata; Ciliophora; Intramacronucleata;
OC   Oligohymenophorea; Peniculida; Parameciidae; Paramecium.
OX   NCBI_TaxID=5888 {ECO:0000313|EMBL:CAK60597.1, ECO:0000313|Proteomes:UP000000600};
RN   [1] {ECO:0000313|EMBL:CAK60597.1, ECO:0000313|Proteomes:UP000000600}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Stock d4-2 {ECO:0000313|EMBL:CAK60597.1,
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; CT868008; CAK60597.1; -; Genomic_DNA.
DR   RefSeq; XP_001427995.1; XM_001427958.1.
DR   AlphaFoldDB; A0BPY0; -.
DR   STRING; 5888.A0BPY0; -.
DR   EnsemblProtists; CAK60597; CAK60597; GSPATT00005348001.
DR   GeneID; 5013779; -.
DR   KEGG; ptm:GSPATT00005348001; -.
DR   eggNOG; KOG0519; Eukaryota.
DR   HOGENOM; CLU_358824_0_0_1; -.
DR   InParanoid; A0BPY0; -.
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        12..31
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        37..57
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        64..84
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          309..535
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   DOMAIN          645..765
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000259|PROSITE:PS50110"
FT   MOD_RES         699
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ   SEQUENCE   779 AA;  89266 MW;  B4EDC3D57F6CA5C1 CRC64;
     MLALCKALNK ERILQFFLII DGLIVHMQTY VTQDFSFLVI GLTLACFHLI ILCFEYMCQK
     KSNLILLICL IKGVVIIGVS YLLMPQWQIY TGIQIVLIIQ LNEQYLKLTT LFFFLACIPC
     ICFGNVSEIT VEILRAVVNF FLILQIYKKK GNQSFINIKS LLSQISSEEF CILDMQYNPV
     YESKLFYSII KEQVMNISDH YQSRILTPRD QTTNLVKQSN CLENITTRPS LLIGDIIDQL
     KKKILKLDQK LIFEPTNTSL YQVSVQKLLI ENQEFILLIK HKLYNIESFK LQSQQQKEQV
     QTMIKTLHKV SHDMRNPLNA IINMQMCLSE LIDPNLFQKF LKPSLNSCHL LLNLINDILD
     AAQIENKSIR IVCRKFNLAK LIDKTISLFD LLKEKKGLNI TFNYDPKLPL KINSDKLRIR
     QIIMNLLSNA VKYTQPKGSI LIECIQSEQK SNSIIISVQD SGMGIKSENL KKLFQEFSKV
     NDLENQKANP FGIGLGLMIS NELAKLLSTN HSIGIQVQSE YGTGSKFYFE IENEEQPSED
     ISDSQISQKL AQKIPTLEFR ILQNIIQQKS PTVSIAIPMG ESSKRIIQKK NLKAINFMTS
     SLNYQATLRI RNESERNLSN KPSIQSRLIQ NLLQKWNELT QQHPPILIVD DNEFNILALQ
     YLLELSGISS DSAMNGIISI EKVNDRLKDN IPFQLIFMDL EMPLMLGLEA STRIHKLDRN
     VTIVACSGHK LTQEIVEQFK DCGIAFGVEK PITKIKLKDL LLKLSDGIRC DSSQFSQLF
//
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