ID A0DBT0_PARTE Unreviewed; 728 AA.
AC A0DBT0;
DT 28-NOV-2006, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2006, sequence version 1.
DT 27-MAR-2024, entry version 74.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=GSPATT00039393001 {ECO:0000313|EMBL:CAK80497.1};
OS Paramecium tetraurelia.
OC Eukaryota; Sar; Alveolata; Ciliophora; Intramacronucleata;
OC Oligohymenophorea; Peniculida; Parameciidae; Paramecium.
OX NCBI_TaxID=5888 {ECO:0000313|EMBL:CAK80497.1, ECO:0000313|Proteomes:UP000000600};
RN [1] {ECO:0000313|EMBL:CAK80497.1, ECO:0000313|Proteomes:UP000000600}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Stock d4-2 {ECO:0000313|EMBL:CAK80497.1,
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; CT868367; CAK80497.1; -; Genomic_DNA.
DR RefSeq; XP_001447894.1; XM_001447857.1.
DR AlphaFoldDB; A0DBT0; -.
DR STRING; 5888.A0DBT0; -.
DR EnsemblProtists; CAK80497; CAK80497; GSPATT00039393001.
DR GeneID; 5033680; -.
DR KEGG; ptm:GSPATT00039393001; -.
DR eggNOG; KOG0519; Eukaryota.
DR HOGENOM; CLU_013410_0_0_1; -.
DR InParanoid; A0DBT0; -.
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; 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 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..28
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 40..67
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 346..558
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 602..727
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT MOD_RES 658
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:CAK80497.1"
SQ SEQUENCE 728 AA; 84169 MW; 239C4237F7EDB4E1 CRC64;
NYILQCPKHQ QLFFLLIYLL TIENILRNSN KCYQILTHLL YLYIFLRMMI QFYSLFALFE
FILFVLWQPL NHTLLHLEKQ PLEKNTTSPN TPPQKQANPI AHLSYGDQVQ QDLLEEKSPH
PEKNANVALD EDLLNCLPYG LALIDKNYHV LHHNKKLLHY LMVQSTDQIV NSLDQLLSNA
ELNSFKTHLH AKHKSPIVPL RKLKQNSANQ CQVNSGRTLN QTNWLSDRLK VNLKYRESFQ
SSIHDEVIYS YVQFVMNEFQ SNIHRRMSIG QDSQSKTSDT THMFQFHVVQ DHKSKKKHYQ
IKVYEVKLQS KLKDPVYLFV IENITNKEEL KELTFRFKFQ QALLNSFSHE LRTPLNCSLP
LLEVLSKKID EELYENLLLP AITSCKRLLL QINDILDYGQ IECQDFKLNL GKFCISEILN
DLKILFQSEC RQKQIELILN FNGSLQLCSD KLRITQILVN LLSNSVKFTK QGGRIVLSVK
KKENQYVFSV WDNGEGINSE QILNVNNKLL QQNGSIKLGL GLRVSQGIVK YLSGDGELQI
KSEKGFYTSV SFSIDEHSQN EIKEIEPSLK DVEEIASNSK DSVQKVYVSS KKFLNQQCKC
PQILIVDDVP FNHIALFALL QAFGWKADSA YDGDSAIRKV KQKLHNTCCK IFRLIFMDIE
MPGKNGFLVS SEIQEILRKE RQKTVIVMCS AYNGQENAQK AHESGMHEIV SKPISLESLQ
TLIGKYFC
//
